|
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 ... |
145-822 |
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: 1456.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVlissHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAV----NPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd14911 157 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGR 464
Cdd:cd14911 237 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 465 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 544
Cdd:cd14911 317 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 545 LFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDF 624
Cdd:cd14911 397 LFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 625 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMFRTV 704
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMFRTV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 705 SHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 784
Cdd:cd14911 557 SHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 636
|
650 660 670
....*....|....*....|....*....|....*...
gi 386768643 785 NVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14911 637 NVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
145-822 |
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: 1292.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASKPKGSGAvphpavlisshqETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES------------GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDV-KSYAFLSNGSLPVPGVDDYA 383
Cdd:cd01377 149 IRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDpSYYFFLSQGELTIDGVDDAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd01377 229 EFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd01377 309 REWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG-GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK- 621
Cdd:cd01377 388 QFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPNmGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKk 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 622 -TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGmaqqaltDTQFGARTRKGM 700
Cdd:cd01377 468 pKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESG-------GGGGKKKKKGGS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 701 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 780
Cdd:cd01377 541 FRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYS 620
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 386768643 781 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd01377 621 ILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
133-822 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1153.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 133 VEDMAELTCLNEASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNML 212
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 213 GDREDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGavphpavlisshqetfaGELEQQLLQANPILEAFGNAKT 292
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV-----------------GRLEEQILQSNPILEAFGNAKT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 293 VKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSN- 371
Cdd:pfam00063 144 VRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQs 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 372 GSLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDM 451
Cdd:pfam00063 224 GCYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 452 TRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFE 531
Cdd:pfam00063 304 EKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 532 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLV 610
Cdd:pfam00063 384 QLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 611 SAHSMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDT 690
Cdd:pfam00063 463 STFSKHPHFQKPRLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 691 QFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRI 770
Cdd:pfam00063 543 STPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRI 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 386768643 771 PFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:pfam00063 623 TFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
145-822 |
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: 1138.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASKpKGSgavphpavlissHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSH-KGR------------KDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd14920 148 IRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGR 464
Cdd:cd14920 228 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 465 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 544
Cdd:cd14920 308 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 545 LFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK 621
Cdd:cd14920 388 LFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 622 T-DFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA--RT 696
Cdd:cd14920 468 PrQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrIVGLDQVTgMTETAFGSayKT 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 697 RKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 776
Cdd:cd14920 548 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 777 QRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14920 628 QRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
899-1979 |
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: 1072.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 899 TKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQEL 978
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 979 ETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEER 1058
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1059 ANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAK 1138
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1139 REEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQE 1218
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1219 LRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSR 1298
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1299 QENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEE 1378
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1379 TRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQ 1458
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1459 VKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLS 1538
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1539 VSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEV 1618
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1619 NMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHA 1698
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1699 KKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLM 1778
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1779 IDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETA 1858
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1859 QRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLD 1938
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 386768643 1939 ETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKL 1979
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
126-834 |
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: 1051.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 126 NPPKFDKVEDMAELTCLNEASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITD 205
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 206 SAYRNMLGDREDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGavphpavlisshqetfageLEQQLLQANPILE 285
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGS-------------------VEDQILESNPILE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 286 AFGNAKTVKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKS 365
Cdd:smart00242 142 AFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 366 YAFLSNG-SLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNT-VAQKIAHL 443
Cdd:smart00242 222 YRYLNQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAEL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 444 LGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFE 523
Cdd:smart00242 302 LGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 524 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLI-DKPGGIMALLDEECWFPKATD 602
Cdd:smart00242 381 IFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIeKKPPGILSLLDEECRFPKGTD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 603 KTFVDKLVSAHSMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgm 682
Cdd:smart00242 460 QTFLEKLNQHHKKHPHFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV---- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 683 aqqaltdtqfGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRIC 762
Cdd:smart00242 536 ----------SNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIR 605
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768643 763 RQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFRAGVLAHLEEERD 834
Cdd:smart00242 606 RAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
145-822 |
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: 1047.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAAS----KPKGSGAVPHpavlisshqetfaGELEQQLLQANPILEAFGNAKTVKNDNSSR 300
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSfktkKDQSSIALSH-------------GELEKQLLQANPILEAFGNAKTVKNDNSSR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 301 FGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVD 380
Cdd:cd14932 148 FGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 381 DYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRI 460
Cdd:cd14932 228 DKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 461 KVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNE 540
Cdd:cd14932 308 KVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 541 KLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHP 617
Cdd:cd14932 388 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNNP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 618 KFMK-TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA 694
Cdd:cd14932 468 KFQKpKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDrIVGLDKVAgMGESLHGA 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 695 -RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 773
Cdd:cd14932 548 fKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 386768643 774 EFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14932 628 EFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
145-822 |
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: 994.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASKpKGSgavphpavlissHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSH-KGK------------KDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd14921 148 IRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGR 464
Cdd:cd14921 228 FQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 465 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 544
Cdd:cd14921 308 DVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 545 LFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK 621
Cdd:cd14921 388 LFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 622 T-DFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF--GART 696
Cdd:cd14921 468 PkQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrIVGLDQMAkMTESSLpsASKT 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 697 RKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 776
Cdd:cd14921 548 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 777 QRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14921 628 QRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
145-822 |
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: 982.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAaskpkgsgavphpavliSSHQ-ETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVA-----------------SSHKsKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYA 383
Cdd:cd14919 144 FIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14919 224 MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14919 304 RDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFM 620
Cdd:cd14919 384 QLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 621 K-TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF-GA-R 695
Cdd:cd14919 464 KpKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAgMSETALpGAfK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 696 TRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEF 775
Cdd:cd14919 544 TRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 386768643 776 RQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14919 624 RQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
145-822 |
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: 981.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASkPKGSgavPHPAVlisshqetfAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASS-PKGR---KEPGV---------PGELERQLLQANPILEAFGNAKTVKNDNSSRFGKF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGvDDYAE 384
Cdd:cd14930 148 IRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QEREL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGR 464
Cdd:cd14930 227 FQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 465 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 544
Cdd:cd14930 307 DYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 545 LFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK 621
Cdd:cd14930 387 LFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 622 T-DFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ-QALTDTQFGARTRK 698
Cdd:cd14930 467 PrHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQvSSLGDGPPGGRPRR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 699 GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 778
Cdd:cd14930 547 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 386768643 779 YELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14930 627 YEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
145-822 |
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: 971.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASkpkgsgavpHPAVLISSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASS---------HKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd15896 152 IRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGR 464
Cdd:cd15896 232 FTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 465 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 544
Cdd:cd15896 312 DYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 545 LFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK 621
Cdd:cd15896 392 LFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 622 -TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQALTDTQFGA-RTRK 698
Cdd:cd15896 472 pKKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDrIVGLDKVSGMSEMPGAfKTRK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 699 GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 778
Cdd:cd15896 552 GMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 386768643 779 YELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd15896 632 YEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
82-1512 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 869.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 82 VWVPHENQGFVAASI-KREHGDEVEVELA--ETGKRVMILRDDIQ--KMNPPKFDKVEDMAELTCLNEASVLHNIKDRYY 156
Cdd:COG5022 12 CWIPDEEKGWIWAEIiKEAFNKGKVTEEGkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 157 SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGESGAGKTENTKK 236
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 237 VIQFLAYVAASKPKGSGAVphpavlisshqetfagelEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGFIS 316
Cdd:COG5022 172 IMQYLASVTSSSTVEISSI------------------EKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEIC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 317 GANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLP-VPGVDDYAEFQATVKSMNIM 395
Cdd:COG5022 234 GAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 396 GMTSEDFNSIFRIVSAVLLFGSMKFRQERnNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQ 475
Cdd:COG5022 314 GIDEEEQDQIFKILAAILHIGNIEFKEDR-NGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 476 VEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGaSFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 555
Cdd:COG5022 393 ALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQ 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 556 EEYQREGIEWKFIDFgLDLQPTIDLIDK--PGGIMALLDEECWFPKATDKTFVDKLVSA--HSMHPKFMKTDFRGVAdFA 631
Cdd:COG5022 472 EEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSNPKFKKSRFRDNK-FV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 632 IVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqqaltdtqfgARTRKGMFRTVSHLYKEQ 711
Cdd:COG5022 550 VKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEE---------------NIESKGRFPTLGSRFKES 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 712 LAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNV----I 787
Cdd:COG5022 615 LNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgE 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 788 PKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFRAGVLAHLEEERDFKISDLIVNFQAFCRGFLARRNYQKRLQQLNAI 867
Cdd:COG5022 695 YTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKI 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 868 RIIQRNCAAYLKLRNWQWWRLYTKVKPLLEVTKQEEKLVQKEDELKQVREKLDT--LAKNTQEYERKYQQA-LVEKTTLA 944
Cdd:COG5022 775 QVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekKLRETEEVEFSLKAEvLIQKFGRS 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 945 EQLQAEIELcaeaeESRSRLMARKQELEDMMQELETRIEEEEERVLALGgekkklELNIQDLEEQLEEEEAARQKLQLEK 1024
Cdd:COG5022 855 LKAKKRFSL-----LKKETIYLQSAQRVELAERQLQELKIDVKSISSLK------LVNLELESEIIELKKSLSSDLIENL 923
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1025 VQLDAKIKKYEEDLALTDDQNQklLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELeerlhkdQQQRQES 1104
Cdd:COG5022 924 EFKTELIARLKKLLNNIDLEEG--PSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREG-------NKANSEL 994
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1105 DRSKRKIeTEVADLKEQLNERRVQVDEMQAQLAkreeELTQTLLRIDEESATKATAQKAQRELESQLAEIQEdleaekaa 1184
Cdd:COG5022 995 KNFKKEL-AELSKQYGALQESTKQLKELPVEVA----ELQSASKIISSESTELSILKPLQKLKGLLLLENNQ-------- 1061
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1185 rakaekvrrdLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSINDQ-- 1262
Cdd:COG5022 1062 ----------LQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQei 1131
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1263 LENLRKAKTVLEKAKGTLEAENADLATELRSVN----------------SSRQEN--DRRRKQAESQIAELQVKLAEIER 1324
Cdd:COG5022 1132 SKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANlealpspppfaalsekRLYQSAlyDEKSKLSSSEVNDLKNELIALFS 1211
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1325 ---ARSELQEKCTKLQQEAENITNQLEEAE-------LKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIES 1394
Cdd:COG5022 1212 kifSGWPRGDKLKKLISEGWVPTEYSTSLKgfnnlnkKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQ 1291
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1395 EKEALQEQ----------LEEDDEAKRNYERK--------LAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALE 1456
Cdd:COG5022 1292 YINVGLFNalrtkasslrWKSATEVNYNSEELddwcrefeISDVDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNP 1371
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*....
gi 386768643 1457 RQVKELIAQNDRLDKS---KKKIQSELEDATIELEAQRTkVLELEKKQKNFDKILAEEK 1512
Cdd:COG5022 1372 AEIQNLKSRYDPADKEnnlPKEILKKIEALLIKQELQLS-LEGKDETEVHLSEIFSEEK 1429
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
145-822 |
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: 854.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRH-EVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 224 GESGAGKTENTKKVIQFLAYVAASKPKGSGAVphpavlisshqetfAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS--------------ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFL-----SNGSLPVPG 378
Cdd:cd00124 147 FIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 379 VDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKF--RQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFL 456
Cdd:cd00124 227 VDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFeeDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 457 TPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQ-GASFIGILDMAGFEIFELNSFEQLCI 535
Cdd:cd00124 307 TRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 536 NYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHS 614
Cdd:cd00124 387 NYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 615 MHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSqdpfvvniwkdaeivgmaqqaltdTQFga 694
Cdd:cd00124 466 SHPRFFSKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG------------------------SQF-- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 695 rtrkgmfrtvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 774
Cdd:cd00124 520 --------------RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDE 585
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 386768643 775 FRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd00124 586 FLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
145-822 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 783.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVLISshqetfaGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTG-------GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYA 383
Cdd:cd14927 154 IRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQGVTTVDNMDDGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14927 234 ELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14927 314 NEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMK- 621
Cdd:cd14927 393 QFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKp 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 622 ---TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDaeIVGMAQQALTDTQFGARTRK 698
Cdd:cd14927 473 rpdKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEN--YVGSDSTEDPKSGVKEKRKK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 699 GM-FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 777
Cdd:cd14927 551 AAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQ 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 778 RYELLTPNVIPK-GFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14927 631 RYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
145-822 |
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: 779.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASKPKgsgavphpavlisSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKT-------------DEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYA 383
Cdd:cd14909 148 IRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14909 228 EFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14909 308 NEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKT 622
Cdd:cd14909 387 QFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 623 D----FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmAQQALTDTQFGARTRK 698
Cdd:cd14909 467 KppkpGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHA----GQSGGGEQAKGGRGKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 699 GM-FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 777
Cdd:cd14909 543 GGgFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKM 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 386768643 778 RYELLTPNVIpKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14909 623 RYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
146-822 |
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: 776.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAASkpkgsgavphpAVLISSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT-----------GDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKF-ILDDVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd14913 151 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLlITTNPYDYPFISQGEILVASIDDAEE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14913 231 LLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14913 310 NEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHP 617
Cdd:cd14913 389 QFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYdqhlgkSNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 618 KFMKTdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmAQQALTDTQFGARTR 697
Cdd:cd14913 469 KVVKG--RAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA----TADADSGKKKVAKKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 698 KGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 777
Cdd:cd14913 543 GSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 778 RYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14913 623 RYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
145-822 |
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: 741.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASKPKGSGAvphpavlisshqetfAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDG---------------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYA 383
Cdd:cd14934 146 IRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQGVTVVDNMDDGE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14934 226 ELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14934 306 NEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKT 622
Cdd:cd14934 385 QFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 623 DF-RGV---ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQaltdtqfgaRTRK 698
Cdd:cd14934 465 KGgKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKK---------QKRG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 699 GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 778
Cdd:cd14934 536 SSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 386768643 779 YELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14934 616 YQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
145-822 |
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: 729.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAA-SKPKGSgavphpavlisshqetfAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAmIESKKK-----------------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYA 383
Cdd:cd14929 144 FIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14929 224 ELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14929 304 NEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHP 617
Cdd:cd14929 383 QFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFdnhfgkSVHFQKP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 618 KFMKTDFRgvADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAqqaltdTQFGARTR 697
Cdd:cd14929 463 KPDKKKFE--AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSA------IQFGEKKR 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 698 K--GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEF 775
Cdd:cd14929 535 KkgASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADF 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 386768643 776 RQRYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14929 615 KQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
146-822 |
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: 719.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAASKPKGSgavphpavlisSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSK-----------KDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd14917 151 RIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTVASIDDAEE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14917 231 LMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTEeADKSAYLMGLNSADLLKGLCHPRVKVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14917 310 NEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHP 617
Cdd:cd14917 389 QFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFdnhlgkSNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 618 KFMKTdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmAQQALTDTQFGARTR 697
Cdd:cd14917 469 RNIKG--KPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYA----GADAPIEKGKGKAKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 698 KGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 777
Cdd:cd14917 543 GSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 778 RYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14917 623 RYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
146-822 |
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: 702.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAvlisshqetfAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAN----------KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd14916 152 RIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGEVSVASIDDSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14916 232 LLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14916 311 NEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHP 617
Cdd:cd14916 390 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYdnhlgkSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 618 KFMKTdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDaeiVGMAQQALTDTQFGARTR 697
Cdd:cd14916 470 RNVKG--KQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFST---YASADTGDSGKGKGGKKK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 698 KGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 777
Cdd:cd14916 545 GSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 778 RYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14916 625 RYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
146-822 |
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: 694.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVlisshqetfAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKM---------QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd14910 153 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14910 233 LMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14910 312 NEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH------SMHP 617
Cdd:cd14910 391 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgksnnFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 618 KFMKTDFRgvADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgMAQQALTDTQFGARTR 697
Cdd:cd14910 471 KPAKGKVE--AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAA---AAEAEEGGGKKGGKKK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 698 KGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 777
Cdd:cd14910 546 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 778 RYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14910 626 RYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
147-822 |
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: 690.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 147 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGES 226
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 227 GAGKTENTKKVIQFLAYVAASKPKGSgavphpavlisSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 306
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKK-----------EESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 307 INFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEF 385
Cdd:cd14918 152 IHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 386 QATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGR 464
Cdd:cd14918 232 MATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 465 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 544
Cdd:cd14918 311 EYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 545 LFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHPK 618
Cdd:cd14918 390 FFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYdqhlgkSANFQKPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 619 FMKTdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmAQQALTDTQFGARTRK 698
Cdd:cd14918 470 VVKG--KAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYA----SAEADSGAKKGAKKKG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 699 GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 778
Cdd:cd14918 544 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQR 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 386768643 779 YELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14918 624 YKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
146-822 |
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: 688.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVlisshqetfAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKM---------QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd14912 153 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISVASIDDQEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14912 233 LMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14912 312 NEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHP 617
Cdd:cd14912 391 QFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYeqhlgkSANFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 618 KFMKTdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEiVGMAQQALTDTQFGARTR 697
Cdd:cd14912 471 KVVKG--KAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQ-TAEGASAGGGAKKGGKKK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 698 KGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 777
Cdd:cd14912 548 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 778 RYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14912 628 RYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
146-822 |
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: 683.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAASKPKGSGAVPhpavlisshqETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQP----------GKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd14923 152 RIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGEVTVASIDDSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14923 232 LLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14923 311 NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH------SMHP 617
Cdd:cd14923 390 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgksnnFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 618 KFMKTdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDaeIVGMAQQALTDTQFGARTR 697
Cdd:cd14923 470 KPAKG--KAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSN--YAGAEAGDSGGSKKGGKKK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 698 KGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 777
Cdd:cd14923 546 GSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 778 RYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14923 626 RYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
146-822 |
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 386768643 146 SVLHNIKDRYYSG-LIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASkpkgsgavphpavlisSHQETfagELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGS----------------SSGET---QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLP-VPGVDDYA 383
Cdd:cd01380 143 IEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd01380 223 EFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGA-SFIGILDMAGFEIFELNSFEQLCINYTNEKL 542
Cdd:cd01380 303 SEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 543 QQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPK--FM 620
Cdd:cd01380 383 QQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 621 KTDFRGVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDpfvvniwkdaeivgmaqqaltdtqfgartRKgm 700
Cdd:cd01380 462 KPRFSNTA-FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN-----------------------------RK-- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 701 fRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 780
Cdd:cd01380 510 -KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYR 588
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 386768643 781 LLTPNVIPKGfMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd01380 589 VLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
146-822 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 679.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAASKPKGSGavphpavliSSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKE---------EAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd14915 153 RIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAFVSQGEITVPSIDDQEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVG 463
Cdd:cd14915 233 LMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14915 312 NEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH------SMHP 617
Cdd:cd14915 391 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgksnnFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 618 KFMKTdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGS---QDPFVVNIWKDAEIVGMAQQAltdtqfGA 694
Cdd:cd14915 471 KPAKG--KAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSgmkTLAFLFSGGQTAEAEGGGGKK------GG 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 695 RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 774
Cdd:cd14915 543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 386768643 775 FRQRYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14915 623 FKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
146-822 |
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: 664.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAaskpkgsgavphpavliSSHQEtfageLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVT-----------------NNHSW-----VEQQILEANTILEAFGNAKTVRNDNSSRFGKFI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGA--TPEQREKFILDDVKSYAFLS-NGSLPVPGVDDY 382
Cdd:cd14883 140 EVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLGEPEDYHYLNqSGCIRIDNINDK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 383 AEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQ-ERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIK 461
Cdd:cd14883 220 KDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQIN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 462 VgRDFVTKAQTK-EQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGaSFIGILDMAGFEIFELNSFEQLCINYTNE 540
Cdd:cd14883 300 V-RGNVTEIPLKvQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 541 KLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDK-PGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKF 619
Cdd:cd14883 378 KLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 620 MKTDFRGVAD-FAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWK--DAEIVGMAQQALTDTQFGART 696
Cdd:cd14883 457 EKPDRRRWKTeFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypDLLALTGLSISLGGDTTSRGT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 697 RKGMfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 776
Cdd:cd14883 537 SKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFV 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 777 QRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14883 616 DRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
146-822 |
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: 651.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQflaYVAASKPKGSGAVPHpavlisshqetfageLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd01378 82 SGAGKTEASKRIMQ---YIAAVSGGSESEVER---------------VKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSN-GSLPVPGVDDYAE 384
Cdd:cd01378 144 EIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKsGCFDVDGIDDAAD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAfLTPRI---- 460
Cdd:cd01378 224 FKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKA-LTHRTietg 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 461 KVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNE 540
Cdd:cd01378 302 GGGRSVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 541 KLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFP-KATDKTFVDKLVSAHSMHPK 618
Cdd:cd01378 382 KLQQIFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPH 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 619 FM--KTDFR-GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIvgmaqqaltdtqfgaR 695
Cdd:cd01378 461 FEcpSGHFElRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD---------------L 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 696 TRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEF 775
Cdd:cd01378 526 DSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKF 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 386768643 776 RQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd01378 606 LERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
145-822 |
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: 645.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 224 GESGAGKTENTKKVIQFLAYVAasKPKGSGAVPhpavlisshqetfageLEQQLLQANPILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG--GRAVTEGRS----------------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDY 382
Cdd:cd01384 143 FVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNqSKCFELDGVDDA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 383 AEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPD---NTVAQKIAHLLGLSVTDMTRAfLTPR 459
Cdd:cd01384 223 EEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDA-LCKR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 460 IKVGRD-FVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYT 538
Cdd:cd01384 302 VIVTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 539 NEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHP 617
Cdd:cd01384 381 NEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 618 KFMKTDfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqqaltdtqfGARTR 697
Cdd:cd01384 460 RFSKPK-LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLP--------------REGTS 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 698 KGM-FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 776
Cdd:cd01384 525 SSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 777 QRYELLTPNViPKGFMDGKKACEKMIQALELDSnlYRVGQSKIFFR 822
Cdd:cd01384 605 DRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
146-822 |
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: 643.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKgiKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAAskpkGSGAVphpavlisshqetfagelEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG----GSSGI------------------ENEILQTNPILEAFGNAKTLRNDNSSRFGKLI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAE 384
Cdd:cd01383 138 DIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGR 464
Cdd:cd01383 218 FHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 465 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 544
Cdd:cd01383 298 DKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 545 LFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTD 623
Cdd:cd01383 378 HFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 624 FRGvadFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLqGSQDPFVVNIWkdAEIVGMAQQALTdTQFGARTRKGMFRT 703
Cdd:cd01383 457 GGA---FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLF--ASKMLDASRKAL-PLTKASGSDSQKQS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 704 VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE-LL 782
Cdd:cd01383 530 VATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGfLL 609
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 386768643 783 TPNVIPKGfmDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd01383 610 PEDVSASQ--DPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
145-822 |
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: 635.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVaaskpkgSGAvpHPAVlisshqetfagelEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAI-------SGQ--HSWI-------------EQQILEANPILEAFGNAKTIRNDNSSRFGKY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNG-SLPVPGVDDYA 383
Cdd:cd01381 139 IDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQ-ERNNDQAT-LPDNTVAQKIAHLLGLSVTDMTRAFLTPRIK 461
Cdd:cd01381 219 EFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtVVDNLDASeVRDPPNLERAAKLLEVPKQDLVDALTTRTIF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 462 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGAS--FIGILDMAGFEIFELNSFEQLCINYTN 539
Cdd:cd01381 299 TRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFAN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 540 EKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPK 618
Cdd:cd01381 379 ENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 619 FMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDaeivgmaqqaltDTQFGARTRK 698
Cdd:cd01381 458 YLKPKSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNE------------DISMGSETRK 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 699 GMfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 778
Cdd:cd01381 526 KS-PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVER 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 386768643 779 YELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd01381 605 YRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
145-822 |
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: 570.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASkpkgsgavphpavlisshqetfAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS----------------------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKW 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKfiLDDVKSYAFLSNGS-LPVPGVDDYA 383
Cdd:cd14872 139 VEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGG--WGSSAAYGYLSLSGcIEVEGVDDVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQA---TLPDNTVAQKIAHLLGLSVTDMTRAFLTPRI 460
Cdd:cd14872 217 DFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVsgsTVANRDVLKEVATLLGVDAATLEEALTSRLM 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 461 KV-GRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTN 539
Cdd:cd14872 297 EIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 540 EKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDK-PGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPK 618
Cdd:cd14872 377 EKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKST 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 619 FMKTDFRGV-ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFvvniwkdaeIVGMAQQALTDTQFGARTR 697
Cdd:cd14872 456 FVYAEVRTSrTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKL---------IAVLFPPSEGDQKTSKVTL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 698 KGMFRtvshlykEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 777
Cdd:cd14872 527 GGQFR-------KQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLK 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 778 RYELLtPNVIPKGFM-DGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14872 600 RYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
145-822 |
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: 566.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 224 GESGAGKTENTKKVIQFLAYVAASKpkgsgavphpavlisshqetfAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG---------------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDdvksyaflsngslpvPGVDDYA 383
Cdd:cd01382 140 FVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKD---------------PLLDDVG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNN-------DQATLPDNTVAqkiAHLLGLSVTDM----- 451
Cdd:cd01382 205 DFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYA---AELLGLDQDELrvslt 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 452 TRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKrqGASFIGILDMAGFEIFELNSFE 531
Cdd:cd01382 282 TRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 532 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLV 610
Cdd:cd01382 360 QFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVH 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 611 SAHSMHPKFMK------TDFRGVAD---FAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVG 681
Cdd:cd01382 439 QKHKNHFRLSIprksklKIHRNLRDdegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNN 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 682 maqqALTDTQFGartrKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRI 761
Cdd:cd01382 519 ----KDSKQKAG----KLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDL 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 762 CRQGFPNRIPFQEFRQRYELLTPNVIPKgfMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd01382 591 MQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
145-822 |
3.10e-175 |
|
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: 548.97 E-value: 3.10e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAaskpkgsgavPHPAVLISshqetfageleQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN----------QRRNNLVT-----------EQILEATPLLEAFGNAKTVRNDNSSRFGKY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDaSGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNG-SLPVPGVDDYA 383
Cdd:cd01387 140 LEVFFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKF--RQERN-NDQATLPDNTVAQKIAHLLGLSVTDMTRAfLTPRI 460
Cdd:cd01387 219 DFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFhkRQLRHgQEGVSVGSDAEIQWVAHLLQISPEGLQKA-LTFKV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 461 KVGR-DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINrSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTN 539
Cdd:cd01387 298 TETRrERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYAN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 540 EKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPK 618
Cdd:cd01387 377 ENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNEL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 619 FMKTDFrGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDaeivgMAQQALTDTQFGAR--- 695
Cdd:cd01387 456 YSKPRM-PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSS-----HRAQTDKAPPRLGKgrf 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 696 -TRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 774
Cdd:cd01387 530 vTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQV 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 386768643 775 FRQRYELLTPNVIPKGfMDGKKACEKMIQALELD-SNLYRVGQSKIFFR 822
Cdd:cd01387 610 FIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
145-822 |
1.71e-173 |
|
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: 544.37 E-value: 1.71e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 224 GESGAGKTENTKKVIQFLAyvaaskpkgsgavphpavlisshqeTFAGELE----QQLLQANPILEAFGNAKTVKNDNSS 299
Cdd:cd14903 81 GESGAGKTETTKILMNHLA-------------------------TIAGGLNdstiKKIIEVNPLLESFGNAKTVRNDNSS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 300 RFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFlSNGSLPVPGV 379
Cdd:cd14903 136 RFGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG-ANKTIKIEGM 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 380 DDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATL--PDNTVAQKIAHLLGLSVTDMTRAFLT 457
Cdd:cd14903 215 SDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 458 PRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINY 537
Cdd:cd14903 295 RTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 538 TNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH--SM 615
Cdd:cd14903 374 ANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHkdEQ 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 616 H----PKFMKTdfrgvaDFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD-AEIVGMAQQALTDT 690
Cdd:cd14903 453 DviefPRTSRT------QFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEkVESPAAASTSLARG 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 691 QFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRI 770
Cdd:cd14903 527 ARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRL 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 386768643 771 PFQEFRQRYELLTPNViPKGFMDGKKACEKMIQALELDS-NLYRVGQSKIFFR 822
Cdd:cd14903 607 LHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
145-820 |
1.87e-171 |
|
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: 538.61 E-value: 1.87e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERY------KGIKRHEVPPHVFAITDSAYRNMLGDRE-- 216
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 217 --DQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVlisshqetfagelEQQLLQANPILEAFGNAKTVK 294
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENV-------------RDRVLESNPILEAFGNARTNR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 295 NDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFL--SNG 372
Cdd:cd14901 148 NNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 373 SLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKF-RQERNNDQATLPDNTVAQKIAHLLGLSVTDM 451
Cdd:cd14901 228 YDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 452 TRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGAS-FIGILDMAGFEIFELNSF 530
Cdd:cd14901 308 EKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 531 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgldlqPTIDLI-----DKPGGIMALLDEECWFPKATDKTF 605
Cdd:cd14901 388 EQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PNNDACvamfeARPTGLFSLLDEQCLLPRGNDEKL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 606 VDKLVSAHSMHPKFMKTDF-RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNiwkdaeivgmaq 684
Cdd:cd14901 463 ANKYYDLLAKHASFSVSKLqQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------ 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 685 qaltdtqfgartrkgmfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQ 764
Cdd:cd14901 531 ------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRS 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 765 GFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNL-----YRVGQSKIF 820
Cdd:cd14901 593 GYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
145-822 |
9.47e-171 |
|
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: 537.05 E-value: 9.47e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAY----RNMLGDREDQS 219
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtqliQSGVLDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 220 ILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAvliSSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSS 299
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAA---SEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 300 RFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGV 379
Cdd:cd14890 158 RFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 380 DDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQErnNDQATLPDNTVAQ---KIAHLLGLSVTDMTRAFL 456
Cdd:cd14890 238 DDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE--NDTTVLEDATTLQslkLAAELLGVNEDALEKALL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 457 TPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCIN 536
Cdd:cd14890 316 TRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 537 YTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLD--EECWFPKAT--DKTFVDKLVS 611
Cdd:cd14890 395 YANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFItlDDCWRFKGEeaNKKFVSQLHA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 612 AH-------------SMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQdpfvvniwkdae 678
Cdd:cd14890 474 SFgrksgsggtrrgsSQHPHFVHPKFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 679 ivgmaqqaltdtqfgaRTRKGMfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEG 758
Cdd:cd14890 542 ----------------RSIREV--SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEA 603
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768643 759 IRICRQGFPNRIPFQEFRQRYELLTPNVipkgfMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14890 604 IQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
146-822 |
1.75e-165 |
|
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: 521.45 E-value: 1.75e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAASKPKgsgavphpavlisshqetfagELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANNR---------------------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQR-EKFILDDVKSYAFLSNGSLPVPGV---DD 381
Cdd:cd01379 141 EMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIvnnSG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 382 YAE-FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQ----ATLPDNTVAQKIAHLLGLSVTDMTRAfL 456
Cdd:cd01379 221 NREkFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEA-L 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 457 TPRIKVGR-DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL--DRTKRQGASFIGILDMAGFEIFELNSFEQL 533
Cdd:cd01379 300 TSHSVVTRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 534 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTID-LIDKPGGIMALLDEECWFPKATDKTFVDK---- 608
Cdd:cd01379 380 CINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKfhnn 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 609 LVSAHSMHPKfmktdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVvniwkdaeivgmaQQalt 688
Cdd:cd01379 459 IKSKYYWRPK------SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-------------RQ--- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 689 dtqfgartrkgmfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPN 768
Cdd:cd01379 517 --------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSH 582
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 386768643 769 RIPFQEFRQRYELLTPN----VIPKgfmdgKKACEKMIQALELDSnlYRVGQSKIFFR 822
Cdd:cd01379 583 RILFADFLKRYYFLAFKwneeVVAN-----RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
145-822 |
1.02e-162 |
|
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: 516.16 E-value: 1.02e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAaSKPKGSGavphpavlisshqetfageLEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTALS-QKGYGSG-------------------VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYA 383
Cdd:cd01385 141 IQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQER-NNDQATLPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIK 461
Cdd:cd01385 221 EFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPeVLDIISELLRVKEETLLEALTTKKTV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 462 -VGRDFVTKAQTKEQVEfAVEAIAKACYERMFKWLVNRINRSL----DRTKRQGASfIGILDMAGFEIFELNSFEQLCIN 536
Cdd:cd01385 301 tVGETLILPYKLPEAIA-TRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCIN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 537 YTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSM 615
Cdd:cd01385 379 YANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 616 HPKFMKTDFRGVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQ----------DPFVVNIWKDAEIVGMAQQ 685
Cdd:cd01385 458 NKYYEKPQVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSsafvreligiDPVAVFRWAVLRAFFRAMA 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 686 ALTDTqfGARTRKG--------MFRTVSHL---------------YKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKID 742
Cdd:cd01385 537 AFREA--GRRRAQRtaghsltlHDRTTKSLlhlhkkkkppsvsaqFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFD 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 743 APLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMiqalELDSNLYRVGQSKIFFR 822
Cdd:cd01385 615 DELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKL----NLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
145-784 |
1.55e-162 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 514.63 E-value: 1.55e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKgIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 224 GESGAGKTENTKKVIQFLAYVAASKPKGSGAVphpavlisshqetfagelEQQLLQANPILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLV------------------EAQVLESNPLLEAFGNARTLRNDNSSRFGK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFD---------ASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSL 374
Cdd:cd14888 142 FIELQFSklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 375 PV------------------------PGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQAT 430
Cdd:cd14888 222 PIsidmssfephlkfryltksschelPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 431 LPDNTVAQ---KIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTK 507
Cdd:cd14888 302 VVSASCTDdleKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 508 RQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLI-DKPGG 586
Cdd:cd14888 382 DNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 587 IMALLDEECWFPKATDKTFVDKLVSAHSMHPKFM--KTDfrgVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQG 664
Cdd:cd14888 461 IFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDvvKTD---PNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 665 SQDPFVVNIWKdaeivgmaqqALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAP 744
Cdd:cd14888 538 SKNPFISNLFS----------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRI 607
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 386768643 745 LVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 784
Cdd:cd14888 608 SVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
145-822 |
1.79e-162 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 513.47 E-value: 1.79e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKG-IKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNlSVRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 224 GESGAGKTENTKKVIQFLAYVAASKpkgsgavphpavlisshqetfAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSD---------------------DSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYA 383
Cdd:cd14897 140 FIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 E-------FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFL 456
Cdd:cd14897 220 EleyyrqmFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 457 TPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL----DRTKRQGASFIGILDMAGFEIFELNSFEQ 532
Cdd:cd14897 300 SNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 533 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVS 611
Cdd:cd14897 380 LCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 612 AHSMHPKFMKTdFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVvniwkdaeivgmaqqaltdtq 691
Cdd:cd14897 459 YCGESPRYVAS-PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFI--------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 692 fgartrKGMFrtVSHlYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIP 771
Cdd:cd14897 517 ------SDLF--TSY-FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIK 587
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 386768643 772 FQEFRQRYELLTPNViPKGFMDGKKACEKMIQALELDSnlYRVGQSKIFFR 822
Cdd:cd14897 588 YEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
145-822 |
1.09e-161 |
|
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: 512.00 E-value: 1.09e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTE--KIMERYKGIKRHEV-PPHVFAITDSAYRNMLGDR----ED 217
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATASSpPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 218 QSILCTGESGAGKTENTKKVIQFLAyvAASKpKGSGAVPHPAVlisshqETFAGELEQQLLQANPILEAFGNAKTVKNDN 297
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLA--TASK-LAKGASTSKGA------ANAHESIEECVLLSNLILEAFGNAKTIRNDN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 298 SSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGS-LPV 376
Cdd:cd14892 152 SSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 377 PGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQ--KIAHLLGLSVTDMTRA 454
Cdd:cd14892 232 DGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 455 FLTPRIKVGRDFVTK-AQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQ---------GASFIGILDMAGFEI 524
Cdd:cd14892 312 LVTQTTSTARGSVLEiKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 525 FELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDK-PGGIMALLDEECWFP-KATD 602
Cdd:cd14892 392 MPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 603 KTFVDKLVSAHSMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQgsqdpfvvniwkdaeivgm 682
Cdd:cd14892 471 KQLLTIYHQTHLDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLR------------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 683 aqqaltdtqfgaRTRKgmFRTvshlykeQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRIC 762
Cdd:cd14892 532 ------------SSSK--FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIR 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 763 RQGFPNRIPFQEFRQRYELLTPNVI-------PKGFMDGKKACEKMIQAlELDSNLYRVGQSKIFFR 822
Cdd:cd14892 591 REGFPIRRQFEEFYEKFWPLARNKAgvaaspdACDATTARKKCEEIVAR-ALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
145-822 |
1.91e-161 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 511.26 E-value: 1.91e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 224 GESGAGKTENTKKVIQFLAYVAASKPKGSGAvphpavlisshqeTFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLK-------------EKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDY 382
Cdd:cd14873 148 FVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 383 AEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrqeRNNDQATLPDNTVAQKIAHLLGLSVTDMTRAfLTPRIKV 462
Cdd:cd14873 228 ESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEF---ITAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 463 GR-DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLdrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEK 541
Cdd:cd14873 304 LRgEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 542 LQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK 621
Cdd:cd14873 382 LQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 622 TDFrGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWkdaEIVGMAQQalTDTQFGARTRKGmf 701
Cdd:cd14873 461 PRV-AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---EHVSSRNN--QDTLKCGSKHRR-- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 702 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 781
Cdd:cd14873 533 PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKV 612
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 386768643 782 LTPNVIPKGFMDGKkaCEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14873 613 LMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
145-822 |
2.29e-150 |
|
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: 481.45 E-value: 2.29e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRH--------EVPPHVFAITDSAYRNMLGDR 215
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 216 EDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVLISSHQETFAgeLEQQLLQANPILEAFGNAKTVKN 295
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATSKSTKS--IEQKILSCNPILEAFGNAKTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 296 DNSSRFGKFIRINFD-ASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKS---YAFLS- 370
Cdd:cd14907 159 DNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSgdrYDYLKk 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 371 NGSLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQER-NNDQATLPDNT-VAQKIAHLLGLSV 448
Cdd:cd14907 239 SNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTlDDNSPCCVKNKeTLQIIAKLLGIDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 449 TDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL-------DRTKRQGASFIGILDMAG 521
Cdd:cd14907 319 EELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 522 FEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKF--IDFgLDLQPTIDLIDK-PGGIMALLDEECWFP 598
Cdd:cd14907 399 FEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 599 KATDKTFVDKLVSAHSMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAe 678
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE- 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 679 ivgmaQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEG 758
Cdd:cd14907 557 -----DGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLES 631
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768643 759 IRICRQGFPNRIPFQEFRQRYELLTPNVIpkgfmdgkkacekmiqaleldsnlyrVGQSKIFFR 822
Cdd:cd14907 632 IRVRKQGYPYRKSYEDFYKQYSLLKKNVL--------------------------FGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
147-822 |
3.18e-148 |
|
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: 475.17 E-value: 3.18e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 147 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLG----DREDQSILC 222
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGrlarGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 223 TGESGAGKTENTKKVIQFLAYVAaskpKGSGavphpavlisshqetfagELEQQLLQANPILEAFGNAKTVKNDNSSRFG 302
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC----RGNS------------------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 303 KFIRINFdASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDY 382
Cdd:cd14889 141 KYIQLRF-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYW 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 383 -AEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrqERNNDQA---TLPDNTVAQKIAHLLGLSVTDMTRAfLTP 458
Cdd:cd14889 220 kKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEAlkvENDSNGWLKAAAGQFGVSEEDLLKT-LTC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 459 RIKVGR-DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQG--ASFIGILDMAGFEIFELNSFEQLCI 535
Cdd:cd14889 297 TVTFTRgEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 536 NYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDL-IDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS 614
Cdd:cd14889 377 NLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 615 MHPKFmKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDP-----FVVNIWKDAEIVGMAQQALTD 689
Cdd:cd14889 456 GNSYY-GKSRSKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPllsvlFTATRSRTGTLMPRAKLPQAG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 690 TQFGARTRKgmfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNR 769
Cdd:cd14889 535 SDNFNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWR 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 386768643 770 IPFQEFRQRYELLtpnVIPKGFMDGKKACEKMIQALELDSnlYRVGQSKIFFR 822
Cdd:cd14889 612 PSFAEFAERYKIL---LCEPALPGTKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
146-779 |
4.77e-141 |
|
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: 453.99 E-value: 4.77e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERY-------------KGikRHEVPPHVFAITDSAYRNM 211
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstrnKG--SDPMPPHIYQVAGEAYKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 212 ----LGDREDQSILCTGESGAGKTENTKKVIQFLAYVaaskpkgsGAVPHPA-VLISSHQETFAGeleqQLLQANPILEA 286
Cdd:cd14900 80 mlglNGVMSDQSILVSGESGSGKTESTKFLMEYLAQA--------GDNNLAAsVSMGKSTSGIAA----KVLQTNILLES 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 287 FGNAKTVKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIlddvksy 366
Cdd:cd14900 148 FGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKRDM------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 367 aflsngslpvpgvddyaeFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQK------- 439
Cdd:cd14900 221 ------------------YRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSsiwsrda 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 440 IAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRIN---RSLDRTKRQGAS-FIG 515
Cdd:cd14900 283 AATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNaflKMDDSSKSHGGLhFIG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 516 ILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLDEE 594
Cdd:cd14900 363 ILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLISqRPTGILSLIDEE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 595 CWFPKATDKTFVDKLVSAHSMHPKFMKTDF-RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQgsqdpfvvni 673
Cdd:cd14900 442 CVMPKGSDTTLASKLYRACGSHPRFSASRIqRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV---------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 674 wkdaeivgmaqqalTDTQFgartrkgmfrtvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCN 753
Cdd:cd14900 512 --------------YGLQF----------------KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCN 561
|
650 660
....*....|....*....|....*.
gi 386768643 754 GVLEGIRICRQGFPNRIPFQEFRQRY 779
Cdd:cd14900 562 GVMEAVRVARAGFPIRLLHDEFVARY 587
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
145-822 |
7.79e-141 |
|
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: 454.02 E-value: 7.79e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 224 GESGAGKTENTKKVIQFLAYVAASKPKGSGAvphpavlisshqetfageleqQLLQANPILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA---------------------KVIDVNPLLESFGNAKTTRNDNSSRFGK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFL--SNGSLPVPGVDD 381
Cdd:cd14904 140 FTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 382 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQkIAHLLGLSVTDMTRAFLTPRIK 461
Cdd:cd14904 220 AKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 462 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEK 541
Cdd:cd14904 299 TRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 542 LQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK 621
Cdd:cd14904 379 LQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKKDNES 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 622 TDFRGV--ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqqaLTDTQFGARTRKG 699
Cdd:cd14904 458 IDFPKVkrTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE--------APSETKEGKSGKG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 700 MF--RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 777
Cdd:cd14904 530 TKapKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELAT 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 778 RYELLTPNVIPKGfmDGKKACEKMIQALELDSNL-YRVGQSKIFFR 822
Cdd:cd14904 610 RYAIMFPPSMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
145-822 |
9.98e-141 |
|
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: 453.73 E-value: 9.98e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRyySGLI----YTYSGLFCVVVNPYKKLPiytEKIMERYKGIKRHEVPPHVFAITDSAYRNML---GDRED 217
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMClgsGRMQN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 218 QSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAvliSSHQETFAGELEQQLLQANPILEAFGNAKTVKNDN 297
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQS---SKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 298 SSRFGKFIRINFDASGF-ISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLP 375
Cdd:cd14891 153 SSRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 376 VPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQ----ERNNDQATLPDNTVAQKIAHLLGLSVTDM 451
Cdd:cd14891 233 DDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 452 TRAFLTPRIkVGRD--FVTKAQTKEQVeFAVEAIAKACYERMFKWLVNRINRSLDRtKRQGASFIGILDMAGFEIFEL-N 528
Cdd:cd14891 313 EKVITQREI-VTRGetFTIKRNAREAV-YSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 529 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVD 607
Cdd:cd14891 390 DFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 608 KLVSAHSMHPKFMKT---DFRGVadFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQdpfvvniwkdaeivgmaq 684
Cdd:cd14891 469 TLHKTHKRHPCFPRPhpkDMREM--FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA------------------ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 685 qaltdtqfgartrkgmfrtvshLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQ 764
Cdd:cd14891 529 ----------------------KFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKV 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 386768643 765 GFPNRIPFQEFRQRY-ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14891 587 GLPTRVTYAELVDVYkPVLPPSVTRLFAENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
143-864 |
8.81e-138 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 451.41 E-value: 8.81e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 143 NEASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHE-VPPHVFAITDSAYRNMLGDREDQSIL 221
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 222 CTGESGAGKTENTKKVIQFLAyvaaskpkgsgavphpavliSSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRF 301
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA--------------------SSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 302 GKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDD 381
Cdd:PTZ00014 248 GRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 382 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNN---DQATLPDNT--VAQKIAHLLGLSVTDMTRAFL 456
Cdd:PTZ00014 328 VKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGgltDAAAISDESleVFNEACELLFLDYESLKKELT 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 457 TPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGAsFIGILDMAGFEIFELNSFEQLCIN 536
Cdd:PTZ00014 408 VKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFIN 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 537 YTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSM 615
Cdd:PTZ00014 487 ITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLcGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKN 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 616 HPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIV--GMAQQALTDTQFg 693
Cdd:PTZ00014 566 NPKYKPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEkgKLAKGQLIGSQF- 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 694 artrkgmfrtvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 773
Cdd:PTZ00014 645 ---------------LNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFA 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 774 EFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR---AGVLAHLEEERDFKISDLIVNFQAFCRG 850
Cdd:PTZ00014 710 EFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILK 789
|
730
....*....|....
gi 386768643 851 FLARRNYQKRLQQL 864
Cdd:PTZ00014 790 IKKKRKVRKNIKSL 803
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
145-822 |
1.13e-137 |
|
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: 446.28 E-value: 1.13e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYK--GIKRHE-------VPPHVFAITDSAYRNML-GD 214
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMsEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 215 REDQSILCTGESGAGKTENTKKVIQFLAYVAAskpkGSGAVPHpavlisSHQETFAGELEQQLLQANPILEAFGNAKTVK 294
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGN----GEEGAPN------EGEELGKLSIMDRVLQSNPILEAFGNARTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 295 NDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKS--------Y 366
Cdd:cd14908 151 NDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITgglqlpneF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 367 AFLSNGSLP-VPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKI----A 441
Cdd:cd14908 231 HYTGQGGAPdLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEF-ESKEEDGAAEIAEEGNEKClarvA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 442 HLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL--DRTKRQGASfIGILDM 519
Cdd:cd14908 310 KLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 520 AGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLDEECWFP 598
Cdd:cd14908 389 FGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 599 -KATDKTFVDKLVSA--------HSMHPKFMKTDF-RGVADFAIVHYAGRVDYSAAKWLM-KNMDPLNENIVSLLQGSQd 667
Cdd:cd14908 468 iRGSDANYASRLYETylpeknqtHSENTRFEATSIqKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIPLTADSLFESGQ- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 668 pfvvniwkdaeivgmaqqaltdtQFgartrkgmfrtvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVL 747
Cdd:cd14908 547 -----------------------QF----------------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVT 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 748 DQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP----NVIPKGFM--DGKKACEKMI----------QALELDSNL 811
Cdd:cd14908 588 EQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPlipeVVLSWSMErlDPQKLCVKKMckdlvkgvlsPAMVSMKNI 667
|
730
....*....|....*
gi 386768643 812 ----YRVGQSKIFFR 822
Cdd:cd14908 668 pedtMQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
145-784 |
1.49e-134 |
|
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: 438.94 E-value: 1.49e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYK--------GIKRHEVPPHVFAITDSAYRNML-GD 214
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 215 REDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVphpavlisshqeTFAGELEQQLLQANPILEAFGNAKTVK 294
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEG------------SDAVEIGKRILQTNPILESFGNAQTIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 295 NDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFL----- 369
Cdd:cd14902 149 NDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnsygp 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 370 SNGSLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVA---QKIAHLLGL 446
Cdd:cd14902 229 SFARKRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 447 SVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLD--------RTKRQGASFIGILD 518
Cdd:cd14902 309 DVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 519 MAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFP 598
Cdd:cd14902 389 IFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 599 KATDKTFVDKLVSAHSmhpkfmktdfrGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE 678
Cdd:cd14902 469 KGSNQALSTKFYRYHG-----------GLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 679 IVGMAqqalTDTQFGARTRKGMFRT--VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVL 756
Cdd:cd14902 538 RDSPG----ADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVL 613
|
650 660
....*....|....*....|....*...
gi 386768643 757 EGIRICRQGFPNRIPFQEFRQRYELLTP 784
Cdd:cd14902 614 EAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
145-820 |
1.64e-134 |
|
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: 436.34 E-value: 1.64e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRH-EVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 224 GESGAGKTENTKKVIQFLAYvaaskpKGSGAVPHpavlisshqetfagELEQQLLQANPILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS------AKSGNMDL--------------RIQTAIMAANPVLEAFGNAKTIRNNNSSRFGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYA 383
Cdd:cd14876 141 FMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNN---DQATL--PDNTVAQKIAHLLGLSVTDMTRAFLTP 458
Cdd:cd14876 221 DFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQgvdDAAAIsnESLEVFKEACSLLFLDPEALKRELTVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 459 RIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrtKRQG-ASFIGILDMAGFEIFELNSFEQLCINY 537
Cdd:cd14876 301 VTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 538 TNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTID-LIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMH 616
Cdd:cd14876 379 TNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 617 PKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVG--MAQQALTDTQFGA 694
Cdd:cd14876 458 GKFKPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKgkIAKGSLIGSQFLK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 695 rtrkgmfrtvshlykeQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 774
Cdd:cd14876 538 ----------------QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEE 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 386768643 775 FRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIF 820
Cdd:cd14876 602 FLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
145-822 |
1.18e-130 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 425.35 E-value: 1.18e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASKPKGSGAvphpavlisshqetfageleqQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDRLR---------------------QPEDVLPILESFGHAKTILNANASRFGQV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDaSGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNG-SLPVPGVDDYA 383
Cdd:cd14896 140 LRLHLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGgACRLQGKEDAQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQ--ATLPDNTVAQKIAHLLGLSVTDMTRAfLTPRIK 461
Cdd:cd14896 219 DFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGA-VTHRVT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 462 V---GRDFvtkaqTKEQVEFAVEA---IAKACYERMFKWLVNRINRSLDRTKRQGA-SFIGILDMAGFEIFELNSFEQLC 534
Cdd:cd14896 298 EtpyGRVS-----RPLPVEGAIDArdaLAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLC 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 535 INYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDfGLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAH 613
Cdd:cd14896 373 INLASERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 614 SMHPKFMKTDFrGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqqaltdTQFG 693
Cdd:cd14896 452 GDHPSYAKPQL-PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAE-----------PQYG 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 694 ARTRKGmfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 773
Cdd:cd14896 520 LGQGKP---TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQ 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 386768643 774 EFRQRYELLTpNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14896 597 AFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
145-822 |
2.05e-124 |
|
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: 409.01 E-value: 2.05e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASkpkgSGAVphpavlisshqetfageLEQQLLQA-NPILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGS----VGGV-----------------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSyaflSNGSLPVPGV---- 379
Cdd:cd01386 140 LFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQkped 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 380 --DDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRA-F- 455
Cdd:cd01386 216 kqKAAAAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAiFk 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 456 ----------LTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASfIGILDMAGFEIF 525
Cdd:cd01386 296 hhlsggpqqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 526 ELN------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwkfIDFGLD---LQPTIDLIDK------------- 583
Cdd:cd01386 375 AHSgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPelsPGALVALIDQapqqalvrsdlrd 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 584 --PGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGVAD----FAIVHYAGR--VDYSAAKWLMK-NMDPL 654
Cdd:cd01386 452 edRRGLLWLLDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSEgplqFVLGHLLGTnpVEYDVSGWLKAaKENPS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 655 NENIVSLLQGSQDpfvvniwkdaeivgmaqqaltdtQFGARTRKGMFRTVshlyKEQLAKLMDTLRNTNPNFVRCIIPNH 734
Cdd:cd01386 532 AQNATQLLQESQK-----------------------ETAAVKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQH 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 735 --EKRAGK----------IDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGF-----MDGKKA 797
Cdd:cd01386 585 naGKDERStsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKA 664
|
730 740
....*....|....*....|....*
gi 386768643 798 CEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd01386 665 VEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
145-784 |
3.91e-121 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 398.45 E-value: 3.91e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKR-HEVPPHVFAITDSAYRNMLGDRE--DQSI 220
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 221 LCTGESGAGKTENTKKVIQFLAYVAASKpkgsgavphpavlISSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSR 300
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASP-------------TSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 301 FGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNgslPVPGVD 380
Cdd:cd14880 148 FGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPN---PERNLE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 381 DyAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTV---AQKIAHLLGLSVTDMTRAFLT 457
Cdd:cd14880 225 E-DCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 458 PRIKVGRDFVT--KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCI 535
Cdd:cd14880 304 RTIRAGKQQQVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 536 NYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLDEECWFPKATDKT-FVDKLVSAH 613
Cdd:cd14880 384 NYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAqLQTRIESAL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 614 SMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqQALTDTQFG 693
Cdd:cd14880 463 AGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANP------EEKTQEEPS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 694 ARTRKGMFRTVSHlYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 773
Cdd:cd14880 537 GQSRAPVLTVVSK-FKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQ 615
|
650
....*....|.
gi 386768643 774 EFRQRYELLTP 784
Cdd:cd14880 616 NFVERYKLLRR 626
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
146-822 |
6.63e-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: 396.63 E-value: 6.63e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNML-------GDREDQ 218
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYDLHKYREEMPGWTALPPHVFSIAEGAYRSLRrrlhepgASKKNQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 219 SILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVLISshqetfageleqQLLQANPILEAFGNAKTVKNDNS 298
Cdd:cd14895 82 TILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGS------------ELLSANPILESFGNARTLRNDNS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 299 SRFGKFIRINF-----DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDV--KSYAFLSN 371
Cdd:cd14895 150 SRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLsaQEFQYISG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 372 GSLPV--PGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNND---------------QATLPDN 434
Cdd:cd14895 230 GQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 435 TVAQK---IAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTK---- 507
Cdd:cd14895 310 TVQQHldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfaln 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 508 ------RQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDlQPTIDLI 581
Cdd:cd14895 390 pnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEML 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 582 D-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFM--KTDFRGVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENI 658
Cdd:cd14895 469 EqRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSasRTDQADVA-FQIHHYAGAVRYQAEGFCEKNKDQPNAEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 659 VSLLQGSQDPFVVNIWKDAEIVGMAQQALTdtQFGARTRKGMFRTVS--HLYKEQLAKLMDTLRNTNPNFVRCIIPNHEK 736
Cdd:cd14895 548 FSVLGKTSDAHLRELFEFFKASESAELSLG--QPKLRRRSSVLSSVGigSQFKQQLASLLDVVQQTQTHYIRCIKPNDES 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 737 RAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPnvipkgfmdGKKACEkmIQALELDSNLYR--- 813
Cdd:cd14895 626 ASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA---------AKNASD--ATASALIETLKVdha 694
|
730
....*....|
gi 386768643 814 -VGQSKIFFR 822
Cdd:cd14895 695 eLGKTRVFLR 704
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
145-822 |
6.58e-117 |
|
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: 386.86 E-value: 6.58e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYS-GLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGI-KRHEVPPHVFAITDSAYRNM-LGDREDQSIL 221
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALpDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 222 CTGESGAGKTENTKKVIQFLAYVAASKPKgsgavphpavliSSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRF 301
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSS------------NTSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 302 GKFIRINFD-ASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKF-ILDDVKSYAFLSNGSLPVP-G 378
Cdd:cd14875 149 GKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVRrG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 379 VD-----DYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQErNNDQATLPDNTVAQKIAHLLGLSVTDMTR 453
Cdd:cd14875 229 VDgktldDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESD-QNDKAQIADETPFLTACRLLQLDPAKLRE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 454 AFLtprIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLD-RTKRQGASFIGILDMAGFEIFELNSFEQ 532
Cdd:cd14875 308 CFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 533 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVS 611
Cdd:cd14875 385 LCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 612 A-HSMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVvniwkdaeivgmaqQALTDT 690
Cdd:cd14875 464 QwANKSPYFVLPKSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFI--------------RTLLST 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 691 QFGARTRKgmfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRI 770
Cdd:cd14875 530 EKGLARRK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRR 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 771 PFQEFRQRYELLTPNVIPKGFMDGK--KACEKMIQALEldsNLYR-------VGQSKIFFR 822
Cdd:cd14875 607 PIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQ---RLYGwakpnyaVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
145-822 |
1.40e-115 |
|
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: 382.31 E-value: 1.40e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKG--IKR---HEVPPHVFAITDSAYRNMLGDREDQ 218
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQadTSRgfpSDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 219 SILCTGESGAGKTENTKKVIQFLAYVaaskpkgsgavphpavlisshQETFAGELEQQLLQANPILEAFGNAKTVKNDNS 298
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYG---------------------HSTSSTDVQSLILGSNPLLESFGNAKTLRNNNS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 299 SRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGS-LPVP 377
Cdd:cd14886 140 SRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKcYDAP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 378 GVDDYAEFQATVKSMNIMgMTSEDFNSIFRIVSAVLLFGSMKFRQERNN---DQATLPDNTVAQKIAHLLGLSVTDMTRA 454
Cdd:cd14886 220 GIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 455 FLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINR--SLDRTKRQgasFIGILDMAGFEIFELNSFEQ 532
Cdd:cd14886 299 IITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEiiQFDADARP---WIGILDIYGFEFFERNTYEQ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 533 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDKPG-GIMALLDEECWFPKATDKTFVDKLVS 611
Cdd:cd14886 376 LLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNlSIFSFLEEQCLIQTGSSEKFTSSCKS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 612 aHSMHPKFMKTDfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVvniwkdaeivgmaQQALTDTQ 691
Cdd:cd14886 455 -KIKNNSFIPGK-GSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV-------------NKAFSDIP 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 692 FGARTRKGMFrtVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIP 771
Cdd:cd14886 520 NEDGNMKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDT 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 386768643 772 FQEFRQRYELLT--PNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14886 598 FEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
145-818 |
2.10e-113 |
|
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: 378.55 E-value: 2.10e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKR-HEVPPHVFAITDSAYRNMLGDREDQSILC 222
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 223 TGESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavlisSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFG 302
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQN-----------NNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 303 KFIRINFDASGF-ISGANIETYLLEKSR-AIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFL---------- 369
Cdd:cd14906 150 KFLKIEFRSSDGkIDGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNnDPSKYRYLdarddvissf 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 370 ----SNGSLPVPGVDDYAE-FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQ---KIA 441
Cdd:cd14906 230 ksqsSNKNSNHNNKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTAsleSVS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 442 HLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKE--QVEFAVEAIAKACYERMFKWLVNRINRSLDR----------TKRQ 509
Cdd:cd14906 310 KLLGYIESVFKQALLNRNLKAGGRGSVYCRPMEvaQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 510 GASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPG-GIM 588
Cdd:cd14906 390 NNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSdGIL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 589 ALLDEECWFPKATDKTFVDKLVSA-HSMHPKFMKTDFRGVadFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQD 667
Cdd:cd14906 469 SLLDDECIMPKGSEQSLLEKYNKQyHNTNQYYQRTLAKGT--LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 668 PFVVNIWKdaeivgmaQQALTDTQFGARTRKGMfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVL 747
Cdd:cd14906 547 FLKKSLFQ--------QQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVL 616
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 748 DQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSK 818
Cdd:cd14906 617 SQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
145-779 |
7.21e-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: 356.71 E-value: 7.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKgiKRHEVP------------PHVFAITDSAYRNM 211
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYA--YDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 212 LGDREDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVLISSHQETfageLEQQLLQANPILEAFGNAK 291
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPASPSRTT----IEEQVLQSNPILEAFGNAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 292 TVKNDNSSRFGKFIRINF-DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG----ATPEQREKFILDDVKSY 366
Cdd:cd14899 155 TVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGGPQS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 367 AFLSNGSLPVP---GVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQ--ERNNDQATLPDNTVAQ--- 438
Cdd:cd14899 235 FRLLNQSLCSKrrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSstt 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 439 -------KIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRT----- 506
Cdd:cd14899 315 gafdhftKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapw 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 507 ---------KRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPT 577
Cdd:cd14899 395 gadesdvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRAC 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 578 IDLID-KPGGIMALLDEECWFPKATDKTFVDKL---VSAHSMHPKFMKTD-FRGVADFAIVHYAGRVDYSAAKWLMKNMD 652
Cdd:cd14899 474 LELFEhRPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPlIQRTTQFVVAHYAGCVTYTIDGFLAKNKD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 653 PLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMFRT----VSHLYKEQLAKLMDTLRNTNPNFVR 728
Cdd:cd14899 554 SFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQLNELLSTVRATTPRYVR 633
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 386768643 729 CIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 779
Cdd:cd14899 634 CIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
142-821 |
5.30e-103 |
|
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: 346.07 E-value: 5.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 142 LNEASVLHNIKDRYYSGLIYTY---SGLfcVVVNPYKKLPIYTEKIMERYK-------GIKRHEVPPHVFAITDSAYRNM 211
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 212 LGDREDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavlisshqetfagELEQQLLQANPILEAFGNAK 291
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGT-------------------KLSSQISAAEFVLDSFGNAK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 292 TVKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFL-S 370
Cdd:cd14879 140 TLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 371 NGSLPV---PGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQER-NNDQATLPDNT-VAQKIAHLLG 445
Cdd:cd14879 220 YGCHPLplgPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHeGGEESAVVKNTdVLDIVAAFLG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 446 LSVTDMTRAfLTPRIK-VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEI 524
Cdd:cd14879 300 VSPEDLETS-LTYKTKlVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 525 F---ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwkfidfgLDLQPTID-------LIDKPGGIMALLDEE 594
Cdd:cd14879 379 RsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVS-------VPATSYFDnsdcvrlLRGKPGGLLGILDDQ 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 595 C-WFPKATDKTFVDKLVSAHSMHPKF----MKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSqdpf 669
Cdd:cd14879 452 TrRMPKKTDEQMLEALRKRFGNHSSFiavgNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGA---- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 670 vvniwkdaeivgmaqqaltdTQFgartrkgmfrtvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQ 749
Cdd:cd14879 528 --------------------TQL----------------NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQ 571
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768643 750 LRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPnvipkgFMDGKKACEKMIQALELDSNLYRVGQSKIFF 821
Cdd:cd14879 572 IRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
146-784 |
3.46e-94 |
|
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: 317.99 E-value: 3.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKlpIYTEKIMERYKGIKRHeVPPHVFAITDSAYRNmLGDREDQSILCTGE 225
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQD-LLVHGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAASKPKgsgavphpavlisshqetfageLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTTS----------------------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDasGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIldDVKSYAflSNGSLPVPGVDDYaef 385
Cdd:cd14898 136 KLKFD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI--DTSSTA--GNKESIVQLSEKY--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 386 QATVKSMNIMGMTSedFNSIFRIVSAVLLFGSMKFrqerNNDQAT-LPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGR 464
Cdd:cd14898 207 KMTCSAMKSLGIAN--FKSIEDCLLGILYLGSIQF----VNDGILkLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 465 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTkrqGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 544
Cdd:cd14898 281 ETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 545 LFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFvdkLVSAHSMHPKFMKTDF 624
Cdd:cd14898 358 DFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNL---LVKIKKYLNGFINTKA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 625 RGvaDFAIVHYAGRVDYSAAKWLMKNMDplnenivsllQGSQDPFvvniwKDAEIVgmaqqaltdtqfgartRKGMFRTV 704
Cdd:cd14898 434 RD--KIKVSHYAGDVEYDLRDFLDKNRE----------KGQLLIF-----KNLLIN----------------DEGSKEDL 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 705 SHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 784
Cdd:cd14898 481 VKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
145-822 |
4.28e-94 |
|
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: 319.65 E-value: 4.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYtekiMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFlaYVAASKPKGsgavphpavlisshqetfagELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd14937 77 ESGSGKTEASKLVIKY--YLSGVKEDN--------------------EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAE 384
Cdd:cd14937 135 IKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 385 FQATVKSMNIMGMtSEDFNSIFRIVSAVLLFGSMKFRQERNNDQAT---LPDNT--VAQKIAHLLGLSVTDMTRAFLTPR 459
Cdd:cd14937 215 FGNLMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQEIEKGGKTNcseLDKNNleLVNEISNLLGINYENLKDCLVFTE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 460 IKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKrQGASFIGILDMAGFEIFELNSFEQLCINYTN 539
Cdd:cd14937 294 KTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIAN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 540 EKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDlQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKF 619
Cdd:cd14937 373 EEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 620 MKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIvgmaqqalTDTQfgarTRKG 699
Cdd:cd14937 452 ASTKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEV--------SESL----GRKN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 700 MfrtVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRIcRQGFPNRIPFQEFRQRY 779
Cdd:cd14937 520 L---ITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 386768643 780 ELLTPNVIPKGFMDGKKACEKMIQAlELDSNLYRVGQSKIFFR 822
Cdd:cd14937 596 EYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
145-822 |
3.80e-92 |
|
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: 316.98 E-value: 3.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYS--------GLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDRE 216
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 217 DQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavlisshqetfAGELEQQLLQANPILEAFGNAKTVKND 296
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGAD-----------------SQGLEARLLQSGPVLEAFGNAHTVLNA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 297 NSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKfilddvksyaflsngSLPV 376
Cdd:cd14887 144 NSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQK---------------SSAG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 377 PGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNT--------VAQKIAHLL---- 444
Cdd:cd14887 209 EGDPESTDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceeTAADRSHSSevkc 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 445 ---GLSVTDMTRAFLT--------PRIKVGRDFVTKAQTKEQVE------------FAVEAIAKACYERMFKWLVNRINR 501
Cdd:cd14887 289 lssGLKVTEASRKHLKtvarllglPPGVEGEEMLRLALVSRSVRetrsffdldgaaAARDAACKNLYSRAFDAVVARINA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 502 SLDRTKR-------------QGASFIGILDMAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREG--I 563
Cdd:cd14887 369 GLQRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQ 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 564 EWKFIDFGLDLQPTIDLIDKPGGIMALL------DEECWFPKATDKTFVDKLVSAHSMHPKFMKTDF------------- 624
Cdd:cd14887 449 NQDCSAFPFSFPLASTLTSSPSSTSPFSptpsfrSSSAFATSPSLPSSLSSLSSSLSSSPPVWEGRDnsdlfyeklnkni 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 625 --------------RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDpfvvniwkdaeivgMAQQALTDT 690
Cdd:cd14887 529 insakyknitpalsRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACST--------------YTRLVGSKK 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 691 QFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRI 770
Cdd:cd14887 595 NSGVRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRL 674
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 386768643 771 PFQEFRQRYELLTPNVIpKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 822
Cdd:cd14887 675 PYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
145-822 |
5.67e-91 |
|
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: 311.36 E-value: 5.67e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERY---KGIKRHEVPPHVFAITDSAYRNMLGDREDQSIL 221
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 222 CTGESGAGKTENTKKVIQFLAYVAASKpkgsgavphpavlisshqetfAGELEQQLLQANPILEAFGNAKTVKNDNSSRF 301
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSS---------------------RTTFDSRFKHVNCILEAFGHAKTTLNDLSSCF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 302 GKFIRINF-DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGslpVPGVD 380
Cdd:cd14878 140 IKYFELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQT---MREDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 381 DYAE-------FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTR 453
Cdd:cd14878 217 STAErslnrekLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 454 AFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRIN---RSLDRTKRQGASFIGILDMAGFEIFELNSF 530
Cdd:cd14878 297 ALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclQSQDEQKSMQTLDIGILDIFGFEEFQKNEF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 531 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTID-LIDKPGGIMALLDEECWFPKATDKTFVDKL 609
Cdd:cd14878 377 EQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 610 -----VSAHSMHPKFMKTDFRGVA------DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVsllqgsqdpFVVNIWKDAE 678
Cdd:cd14878 457 qslleSSNTNAVYSPMKDGNGNVAlkdqgtAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLL---------FVMKTSENVV 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 679 IVGMAQQALTdtqfgartrkgmfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEG 758
Cdd:cd14878 528 INHLFQSKLV--------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEM 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386768643 759 IRICRQGFPNRIPFQEFRQRYELLTPNVI-PKGFMDGKKACEKMIQALELDSnlYRVGQSKIFFR 822
Cdd:cd14878 594 VKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
146-821 |
5.46e-81 |
|
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: 281.23 E-value: 5.46e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKK----LPIYTEKIMERYkgikrhevpPHVFAITDSAYRNMLGDREDQSIL 221
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDvgnpLTLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 222 CTGESGAGKTENTKKVIQFLAYVAASKPKgSGAVPHPAVLISshqetfageleqqllqanpILEAFGNAKTVKNDNSSRF 301
Cdd:cd14881 73 LSGTSGSGKTYASMLLLRQLFDVAGGGPE-TDAFKHLAAAFT-------------------VLRSLGSAKTATNSESSRI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 302 GKFIRINFdASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD--DVKSYAFLSNGSLPVPGV 379
Cdd:cd14881 133 GHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHGDTRQNEA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 380 DDYAEFQATVKSMNIMGMTsedFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPR 459
Cdd:cd14881 212 EDAARFQAWKACLGILGIP---FLDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 460 IKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINrSLdrtKRQGAS--------FIGILDMAGFEIFELNSFE 531
Cdd:cd14881 288 HNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRAN-SL---KRLGSTlgthatdgFIGILDMFGFEDPKPSQLE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 532 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKF-IDFgLDLQPTIDLIDK-PGGIMALLDEECwFPKATDKTFVDKL 609
Cdd:cd14881 364 HLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVEC-SPRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 610 VSAHSMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGsqdpfvvniwkdaeivgmaqqalTD 689
Cdd:cd14881 442 KVQHRQNPRLFEAKPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK-----------------------QN 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 690 TQFGARTRKGMFRTvshlykeQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNR 769
Cdd:cd14881 499 CNFGFATHTQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHR 571
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 770 IPFQEFRQRYELLTPNVIPKGFMDGKKACEKMI------QALELDSNL---YRVGQSKIFF 821
Cdd:cd14881 572 MRFKAFNARYRLLAPFRLLRRVEEKALEDCALIlqfleaQPPSKLSSVstsWALGKRHIFL 632
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
145-774 |
1.47e-78 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 275.63 E-value: 1.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHE-------VPPHVFAITDSAYRNMLGDRE 216
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 217 DQSILCTGESGAGKTENTKKVIQFLAYVAASkpkgsgavphpavliSSHQEtfageLEQQLLQANPILEAFGNAKTVKND 296
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTD---------------SQMTE-----RIDKLIYINNILESMSNATTIKNN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 297 NSSRFGKFIRINFDA---------SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQ-REKFILDDVKSY 366
Cdd:cd14884 141 NSSRCGRINLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDlARRNLVRNCGVY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 367 AFLSN----------GSLPVPGVD----------DYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQernn 426
Cdd:cd14884 221 GLLNPdeshqkrsvkGTLRLGSDSldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA---- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 427 dqatlpdntvaqkIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRT 506
Cdd:cd14884 297 -------------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKC 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 507 KRQGA-----------SFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQ 575
Cdd:cd14884 364 KEKDEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYS 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 576 PTIDLIDKpggIMALLDE-----ECWFPKATDKTFVD-----------KLVSAHSMHPKfmktDFRGVAD--------FA 631
Cdd:cd14884 443 DTLIFIAK---IFRRLDDitklkNQGQKKTDDHFFRYllnnerqqqleGKVSYGFVLNH----DADGTAKkqnikkniFF 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 632 IVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFvvniwkdaeivgmaqqaLTDTQFGArtRKGMFRTVSHLYKEQ 711
Cdd:cd14884 516 IRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRF-----------------LREANNGG--NKGNFLSVSKKYIKE 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768643 712 LAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 774
Cdd:cd14884 577 LDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
146-822 |
2.47e-76 |
|
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: 268.88 E-value: 2.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKgiKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAYVAASKPKgsgavphpavlisshqetfagELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 304
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLSRSK---------------------YLRDYILESGIILESFGHASTDSNHNSSRWGKY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 305 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSN-GSLPVPGVDDYA 383
Cdd:cd14905 139 FEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 384 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQErnNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRikvg 463
Cdd:cd14905 219 VFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQK--NGKTEVKDRTLIESLSHNITFDSTKLENILISDR---- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 464 rdfvtKAQTKEQVEfAVEAIAKACYERMFKWLVNRINRSLDRTkrQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 543
Cdd:cd14905 293 -----SMPVNEAVE-NRDSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 544 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKpggIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTD 623
Cdd:cd14905 365 QIYLQTVLKQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 624 FRgvadFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNiwKDAEIVGMAQQALTDTQFGAR--TRKGMF 701
Cdd:cd14905 442 NK----FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFS--RDGVFNINATVAELNQMFDAKntAKKSPL 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 702 RTVSHLYK------------------------------------EQLAKLMDTLRNTNPN--FVRCIIPNHEKRAGKIDA 743
Cdd:cd14905 516 SIVKVLLScgsnnpnnvnnpnnnsgggggggnsgggsgsggstyTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDV 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 744 PLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELltpnvipkgFMDGKKACEKMIQALE-----LDSNL---YRVG 815
Cdd:cd14905 596 KSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSF---------FFQNQRNFQNLFEKLKendinIDSILpppIQVG 666
|
....*..
gi 386768643 816 QSKIFFR 822
Cdd:cd14905 667 NTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
145-784 |
9.85e-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: 259.80 E-value: 9.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYkgikrhevppHVFAITDSAYRNMLGDRED-QSILCT 223
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 224 GESGAGKTENTKKVIQFLAyvaaSKPKGSGAVPHpavliSSHQETfageleqqllqanpILEAFGNAKTVKNDNSSRFGK 303
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT----SQPKSKVTTKH-----SSAIES--------------VFKSFGCAKTLKNDEATRFGC 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 304 FIRINFDASgFISGANIE-TYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDY 382
Cdd:cd14874 128 SIDLLYKRN-VLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 383 AEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERN----NDQATLPDNTVAQKIAHLLGLSVtDMTRAFLTP 458
Cdd:cd14874 207 NHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnveQDVVEIGNMSEVKWVAFLLEVDF-DQLVNFLLP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 459 RIKVGRDFVTKAQTKEQvefavEAIAKACYERMFKWLVNRINRSLDRTKRQGAsfIGILDMAGFEIFELNSFEQLCINYT 538
Cdd:cd14874 286 KSEDGTTIDLNAALDNR-----DSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 539 NEKLQQLFNHTMFILEQEEYQREGIEwkfIDF----GLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAH 613
Cdd:cd14874 359 NERIENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNH 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 614 SMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDA------EIVGMAQQAL 687
Cdd:cd14874 436 TDRSSYGKARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYssntsdMIVSQAQFIL 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 688 TDTQfgartrkgmfrtvshlykeqlaKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFP 767
Cdd:cd14874 516 RGAQ----------------------EIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYP 573
|
650
....*....|....*..
gi 386768643 768 NRIPFQEFRQRYELLTP 784
Cdd:cd14874 574 VKISKTTFARQYRCLLP 590
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
146-782 |
1.89e-71 |
|
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: 253.51 E-value: 1.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 226 SGAGKTENTKKVIQFLAYVAASKPKGSGAVphpavlisshqetfageleqqlLQANPILEAFGNAKTVKNDNSSRFGKFI 305
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRGATGRV----------------------ESSIKAILALVNAGTPLNADSTRCILQY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 306 RINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREK-FILDDVKSYAFL------------SNG 372
Cdd:cd14882 140 QLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRLKeYNLKAGRNYRYLrippevppsklkYRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 373 SLPVPGVDDYAEFQATVKSMNimgMTSEDFNSIFRIVSAVLLFGSMKFRQerNNDQATLPDNTVAQKIAHLLGLSVTDMT 452
Cdd:cd14882 220 DDPEGNVERYKEFEEILKDLD---FNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 453 RAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKrqgASF-----IGILDMAGFEIFEL 527
Cdd:cd14882 295 WALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 528 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTID-LIDKPGGIMALLDEECwfPKATDKTFV 606
Cdd:cd14882 372 NRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDqLMTKPDGLFYIIDDAS--RSCQDQNYI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 607 dkLVSAHSMHPKFMKTDfrGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMaqqa 686
Cdd:cd14882 449 --MDRIKEKHSQFVKKH--SAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQVRNM---- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 687 ltdtqfgaRTRKGMFRTVShlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGF 766
Cdd:cd14882 521 --------RTLAATFRATS---LELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGF 589
|
650
....*....|....*.
gi 386768643 767 PNRIPFQEFRQRYELL 782
Cdd:cd14882 590 SYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
148-780 |
3.76e-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: 243.34 E-value: 3.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 148 LHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKR----------HEVPPHVFAITDSAYRNMLGDRED 217
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 218 QSILCTGESGAGKTENTKKVIQFLAYVaaskpkGSGAVPHPAVLISShqeTFAGELEQQLLQANPILEAFGNAKTVKNDN 297
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEI------GDETEPRPDSEGAS---GVLHPIGQQILHAFTILEAFGNAATRQNRN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 298 SSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAT--PEQREKFILDD-VKSYAFLSN--- 371
Cdd:cd14893 155 SSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKcVNEFVMLKQadp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 372 --GSLPVpgvdDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKF-------------RQERNNDQAT--LPDN 434
Cdd:cd14893 235 laTNFAL----DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggaNSTTVSDAQScaLKDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 435 TVAQKIAHLLGLS--VTD---MTRAFLTpriKVGRDFVT--KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL---- 503
Cdd:cd14893 311 AQILLAAKLLEVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggif 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 504 DRTKRQG----ASFIGILDMAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWKFIDF 570
Cdd:cd14893 388 DRYEKSNivinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 571 GLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAH---------SMHPKFMKTDFRGVAD----FAIVHYA 636
Cdd:cd14893 468 TSEQEKCLQLFeDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavgglsrpNMGADTTNEYLAPSKDwrllFIVQHHC 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 637 GRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVvniwkdaEIVGMAQQALTDTQFGA------RTRKGMFRTVSHLYKE 710
Cdd:cd14893 548 GKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVL-------HAVGAAQMAAASSEKAAkqteerGSTSSKFRKSASSARE 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 711 --------------QLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 776
Cdd:cd14893 621 sknitdsaatdvynQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFF 700
|
....
gi 386768643 777 QRYE 780
Cdd:cd14893 701 RRYK 704
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
146-820 |
1.74e-60 |
|
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: 222.79 E-value: 1.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKR-HEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCiEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 225 ESGAGKTENTKKVIQFLAY-VAASKPKGSGAVPHPAVLISSHQET-FAGELEQQLLQANPILEAFGNAKTVKNDNSSRFG 302
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYqVKGSRRLPTNLNDQEEDNIHNEENTdYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 303 KFIRINFDASGfISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDY 382
Cdd:cd14938 162 KFCTIHIENEE-IKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 383 AEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGS-------------MKFRQE-------------RNNDQATLPDNTV 436
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 437 AQKIA-HLLGLSVTDMTRAFLTPRIkVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKR--QGASF 513
Cdd:cd14938 321 NLLLAcKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 514 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGgimalldE 593
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPT-------E 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 594 ECWFP---KATDKTFVDK------LVSAHSMHPKFMKTD--FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLL 662
Cdd:cd14938 473 GSLFSlleNVSTKTIFDKsnlhssIIRKFSRNSKYIKKDdiTGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 663 QGSQDPFV------VNIWKDAEIVG-----MAQQALTDTQFGARTRKGMFRTvshLYKEQLAKLMDTLRNTNPNFVRCII 731
Cdd:cd14938 553 KQSENEYMrqfcmfYNYDNSGNIVEekrrySIQSALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQETTFCHFIVCMK 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 732 PNHEKRA-GKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPnvipkgfmDGKKACEKMIQALELDSN 810
Cdd:cd14938 630 PNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNY 701
|
730
....*....|
gi 386768643 811 LYRVGQSKIF 820
Cdd:cd14938 702 EWMIGNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
167-314 |
5.63e-55 |
|
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: 189.48 E-value: 5.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 167 FCVVVNPYKKLPIYTE-KIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGESGAGKTENTKKVIQFLAYVA 245
Cdd:cd01363 1 VLVRVNPFKELPIYRDsKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768643 246 ASKPKGSGAvphpavLISSHQETFAGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGF 314
Cdd:cd01363 81 FNGINKGET------EGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1259-1989 |
2.13e-35 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 148.28 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1259 INDQLENLRKAKTVLEKAkgtleaenaDLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQ 1338
Cdd:TIGR02168 218 LKAELRELELALLVLRLE---------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1339 EAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLA 1418
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1419 EVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQR--TKVLE 1496
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1497 LEKKQKNFDKILAEEKAISEQIAQERdTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADK 1576
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAE-QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1577 NVHELEKAKRALESQLAELkAQNEELEDDlqltEDAKLRLE---------VNMQALRSQFERDLLAKEEGAEEKRRGLVK 1647
Cdd:TIGR02168 528 LISVDEGYEAAIEAALGGR-LQAVVVENL----NAAKKAIAflkqnelgrVTFLPLDSIKGTEIQGNDREILKNIEGFLG 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1648 QLRDLETELDEERK---------------QRTAAVASKKK-------LEGDL----------------------KEIEtt 1683
Cdd:TIGR02168 603 VAKDLVKFDPKLRKalsyllggvlvvddlDNALELAKKLRpgyrivtLDGDLvrpggvitggsaktnssilerrREIE-- 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1684 mEMHNKVKEDALKhAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDE 1763
Cdd:TIGR02168 681 -ELEEKIEELEEK-IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1764 LAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLER 1843
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1844 QNKELKAKLAEIEtAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQM 1923
Cdd:TIGR02168 839 RLEDLEEQIEELS-EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1924 DKLNSRIKLLKRNLDETEEELQKEKTQKR-KYQRECEDMIE-------SQEAMNREINSLKTKLRRTGGIGLSS 1989
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEAlenkiedDEEEARRRLKRLENKIKELGPVNLAA 991
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
891-1663 |
1.46e-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: 139.04 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 891 KVKPLLEVTKQEEKLVQKEDELKQVreKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQE 970
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 971 LEDMMQELETrieeeeeRVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLK 1050
Cdd:TIGR02168 279 LEEEIEELQK-------ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1051 EKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNER----- 1125
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkle 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1126 RVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNE 1205
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1206 LL------DSLDTTAAQQELRSKREQEL-----------------------ATLKKSLEEETVNHEGVLADMRHKHSQEL 1256
Cdd:TIGR02168 512 LKnqsglsGILGVLSELISVDEGYEAAIeaalggrlqavvvenlnaakkaiAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1257 NSINDQ------LENLRKAKTVLEKA-----KGTLEAENADLATELR----------------------------SVNSS 1297
Cdd:TIGR02168 592 EILKNIegflgvAKDLVKFDPKLRKAlsyllGGVLVVDDLDNALELAkklrpgyrivtldgdlvrpggvitggsaKTNSS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1298 RQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMEsqlTEAQQLLEE 1377
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE---AEVEQLEER 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1378 ETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNK---DIEA 1454
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlreRLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1455 LERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKET 1534
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1535 KVLSVSRELDEAFDKIEDLENKRKTLQNELDDLAN--------TQGTADKNVHELEKAKRALESQLAELKAQNEELEddl 1606
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlseeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKELG--- 985
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768643 1607 qltedaklrlEVNMQAL---RSQFER--DLLAKEEGAEEKRrglvKQLRDLETELDEERKQR 1663
Cdd:TIGR02168 986 ----------PVNLAAIeeyEELKERydFLTAQKEDLTEAK----ETLEEAIEEIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1302-1964 |
3.44e-32 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 137.38 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1302 DRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAEnitnQLEEA-ELKAsaavksasnmesqlteaqqllEEETR 1380
Cdd:COG1196 171 KERKEEAERKLEATEENLERLEDILGELERQLEPLERQAE----KAERYrELKE---------------------ELKEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1381 QKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVK 1460
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1461 ELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKEtkvlsvs 1540
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1541 RELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEvnm 1620
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE--- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1621 qalrsQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIEttmEMHNKVKEDALKHAKK 1700
Cdd:COG1196 456 -----EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK---AALLLAGLRGLAGAVA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1701 LQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQ----LTEDLASSERARRAAETERDELAEEIANNANKGS 1776
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagrATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1777 LMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANE-KSNSQKNENGRALLERQNKELKAKLAEI 1855
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAgGSLTGGSRRELLAALLEAEAELEELAER 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1856 ETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQH-------KEQMDKLNS 1928
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpePPDLEELER 767
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 386768643 1929 RIKLLKRNLDE-------TEEELQKEKTQKRKYQRECEDMIES 1964
Cdd:COG1196 768 ELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEA 810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1145-1966 |
8.66e-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: 8.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1145 QTLLRIDEESA--TKATAQKaqRELESQLAEIQEDLEAEKAARAKaekVRRDL---------SEELEALKNELlDSLDTT 1213
Cdd:TIGR02168 155 EERRAIFEEAAgiSKYKERR--KETERKLERTRENLDRLEDILNE---LERQLkslerqaekAERYKELKAEL-RELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1214 AAQQELRSKREqELATLKKSLEEetvnhegvLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRS 1293
Cdd:TIGR02168 229 LLVLRLEELRE-ELEELQEELKE--------AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1294 VNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQ 1373
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1374 LLE-------EETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEvttqmQEIKKKAEEDADLAKELEEGKK 1446
Cdd:TIGR02168 380 QLEtlrskvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE-----AELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1447 RLNKDIEALERQVKELIAQNDRLDKSKKKIQS------ELEDATIELEAQRTKVLELEKKQKNFDKILAeekAISEQI-A 1519
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILG---VLSELIsV 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1520 QERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKR--KTLQNELDDLANTQ----------------GTADKNVHEL 1581
Cdd:TIGR02168 532 DEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNElgRVTFLPLDSIKGTEiqgndreilkniegflGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1582 EKAKRALESQLAE----------LKAQNEELEDDLQLTEDAKL----------RLEVNMQAL-RSQFERDLLAKEEGAEE 1640
Cdd:TIGR02168 612 PKLRKALSYLLGGvlvvddldnaLELAKKLRPGYRIVTLDGDLvrpggvitggSAKTNSSILeRRREIEELEEKIEELEE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1641 KRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKE 1720
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1721 ELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKgslmideKRRLEARIATLEEELEEEQ 1800
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-------LESLERRIAATERRLEDLE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1801 SNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRtKVKATIATLEAKIANLEEQ 1880
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR-ELESKRSELRRELEELREK 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1881 LEnegKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMD----KLNSRIKLLKRNLDE-------TEEELQKEKT 1949
Cdd:TIGR02168 924 LA---QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEddeeEARRRLKRLENKIKElgpvnlaAIEEYEELKE 1000
|
890
....*....|....*..
gi 386768643 1950 QKRKYQRECEDMIESQE 1966
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1067-1855 |
4.48e-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: 4.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1067 AEEEEKAKHLAKLKAKheatisELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQT 1146
Cdd:TIGR02168 220 AELRELELALLVLRLE------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1147 LLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELldsldttAAQQELRSKREQE 1226
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-------ESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1227 LATLKKSLEEETVNHEGvLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLatelrsvnssrqendrRRK 1306
Cdd:TIGR02168 367 LEELESRLEELEEQLET-LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL----------------LKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1307 QAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAElkasAAVKSASNMESQLTEAQQLLEEETRQKLGLS 1386
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE----QALDAAERELAQLQARLDSLERLQENLEGFS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1387 SKLRQIESEKEA-------LQEQLEEDDEAKRNYERKLAEvttQMQEIKKKAEEDADLA----KELEEGK-------KRL 1448
Cdd:TIGR02168 506 EGVKALLKNQSGlsgilgvLSELISVDEGYEAAIEAALGG---RLQAVVVENLNAAKKAiaflKQNELGRvtflpldSIK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1449 NKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQ---------IA 1519
Cdd:TIGR02168 583 GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvrpggvIT 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1520 QERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQN 1599
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1600 EELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEgAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKE 1679
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE-AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1680 IETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVlqltedlASSERARRAAET 1759
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER-------ASLEEALALLRS 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1760 ERDELAEEIANnankgslmiDEKRRLEARiatleEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANE--------KSNS 1831
Cdd:TIGR02168 895 ELEELSEELRE---------LESKRSELR-----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaEALE 960
|
810 820
....*....|....*....|....
gi 386768643 1832 QKNENGRALLERQNKELKAKLAEI 1855
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1259-1969 |
2.76e-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: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1259 INDQLENLRKAKTVLEKAKgTLEAENADLATELRSvnSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQ 1338
Cdd:TIGR02169 196 KRQQLERLRREREKAERYQ-ALLKEKREYEGYELL--KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1339 EAENITNQLEEAELKASAAVKSA--------SNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAK 1410
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1411 RNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQ 1490
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1491 RTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANT 1570
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1571 QGTADKN-------VHELEKAKR----ALESQlAELKAQNEELEDDL--------------------------------- 1606
Cdd:TIGR02169 513 EEVLKASiqgvhgtVAQLGSVGEryatAIEVA-AGNRLNNVVVEDDAvakeaiellkrrkagratflplnkmrderrdls 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1607 QLTEDAKLRLEVNMQALRSQFE-------RDLLAKEEGAEEKRRGLVKQLRDLETELDEE--------RKQRTAAVASkK 1671
Cdd:TIGR02169 592 ILSEDGVIGFAVDLVEFDPKYEpafkyvfGDTLVVEDIEAARRLMGKYRMVTLEGELFEKsgamtggsRAPRGGILFS-R 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1672 KLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSE 1751
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1752 RARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQ-----IEQLTTELAN 1826
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieqkLNRLTLEKEY 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1827 EKSNSQKNENGRALLERQNKELKAKLAEIETAQRtKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELT 1906
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 1907 MNIEDERRHVDQHKEQMDKLNSRIK----LLKRNLDETEEELQKEKTQKRKyqRECEDMIESQEAMN 1969
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSeiedPKGEDEEIPEEELSLEDVQAEL--QRVEEEIRALEPVN 974
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
991-1567 |
3.28e-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: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 991 ALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEE 1070
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1071 EKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRI 1150
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1151 DEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATL 1230
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1231 KKSLEEETVNHEgVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAES 1310
Cdd:COG1196 483 LEELAEAAARLL-LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1311 QIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSasnmESQLTEAQQLLEEETRQKLGLSSKLR 1390
Cdd:COG1196 562 AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA----DARYYVLGDTLLGRTLVAARLEAALR 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1391 QIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLD 1470
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1471 KSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKI 1550
Cdd:COG1196 718 EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERY 797
|
570
....*....|....*..
gi 386768643 1551 EDLENKRKTLQNELDDL 1567
Cdd:COG1196 798 DFLSEQREDLEEARETL 814
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
151-763 |
1.68e-26 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 118.69 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 151 IKDRYYSGLIYTYSGLFCV-VVNPYKKL------PIYTEKIMERYKGIKRHE--VPPHVFAITDSAYRNMLGDRED---- 217
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLVRLFFDNEHtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 218 ---------------QSILCTGESGAGKTENTKKVIQFLAYVA----------ASKPKGSGAVPHPAVLISSHQET---- 268
Cdd:cd14894 87 pstissnrsmtegrgQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseeTCKVSGSTRQPKIKLFTSSTKSTiqmr 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 269 --------------------------------------------------FAG--------ELEQQL------------- 277
Cdd:cd14894 167 teeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglFFGfyeklehlEDEEQLrmyfknphaakkl 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 278 ---LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDASGF---ISGANIETYLLEKSRAIRQA------KDERTFHIF 343
Cdd:cd14894 247 sivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHIL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 344 YQLLAG--ATPEQR---EKFILD--DVKSYAFLSNGSLPVPGV--------DDYAEFQATVKSMNIMGMTSEDFNSIFRI 408
Cdd:cd14894 327 YAMVAGvnAFPFMRllaKELHLDgiDCSALTYLGRSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFKV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 409 VSAVLLFGSMKFRQERNNDQATLPDN---TVAQKIAHLLGL-SVTDMTRAFLTPRIKVGRDFVTKAQTKE--QVEFAVEA 482
Cdd:cd14894 407 LSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEkgQVNHVRDT 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 483 IAKACYERMFKWLVNRINR-------SLDRTKRQ---------GASFIGILDMAGFEIFELNSFEQLCINYTNEKLqqlf 546
Cdd:cd14894 487 LARLLYQLAFNYVVFVMNEatkmsalSTDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL---- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 547 nhtmfileqeeYQREGiewKFIDFGLDLQP----------TIDLIDKPGGIMALLDEECWFPKAT----------DKTFV 606
Cdd:cd14894 563 -----------YAREE---QVIAVAYSSRPhltardsekdVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFV 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 607 DKLVSAHSMH----PKFMKTDFR------GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD 676
Cdd:cd14894 629 RNIYDRNSSRlpepPRVLSNAKRhtpvllNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNE 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 677 AEIVGMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVL 756
Cdd:cd14894 709 SSQLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLI 788
|
....*..
gi 386768643 757 EGIRICR 763
Cdd:cd14894 789 RQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1015-1764 |
4.62e-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: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1015 AARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERL 1094
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1095 HKDQQQRQESdrskrkiETEVADLKEQLNERRVQVDEMQAQLAKREEELtqtllrideesatkataqkaqRELESQLAEI 1174
Cdd:TIGR02168 326 EELESKLDEL-------AEELAELEEKLEELKEELESLEAELEELEAEL---------------------EELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1175 QEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVnheGVLADMRHKHSQ 1254
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL---EELEEELEELQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1255 ELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQEND------RRRKQAESQIAELQVKLAEIERARSE 1328
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvKALLKNQSGLSGILGVLSELISVDEG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1329 ------------LQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESE- 1395
Cdd:TIGR02168 535 yeaaieaalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKl 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1396 KEALQ---------EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAeedADLAKELEEGKKRLNKD--IEALERQVKELIA 1464
Cdd:TIGR02168 615 RKALSyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGG---VITGGSAKTNSSILERRreIEELEEKIEELEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1465 QNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELD 1544
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1545 EAFDKIEDLENKRKTLQNELDDLANtqgtadkNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALR 1624
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKE-------ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1625 SQFERdLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQ 1704
Cdd:TIGR02168 845 EQIEE-LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1705 VKDA-LRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDEL 1764
Cdd:TIGR02168 924 LAQLeLRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1304-1982 |
9.34e-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: 116.69 E-value: 9.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1304 RRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAE------NITNQLEEAELKASAAvksasnmesQLTEAQQLLEE 1377
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAELRELELALLVL---------RLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1378 ETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadlakeLEEGKKRLNKDIEALER 1457
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1458 QVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVL 1537
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1538 SVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKraLESQLAELKAQNEELEDDLQLTEDAKLRLE 1617
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE--LEEELEELQEELERLEEALEELREELEEAE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1618 VNMQALRSQFERdllakeegaeekRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGD---LKEIETTMEMHNKVKEDA 1694
Cdd:TIGR02168 475 QALDAAERELAQ------------LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIlgvLSELISVDEGYEAAIEAA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1695 LkhAKKLQAQVKDALrdaeeaKAAKEELQALSKEAERKVKALEAEVLQLTEdLASSERARRAAETERDELAEEIANNANK 1774
Cdd:TIGR02168 543 L--GGRLQAVVVENL------NAAKKAIAFLKQNELGRVTFLPLDSIKGTE-IQGNDREILKNIEGFLGVAKDLVKFDPK 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1775 ----------GSLMIDE---------KRRLEARIATLEEELEEEQ--------SNSEVLLDRSR---KAQLQIEQLTTEL 1824
Cdd:TIGR02168 614 lrkalsyllgGVLVVDDldnalelakKLRPGYRIVTLDGDLVRPGgvitggsaKTNSSILERRReieELEEKIEELEEKI 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1825 ANEKSNSQKNENGRALLERQNKELKAKLAEIETaQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKE 1904
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSR-QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768643 1905 LTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRRT 1982
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1069-1873 |
2.37e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.08 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1069 EEEKAKHLAKLKA------KHEATISELEERLHKDQQQRQESDR----SKRKIETEVADLKEQLNERRVQVDEMQAQLAK 1138
Cdd:TIGR02169 169 DRKKEKALEELEEveenieRLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1139 REEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDleaekaaraKAEKVRRDLsEELEALKNELLDSLDTTAAQQE 1218
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE---------EQLRVKEKI-GELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1219 LRSKREQElatlkksLEEEtvnhegvladmRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSR 1298
Cdd:TIGR02169 319 DAEERLAK-------LEAE-----------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1299 QENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLE--EAELKASAAVKSA-----SNMESQLTEA 1371
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgiEAKINELEEEKEDkaleiKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1372 QQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKD 1451
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1452 IE-ALERQVKELIAQND-------RLDKSKK----------KIQSELEDATIELEAQRT----KVLELEKKQKNFDKILA 1509
Cdd:TIGR02169 541 IEvAAGNRLNNVVVEDDavakeaiELLKRRKagratflplnKMRDERRDLSILSEDGVIgfavDLVEFDPKYEPAFKYVF 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1510 EEKAISEQIAQERD-----------------------------TAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTL 1560
Cdd:TIGR02169 621 GDTLVVEDIEAARRlmgkyrmvtlegelfeksgamtggsraprGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1561 QNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRS---QFERDLLA-KEE 1636
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEArieELEEDLHKlEEA 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1637 GAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAK 1716
Cdd:TIGR02169 781 LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1717 AAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEEL 1796
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768643 1797 EEEQSNSEVLLDrSRKAQLQIEQLTTEL-ANEKSNSQKNENGRALLERQNkELKAKLAEIEtAQRTKVKATIATLEAK 1873
Cdd:TIGR02169 941 GEDEEIPEEELS-LEDVQAELQRVEEEIrALEPVNMLAIQEYEEVLKRLD-ELKEKRAKLE-EERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
895-1507 |
3.31e-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: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 895 LLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDM 974
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 975 MQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKL 1054
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1055 LEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQA 1134
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1135 QLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEdleaeKAARAKAEKVRRDLSEELEALKneLLDSLDTTA 1214
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA-----ALLLAGLRGLAGAVAVLIGVEA--AYEAALEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1215 AQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAkgTLEAENADLATELRSV 1294
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVA--SDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1295 NSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQL 1374
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1375 LEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADlakELEEGKKRLNKDIEA 1454
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE---ELERELERLEREIEA 778
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 1455 LE----------RQVKE----LIAQNDRLDKSKKkiqsELEDATIELEAQRTKVLelekkQKNFDKI 1507
Cdd:COG1196 779 LGpvnllaieeyEELEErydfLSEQREDLEEARE----TLEEAIEEIDRETRERF-----LETFDAV 836
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1161-1982 |
5.55e-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: 5.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1161 QKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVN 1240
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1241 HEGVLadmrhkhsQELNSIndqlenlrkaKTVLEKAKGTLEAENADLAT-ELRSVNSSrqendrrrkqaesqiaelqvkl 1319
Cdd:pfam15921 182 HEGVL--------QEIRSI----------LVDFEEASGKKIYEHDSMSTmHFRSLGSA---------------------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1320 aeIERARSELQEKCTKLQQEAENITNQLEEaeLKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEAL 1399
Cdd:pfam15921 222 --ISKILRELDTEISYLKGRIFPVEDQLEA--LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1400 QEQLEEDDEAKRN----YERKLAEVTTQMQEIKKkaeedadlakELEEGKKRLNKDIEALERQvkeLIAQNDRLDKSKKK 1475
Cdd:pfam15921 298 QSQLEIIQEQARNqnsmYMRQLSDLESTVSQLRS----------ELREAKRMYEDKIEELEKQ---LVLANSELTEARTE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1476 iQSELEDATIELEAQRTKVL-ELEKKQKNfdkiLAEEKAISEQIaQERDTAereareKETKVLSVSRELDEAFDKIEDLE 1554
Cdd:pfam15921 365 -RDQFSQESGNLDDQLQKLLaDLHKREKE----LSLEKEQNKRL-WDRDTG------NSITIDHLRRELDDRNMEVQRLE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1555 NKRKTLQNElddlanTQGTADKNVHELEKAKRALE---SQLAELKAQNEELEDDLQLTEDAKLRLEvNMQALRSQFERDL 1631
Cdd:pfam15921 433 ALLKAMKSE------CQGQMERQMAAIQGKNESLEkvsSLTAQLESTKEMLRKVVEELTAKKMTLE-SSERTVSDLTASL 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1632 LAKEEGAEEKRRGLVK----------QLRDLETELDEERKQRTAAVASKKKLEGDLK-------EIETTMEM---HNKVK 1691
Cdd:pfam15921 506 QEKERAIEATNAEITKlrsrvdlklqELQHLKNEGDHLRNVQTECEALKLQMAEKDKvieilrqQIENMTQLvgqHGRTA 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1692 EDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANN 1771
Cdd:pfam15921 586 GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTS 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1772 ANKGSLMIDEKRRLEARIatleeeleeeQSNSEVLLDRSRKAQLQIEQLTTELANEKSN--SQKNENGRALlerqnkelk 1849
Cdd:pfam15921 666 RNELNSLSEDYEVLKRNF----------RNKSEEMETTTNKLKMQLKSAQSELEQTRNTlkSMEGSDGHAM--------- 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1850 aKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKelTMNIEDerrhvDQHKEQMDKLNSR 1929
Cdd:pfam15921 727 -KVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS--TVATEK-----NKMAGELEVLRSQ 798
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 386768643 1930 IKLLKRNLDETEEELQKEKTQKrkyqRECEDMIESQEAmnreiNSLKTKLRRT 1982
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 ... |
1365-1981 |
1.24e-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: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1365 ESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLE-------EDDEAKRNYERKLAEVTTQMQEIKKKAEEDADL 1437
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1438 AKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQS---ELEDATIELEAQRtkvlelekkqknfDKILAEEKAI 1514
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAkikKLEEDILLLEDQN-------------SKLSKERKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1515 SEQIAQERDTAEREarEKETKVLSVSRELDEAFdkIEDLENKRKTlqnelddlantqgtADKNVHELEKAKRALESQLAE 1594
Cdd:pfam01576 158 EERISEFTSNLAEE--EEKAKSLSKLKNKHEAM--ISDLEERLKK--------------EEKGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1595 LKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEgAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLE 1674
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN-ALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1675 GDLK----EIETTMEMHNKVKEDALKHAKKLqAQVKDALRDAEEAKAAKeeLQALSKEAERKVKALEAEVLQLTEDLASS 1750
Cdd:pfam01576 299 EELEalktELEDTLDTTAAQQELRSKREQEV-TELKKALEEETRSHEAQ--LQEMRQKHTQALEELTEQLEQAKRNKANL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1751 ERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSN 1830
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1831 SQKNENGRALLERQNKELKAKLAEiETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIE 1910
Cdd:pfam01576 456 NIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1911 DERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1981
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1300-1982 |
1.74e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 109.00 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1300 ENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAEN------ITNQLEEAELKA-----SAAVKSASNMESQL 1368
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqaLLKEKREYEGYEllkekEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1369 TEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEE-DDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKR 1447
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1448 LNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKK-QKNFDKILAEEKAIsEQIAQERDTAE 1526
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfAETRDELKDYREKL-EKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1527 REAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDL 1606
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1607 QLTEDAKLRLEVNMQALRSQfERDLLAKEEGAEEKRRGLVKQLRDLETEldEERKQRTAAVASKKKL-------EGDLKE 1679
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEER-VRGGRAVEEVLKASIQGVHGTVAQLGSV--GERYATAIEVAAGNRLnnvvvedDAVAKE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1680 -IETTMEMH---------NKVKE------------------DALKHAKKLQAQVKDALRDAEEAKAAKEELQAL------ 1725
Cdd:TIGR02169 563 aIELLKRRKagratflplNKMRDerrdlsilsedgvigfavDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMgkyrmv 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1726 -------------------SKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIannANKGSLMIDEKRRLE 1786
Cdd:TIGR02169 643 tlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRL---DELSQELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1787 ARIATLEEELEEEQSNSEVLLDRSRKaqlqIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIE---------- 1856
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEED----LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshsripe 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1857 -TAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKR 1935
Cdd:TIGR02169 796 iQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 386768643 1936 NLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRRT 1982
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
895-1672 |
1.78e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 109.00 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 895 LLEVTKQEEKLVQKEDELKQVREKL----------DTLAKNTQEYE-----RKYQQALVEKTTLAEQL---QAEIE-LCA 955
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLrrerekaeryQALLKEKREYEgyellKEKEALERQKEAIERQLaslEEELEkLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 956 EAEESRSRLMARKQELED----MMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKI 1031
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEElnkkIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1032 KKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAK----HLAKLKAKHEATISELEE---RLHKDQQQRQES 1104
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdELKDYREKLEKLKREINElkrELDRLQEELQRL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1105 DRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAA 1184
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1185 RAKAEKVRRDLSEELEALKNELLDSLDTTAaqqELRSKREQELATLKKSL---------EEETVNHEGVLADMRHKHSQ- 1254
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVLKASIQGVHGTVA---QLGSVGERYATAIEVAAgnrlnnvvvEDDAVAKEAIELLKRRKAGRa 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1255 ---ELNSINDQLENLRKAKT--VLEKA------------------KGTLEAENADLATEL----RSV---------NSSR 1298
Cdd:TIGR02169 576 tflPLNKMRDERRDLSILSEdgVIGFAvdlvefdpkyepafkyvfGDTLVVEDIEAARRLmgkyRMVtlegelfekSGAM 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1299 QENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEE 1378
Cdd:TIGR02169 656 TGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1379 TRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKkkaeedadlAKELEEGKKRLNKDIEALERQ 1458
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---------ARLSHSRIPEIQAELSKLEEE 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1459 VKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEkkqknfDKILAEEKAISEQIAQERDTaEREAREKETKVLS 1538
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK------EQIKSIEKEIENLNGKKEEL-EEELEELEAALRD 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1539 VSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLT---EDAKLR 1615
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAE 959
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 386768643 1616 LEVNMQALRSQFERDLLAKEEGAEEKRR--GLVKQLRDLETElDEERKQRTAAVASKKK 1672
Cdd:TIGR02169 960 LQRVEEEIRALEPVNMLAIQEYEEVLKRldELKEKRAKLEEE-RKAILERIEEYEKKKR 1017
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1162-1705 |
2.43e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 108.23 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1162 KAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDsLDTTAAQQELRSKREQELATLKKSLEEETVNH 1241
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-LEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1242 EGVLADMRhKHSQELNSINDQLENLRKAKT---VLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAES---QIAEL 1315
Cdd:PRK03918 265 EERIEELK-KEIEELEEKVKELKELKEKAEeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1316 QVKLAEIERARSELQEKcTKLQQEAENITNQLEEaeLKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESE 1395
Cdd:PRK03918 344 KKKLKELEKRLEELEER-HELYEEAKAKKEELER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1396 KEALQEQLEEDDEAKR------------NYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALER--QVKE 1461
Cdd:PRK03918 421 IKELKKAIEELKKAKGkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1462 LIAQNDRLDKSKKKIQSE-LEDATIELEAQRTKVLELEKKQKNFDKILAEEKAI---SEQIAQERDTAEREAREKETKVL 1537
Cdd:PRK03918 501 LAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELkkkLAELEKKLDELEEELAELLKELE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1538 SVS-----------RELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALEsqlaELKAQNEELEDDL 1606
Cdd:PRK03918 581 ELGfesveeleerlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE----ELRKELEELEKKY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1607 QLTEDAKLRLEvnMQALRSQFERdLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEgDLKEI-ETTME 1685
Cdd:PRK03918 657 SEEEYEELREE--YLELSRELAG-LRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELrEKVKK 732
|
570 580
....*....|....*....|
gi 386768643 1686 MHNKVKEDALKHAKKLQAQV 1705
Cdd:PRK03918 733 YKALLKERALSKVGEIASEI 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1039-1603 |
5.71e-23 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 107.05 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1039 ALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADL 1118
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1119 KEQLNER---RVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLeaekaarakaEKVRRDL 1195
Cdd:PRK02224 268 AETEREReelAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL----------EECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1196 SEelealKNELLDSLDTTAAQQELRSKREQELAtlkKSLEEETVNHEGVLADMRhkhsQELNSINDQLENLRKAKTVLEK 1275
Cdd:PRK02224 338 QA-----HNEEAESLREDADDLEERAEELREEA---AELESELEEAREAVEDRR----EEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1276 AKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQ--------------VKLAEIERARSELQEKCTKLQQEAE 1341
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpVEGSPHVETIEEDRERVEELEAELE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1342 NITNQLEEAELK---ASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEqLEEDDEAKRnyerklA 1418
Cdd:PRK02224 486 DLEEEVEEVEERlerAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE-LEAEAEEKR------E 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1419 EVTTQMQEIKKKAEEDADLAKELEEGKKRLNK--DIEALERQVKELIAQNDRLdKSKKKIQSELEDATIE-LEAQRTKVL 1495
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERL-REKREALAELNDERRErLAEKRERKR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1496 ELEKK-QKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLAntqgTA 1574
Cdd:PRK02224 638 ELEAEfDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALE----AL 713
|
570 580 590
....*....|....*....|....*....|
gi 386768643 1575 DKNVHELEKAKRALEsqlAELKAQN-EELE 1603
Cdd:PRK02224 714 YDEAEELESMYGDLR---AELRQRNvETLE 740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1064-1767 |
1.17e-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: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1064 QTLAEEEEKAKHLAKLKAKHEATisELEERLHkdqqQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEEL 1143
Cdd:TIGR02169 201 ERLRREREKAERYQALLKEKREY--EGYELLK----EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1144 TQTLLRIDEESATKATAQKAQ-RELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELlDSLDTTAAQQELR-- 1220
Cdd:TIGR02169 275 EELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI-EELEREIEEERKRrd 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1221 ------SKREQELATLKKSLEEETVNHegvlADMRHKHSQ----------ELNSIND--------------QLENLRKAK 1270
Cdd:TIGR02169 354 klteeyAELKEELEDLRAELEEVDKEF----AETRDELKDyrekleklkrEINELKReldrlqeelqrlseELADLNAAI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1271 TVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLqqEAENITNQLEEA 1350
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA--EAQARASEERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1351 ELKASAAVKSASN-----MESQLTE---------------------------AQQLLEEETRQKLGLSS-----KLRQIE 1393
Cdd:TIGR02169 508 GGRAVEEVLKASIqgvhgTVAQLGSvgeryataievaagnrlnnvvveddavAKEAIELLKRRKAGRATflplnKMRDER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1394 SEKEALQEQ----------------------------LEEDDEAKRNYERKLAEVTTQMQEIKK---------KAEEDAD 1436
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlVVEDIEAARRLMGKYRMVTLEGELFEKsgamtggsrAPRGGIL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1437 LAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISE 1516
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1517 QIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLEnkRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELK 1596
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1597 AQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRgLVKQLRDLETELDEERKQRTAAVASKKKLEGD 1676
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE-LEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1677 LKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEE------AKAAKEELQALSKEAERKVKALEAEVLQLTEDLASS 1750
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
810
....*....|....*..
gi 386768643 1751 ERARRAAETERDELAEE 1767
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEE 1001
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1077-1963 |
1.20e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 106.76 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1077 AKLKAKHEATISE---LEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQvDEMQAQLAKREEEltqtllriDEE 1153
Cdd:PTZ00121 1083 AKEDNRADEATEEafgKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE-DARKAEEARKAED--------AKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1154 SATKATAQKAQRELESQLAEiqEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKS 1233
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAE--DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1234 LEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIA 1313
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1314 ELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIE 1393
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1394 SEKEALQEQleEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadlAKELEEGKKRLNKDIEALErqVKELIAQNDRLDKSK 1473
Cdd:PTZ00121 1392 KADEAKKKA--EEDKKKADELKKAAAAKKKADEAKKKAEE----KKKADEAKKKAEEAKKADE--AKKKAEEAKKAEEAK 1463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1474 KKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEE---KAISEQIAQERDTAEREAREKETKVLSVSRELDEAfdki 1550
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA---- 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1551 EDLENKRKTlqnelddlantqgtadKNVHELEKAKRALESQLAELKAQNEELED-DLQLTEDAKLRLEVNMQALRSQFER 1629
Cdd:PTZ00121 1540 KKAEEKKKA----------------DELKKAEELKKAEEKKKAEEAKKAEEDKNmALRKAEEAKKAEEARIEEVMKLYEE 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1630 DLLAKEEGA--EEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEiettmEMHNKVKEDALKhaKKLQAQVKD 1707
Cdd:PTZ00121 1604 EKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-----EEENKIKAAEEA--KKAEEDKKK 1676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1708 ALRDAEEAKAAKEELQALSKEAERK-----VKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEK 1782
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAkkaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1783 RRLEARIATLEEELEEEQSNSEVLL-----DRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELkaklaEIET 1857
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIeeeldEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM-----EDSA 1831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1858 AQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKE-LTMNIEDERRHVDQHKEQMDKLNSRIKLLKRN 1936
Cdd:PTZ00121 1832 IKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEdDEEEIEEADEIEKIDKDDIEREIPNNNMAGKN 1911
|
890 900
....*....|....*....|....*..
gi 386768643 1937 LDETEEELQKEKTQKRKYQRECEDMIE 1963
Cdd:PTZ00121 1912 NDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1092-1692 |
2.96e-22 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 104.74 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1092 ERLHKDQQQRQESDRSKRKiETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRE---LE 1168
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIE-EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEletLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1169 SQLAEIQEDLEAEKAARAKAE---KVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEEtvnhegvL 1245
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAeevRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR-------L 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1246 ADMRhkhsQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERA 1325
Cdd:PRK02224 331 EECR----VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1326 RSELQEKCTKLQQEAENITNqlEEAELKASAavksaSNMESQLTEAQQLLEE----ETRQKLGLSSKLrqiesekealqE 1401
Cdd:PRK02224 407 LGNAEDFLEELREERDELRE--REAELEATL-----RTARERVEEAEALLEAgkcpECGQPVEGSPHV-----------E 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1402 QLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadlAKELEEGKKRLnkdiealerqvkeliaqnDRLDKSKKKIQSELE 1481
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVEERLER----AEDLVEAEDRI------------------ERLEERREDLEELIA 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1482 DATIELEAQRTKVLELEKKqknfdkilaeekaiseqiAQERDTAEREAREKETKVLSvsrELDEAFDKIEDLENKRKTLQ 1561
Cdd:PRK02224 527 ERRETIEEKRERAEELRER------------------AAELEAEAEEKREAAAEAEE---EAEEAREEVAELNSKLAELK 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1562 NELDDLANTQGTADKnVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKlrlevnmQALRSQFERDLLakeEGAEEK 1641
Cdd:PRK02224 586 ERIESLERIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERK-------RELEAEFDEARI---EEARED 654
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1642 RRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKE 1692
Cdd:PRK02224 655 KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALEN 705
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
866-1622 |
2.86e-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: 102.07 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 866 AIRIIQRNCAAYLKLRNWQwwrlyTKVKPLLEVTKQeekLVQKEDELKQVREKLDTLAKNTQEYERKYQQ--ALVEKTTL 943
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKE-----ALERQKEAIERQ---LASLEEELEKLTEEISELEKRLEEIEQLLEElnKKIKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 944 AEQLQAEIELcAEAEESRSRLMARKQELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLE 1023
Cdd:TIGR02169 287 EEQLRVKEKI-GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1024 KVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQE 1103
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1104 SDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKA 1183
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHG 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1184 ARAKAEKVRRDLSEELE-ALKNELL-----DSLDTTAAQQELRSKR------------EQELATLKKSLEEETVNHEGVL 1245
Cdd:TIGR02169 526 TVAQLGSVGERYATAIEvAAGNRLNnvvveDDAVAKEAIELLKRRKagratflplnkmRDERRDLSILSEDGVIGFAVDL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1246 ADMRHKHSQELN-SINDQL--ENLRKAKTVLEKAKG-TLEAENAD---------LATELRSVNSSRQENDRRRKQA---- 1308
Cdd:TIGR02169 606 VEFDPKYEPAFKyVFGDTLvvEDIEAARRLMGKYRMvTLEGELFEksgamtggsRAPRGGILFSRSEPAELQRLRErleg 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1309 -ESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSS 1387
Cdd:TIGR02169 686 lKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1388 KLRQIESEKEALQEQLEE-----DDEAKRNYERKLAEVTTQMQEIKKKAEE-DADLAKE------LEEGKKRLNKDIEAL 1455
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREiEQKLNRLtlekeyLEKEIQELQEQRIDL 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1456 ERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETK 1535
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1536 VLSVSRELDEAFDK-------------IEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEEL 1602
Cdd:TIGR02169 926 LEALEEELSEIEDPkgedeeipeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
810 820
....*....|....*....|
gi 386768643 1603 EDDLQLTEdaKLRLEVNMQA 1622
Cdd:TIGR02169 1006 LERIEEYE--KKKREVFMEA 1023
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
923-1775 |
4.31e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 101.76 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 923 AKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKqeLEDMMQELETRIEEEEERVlalgGEKKKLEln 1002
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK--AEEARKAEDAKRVEIARKA----EDARKAE-- 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1003 IQDLEEQLEEEEAARQKLQLEKVqldakikkyeEDLALTDDQNQKLLKEKKLLEERANDLSQtlAEEEEKAKHLAK---L 1079
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKA----------EELRKAEDARKAEAARKAEEERKAEEARK--AEDAKKAEAVKKaeeA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1080 KAKHEATISELEERLHKDQQQRQESDRS--KRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTllridEESATK 1157
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAhfARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA-----DEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1158 ATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEE 1237
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1238 TVnhegvlADMRHKHSQELNSINDQLENLRKAKTVLEKAKGtlEAENADLATELRSVNSSRQENDRRRKQA-ESQIAELQ 1316
Cdd:PTZ00121 1391 KK------ADEAKKKAEEDKKKADELKKAAAAKKKADEAKK--KAEEKKKADEAKKKAEEAKKADEAKKKAeEAKKAEEA 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1317 VKLAEIERARSELQEKCTKlQQEAENITNQLEEAELKASAAVKSASNMEsqltEAQQLLEEETRQKlglSSKLRQIESEK 1396
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKK----KADEAKKAEEAKK---ADEAKKAEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1397 EAlqeqleedDEAKRNYERKLAEVTTQMQEIKKKAE-EDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKK 1475
Cdd:PTZ00121 1535 KA--------DEAKKAEEKKKADELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1476 IQSE----LEDATIELEAQRtKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIE 1551
Cdd:PTZ00121 1607 MKAEeakkAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1552 DLENKRKTLQNELDDLANTQGTADKNVHELEKA---KRALESQLAELKAQNEELEDDLQLTEDAKLRLEvnmqalrsqfE 1628
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAeelKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE----------E 1755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1629 RDLLAKEEGAEEKRRGLVKQLRD--LETELDEERKQRTAAVASKKKLEGDLKE--IETTMEMH---NKVKEDALKHAKKL 1701
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEavIEEELDEEDEKRRMEVDKKIKDIFDNFAniIEGGKEGNlviNDSKEMEDSAIKEV 1835
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1702 QAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKG 1775
Cdd:PTZ00121 1836 ADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAG 1909
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
916-1681 |
7.02e-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: 7.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 916 REKLDTLAkNTQEYERKYQQALVEKTTLAEQLQaeiELCAEAEESRSRLMARKQELEDMMQELETRIEEEEERVLALGGE 995
Cdd:TIGR02169 156 RKIIDEIA-GVAEFDRKKEKALEELEEVEENIE---RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 996 KKKLELNIQDLEEQLEEEEAARQKLQlekVQLDAKIKKYEEdlaLTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKakh 1075
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLT---EEISELEKRLEE---IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE--- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1076 laklKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESA 1155
Cdd:TIGR02169 303 ----IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1156 TKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLE 1235
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1236 EetvnhegvLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAEL 1315
Cdd:TIGR02169 459 Q--------LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1316 -QVK---LAEIERA---------------------------------------RSELQEKCTKLQQEAENITNQLEEAEL 1352
Cdd:TIGR02169 531 gSVGeryATAIEVAagnrlnnvvveddavakeaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDP 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1353 KASAAVKSA-------SNMES---QLTEAQQL-LEEETRQKLGL----SSKLRQIESEKEALQEQLEEDDEAKRNYERKL 1417
Cdd:TIGR02169 611 KYEPAFKYVfgdtlvvEDIEAarrLMGKYRMVtLEGELFEKSGAmtggSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1418 AEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLEL 1497
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1498 EKKQKNFDKILAEEKA-----ISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQG 1572
Cdd:TIGR02169 771 EEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1573 TADKNVHELEKAKRALESQLAELKAQNEELEDDLQltedaklrlevnmqalrsqferDLLAKEEGAEEKRRGLVKQLRDL 1652
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEEL 908
|
810 820
....*....|....*....|....*....
gi 386768643 1653 ETELDEERKQRTAAVASKKKLEGDLKEIE 1681
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1066-1589 |
8.93e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 100.14 E-value: 8.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1066 LAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIEtEVADLKEQLNERRVQVDEMQAQLAKREEELTQ 1145
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1146 TLLRIDEESATKATAQKAQRELESqLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELlDSLDTTAAQQELRSKREQ 1225
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI-NGIEERIKELEEKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1226 ELATLKKSLEEETVNHEGvladmRHKHSQELNSINDQLENLRKAKTVLEKAKgtLEAENADLATELRSVNSSRQENDRRR 1305
Cdd:PRK03918 342 ELKKKLKELEKRLEELEE-----RHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1306 KQAESQIAELQVKLAEIERA---------------RSELQEKCTKlqqEAENITNQLEEAELKASAAVKSASNMESQLTE 1370
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAkgkcpvcgrelteehRKELLEEYTA---ELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1371 AQQLLEEETrqklgLSSKLRQIESE-KEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEgkkrLN 1449
Cdd:PRK03918 492 ESELIKLKE-----LAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1450 KDIEALERQVKELIAQNDRL-----DKSKKKIQS---------ELEDATIELEAQRTKV----LELEKKQKNFDKILAEE 1511
Cdd:PRK03918 563 KKLDELEEELAELLKELEELgfesvEELEERLKElepfyneylELKDAEKELEREEKELkkleEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768643 1512 KAISEQIAQ-ERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALE 1589
Cdd:PRK03918 643 EELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
897-1626 |
1.26e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.22 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 897 EVTKQEEklVQKEDELKQVREKLDTLAKNTQEYERKYQQAL-VEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMM 975
Cdd:PTZ00121 1186 EVRKAEE--LRKAEDARKAEAARKAEEERKAEEARKAEDAKkAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA 1263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 976 QELETRIEEEEERvlalggEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLL 1055
Cdd:PTZ00121 1264 HFARRQAAIKAEE------ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1056 EERANDLSQTLAEEEEKAKHLAKlKAKHEATISELeerlhKDQQQRQESDRSKRKIET--EVADLKEQLNERRVQVDEMQ 1133
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAE-AAEEKAEAAEK-----KKEEAKKKADAAKKKAEEkkKADEAKKKAEEDKKKADELK 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1134 --AQLAKREEELTQTL--LRIDEESATKATAQKAQRELESQLAEIQ--EDLEAEKAARAKAEKVRRDLSEELEAlknell 1207
Cdd:PTZ00121 1412 kaAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKKA------ 1485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1208 DSLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQElnsinDQLENLRKAKTVlEKAKGTLEAENADL 1287
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA-----KKADEAKKAEEK-KKADELKKAEELKK 1559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1288 ATELRSVNSSRQENDRRRKQAESqiAELqvkLAEIERARSElqekctklqqeaENITNQLEEAELKASAAVKSasnmESQ 1367
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRK--AEE---AKKAEEARIE------------EVMKLYEEEKKMKAEEAKKA----EEA 1618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1368 LTEAQQLLEEETRQKLGLSSKLRQIESEKEALQ-EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKK 1446
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1447 RLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKI---LAEEKAISEQIAQERD 1523
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIahlKKEEEKKAEEIRKEKE 1778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1524 TAEREA--REKETKVLSVSRELDEAFDKIEDLE-----------NKRKTLQNELDDLANTQGTADKNVHELEKAKRALES 1590
Cdd:PTZ00121 1779 AVIEEEldEEDEKRRMEVDKKIKDIFDNFANIIeggkegnlvinDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNN 1858
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 386768643 1591 QLAELKAQNEE-------LEDDLQLTEDAKLRLEVNMQALRSQ 1626
Cdd:PTZ00121 1859 ENGEDGNKEADfnkekdlKEDDEEEIEEADEIEKIDKDDIERE 1901
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1068-1903 |
3.16e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.67 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1068 EEEEKAKHLAKLKAKHEATISElEERLHKDQQQRQESDRskRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTL 1147
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAE-EARKAEEAKKKAEDAR--KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1148 LRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRdlseELEALKNELLDSLDTTAAQQELRSKREQel 1227
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERK----AEEARKAEDAKKAEAVKKAEEAKKDAEE-- 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1228 atlKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVlEKAKGTLEAENADLATELRSVNSSRQENDRRRK- 1306
Cdd:PTZ00121 1242 ---AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL-KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKa 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1307 -QAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEE-----ETR 1380
Cdd:PTZ00121 1318 dEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkadEAK 1397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1381 QKLGLSSK----LRQIESEKEALQEQLEEDDEAKRNYE-RKLAEVTTQMQEIKKKAEE---------DADLAKELEEGKK 1446
Cdd:PTZ00121 1398 KKAEEDKKkadeLKKAAAAKKKADEAKKKAEEKKKADEaKKKAEEAKKADEAKKKAEEakkaeeakkKAEEAKKADEAKK 1477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1447 RLN--KDIEALERQVKELIAQNDRLDKSK--KKIQSELEDATIELEAQRTKVLELEKKQKNFDKilAEEKAISEQI---- 1518
Cdd:PTZ00121 1478 KAEeaKKADEAKKKAEEAKKKADEAKKAAeaKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKKKADELkkae 1555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1519 ----AQERDTAEREAREKETKVLSVSR---------ELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAK 1585
Cdd:PTZ00121 1556 elkkAEEKKKAEEAKKAEEDKNMALRKaeeakkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1586 RALESQLAELKAQNEELEDDlqlTEDAKLRLEvnmqalrsqferDLLAKEEgaEEKRRGlvKQLRDLETELDEERKQRTA 1665
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKA---EEENKIKAA------------EEAKKAE--EDKKKA--EEAKKAEEDEKKAAEALKK 1696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1666 AVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKA------AKEELQALSKEAERKVKALEAE 1739
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEakkdeeEKKKIAHLKKEEEKKAEEIRKE 1776
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1740 VLQLTEDLASSERARRAAETERD-----ELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEvlldrsrKAQ 1814
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRMEVDKKikdifDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEA-------DAF 1849
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1815 LQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKA 1894
Cdd:PTZ00121 1850 EKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDA 1929
|
....*....
gi 386768643 1895 NRKMDKKIK 1903
Cdd:PTZ00121 1930 EETREEIIK 1938
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1218-1692 |
5.49e-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: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1218 ELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSqELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSS 1297
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK-ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1298 R----------QENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQ 1367
Cdd:TIGR04523 196 LlklelllsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1368 LTEAQQLLEEETRQKLGLSSKLRQIESEKEA-----LQEQLEEDDEAKRNYE---------------------------- 1414
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQnqisqnnkiisqlneqisqlkkeltnse 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1415 -------RKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIEL 1487
Cdd:TIGR04523 356 sensekqRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1488 EAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL 1567
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1568 ANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQ----------ALRSQFERDLLAKEEg 1637
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieelkqtqksLKKKQEEKQELIDQK- 594
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 386768643 1638 aEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIEttmEMHNKVKE 1692
Cdd:TIGR04523 595 -EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK---SKKNKLKQ 645
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1358-1900 |
2.23e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 95.52 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1358 VKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRnyerKLAEVTTQMQEIKKKAEEDADL 1437
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE----EIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1438 AKELEEGKKRLNKDIEALERQVKE-------------LIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNF 1504
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKElkelkekaeeyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1505 DKILAEEKAISEQIA--QERDTAEREAREKETKVLSVSREL-----DEAFDKIEDLENKRKTLQNELDDLANTQGTADKN 1577
Cdd:PRK03918 341 EELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1578 VHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNmqalrsqferDLLAKEEGAEEKRRGLVKQLRDLETELD 1657
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELK----------RIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1658 EERKqrtaaVASKKKLEGDLKEIETTMEMHN--KVKEDA--LKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKV 1733
Cdd:PRK03918 491 KESE-----LIKLKELAEQLKELEEKLKKYNleELEKKAeeYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1734 KALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKA 1813
Cdd:PRK03918 566 DELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1814 QLQIEQLttelaNEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKvkatiATLEAKIANLEEQLENEGKERLLQQK 1893
Cdd:PRK03918 646 RKELEEL-----EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRR-----EEIKKTLEKLKEELEEREKAKKELEK 715
|
....*..
gi 386768643 1894 ANRKMDK 1900
Cdd:PRK03918 716 LEKALER 722
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1398-1967 |
3.94e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.72 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1398 ALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadlaKELEEGKKRLNkdieALERQVKELIAQNDRLDKSKKKIQ 1477
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEE-----KEEKDLHERLN----GLESELAELDEEIERYEEQREQAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1478 SELEDATIELEAQRTKVLELEKKQKNFDKiLAEEKAISEQiaqERDTAEREAREKETKVLSVSRELDEAFDK-------- 1549
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELETLEAEIED-LRETIAETER---EREELAEEVRDLRERLEELEEERDDLLAEaglddada 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1550 ------IEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQAL 1623
Cdd:PRK02224 310 eavearREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1624 RSQFErDLLAKEEGAEEkrrglvkQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEmhnkvKEDALKHAKKLQA 1703
Cdd:PRK02224 390 EEEIE-ELRERFGDAPV-------DLGNAEDFLEELREERDELREREAELEATLRTARERVE-----EAEALLEAGKCPE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1704 ---QVKDALRDAEEAkaakeelqalskEAERKVKALEAEVLQLTEdlassERARRAAETERDELAEEIANNANKgslmID 1780
Cdd:PRK02224 457 cgqPVEGSPHVETIE------------EDRERVEELEAELEDLEE-----EVEEVEERLERAEDLVEAEDRIER----LE 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1781 EKR-RLEARIATLEEELEEEQSNSEVLldRSRKAQLQIEQLTTELANEKSNSQKNENGRALlerqnKELKAKLAEIetAQ 1859
Cdd:PRK02224 516 ERReDLEELIAERRETIEEKRERAEEL--RERAAELEAEAEEKREAAAEAEEEAEEAREEV-----AELNSKLAEL--KE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1860 RTKVKATIATLEAKIANLEEQLEnEGKERLLQQKAnrkmdkkikeltmnIEDERRhvdqhkEQMDKLNSRIKLLKRNLDE 1939
Cdd:PRK02224 587 RIESLERIRTLLAAIADAEDEIE-RLREKREALAE--------------LNDERR------ERLAEKRERKRELEAEFDE 645
|
570 580
....*....|....*....|....*....
gi 386768643 1940 TE-EELQKEKTQKRKYQRECEDMIESQEA 1967
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 ... |
891-1708 |
3.59e-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: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 891 KVKPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIE-LCAEAEESRSRLMARKQ 969
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLkLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 970 ELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEA-ARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKL 1048
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEeLKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1049 LKEKKLLEERANdlsqtlaEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQ 1128
Cdd:pfam02463 331 KKEKEEIEELEK-------ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1129 VDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELL- 1207
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLq 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1208 --DSLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQEL----------NSINDQLENLRKAKTVLEK 1275
Cdd:pfam02463 484 eqLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLgvavenykvaISTAVIVEVSATADEVEER 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1276 AKGTL-EAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEI------ERARSELQEKCTKLQQEAENITNQLE 1348
Cdd:pfam02463 564 QKLVRaLTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAtleadeDDKRAKVVEGILKDTELTKLKESAKA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1349 EAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYE---RKLAEVTTQMQ 1425
Cdd:pfam02463 644 KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKeelKKLKLEAEELL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1426 EIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFD 1505
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1506 KILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAK 1585
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1586 RALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTA 1665
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 386768643 1666 AVASKKKLEGdLKEIETTMEMHNKVKEDALKHAKKLQAQVKDA 1708
Cdd:pfam02463 964 RLLLAKEELG-KVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1347-1927 |
3.80e-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: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1347 LEEAELKAsaAVKSASNMESQLTEAQQLLEEETRQKlglsSKLRQIESEKEALQEQLEEDDEAKrnYERKLAEV---TTQ 1423
Cdd:COG4913 218 LEEPDTFE--AADALVEHFDDLERAHEALEDAREQI----ELLEPIRELAERYAAARERLAELE--YLRAALRLwfaQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1424 MQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLD-KSKKKIQSELEDATIELEAQRTKVLELEKKQK 1502
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1503 NFD-KILAEEKAISEQIAQERDTAEREAREKEtkvlSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHEL 1581
Cdd:COG4913 370 ALGlPLPASAEEFAALRAEAAALLEALEEELE----ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1582 ekaKRALESQL----------AEL---KAQNEE----------------------LEDDLQLTEDAKLRLEVNMQ----- 1621
Cdd:COG4913 446 ---RDALAEALgldeaelpfvGELievRPEEERwrgaiervlggfaltllvppehYAAALRWVNRLHLRGRLVYErvrtg 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1622 ---ALRSQFERDLLAKE-------------------------EGAEEKRR--------GLVKQLRDLEtELDEERKQRTA 1665
Cdd:COG4913 523 lpdPERPRLDPDSLAGKldfkphpfrawleaelgrrfdyvcvDSPEELRRhpraitraGQVKGNGTRH-EKDDRRRIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1666 AV---ASKKKLEGDLKEIETTmemhnkvkEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALS------KEAERKVKAL 1736
Cdd:COG4913 602 YVlgfDNRAKLAALEAELAEL--------EEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAEL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1737 EAEVLQLTE---DLASSERARRAAETERDELAEEIAnnankgsLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKA 1813
Cdd:COG4913 674 EAELERLDAssdDLAALEEQLEELEAELEELEEELD-------ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1814 Q-LQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRT---KVKATIATLEAKIANLEE------QLEN 1883
Cdd:COG4913 747 LrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrEWPAETADLDADLESLPEylalldRLEE 826
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 386768643 1884 EG----KERLLQQKaNRKMDKKIKELTMNIEDERRHVdqhKEQMDKLN 1927
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 ... |
916-1775 |
3.86e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.49 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 916 REKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQELETRIEEEEERVLA-LGG 994
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDyLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 995 EKKKLELNIQDLEEQLEEEEAARQKLQLEK---VQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEE 1071
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEeklAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1072 KAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRID 1151
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1152 EESATKATAQKAQR---ELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELA 1228
Cdd:pfam02463 395 EELELKSEEEKEAQlllELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1229 TLKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEA---ENADLATELRSVNSSRQENDRRR 1305
Cdd:pfam02463 475 KETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgrlGDLGVAVENYKVAISTAVIVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1306 KQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLL----EEETRQ 1381
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVvegiLKDTEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1382 KLGLSSKLRQIESEKEALQEQLEEDDEAKRNYE-RKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDiEALERQVK 1460
Cdd:pfam02463 635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASlSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE-QREKEELK 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1461 ELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKEtkvlSVS 1540
Cdd:pfam02463 714 KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL----KVE 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1541 RELDEAFDKIEDLENKRKTLQNELDDLANTQGtadknvhELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNM 1620
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEEELKEEAELLEEEQ-------LLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1621 QALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKK 1700
Cdd:pfam02463 863 ITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1701 LQAQVKDALRDAEEAKAAKEELQALSKEAERKVKAL--------EAEVLQLTEDLASSERARRAAETERDELAEEIANNA 1772
Cdd:pfam02463 943 EEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMaieefeekEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
...
gi 386768643 1773 NKG 1775
Cdd:pfam02463 1023 LEL 1025
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1327-1982 |
2.76e-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: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1327 SELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEED 1406
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1407 DEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIE 1486
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1487 LEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLsvsrELDEAFDKIEDLENKRKTLQNELDD 1566
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT----EISNTQTQLNQLKDEQNKIKKQLSE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1567 LANTQGTADKNVHELEKAKRALESQLAELKAQNEeleddlqltedaklrlevnmQALRSQFERDLLAKEegaeekrrglv 1646
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--------------------QDWNKELKSELKNQE----------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1647 KQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTmemhNKVKEDALKhakKLQAQVKDALRDAEEAKAAKEELQALS 1726
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE----NSEKQRELE---EKQNEIEKLKKENQSYKQEIKNLESQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1727 KEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVL 1806
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1807 LDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRtKVKATIATLEAKIANLEEQLE--NE 1884
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNkdDF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1885 GKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNL-------DETEEELQKEKTQKRKYQRE 1957
Cdd:TIGR04523 553 ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIeekekkiSSLEKELEKAKKENEKLSSI 632
|
650 660
....*....|....*....|....*
gi 386768643 1958 CEDMIESQEAMNREINSLKTKLRRT 1982
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1192-1711 |
3.21e-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: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1192 RRDLSEELEALKnELLDSLDttAAQQELRSKREQ--------ELATLKKSLEEETVNHEGVLADMRH-KHSQELNSINDQ 1262
Cdd:COG4913 220 EPDTFEAADALV-EHFDDLE--RAHEALEDAREQiellepirELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1263 LENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQEND-RRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAE 1341
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1342 NITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQklgLSSKLRQIESEKEALQE-------------------- 1401
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERrksniparllalrdalaeal 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1402 --------------QLEEDDEAKRN------------------YERKLAE---------------VTTQMQEIKKKAEED 1434
Cdd:COG4913 454 gldeaelpfvgeliEVRPEEERWRGaiervlggfaltllvppeHYAAALRwvnrlhlrgrlvyerVRTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1435 ADLAKELE--EG------KKRLNK--------DIEALER---------QVK---ELIAQNDRLDK---------SKKKI- 1476
Cdd:COG4913 534 DSLAGKLDfkPHpfrawlEAELGRrfdyvcvdSPEELRRhpraitragQVKgngTRHEKDDRRRIrsryvlgfdNRAKLa 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1477 --QSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDT--AEREAREKETKVlsvsRELDEAFDKIED 1552
Cdd:COG4913 614 alEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAEL----ERLDASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1553 LENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKL---RLEVNMQALRSQFER 1629
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeerFAAALGDAVERELRE 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1630 DLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASkkklegDLKEIETTMEMHNKVKEDALkhaKKLQAQVKDAL 1709
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDA------DLESLPEYLALLDRLEEDGL---PEYEERFKELL 840
|
..
gi 386768643 1710 RD 1711
Cdd:COG4913 841 NE 842
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1015-1667 |
4.28e-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: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1015 AARQKLQLEkvQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAE--EEEKAKHLAKLkAKHEATISELEE 1092
Cdd:COG4913 247 AREQIELLE--PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEelRAELARLEAEL-ERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1093 RLHKDQQQRQESD-RSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTqtllrideesATKATAQKAQRELESQL 1171
Cdd:COG4913 324 ELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP----------ASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1172 AEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELldsldttaaqQELRSKR---EQELATLKKSLEEETVNH------- 1241
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEI----------ASLERRKsniPARLLALRDALAEALGLDeaelpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1242 -----------------EGVLADMR------HKHSQELNSINDQLE-----NLRKAKTVLEKAKgTLEAENADLATEL-- 1291
Cdd:COG4913 464 gelievrpeeerwrgaiERVLGGFAltllvpPEHYAAALRWVNRLHlrgrlVYERVRTGLPDPE-RPRLDPDSLAGKLdf 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1292 --------------------------------RSV--------NSSRQENDRRRK---------QAESQIAELQVKLAEI 1322
Cdd:COG4913 543 kphpfrawleaelgrrfdyvcvdspeelrrhpRAItragqvkgNGTRHEKDDRRRirsryvlgfDNRAKLAALEAELAEL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1323 ERARSELQEKCTKLQQEAENITNQLeeaelkasaavksasnmesqltEAQQLLEEETRQKLGLSSKLRQIEsEKEALQEQ 1402
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERR----------------------EALQRLAEYSWDEIDVASAEREIA-ELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1403 LEEDDEakrnyerKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELED 1482
Cdd:COG4913 680 LDASSD-------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1483 ATIELEAQRTKvlelekkqknfdkilaeEKAISEQIAQERDTAEREAREKETKVL-----------SVSRELDEAFDKIE 1551
Cdd:COG4913 753 ERFAAALGDAV-----------------ERELRENLEERIDALRARLNRAEEELEramrafnrewpAETADLDADLESLP 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1552 DLENKRKTLQNE--------LDDLANTQGTADKN--VHELEKAKRALESQLAELkaqNEELEdDLQLTEDAKLRLEVNMQ 1621
Cdd:COG4913 816 EYLALLDRLEEDglpeyeerFKELLNENSIEFVAdlLSKLRRAIREIKERIDPL---NDSLK-RIPFGPGRYLRLEARPR 891
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 386768643 1622 ALRS--QFERDLLAKEEGAE-------EKRRGLVKQLRD-LETELDEERKQRTAAV 1667
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 ... |
1285-1981 |
5.87e-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: 84.64 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1285 ADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKlQQEAENITNQLEEAELKASAAVKSASNM 1364
Cdd:pfam02463 186 AELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE-ERIDLLQELLRDEQEEIESSKQEIEKEE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1365 ESQLTEaQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEG 1444
Cdd:pfam02463 265 EKLAQV-LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1445 KKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQrTKVLELEKKQKNFDKILAEEKAISEQIAQERDT 1524
Cdd:pfam02463 344 LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA-AKLKEEELELKSEEEKEAQLLLELARQLEDLLK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1525 AEREAREKETKVLSVSRELDEAFDKI----EDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNE 1600
Cdd:pfam02463 423 EEKKEELEILEEEEESIELKQGKLTEekeeLEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1601 ELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEI 1680
Cdd:pfam02463 503 SKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRL 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1681 ETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETE 1760
Cdd:pfam02463 583 LIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKS 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1761 RDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNEngRAL 1840
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEE--LKL 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1841 LERQNKELKAKLAEIETAQRTKvKATIATLEAKIANLEEQLENEGKERLLQQKanrkmDKKIKELTMNIEDERRHVDQHK 1920
Cdd:pfam02463 741 LKQKIDEEEEEEEKSRLKKEEK-EEEKSELSLKEKELAEEREKTEKLKVEEEK-----EEKLKAQEEELRALEEELKEEA 814
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1921 EQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1981
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK 875
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1385-1981 |
4.22e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 81.65 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1385 LSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLnKDIEALERQVKELIA 1464
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1465 QNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEqIAQERDTAEREAREKETKVLSVSRELD 1544
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1545 EAFDKIEDLENKrktlqnelddlantqgtadknvhelEKAKRALESQLAELKAQNEELEDDLQLTEDAKlRLEVNMQALR 1624
Cdd:PRK03918 325 GIEERIKELEEK-------------------------EERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1625 sqferdllaKEEGAEEKRRgLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEmhnkvkedALKHAKKLQAQ 1704
Cdd:PRK03918 379 ---------KRLTGLTPEK-LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE--------ELKKAKGKCPV 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1705 VKDALRDAEEAKaakeelqaLSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNAnkgslMIDEKRR 1784
Cdd:PRK03918 441 CGRELTEEHRKE--------LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1785 LEARIATLEEELEEEQSNS-EVLLDRSRKAQLQIEQLTTELanEKSNSQKNEngRALLERQNKELKAKLAEIETAQRTKV 1863
Cdd:PRK03918 508 LEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKKEL--EKLEELKKK--LAELEKKLDELEEELAELLKELEELG 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1864 KATIATLEAKIANLEEqLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETE-E 1942
Cdd:PRK03918 584 FESVEELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyE 662
|
570 580 590
....*....|....*....|....*....|....*....
gi 386768643 1943 ELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1981
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
966-1856 |
5.05e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 81.63 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 966 ARKQELEDMMQELETRIEEEEER--VLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAK---IKKYEEDLAL 1040
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETLRqvRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSreiVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1041 TDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKE 1120
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1121 QLNERRVQVDEMQAQLAKREEELTQTLLRIDEESaTKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELE 1200
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHI-RARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1201 ALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHS--QELNSINDQL----ENLRKAKTVLE 1274
Cdd:TIGR00606 409 TAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKelQQLEGSSDRIleldQELRKAERELS 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1275 KAKgtleaENADLATELRSVNSSRQEN---DRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEE-- 1349
Cdd:TIGR00606 489 KAE-----KNSLTETLKKEVKSLQNEKadlDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDElt 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1350 AELKASAAVKSASNMESQLTEAQQLLEEETRQklgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVT------TQ 1423
Cdd:TIGR00606 564 SLLGYFPNKKQLEDWLHSKSKEINQTRDRLAK---LNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCgsqdeeSD 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1424 MQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKN 1503
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKK 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1504 FDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELD---DLANTQGTADKNVHE 1580
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEEsakVCLTDVTIMERFQME 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1581 LEKAKRALESQLAELKAQ---------NEELEDDLQLTEDAKLRLEVNMQALRSQFERDL-------------------L 1632
Cdd:TIGR00606 801 LKDVERKIAQQAAKLQGSdldrtvqqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQhlksktnelkseklqigtnL 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1633 AKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDA 1712
Cdd:TIGR00606 881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI 960
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1713 EEAkaakeelqaLSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATL 1792
Cdd:TIGR00606 961 ENK---------IQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELK 1031
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1793 EEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIE 1856
Cdd:TIGR00606 1032 EVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
908-1601 |
5.40e-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: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 908 KEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQeletrieeeee 987
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD----------- 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 988 RVLALGGE--KKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQT 1065
Cdd:TIGR00606 472 RILELDQElrKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1066 LAEEEEKAKHLAKLKAKHEATiSELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQ 1145
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1146 TLLRIDEESAT---KATAQKAQREL----------ESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELL---DS 1209
Cdd:TIGR00606 631 VCGSQDEESDLerlKEEIEKSSKQRamlagatavySQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRlapDK 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1210 LDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENaDLAT 1289
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK-VCLT 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1290 ELRSVNSSRQENDRRRKQAESQIAELQVklAEIERARSELQEKCTKLQQEAENITNQLEEAelkasaavksasnmesqlt 1369
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQG--SDLDRTVQQVNQEKQEKQHELDTVVSKIELN------------------- 848
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1370 eaQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELE------- 1442
Cdd:TIGR00606 849 --RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEkdqqeke 926
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1443 -------EGKKRLNKDIEALERQVKELIAQNDRLDkskKKIQSELEDATIELEAQRTKVL----ELEKKQKNFDKIL-AE 1510
Cdd:TIGR00606 927 elisskeTSNKKAQDKVNDIKEKVKNIHGYMKDIE---NKIQDGKDDYLKQKETELNTVNaqleECEKHQEKINEDMrLM 1003
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1511 EKAISEQIAQER---DTAEREAREKETKVLSVSR-----ELDEafDKIEDLENKRKTLQNELDDLANTQGTADKNVHELE 1582
Cdd:TIGR00606 1004 RQDIDTQKIQERwlqDNLTLRKRENELKEVEEELkqhlkEMGQ--MQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYE 1081
|
730
....*....|....*....
gi 386768643 1583 KAKRALESQLAELKAQNEE 1601
Cdd:TIGR00606 1082 KEIKHFKKELREPQFRDAE 1100
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1081-1694 |
5.91e-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: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1081 AKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLlrideeSATKATA 1160
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGEL------SAADAAV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1161 QKAQRELES----QLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEE 1236
Cdd:pfam12128 318 AKDRSELEAledqHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1237 ETVN---------------HEGVLADMRHKHSQELNSINDQ------------------------LENLRKAKTVLEKAK 1277
Cdd:pfam12128 398 KLAKireardrqlavaeddLQALESELREQLEAGKLEFNEEeyrlksrlgelklrlnqatatpelLLQLENFDERIERAR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1278 GTLEAENA---DLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIE-----RARSELQEKCTKLQQEAENITNQLEE 1349
Cdd:pfam12128 478 EEQEAANAeveRLQSELRQARKRRDQASEALRQASRRLEERQSALDELElqlfpQAGTLLHFLRKEAPDWEQSIGKVISP 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1350 AEL--------KASAAVKSASNMESQLTEAQQL-------LEEETRQKLGLSSKLRQIESEKEALQEqlEEDDEAKRNYE 1414
Cdd:pfam12128 558 ELLhrtdldpeVWDGSVGGELNLYGVKLDLKRIdvpewaaSEEELRERLDKAEEALQSAREKQAAAE--EQLVQANGELE 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1415 RKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQndrLDKSKKKIQSELEDAtieLEAQRTKV 1494
Cdd:pfam12128 636 KASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS---LEAQLKQLDKKHQAW---LEEQKEQK 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1495 LELEKKQKNFDKILAEEK-----AISEQIAQERDTAERE--AREKETKVLSVSRELDEafDKIEDLENKRKTLQNELDDL 1567
Cdd:pfam12128 710 REARTEKQAYWQVVEGALdaqlaLLKAAIAARRSGAKAElkALETWYKRDLASLGVDP--DVIAKLKREIRTLERKIERI 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1568 ANTQGTA----DKNVHELEKAKRALESQLAELKAQNEELEDDL-QLTEDAKLRlevnmqalRSQFERDLlakeegaeekr 1642
Cdd:pfam12128 788 AVRRQEVlryfDWYQETWLQRRPRLATQLSNIERAISELQQQLaRLIADTKLR--------RAKLEMER----------- 848
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 386768643 1643 rglvKQLRDLETELDEErkqrtaavaskkklegdLKEIETTMEMHNKVKEDA 1694
Cdd:pfam12128 849 ----KASEKQQVRLSEN-----------------LRGLRCEMSKLATLKEDA 879
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1306-1950 |
7.01e-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: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1306 KQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQlleeetrQKLGL 1385
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE-------QKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1386 SSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALErqvKELIAQ 1465
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK---NKLLKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1466 NDRLDKSKKKIQ--SELEDATIELEAQRTKVLE-LEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLsvsrE 1542
Cdd:TIGR04523 200 ELLLSNLKKKIQknKSLESQISELKKQNNQLKDnIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK----E 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1543 LDEAFDKIEDLENKRKTLQNELDDLAN-TQGTADKNVHE----LEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLE 1617
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNqKEQDWNKELKSelknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1618 VNMQALRSQFE------RDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQrtaavasKKKLEGDLKEIETTMEMHNKVK 1691
Cdd:TIGR04523 356 SENSEKQRELEekqneiEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL-------NQQKDEQIKKLQQEKELLEKEI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1692 EDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVlqltedlasserarRAAETERDELAEEIANN 1771
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI--------------NKIKQNLEQKQKELKSK 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1772 ANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELaneksNSQKNENGRALLErqnKELKAK 1851
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL-----NKDDFELKKENLE---KEIDEK 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1852 LAEIEtaqrtKVKATIATLEAKianleeqleNEGKERLLQQKANRKMD--KKIKELTMNIEDERRHVDQHKEQMDKLNSR 1929
Cdd:TIGR04523 567 NKEIE-----ELKQTQKSLKKK---------QEEKQELIDQKEKEKKDliKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
|
650 660
....*....|....*....|.
gi 386768643 1930 IKLLKRNLDETEEELQKEKTQ 1950
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKET 653
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
901-1643 |
1.41e-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: 80.02 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 901 QEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQELET 980
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 981 RIEEEEERVLALGGEKKKLELNIQ------DLEEQLEEEEAARQ-----KLQLEKVQLDAKIKKYEEDLALTD------- 1042
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREaeeeeeEELEKLQEKLEQLEeellaKKKLESERLSSAAKLKEEELELKSeeekeaq 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1043 DQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQ-RQESDRSKRKIETEVADLKEQ 1121
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELElKKSEDLLKETQLVKLQEQLEL 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1122 LNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEA 1201
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1202 LKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNH-----EGVLADMRHKHSQELNSINDQLENLRKAKTVLEKA 1276
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLdkatlEADEDDKRAKVVEGILKDTELTKLKESAKAKESGL 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1277 KGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIeraRSELQEKCTKLQQEAENITNQLEEAELKASA 1356
Cdd:pfam02463 649 RKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI---LRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1357 AVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAD 1436
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1437 LAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSE----LEDATIELEAQRTKVL---ELEKKQKNFDKILA 1509
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLeklaEEELERLEEEITKEELlqeLLLKEEELEEQKLK 885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1510 EEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKaKRALE 1589
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEE-ERNKR 964
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1590 SQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRR 1643
Cdd:pfam02463 965 LLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1390-1983 |
1.47e-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: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1390 RQIESEKEALQEQLEEDDEAKRNYERKLAEVTT--QMQEIKKKAEEDADLAKELEEGKKRLnkDIEALERQVKELIAQND 1467
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1468 RLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDkilAEEKaisEQIAQERDTAEREAREKETKVLSVSRELD--- 1544
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNG---GDRL---EQLEREIERLERELEERERRRARLEALLAalg 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1545 -EAFDKIEDLENKRKTLQNELDDLANTQgtadknvHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQAL 1623
Cdd:COG4913 373 lPLPASAEEFAALRAEAAALLEALEEEL-------EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1624 RSQFERDLLAKE-------------------EGAEEK------------------------RRGLVKQLRDLETELDEER 1660
Cdd:COG4913 446 RDALAEALGLDEaelpfvgelievrpeeerwRGAIERvlggfaltllvppehyaaalrwvnRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1661 KQRTAAVASK--KKLEGDLKEIETTMEMH-----NKVK---EDALKHAKK---LQAQVKD--ALRDAEEAKAAKEELQaL 1725
Cdd:COG4913 526 PERPRLDPDSlaGKLDFKPHPFRAWLEAElgrrfDYVCvdsPEELRRHPRaitRAGQVKGngTRHEKDDRRRIRSRYV-L 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1726 SKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELaeeiannankgslmiDEKRRLEARIATLEEELEEEQSnsev 1805
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDAL---------------QERREALQRLAEYSWDEIDVAS---- 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1806 lldrsrkAQLQIEQLTTELAN-EKSNSQKNEngralLERQNKELKAKLAEIEtAQRTKVKATIATLEAKIANLEEQLENe 1884
Cdd:COG4913 666 -------AEREIAELEAELERlDASSDDLAA-----LEEQLEELEAELEELE-EELDELKGEIGRLEKELEQAEEELDE- 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1885 gkerlLQQKANRKMDKKIKELTMNIEDERRHVDQ---HKEQMDKLNSRIKLLKRNLDETEEELQKEKTQ-KRKYQRECED 1960
Cdd:COG4913 732 -----LQDRLEAAEDLARLELRALLEERFAAALGdavERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETAD 806
|
650 660
....*....|....*....|...
gi 386768643 1961 MIESQEAmNREINSLKTKLRRTG 1983
Cdd:COG4913 807 LDADLES-LPEYLALLDRLEEDG 828
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1246-1461 |
2.43e-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: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1246 ADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERA 1325
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1326 RSELQEKCTKLQQEAENITNQLEEAEL----KASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQE 1401
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLlspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1402 QLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKE 1461
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1064-1921 |
2.94e-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: 79.23 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1064 QTLAEEEEKAKHLAKLKAKHEATISELEERLH--KDQQQR-QESDRSKRKIE---TEVADLKEQLNERRVQVDEMQAQLA 1137
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQaaSDHLNLvQTALRQQEKIEryqEDLEELTERLEEQEEVVEEAAEQLA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1138 KREEELTQTLLRIDEesatkataqkaqreLESQLAEIQEDLEAEKAARAKAEKVRRDLsEELEALKNelLDSLDTTAAQQ 1217
Cdd:COG3096 379 EAEARLEAAEEEVDS--------------LKSQLADYQQALDVQQTRAIQYQQAVQAL-EKARALCG--LPDLTPENAED 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1218 ELRSKREQElatlkKSLEEETVNHEGVLADMRHKHSQelnsindqlenLRKAKTVLEKAKGTLEAENA-DLATELRSVNS 1296
Cdd:COG3096 442 YLAAFRAKE-----QQATEEVLELEQKLSVADAARRQ-----------FEKAYELVCKIAGEVERSQAwQTARELLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1297 SRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQE---AENITNQLEEAELKASAAVKSASNMESQLTEAQQ 1373
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1374 LLEEETRQKlglsSKLRQIESEKEALQEQL----EEDDEAKRNyerkLAEVTTQMQEIkkkaeedADLAKELEEGKKRLN 1449
Cdd:COG3096 586 QLEQLRARI----KELAARAPAWLAAQDALerlrEQSGEALAD----SQEVTAAMQQL-------LEREREATVERDELA 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1450 KDIEALERQVKELI----AQNDRLDKSKKKIQSEL-----EDATIE--------------------LEAQRTKVLELEKk 1500
Cdd:COG3096 651 ARKQALESQIERLSqpggAEDPRLLALAERLGGVLlseiyDDVTLEdapyfsalygparhaivvpdLSAVKEQLAGLED- 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1501 qknfdkiLAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDL--------ENKRKTLQNELDDLANTQG 1572
Cdd:COG3096 730 -------CPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYSRFPEVplfgraarEKRLEELRAERDELAEQYA 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1573 TADKNVHELEKAKRAL----------------ESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFerDLLakee 1636
Cdd:COG3096 803 KASFDVQKLQRLHQAFsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQL--QLL---- 876
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1637 gaeekrRGLVKQL-----RDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKkLQAQVKDAlrd 1711
Cdd:COG3096 877 ------NKLLPQAnlladETLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQ-LQADYLQA--- 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1712 aeeakaakeelQALSKEAERKVKALEaEVLQLTEDLASSERARRAAETErdELAEEIannanKGSLMIDEKRRLEARIAT 1791
Cdd:COG3096 947 -----------KEQQRRLKQQIFALS-EVVQRRPHFSYEDAVGLLGENS--DLNEKL-----RARLEQAEEARREAREQL 1007
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1792 LEEELEEEQSNSEVL-LDRSRKAQLQIEQ-LTTELANEKSNSQKNENGRALLERQnkELKAKLAEiETAQRTKVKATIAT 1869
Cdd:COG3096 1008 RQAQAQYSQYNQVLAsLKSSRDAKQQTLQeLEQELEELGVQADAEAEERARIRRD--ELHEELSQ-NRSRRSQLEKQLTR 1084
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 386768643 1870 LEAKIANLEEQLenegkerllqqkanRKMDKKIKeltmnieDERRHVDQHKE 1921
Cdd:COG3096 1085 CEAEMDSLQKRL--------------RKAERDYK-------QEREQVVQAKA 1115
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
900-1538 |
3.27e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 900 KQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEdmmqELE 979
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 980 TRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQlEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERA 1059
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1060 NDLSQTLAEEEEKAKHLAKLKAKHEAT---ISELEERLHKDQQQRQESDRSKRKiETEVADLKEQLNERRVQ-VDEMQAQ 1135
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELkkkLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTGLTPEkLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1136 LAKREEELTQTLLRIDEESAtkataqkaqrELESQLAEIQEDLEAEKAARAKAEKVRRDLSEE-----LEALKNELLDSL 1210
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIG----------ELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1211 DTTAAQQELRSKREQELATLKKSLEEE-TVNHEGVLADMRHKHSQELNSINdqLENLRKAKTVLEKAKGTLeaenADLAT 1289
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKEsELIKLKELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKL----IKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1290 ELRSVNSSRQEndrrrkqaesqIAELQVKLAEIERARSELQEKCTKLQQEAENItnqleeaelkasaAVKSASNMESQLT 1369
Cdd:PRK03918 540 EIKSLKKELEK-----------LEELKKKLAELEKKLDELEEELAELLKELEEL-------------GFESVEELEERLK 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1370 EaqqlLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAkrnyERKLAEVTTQMQEIKKKAEEdadLAKEL-EEGKKRL 1448
Cdd:PRK03918 596 E----LEPFYNEYLELKDAEKELEREEKELKKLEEELDKA----FEELAETEKRLEELRKELEE---LEKKYsEEEYEEL 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1449 NKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKkqknFDKILAEEKAISEQIAQERDTAERE 1528
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELREKVKKYKALLKER 740
|
650
....*....|
gi 386768643 1529 AREKETKVLS 1538
Cdd:PRK03918 741 ALSKVGEIAS 750
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
897-1461 |
4.04e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.18 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 897 EVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYER---KYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELED 973
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 974 MMQeLETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEdlalTDDQNQKLLKEKK 1053
Cdd:PRK03918 281 KVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1054 LLEERANDLSQTLAEEEEKAKHLAKLKAKheaTISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQ 1133
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGL---TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1134 AQLAK------------REEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKaekvrRDLSEELEA 1201
Cdd:PRK03918 433 KAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-----KELAEQLKE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1202 LKNEL--LDSLDTTAAQQELRSKREqELATLKKSLEeetvnhegvladmrhkhsqELNSINDQLENLRKAKTVLEKAKGT 1279
Cdd:PRK03918 508 LEEKLkkYNLEELEKKAEEYEKLKE-KLIKLKGEIK-------------------SLKKELEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1280 LEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAElkasaavK 1359
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE-------K 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1360 SASNMESQLTEAQQLLEEETRQKlgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAK 1439
Cdd:PRK03918 641 RLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
570 580
....*....|....*....|..
gi 386768643 1440 ELEEgKKRLNKDIEALERQVKE 1461
Cdd:PRK03918 719 ALER-VEELREKVKKYKALLKE 739
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1106-1507 |
1.12e-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: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1106 RSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAAR 1185
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1186 AKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEEtvnhegvladmrhkhsqELNSINDQLEN 1265
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS-----------------RIPEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1266 LrkaktvlekakgtlEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITN 1345
Cdd:TIGR02169 803 L--------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1346 QLEEAELKASAAVKSASNMESQLTEAQQLLEEetrqklgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQ 1425
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRE-------LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1426 EIKKKAEEDADLAKeLEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKN-- 1503
Cdd:TIGR02169 942 EDEEIPEEELSLED-VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREvf 1020
|
....*..
gi 386768643 1504 ---FDKI 1507
Cdd:TIGR02169 1021 meaFEAI 1027
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1027-1627 |
1.55e-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: 76.21 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1027 LDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKheatISELEERLHKDQQQRQESDR 1106
Cdd:TIGR04523 164 LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQ----ISELKKQNNQLKDNIEKKQQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1107 SKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEesatkataqkaqreLESQLAEIQEDLEAEKAARA 1186
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE--------------LEKQLNQLKSEISDLNNQKE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1187 KAEKvrRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHegvladmrhkhsqelNSINDQLENL 1266
Cdd:TIGR04523 306 QDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN---------------SEKQRELEEK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1267 RKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQ 1346
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1347 LEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQ- 1425
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEk 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1426 ---EIKKKAEEDADLAKELEEGKKRLNKD-----IEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLEL 1497
Cdd:TIGR04523 529 lesEKKEKESKISDLEDELNKDDFELKKEnlekeIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1498 EKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADK- 1576
Cdd:TIGR04523 609 EKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKe 688
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 386768643 1577 -NVHELEKAKRALESQ-LAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQF 1627
Cdd:TIGR04523 689 lSLHYKKYITRMIRIKdLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKF 741
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1254-1648 |
2.15e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.57 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1254 QELNSINDQLENLRKAKTVLEKAKGTLEA--ENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQE 1331
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1332 KCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEEtrqklglsskLRQIESEKEALQEQLEEDDEAKR 1411
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE----------LEELEEELEQLENELEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1412 NYERK--------LAEVTTQMQEIKKKAEEDADLAKELEE----GKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSE 1479
Cdd:COG4717 245 LKEARlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1480 LEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVlsvsrELDEAFDKIEDLENKRKT 1559
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV-----EDEEELRAALEQAEEYQE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1560 LQNELDDLANTQGTADKNVHELEKA--KRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFE-RDLLAKEE 1636
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElAELLQELE 479
|
410
....*....|..
gi 386768643 1637 GAEEKRRGLVKQ 1648
Cdd:COG4717 480 ELKAELRELAEE 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1303-1789 |
2.24e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.85 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1303 RRRKQAESQIAELQVKLAEIERArsELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEetrqk 1382
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREE----- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1383 lglsskLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIkkkAEEDADLAKELEEGkkrlNKDIEALERQVKEL 1462
Cdd:PRK02224 253 ------LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL---EEERDDLLAEAGLD----DADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1463 IAQN----DRLDKSKKKIQ---SELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETK 1535
Cdd:PRK02224 320 EDRDeelrDRLEECRVAAQahnEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1536 VLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEK----------------------------AKRA 1587
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieedreRVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1588 LESQLAELKAQNEELEDDLQLTEDAKlRLEVNMQALRSQFER--DLLA-KEEGAEEKR---RGLVKQLRDLETELDEERK 1661
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDleELIAeRRETIEEKReraEELRERAAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1662 QRTAAVASKKKLEGDLKEIETTMEmHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVL 1741
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLA-ELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKR 637
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 386768643 1742 QLTEDLasSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARI 1789
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 ... |
967-1837 |
4.82e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.01 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 967 RKQELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQ 1046
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1047 KLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEE-RLHKDQQQRQESDRSKRKIETEVADLKEQLNER 1125
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEkKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1126 RVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELE-SQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKN 1204
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEeEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1205 ELLDSLDTTAAQQELRSKREQELATLKKSLEEETVnhEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAEN 1284
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL--EILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1285 ADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNM 1364
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1365 ES----QLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIK-----KKAEEDA 1435
Cdd:pfam02463 553 VSatadEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKrakvvEGILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1436 DLAKELEEGKKRLNKDIEAleRQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAIS 1515
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKG--VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1516 EQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAEL 1595
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1596 KAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEG 1675
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1676 DLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARR 1755
Cdd:pfam02463 871 ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEK 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1756 AAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNE 1835
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
..
gi 386768643 1836 NG 1837
Cdd:pfam02463 1031 KG 1032
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
895-1467 |
7.41e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 74.31 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 895 LLEVTKQEEKLVQKE--DELKQVREKLDTLAKNTQEYERKYQQAlvekttlAEQLQAEIELCAEAEESRSRLMARKQELE 972
Cdd:PRK02224 189 LDQLKAQIEEKEEKDlhERLNGLESELAELDEEIERYEEQREQA-------RETRDEADEVLEEHEERREELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 973 DMMQELETRIEeeeervlalggEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYE---EDLALTDDQNQKLL 1049
Cdd:PRK02224 262 DLRETIAETER-----------EREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEarrEELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1050 KEKKLLEERANDLSQTLAEEEEKAKHLAKlKAKHEAtiSELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQV 1129
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAE-ELREEA--AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1130 DEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLA-----EIQEDLEAEKAARAKAEkvRRDLSEELEALKN 1204
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVETIEE--DRERVEELEAELE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1205 ELLDSLDTTAAQQElRSKREQELATLKKSLEEETVNHEGVLADmrhkHSQELNSINDQLENLRKAKTVLE-------KAK 1277
Cdd:PRK02224 486 DLEEEVEEVEERLE-RAEDLVEAEDRIERLEERREDLEELIAE----RRETIEEKRERAEELRERAAELEaeaeekrEAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1278 GTLEAENADLATELRSVNSSRQENDRRRKQAEsQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEE-----AEL 1352
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEkrerkREL 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1353 KAS---AAVKSASNMESQLTEAQQLLEEETR----QKLGLSSKLRQIESEKEALQEQLEEDD--EAKRNYERKLAEVTTQ 1423
Cdd:PRK02224 640 EAEfdeARIEEAREDKERAEEYLEQVEEKLDelreERDDLQAEIGAVENELEELEELRERREalENRVEALEALYDEAEE 719
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 386768643 1424 MQEIKkkaeedADLAKELEegkkrlNKDIEALER---QVKELIAQND 1467
Cdd:PRK02224 720 LESMY------GDLRAELR------QRNVETLERmlnETFDLVYQND 754
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1308-1540 |
1.06e-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: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1308 AESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSs 1387
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1388 klRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQND 1467
Cdd:COG4942 97 --AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768643 1468 RLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVS 1540
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1072-1488 |
2.13e-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: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1072 KAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEV-------ADLKEQLNERRVQVDEMQAQLAKREEELT 1144
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLdelsqelSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1145 QTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAekaarakaekvrrdLSEELEALKNELLDSldttaaqqelrskRE 1224
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK--------------LEEALNDLEARLSHS-------------RI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1225 QELATLKKSLEEETVNHEGVLADMrhkhSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRR 1304
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREI----EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1305 RKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLG 1384
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1385 LSSkLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEedadlakELEEGKKRLNKDIEALERQVKELIA 1464
Cdd:TIGR02169 950 ELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRA-------KLEEERKAILERIEEYEKKKREVFM 1021
|
410 420
....*....|....*....|....*
gi 386768643 1465 QN-DRLDKSKKKIQSELEDATIELE 1488
Cdd:TIGR02169 1022 EAfEAINENFNEIFAELSGGTGELI 1046
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1263-1761 |
3.75e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.72 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1263 LENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAEN 1342
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1343 ITNQLEEAELKASAAvksasNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNyerklaevtt 1422
Cdd:COG4717 128 LPLYQELEALEAELA-----ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1423 QMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKsKKKIQSELedATIELEAQRTKVLELEKKQK 1502
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL-EERLKEAR--LLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1503 NFDKILAEEKAISEQIAqerdTAEREAREKETKVLSVSRELDEAFDKIEDLENKRktLQNELDDLANTQGTADKNVHELE 1582
Cdd:COG4717 270 SLILTIAGVLFLVLGLL----ALLFLLLAREKASLGKEAEELQALPALEELEEEE--LEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1583 KAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQAlrsqfERDLLAKEEGAEEKRRgLVKQLRDLETELDEERKQ 1662
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED-----EEELRAALEQAEEYQE-LKEELEELEEQLEELLGE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1663 RTAAVA--SKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKeelQALSKEAERKVKALEAEV 1740
Cdd:COG4717 418 LEELLEalDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ---ELEELKAELRELAEEWAA 494
|
490 500
....*....|....*....|.
gi 386768643 1741 LQLTEDLAssERARRAAETER 1761
Cdd:COG4717 495 LKLALELL--EEAREEYREER 513
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
893-1667 |
7.47e-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: 71.23 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 893 KPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAE------------QLQAEIELCAEAEES 960
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpfserQIKNFHTLVIERQED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 961 RSRLMARK-QELEDMMQELETRIEEEEERVLALGG----EKKKLELNIQDLEEQLEEEEAARQKLQlEKVQLDAKIKKYE 1035
Cdd:TIGR00606 406 EAKTAAQLcADLQSKERLKQEQADEIRDEKKGLGRtielKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELRKAE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1036 EDLALTDDQNQKLLKEKKLLEERAN--DLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIET 1113
Cdd:TIGR00606 485 RELSKAEKNSLTETLKKEVKSLQNEkaDLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTS 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1114 EVAD------LKEQLNERRVQVDEMQAQLAKREEELTQTllrideeSATKATAQKAQRELESQLAEIQEDLEAEKAArak 1187
Cdd:TIGR00606 565 LLGYfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASL-------EQNKNHINNELESKEEQLSSYEDKLFDVCGS--- 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1188 aekvrRDLSEELEALKNELLDS---LDTTAAQQELRSKREQELATLKKS---LEEETVNHEGVLADMRHKHSQELNSIND 1261
Cdd:TIGR00606 635 -----QDEESDLERLKEEIEKSskqRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1262 QLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIER------ARSELQEKCTK 1335
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllgtimPEEESAKVCLT 789
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1336 LQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKlglssKLRQIESEKEALQEQLEEDDEAKRNYER 1415
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQH-----ELDTVVSKIELNRKLIQDQQEQIQHLKS 864
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1416 KLAEVTTQMQEIKKKAEEDADLAKELEEgkkrLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKV- 1494
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRRQQFEEQLVE----LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAq 940
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1495 LELEKKQKNFDKILAEEKAISEQIaqeRDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDD------LA 1568
Cdd:TIGR00606 941 DKVNDIKEKVKNIHGYMKDIENKI---QDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTqkiqerWL 1017
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1569 NTQGTADKNVHELEKAKRAL--------ESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQ---FERDLLAKE-E 1636
Cdd:TIGR00606 1018 QDNLTLRKRENELKEVEEELkqhlkemgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEikhFKKELREPQfR 1097
|
810 820 830
....*....|....*....|....*....|....
gi 386768643 1637 GAEEKRRGLVKQLRDLE---TELDEERKQRTAAV 1667
Cdd:TIGR00606 1098 DAEEKYREMMIVMRTTElvnKDLDIYYKTLDQAI 1131
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
887-1621 |
8.01e-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: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 887 RLYTKVKPLLEVTKQ-----EEKLVQKEDELKQVREKLDTLAKNTQEYE-------RKYQQALVEKTTLAEQLQAEIELC 954
Cdd:pfam05483 78 RLYSKLYKEAEKIKKwkvsiEAELKQKENKLQENRKIIEAQRKAIQELQfenekvsLKLEEEIQENKDLIKENNATRHLC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 955 AEAEESRSRLMARKQELEdmmqeleTRIEEEEERVLALGGEKKKLELNIQDLeeqleeeeaarqKLQLEKVQLDAKIKkY 1034
Cdd:pfam05483 158 NLLKETCARSAEKTKKYE-------YEREETRQVYMDLNNNIEKMILAFEEL------------RVQAENARLEMHFK-L 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1035 EEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETE 1114
Cdd:pfam05483 218 KEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1115 VADLKEQLnERRVQVdemQAQLAKREEELTQTLLRIDEESAT--------KATAQKAQRELESQLAEIQEDLEAEKAARA 1186
Cdd:pfam05483 298 LEDIKMSL-QRSMST---QKALEEDLQIATKTICQLTEEKEAqmeelnkaKAAHSFVVTEFEATTCSLEELLRTEQQRLE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1187 KAEKVRRDLSEELEALKNELLDsldttaaQQELRSKREQELATLKKSL-EEETVNHEgvladmrhkhSQELNSINDQLEN 1265
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEE-------MTKFKNNKEVELEELKKILaEDEKLLDE----------KKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1266 LRKAKTVLEKAKgtlEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITN 1345
Cdd:pfam05483 437 KEQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTL 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1346 QLEEAELKASAAVKSASNMESQLteaQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQ 1425
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQI---ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1426 EIKKKAEedaDLAKELEEGkkrlNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLEL-EKKQKNF 1504
Cdd:pfam05483 591 ILENKCN---NLKKQIENK----NKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIiDNYQKEI 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1505 DKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDdlaNTQGTADKNVHELEKA 1584
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERD---SELGLYKNKEQEQSSA 740
|
730 740 750
....*....|....*....|....*....|....*..
gi 386768643 1585 KRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQ 1621
Cdd:pfam05483 741 KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
895-1952 |
1.69e-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: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 895 LLEVTKQEEKLVQKEDELKQVREKLD-TLAKNTQEYERKYQQALVEKTTLAE----QLQAEIELCAEAEESRSRLMARKQ 969
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKfYLRQSVIDLQTKLQEMQMERDAMADirrrESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 970 ELEDMMQELETRIEEEEERVLALGG---EKKKLELNIQDLEEQLEEEEAARQKLQLEKV---------QLDAKIKKYEED 1037
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSHEGvlqEIRSILVDFEEASGKKIYEHDSMSTMHFRSLgsaiskilrELDTEISYLKGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1038 LALTDDQ-----NQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESD----RSK 1108
Cdd:pfam15921 240 IFPVEDQlealkSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmymRQL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1109 RKIETEVADLKEQLNERRV----QVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAA 1184
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRmyedKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1185 RAKAEKVRRDLSEELEALKNELLDsldttaaqqelRSKREQELATLKKSLEEETVNH-EGVLADMRHKHS--QELNSIND 1261
Cdd:pfam15921 400 NKRLWDRDTGNSITIDHLRRELDD-----------RNMEVQRLEALLKAMKSECQGQmERQMAAIQGKNEslEKVSSLTA 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1262 QLENlrkAKTVLEKAKGTLEAENADLATELRSVN---SSRQENDRRRKQAESQIAELQ----VKLAEIERARSElQEKCT 1334
Cdd:pfam15921 469 QLES---TKEMLRKVVEELTAKKMTLESSERTVSdltASLQEKERAIEATNAEITKLRsrvdLKLQELQHLKNE-GDHLR 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1335 KLQQEAENITNQLEEAElkasaavKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYE 1414
Cdd:pfam15921 545 NVQTECEALKLQMAEKD-------KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKD 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1415 RKLAEVTTQMQEIkkkaeeDADLAKELEEGKKRLnkdiealeRQVKELIAQNDRLDKSKKKIQSELEDATIELEA-QRTK 1493
Cdd:pfam15921 618 AKIRELEARVSDL------ELEKVKLVNAGSERL--------RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVlKRNF 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1494 VLELEKKQKNFDKILAEEKAISEQIAQERDTAeREAREKETKVLSVSRELDEafdKIEDLENKRKTLQNELDDLANTQGT 1573
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQLKSAQSELEQTRNTL-KSMEGSDGHAMKVAMGMQK---QITAKRGQIDALQSKIQFLEEAMTN 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1574 ADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRL-------EVNMQALRSQFE--RDLLAKEEgAEEKRRG 1644
Cdd:pfam15921 760 ANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLkekvanmEVALDKASLQFAecQDIIQRQE-QESVRLK 838
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1645 L-----VKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEM--HNKVKEDALKhakklqaqvKDALRDaeeaka 1717
Cdd:pfam15921 839 LqhtldVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFlsHHSRKTNALK---------EDPTRD------ 903
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1718 akeeLQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEiannankgSLMIDEKRRLEARIATLEEELE 1797
Cdd:pfam15921 904 ----LKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIES--------SLRSDICHSSSNSLQTEGSKSS 971
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1798 EEQSNSEVLLdrsRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNK----ELKAKLAE--IETAQRTKVKATIATLE 1871
Cdd:pfam15921 972 ETCSREPVLL---HAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKspvhSLLTSSAEgsIGSSSQYRSAKTIHSPD 1048
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1872 AKIANLEEQLENEGkerllqqKANRKMDKKIKELTMNIEDerrhvdqhkeqMDKLNSRIKLLKRNldeTEEELQKEKTQK 1951
Cdd:pfam15921 1049 SVKDSQSLPIETTG-------KTCRKLQNRLESLQTLVED-----------LQLKNQAMSSMIRN---QEKRIQKVKDQE 1107
|
.
gi 386768643 1952 R 1952
Cdd:pfam15921 1108 K 1108
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1112-1853 |
2.03e-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: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1112 ETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATA-------QKAQRELESQLAEIQEDLeaekaa 1184
Cdd:pfam12128 208 DDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAelrlshlHFGYKSDETLIASRQEER------ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1185 rakaekvrrdlsEELEALKNELLDSLDttAAQQELRSKREQELATLKKSLEEEtvNHEGVLADMRHKHSQElnsinDQLE 1264
Cdd:pfam12128 282 ------------QETSAELNQLLRTLD--DQWKEKRDELNGELSAADAAVAKD--RSELEALEDQHGAFLD-----ADIE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1265 NLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAElqvKLAEIERARSELQEKCTKLQQEAENIT 1344
Cdd:pfam12128 341 TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNR---DIAGIKDKLAKIREARDRQLAVAEDDL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1345 NQLEeAELKasaavksaSNMESQLTEAQQlleeetrQKLGLSSKLrqieSEKEALQEQLEEDDEAKRNYERKLAEVTTQM 1424
Cdd:pfam12128 418 QALE-SELR--------EQLEAGKLEFNE-------EEYRLKSRL----GELKLRLNQATATPELLLQLENFDERIERAR 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1425 QEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQndrldkskkkiQSELEDATIELEAQRTKVLELEKKQ--- 1501
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEER-----------QSALDELELQLFPQAGTLLHFLRKEapd 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1502 --KNFDKILAEEKAISEQIAQERDTAereAREKETKVLSVSRELDEAfdKIEDLENKRKTLQNELDDLANTQGTADKNVH 1579
Cdd:pfam12128 547 weQSIGKVISPELLHRTDLDPEVWDG---SVGGELNLYGVKLDLKRI--DVPEWAASEEELRERLDKAEEALQSAREKQA 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1580 ELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETEL--- 1656
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHqaw 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1657 -----DEERKQRTAAVASKKKLEGDLKeiettmemhnkVKEDALKHAKkLQAQVKDALRDAEEAKAAKEELQALSKEAER 1731
Cdd:pfam12128 702 leeqkEQKREARTEKQAYWQVVEGALD-----------AQLALLKAAI-AARRSGAKAELKALETWYKRDLASLGVDPDV 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1732 KVKaLEAEVLQLTEDLASSERARRAA-----------ETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQ 1800
Cdd:pfam12128 770 IAK-LKREIRTLERKIERIAVRRQEVlryfdwyqetwLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMER 848
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 1801 SNSEVLLDRS----RKAQLQIEQLTTelANEKSNSQKNENGRALLERQNKELKAKLA 1853
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 |
3.20e-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: 3.20e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 386768643 79 KRLVWVPHENQGFVAASIKREHGDEVEVELaETGKRVMILRDDI 122
Cdd:pfam02736 3 KKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1083-1563 |
4.00e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1083 HEATISELEERLHKDQQQRQ-ESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEeltqtllrideesatkatAQ 1161
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE------------------LE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1162 KAQRELESQLAEIQEDLEAEKAARAKAEKVRRdlSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNH 1241
Cdd:COG4717 102 EELEELEAELEELREELEKLEKLLQLLPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1242 EGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSV-NSSRQENDRRRKQAESQIAELQVKLA 1320
Cdd:COG4717 180 EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLeNELEAAALEERLKEARLLLLIAAALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1321 EIERARSELQEKCTKLqqeAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQ 1400
Cdd:COG4717 260 ALLGLGGSLLSLILTI---AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1401 EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAdLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSEL 1480
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQE-IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1481 EDATIELEAQRTKVLELEKKQKNfdkilAEEKAISEQIAQERdtAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTL 1560
Cdd:COG4717 416 GELEELLEALDEEELEEELEELE-----EELEELEEELEELR--EELAELEAELEQLEEDGELAELLQELEELKAELREL 488
|
...
gi 386768643 1561 QNE 1563
Cdd:COG4717 489 AEE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1699-1981 |
4.35e-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: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1699 KKLQAQVKDALRdaeeakaakeeLQALSKEA-ERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANkgsl 1777
Cdd:COG1196 203 EPLERQAEKAER-----------YRELKEELkELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA---- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1778 midEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIET 1857
Cdd:COG1196 268 ---ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1858 -------------AQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMD 1924
Cdd:COG1196 345 eleeaeeeleeaeAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 1925 KLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1981
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1137-1905 |
5.59e-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: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1137 AKREEELTQTLLRIDEESATK---------ATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELl 1207
Cdd:TIGR00618 125 KSETEEVIHDLLKLDYKTFTRvvllpqgefAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRS- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1208 dSLDTTAAQQelrskREQELATLKKSLEEETVNHEGVLADMRHKHSQElnsinDQLENLRKAKTVLEKAKGTLEAENADL 1287
Cdd:TIGR00618 204 -QLLTLCTPC-----MPDTYHERKQVLEKELKHLREALQQTQQSHAYL-----TQKREAQEEQLKKQQLLKQLRARIEEL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1288 ATELRSVNSSRQENDRRRKQAesQIAELQVKLAEIERAR----SELQEKCTKLQQEAENITNQLE-----EAELKASAAV 1358
Cdd:TIGR00618 273 RAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAqrihTELQSKMRSRAKLLMKRAAHVKqqssiEEQRRLLQTL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1359 KSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLA 1438
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1439 KELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSEledatieleaqrtkvLELEKKQKNFDKILAEEKAISEQI 1518
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER---------------EQQLQTKEQIHLQETRKKAVVLAR 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1519 AQERDTAEREAREKEtkvlsvsRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEkakrALESQLAELKAQ 1598
Cdd:TIGR00618 496 LLELQEEPCPLCGSC-------IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT----SERKQRASLKEQ 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1599 NEELEDDLQLTEDAKLRLEVNMQALRSqferdllakeegaeekrrgLVKQLRDLETELDEERKQ-RTAAVASKKKLEGDL 1677
Cdd:TIGR00618 565 MQEIQQSFSILTQCDNRSKEDIPNLQN-------------------ITVRLQDLTEKLSEAEDMlACEQHALLRKLQPEQ 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1678 KEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEA-ERKVKALEAEVLQLT---EDLASSERA 1753
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASrQLALQKMQSEKEQLTywkEMLAQCQTL 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1754 RRAAETERDELAEEIANNANKGSLMIDE-------------KRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQieQL 1820
Cdd:TIGR00618 706 LRELETHIEEYDREFNEIENASSSLGSDlaaredalnqslkELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS--HL 783
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1821 TTELANEKSNSQKNENGRALLERQNKE-----LKAKLAEIETAQ--RTKVKATIATLEAKIANLEEQLENEGkERLLQQK 1893
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQeipsdEDILNLQCETLVqeEEQFLSRLEEKSATLGEITHQLLKYE-ECSKQLA 862
|
810
....*....|..
gi 386768643 1894 ANRKMDKKIKEL 1905
Cdd:TIGR00618 863 QLTQEQAKIIQL 874
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1148-1920 |
7.15e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.06 E-value: 7.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1148 LRIDEESATkaTAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKnELLDSLDTTAAQQELRSKREQEL 1227
Cdd:PRK04863 281 RRVHLEEAL--ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAS-DHLNLVQTALRQQEKIERYQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1228 ATLKKSLEEETV----NHEGVLADMRHKHS--QELNSINDQLENL--------------RKAKTVLEKAKGTLEAenADL 1287
Cdd:PRK04863 358 EELEERLEEQNEvveeADEQQEENEARAEAaeEEVDELKSQLADYqqaldvqqtraiqyQQAVQALERAKQLCGL--PDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1288 ATElrsvnssrqendrrrkQAESQIAELQVKLAEIERARSELQEKCtklqQEAENITNQLEEA---------ELKASAAV 1358
Cdd:PRK04863 436 TAD----------------NAEDWLEEFQAKEQEATEELLSLEQKL----SVAQAAHSQFEQAyqlvrkiagEVSRSEAW 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1359 KSASNMESQLTEAQQLLE--EETRQKLG-LSSKLRQIESEKEALQE-----QLEEDDEAkrNYERKLAEVTTQMQEIKKK 1430
Cdd:PRK04863 496 DVARELLRRLREQRHLAEqlQQLRMRLSeLEQRLRQQQRAERLLAEfckrlGKNLDDED--ELEQLQEELEARLESLSES 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1431 AEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATiELEAQRTKVLELEKK-QKNFDKILA 1509
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ-DVTEYMQQLLERERElTVERDELAA 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1510 EEKAISEQIA--QERDTAE--REAREKET--KVLsvsreLDEAFDKIE---------------------DLENKRKTLQN 1562
Cdd:PRK04863 653 RKQALDEEIErlSQPGGSEdpRLNALAERfgGVL-----LSEIYDDVSledapyfsalygparhaivvpDLSDAAEQLAG 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1563 E---LDDLANTQGTADK------NVHELEKA----------------------KRALESQLAELKAQNEELEddlqlTED 1611
Cdd:PRK04863 728 LedcPEDLYLIEGDPDSfddsvfSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAEREELA-----ERY 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1612 AKLRLEVN-MQALRSQFERDL-----LAKEEGAEEKRRGLVKQLRDLETEL----DEERKQRTAAVASKKKLEGdLKEIE 1681
Cdd:PRK04863 803 ATLSFDVQkLQRLHQAFSRFIgshlaVAFEADPEAELRQLNRRRVELERALadheSQEQQQRSQLEQAKEGLSA-LNRLL 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1682 TTMemhNKVKEDAL-KHAKKLQAQVKDALRDAEEAKAAKEELQALSKEA------ERKVKALEAEVLQLTEDLA------ 1748
Cdd:PRK04863 882 PRL---NLLADETLaDRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVsvlqsdPEQFEQLKQDYQQAQQTQRdakqqa 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1749 ---SSERARRAA---ETERDELAEEIANN-ANKGSLMIDEKRRLEARIATLEEELEEEQsNSEVL--LDRSRKAQlqiEQ 1819
Cdd:PRK04863 959 falTEVVQRRAHfsyEDAAEMLAKNSDLNeKLRQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLasLKSSYDAK---RQ 1034
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1820 LTTELANEKSN--SQKNENGRALLERQNKELKAKLaeieTAQRTKVKAtiatLEAKIANLEEQLENegkerllqqkanrk 1897
Cdd:PRK04863 1035 MLQELKQELQDlgVPADSGAEERARARRDELHARL----SANRSRRNQ----LEKQLTFCEAEMDN-------------- 1092
|
890 900
....*....|....*....|...
gi 386768643 1898 MDKKIKELTMNIEDERRHVDQHK 1920
Cdd:PRK04863 1093 LTKKLRKLERDYHEMREQVVNAK 1115
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1525-1740 |
1.46e-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: 65.56 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1525 AEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELED 1604
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1605 DLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLV----------KQLRDLETELDEERKQRTAAVASKKKLE 1674
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768643 1675 GDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEV 1740
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1114-1357 |
1.53e-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: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1114 EVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAArakaekvRR 1193
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-------IA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1194 DLSEELEALKNELLDSLDttAAQQELRSKREQELATLKKSLEeetvnhegvLADMRHKHSQELNSINDQLENLRKAKTVL 1273
Cdd:COG4942 94 ELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLD---------AVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1274 EKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELK 1353
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....
gi 386768643 1354 ASAA 1357
Cdd:COG4942 243 TPAA 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1074-1786 |
1.78e-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: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1074 KHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIEtevadlKEQLNERRVQVdemqaqlaKREEELTQTLLRIDEE 1153
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQ------ELQFENEKVSL--------KLEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1154 SATKATAQKaqreLESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALK---NELLDSLDTTAAQQELRSKREQE-LAT 1229
Cdd:pfam05483 151 NATRHLCNL----LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMIlafEELRVQAENARLEMHFKLKEDHEkIQH 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1230 LKKSLEEETVNHEGVLADMRHKHSQELNSINDQ---LENLRKAKTVLEKaKGTLEAENadlatelrsVNSSRQENDRRRK 1306
Cdd:pfam05483 227 LEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEE-KTKLQDEN---------LKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1307 QAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLS 1386
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1387 SKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAD---LAKELEEGKKRLNKDIEALERQVKELI 1463
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekIAEELKGKEQELIFLLQAREKEIHDLE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1464 AQNDRLDKSKKKIQSELEDATIELEAQRTKVLELekkQKNFDKILAEEKaiseQIAQERDTAEREAREKETKVLSVSREL 1543
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEL---TAHCDKLLLENK----ELTQEASDMTLELKKHQEDIINCKKQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1544 DEAFDKIEDLENKRKTLQNELDDLANT-QGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQA 1622
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1623 LRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELD-EERKQRTAAVASKKKLEGDLKEI--ETTMEMHNKVKEDAlKHAK 1699
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELElASAKQKFEEIIDNYQKEIEDKKIseEKLLEEVEKAKAIA-DEAV 688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1700 KLQAQVKdaLRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMI 1779
Cdd:pfam05483 689 KLQKEID--KRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEK 766
|
....*..
gi 386768643 1780 DEKRRLE 1786
Cdd:pfam05483 767 EEKEKLK 773
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1138-1980 |
1.87e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.61 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1138 KREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQ 1217
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1218 ELRS------KREQELATLKKSLEEETVN----HEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADL 1287
Cdd:TIGR00606 266 KLDNeikalkSRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1288 ATEL--RSVNSSRQENDRRRKQAESQIAELQVKLAEIER-ARSELQEKctklqqeaENITNQLEEAELKASAAVKSASNM 1364
Cdd:TIGR00606 346 LVEQgrLQLQADRHQEHIRARDSLIQSLATRLELDGFERgPFSERQIK--------NFHTLVIERQEDEAKTAAQLCADL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1365 ESQLTEAQQLLEEETRQKLGLSsklRQIESEKEALQEQLEEddeaKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEG 1444
Cdd:TIGR00606 418 QSKERLKQEQADEIRDEKKGLG---RTIELKKEILEKKQEE----LKFVIKELQQLEGSSDRILELDQELRKAERELSKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1445 KKrlNKDIEALERQVKELIAQNDRLDKSKKKIQSELEdatieleaqrtkvlelekkQKNFDKilaEEKAISEQIAQERDT 1524
Cdd:TIGR00606 491 EK--NSLTETLKKEVKSLQNEKADLDRKLRKLDQEME-------------------QLNHHT---TTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1525 AEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELED 1604
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1605 dlqltedaKLRLEVNMQALRSQFERdllakeegaeekrrglvkqlrdLETELDEERKQRTAAVASKKKLEGDLKEIETTM 1684
Cdd:TIGR00606 627 --------KLFDVCGSQDEESDLER----------------------LKEEIEKSSKQRAMLAGATAVYSQFITQLTDEN 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1685 EMHNKVKEDALKHAKKLQAQVKDalrdaeeakaakeeLQALSKEAERKVKALEAEVLQLtedlasserarraaETERDEL 1764
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEFISD--------------LQSKLRLAPDKLKSTESELKKK--------------EKRRDEM 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1765 AEEIANNANKGSLMIDEKRRLEARIatleeeleeeqsnsevlldrsrkaqlqiEQLTTELANEKSNSQKNENgraLLERQ 1844
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKL----------------------------QKVNRDIQRLKNDIEEQET---LLGTI 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1845 NKELK-AKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDK--KIKELTMNIEDERRHVDQHKE 1921
Cdd:TIGR00606 778 MPEEEsAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKqhELDTVVSKIELNRKLIQDQQE 857
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 386768643 1922 QMDKLNSRIKllkrnldeteeELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLR 1980
Cdd:TIGR00606 858 QIQHLKSKTN-----------ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK 905
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1595-1985 |
2.72e-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: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1595 LKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERdlLAKEEGAEEKRRGLVKQLRDLE-----TELDEERKQRTAAVAS 1669
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKS--LERQAEKAERYKELKAELRELElallvLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1670 KKKLEGDLKEIETTMemhnkvkedalkhaKKLQAQVkDALRDAEEAkaakeeLQALSKEAERKVKALEAEVLQLTEDLAS 1749
Cdd:TIGR02168 248 LKEAEEELEELTAEL--------------QELEEKL-EELRLEVSE------LEEEIEELQKELYALANEISRLEQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1750 SERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATleeeleeeqsnsevlldrsrkAQLQIEQLTTELANEKS 1829
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE---------------------LKEELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1830 NSQKNENGRALLERQNKELKAKLAEIEtAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKanRKMDKKIKELTMNI 1909
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLE-LQIASLNNEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAEL 442
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768643 1910 EDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRE---CEDMIESQEAMNREINSLKTKLRRTGGI 1985
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENLEGFSEGVKALLKNQSGLSGI 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1061-1495 |
4.29e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1061 DLSQTLAEEEEKAKHLAKLKAKheatISELEERLHKDQQQRQESDRSKRKIET---------EVADLKEQLNERRVQVDE 1131
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEKllqllplyqELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1132 MQAQLAKREEeltqtllrideesatkatAQKAQRELESQLAEIQEDLEAEKAARAKAEKVR-RDLSEELEALKNELLDSL 1210
Cdd:COG4717 151 LEERLEELRE------------------LEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1211 DTTAAQQELRSKREQELATLKKSLEEETVNHE-----------GVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGT 1279
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1280 LEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAvk 1359
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ-- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1360 sasNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEvttqmQEIKKKAEEDADLAK 1439
Cdd:COG4717 371 ---EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELE 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 386768643 1440 ELEEGKKRLNKDIEALERQVKELiAQNDRLDKSKKKIQSELEDATIELEAQRTKVL 1495
Cdd:COG4717 443 ELEEELEELREELAELEAELEQL-EEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1408-1672 |
4.92e-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: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1408 EAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIEL 1487
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1488 EAQRtkvlelekkqknfdkilaeekaisEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL 1567
Cdd:COG4942 100 EAQK------------------------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1568 ANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQferdllAKEEGAEEKRrgLVK 1647
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE------LAELQQEAEE--LEA 227
|
250 260
....*....|....*....|....*
gi 386768643 1648 QLRDLETELDEERKQRTAAVASKKK 1672
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1496-1948 |
6.86e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1496 ELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLAntqgtAD 1575
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----KL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1576 KNVHELEKAKRALESQLAELKAQNEELEDDLQL---TEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDL 1652
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1653 ETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEdaLKHAK----------KLQAQVKDALRDAEEAKAAKEEL 1722
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER--LKEARlllliaaallALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1723 QALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEI-ANNANKGSLMIDEKRRLEARIATLEEELEEEQS 1801
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALgLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1802 NSEVLLDRSRKAQLQIEQLTTE-----LANEKSNSQKNENGRALLERQ-NKELKAKLAEIETAQRTKVKATIATLEAKIA 1875
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEeelraALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768643 1876 NLEEQLENEGKERLLQQKANRKMDKkiKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEK 1948
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1550-1981 |
7.23e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1550 IEDLENKRKTLQNELDdlANTQGTADKNVHElekAKRALESQLAELKAQNEELEDD----LQLTEDAKLRLEVNMQALRS 1625
Cdd:PRK02224 178 VERVLSDQRGSLDQLK--AQIEEKEEKDLHE---RLNGLESELAELDEEIERYEEQreqaRETRDEADEVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1626 QFE-----RDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKK 1700
Cdd:PRK02224 253 LETleaeiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1701 LQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEvlqltedLASSERARRAAETERDELAEEIannankgslmid 1780
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE-------LEEAREAVEDRREEIEELEEEI------------ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1781 ekRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNEngrALLERQN-KELKAKLAEIETAQ 1859
Cdd:PRK02224 394 --EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE---ALLEAGKcPECGQPVEGSPHVE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1860 RTKVK-ATIATLEAKIANLEEQLEnEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLD 1938
Cdd:PRK02224 469 TIEEDrERVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 386768643 1939 ETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1981
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1311-1487 |
7.46e-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: 61.48 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1311 QIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLeEETRQKLGLSSKLR 1390
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1391 QIesekEALQEQLEEDDEAKRNYERKLAEVttqMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLD 1470
Cdd:COG1579 90 EY----EALQKEIESLKRRISDLEDEILEL---MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|....*..
gi 386768643 1471 KSKKKIQSELEDATIEL 1487
Cdd:COG1579 163 AEREELAAKIPPELLAL 179
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1307-1533 |
7.98e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.93 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1307 QAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEeTRQKLGLS 1386
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE-RREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1387 SKLRQIESEKEALQEQLEEDDEakrnyerkLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQN 1466
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSES--------FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 1467 DRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKE 1533
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1098-1355 |
1.06e-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: 62.86 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1098 QQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQED 1177
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1178 LEAEkaarakaekvRRDLSEELEAL-KNELLDSLDTTAAQQELrskreqelatlkksleEETVNHEGVLADMRHKHSQEL 1256
Cdd:COG4942 99 LEAQ----------KEELAELLRALyRLGRQPPLALLLSPEDF----------------LDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1257 NSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKL 1336
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|....*....
gi 386768643 1337 QQEAENITNQLEEAELKAS 1355
Cdd:COG4942 233 EAEAAAAAERTPAAGFAAL 251
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1279-1521 |
1.11e-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: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1279 TLEAENADLATEL----------RSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKctklqqeaenitNQLE 1348
Cdd:COG3206 141 SYTSPDPELAAAVanalaeayleQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1349 EAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQE--QLEEDDEAKRNYERKLAEVTT---- 1422
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSArytp 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1423 ---QMQEIKKK-AEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLdKSKKKIQSELEDATIELEAqrtkvlELE 1498
Cdd:COG3206 289 nhpDVIALRAQiAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL-EARLAELPELEAELRRLER------EVE 361
|
250 260
....*....|....*....|...
gi 386768643 1499 KKQKNFDKILAEEKAISEQIAQE 1521
Cdd:COG3206 362 VARELYESLLQRLEEARLAEALT 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1366-1576 |
1.16e-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: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1366 SQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQM----QEIKKKAEEDADLAKEL 1441
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1442 EEGKKRLNKDIEALERQ-----VKELIAQND--RLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAI 1514
Cdd:COG4942 100 EAQKEELAELLRALYRLgrqppLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768643 1515 SEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADK 1576
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1070-1422 |
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 386768643 1070 EEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLR 1149
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1150 IDEESATKATAQKAQRELE-------SQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLdsldttAAQQELRSk 1222
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEediktltQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ------QTEEELRS- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1223 REQELATLKKSLEE---------ETVNHEGVLADMRHKHSQELNSIndqLENLRKAKTVLEKAKGTLEAenadLATELRS 1293
Cdd:pfam07888 190 LSKEFQELRNSLAQrdtqvlqlqDTITTLTQKLTTAHRKEAENEAL---LEELRSLQERLNASERKVEG----LGEELSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1294 VNSSRQENDRRRKQAESQIAELQVKLAEIERA----RSELQEKCTKLQQEAENITNQLEE--AELKASAAVKSASNMESQ 1367
Cdd:pfam07888 263 MAAQRDRTQAELHQARLQAAQLTLQLADASLAlregRARWAQERETLQQSAEADKDRIEKlsAELQRLEERLQEERMERE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1368 LTEAQ---------QLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTT 1422
Cdd:pfam07888 343 KLEVElgrekdcnrVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
936-1659 |
1.28e-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: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 936 ALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQELETRIeeeeerVLALGGEKKKLELNIQDLEEQLEEEEA 1015
Cdd:pfam12128 256 AELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK------RDELNGELSAADAAVAKDRSELEALED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1016 ---ARQKLQLEKVQLDA--------KIKKYEEDL-ALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKH 1083
Cdd:pfam12128 330 qhgAFLDADIETAAADQeqlpswqsELENLEERLkALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1084 EATISELEERLhkDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQA------QLAKREEELTQTLLRIDEESATK 1157
Cdd:pfam12128 410 LAVAEDDLQAL--ESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAtpelllQLENFDERIERAREEQEAANAEV 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1158 ATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKR----EQELAT-LKK 1232
Cdd:pfam12128 488 ERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKvispELLHRTdLDP 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1233 SLEEETVNHEGVLADMR-HKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNssrqendrrrKQAESQ 1311
Cdd:pfam12128 568 EVWDGSVGGELNLYGVKlDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQAN----------GELEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1312 IAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKL-------- 1383
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKreartekq 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1384 --------GLSSKLRQIESEKEALQEQLE-EDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEA 1454
Cdd:pfam12128 718 aywqvvegALDAQLALLKAAIAARRSGAKaELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1455 LERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQ----RTKVLELEKKQKNFDKILAEekaISEQIAQERDTAEREAR 1530
Cdd:pfam12128 798 FDWYQETWLQRRPRLATQLSNIERAISELQQQLARLiadtKLRRAKLEMERKASEKQQVR---LSENLRGLRCEMSKLAT 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1531 EKE-TKVLSVSRELDEAFDKIEDLENKRKTL----QNELDDLANTqgTADKNVHELEKAKRALESQLAELKAQNEELEDD 1605
Cdd:pfam12128 875 LKEdANSEQAQGSIGERLAQLEDLKLKRDYLsesvKKYVEHFKNV--IADHSGSGLAETWESLREEDHYQNDKGIRLLDY 952
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1606 LQ----LTEDAKLRLEVNMQALRSQ---FERDLLAKEEGAEEKRRGLVKQLRDLETELDEE 1659
Cdd:pfam12128 953 RKlvpyLEQWFDVRVPQSIMVLREQvsiLGVDLTEFYDVLADFDRRIASFSRELQREVGEE 1013
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1203-1561 |
2.61e-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: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1203 KNELLDSLDTTAAQQELRSKREQELATLKksLEEETVNHEgvladmRHKHSQELNSiNDQLENLRKAKTVLEKAKGTLEA 1282
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKFEK--MEQERLRQE------KEEKAREVER-RRKLEEAEKARQAEMDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1283 ENADLATEL-RSVNSSRQENDRRRKQA--ESQIAELQVKLAEIERARSELQEKCTKLQQE---AENITNQLEEAELKASA 1356
Cdd:pfam17380 338 EQERMAMEReRELERIRQEERKRELERirQEEIAMEISRMRELERLQMERQQKNERVRQEleaARKVKILEEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1357 AVKSASNMESQLTEAQQL----LEEETRQKLglsSKLRQIESEKEALQEQLEEDDEAKRnyeRKLAEvttqmqeiKKKAE 1432
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQRevrrLEEERAREM---ERVRLEEQERQQQVERLRQQEEERK---RKKLE--------LEKEK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1433 EDADLAKelEEGKKRLNKDIEALERQVKEliaqndrlDKSKKKI-QSELED--ATIELEAQRTKVLELEKKQKNFDkila 1509
Cdd:pfam17380 484 RDRKRAE--EQRRKILEKELEERKQAMIE--------EERKRKLlEKEMEErqKAIYEEERRREAEEERRKQQEME---- 549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 386768643 1510 EEKAISEQIaqerdtaeREAREKETKVLSVSRElDEAFDKIEDLENKRKTLQ 1561
Cdd:pfam17380 550 ERRRIQEQM--------RKATEERSRLEAMERE-REMMRQIVESEKARAEYE 592
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1154-1362 |
2.63e-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: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1154 SATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKS 1233
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1234 ---LEEETVNHEGVLADM--------RHKHSQELNSINDQLENLRKAK-------------TVLEKAKGTLEAENADLAT 1289
Cdd:COG4942 92 iaeLRAELEAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768643 1290 ELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSAS 1362
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1254-1739 |
3.45e-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: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1254 QELNSINDQLEN-LRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKL-AEIERARSELQE 1331
Cdd:pfam05557 5 IESKARLSQLQNeKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALrEQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1332 KCTKLQQEAENITNQLEEAELKasaavksaSNMESQLTEAQQLLEeetRQKLGLSSKlrqiESEKEALQEQLEEDDEAKR 1411
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVI--------SCLKNELSELRRQIQ---RAELELQST----NSELEELQERLDLLKAKAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1412 NYERKLAEVTTQMQEIKKKAEEDADLAKELE--EGKKRLNKDIEA-------LERQVKELIAQNDRLDKSK--------- 1473
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKELEFEIQsqEQDSEIVKNSKSelaripeLEKELERLREHNKHLNENIenklllkee 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1474 -----------KKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQ----------ERDTAEREAREK 1532
Cdd:pfam05557 230 vedlkrklereEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQlqqreivlkeENSSLTSSARQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1533 ETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL---------------------------ANTQGTADKNVHELEKAK 1585
Cdd:pfam05557 310 EKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLqrrvllltkerdgyrailesydkeltmSNYSPQLLERIEEAEDMT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1586 RALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQferDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRta 1665
Cdd:pfam05557 390 QKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQ---ESLADPSYSKEEVDSLRRKLETLELERQRLREQK-- 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1666 avaskkklegdlKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAE 1739
Cdd:pfam05557 465 ------------NELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDD 526
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
865-1606 |
6.80e-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: 61.14 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 865 NAIRIIQRNCAAYLKLRNWQWWRLYTKVKPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVE-KTTL 943
Cdd:TIGR00618 145 RVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHErKQVL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 944 AEQLQAEIELCAEAEESRSRLmARKQELEDMMQELETRIEEEEERVLALGGEKKKLE-----LNIQDLEEQLEEEEAARQ 1018
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEetqerINRARKAAPLAAHIKAVT 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1019 KLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQ 1098
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1099 QQRQesdrskrkIETevadLKEQLNERRVQVDEMQAQLAKRE-EELTQTLLRIDEESAtKATAQKAQRELESQLAEIQED 1177
Cdd:TIGR00618 384 LQQQ--------KTT----LTQKLQSLCKELDILQREQATIDtRTSAFRDLQGQLAHA-KKQQELQQRYAELCAAAITCT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1178 LEAEKAARAKAEKVRRDLSEELEALKNeLLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADM--------- 1248
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQT-KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrr 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1249 -------RHKHSQELNSINDQLENLRKAKTVLeKAKGTLEAENADLATELRsvNSSRQENDRRRKQAESQIAELQVKLAE 1321
Cdd:TIGR00618 530 mqrgeqtYAQLETSEEDVYHQLTSERKQRASL-KEQMQEIQQSFSILTQCD--NRSKEDIPNLQNITVRLQDLTEKLSEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1322 IERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTeaqqLLEEETRQKLGLSSKLRQIESEKEALQE 1401
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT----LTQERVREHALSIRVLPKELLASRQLAL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1402 QLEEDDEAKRNYERK-LAEVTTQMQEIKKKAEEDADLAKELEEG----KKRLNKDIEALERQVKELIAQNDRLDKSKKKI 1476
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEmLAQCQTLLRELETHIEEYDREFNEIENAssslGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1477 QSELEDATIELEAQRTKVLELEKKQKNFDKILAEE----KAISEQIAQERDTAEREareketkvLSVSRELdeafdkied 1552
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDthllKTLEAEIGQEIPSDEDI--------LNLQCET--------- 825
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1553 LENKRKTLQNELDDLANTQGTADKNVHELEKAKRALEsQLAELKAQNEELEDDL 1606
Cdd:TIGR00618 826 LVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA-QLTQEQAKIIQLSDKL 878
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1375-1976 |
6.96e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.28 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1375 LEEETRQKLG-LSSKLRQIESEKEALQEQLEEDDEAkrnyERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIE 1453
Cdd:pfam05483 97 IEAELKQKENkLQENRKIIEAQRKAIQELQFENEKV----SLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1454 ALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRtkvLELEKKQK-NFDKILAEEKAISEQIAQERDTAER---EA 1529
Cdd:pfam05483 173 KYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENAR---LEMHFKLKeDHEKIQHLEEEYKKEINDKEKQVSLlliQI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1530 REKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQgtaDKNVHELEKAKRALESQLAELKAqneeLEDDLQLT 1609
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKK---DHLTKELEDIKMSLQRSMSTQKA----LEEDLQIA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1610 EDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNK 1689
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1690 vKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEV----LQLTEDLASSERARRAAETERDELA 1765
Cdd:pfam05483 403 -KEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIhdleIQLTAIKTSEEHYLKEVEDLKTELE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1766 EEIANN----ANKGSLMIDEKRRLEAriatLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALL 1841
Cdd:pfam05483 482 KEKLKNieltAHCDKLLLENKELTQE----ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1842 ERQNKELKAKLAEIETAQRT------KVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKEltmniedERRH 1915
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSieyevlKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA-------ENKQ 630
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1916 VDQHKEQMDKLNSRIKLLKRNLDETEEelqkektqkrKYQRECEDMIESQEAMNREINSLK 1976
Cdd:pfam05483 631 LNAYEIKVNKLELELASAKQKFEEIID----------NYQKEIEDKKISEEKLLEEVEKAK 681
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
820-1449 |
7.96e-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: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 820 FFRAGVLahleEERDF--KISDLIVNFQAFCRgflARRNYQKRLQQLNAIRIIQRNCAAYLKLRN-----------WQWW 886
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARErlaeleylraaLRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 887 RLYTKVKpLL--EVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQA-LVEKTTLAEQLQAEIELCAEAEESRSR 963
Cdd:COG4913 285 FAQRRLE-LLeaELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 964 LMAR----KQELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLA 1039
Cdd:COG4913 364 LEALlaalGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1040 LTDDQNQKLLKEKKLLEERANDLSQTLAEEE------EKA------------KHLAK-------LKAKHEATISELEERL 1094
Cdd:COG4913 444 ALRDALAEALGLDEAELPFVGELIEVRPEEErwrgaiERVlggfaltllvppEHYAAalrwvnrLHLRGRLVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1095 HKDQQQRQESDRSKRKIETEVAD----LKEQLNER--RVQVDEmQAQLAKREEELTQTLL--------------RIDEES 1154
Cdd:COG4913 524 PDPERPRLDPDSLAGKLDFKPHPfrawLEAELGRRfdYVCVDS-PEELRRHPRAITRAGQvkgngtrhekddrrRIRSRY 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1155 ATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEA---LKNELLDSLDTTAAQQELRSKrEQELATLK 1231
Cdd:COG4913 603 VLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrLAEYSWDEIDVASAEREIAEL-EAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1232 KSleeetvnhegvladmrhkhSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQ 1311
Cdd:COG4913 682 AS-------------------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1312 IAELQVKLAEiERARSELQEKctKLQQEAENITNQLEEAELKASAAvksASNMESQLTEAQQLLEEETRqklGLSSKLRQ 1391
Cdd:COG4913 743 ARLELRALLE-ERFAAALGDA--VERELRENLEERIDALRARLNRA---EEELERAMRAFNREWPAETA---DLDADLES 813
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 386768643 1392 IEsEKEALQEQLEEDDEAKrnYERKLAEVTTQmQEIKKKAEEDADLAKELEEGKKRLN 1449
Cdd:COG4913 814 LP-EYLALLDRLEEDGLPE--YEERFKELLNE-NSIEFVADLLSKLRRAIREIKERID 867
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1486-1957 |
1.24e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1486 ELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQerdtAEREAREKETKVLSVSRELDeafdkIEDLENKRKTLQNELD 1565
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEE----LEAELEELREELEKLEKLLQ-----LLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1566 DlantqgtadknvhelekakraLESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEkrrgL 1645
Cdd:COG4717 143 E---------------------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----L 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1646 VKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEdalkhakklqaqvKDALRDAEEAKAAKEELQAL 1725
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER-------------LKEARLLLLIAAALLALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1726 SKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLmidEKRRLEARIATLEEELEEEQSNSEV 1805
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL---EEEELEELLAALGLPPDLSPEELLE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1806 LLDRSRKAQLQIEQLtTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKVKatiatLEAKIANLEEQLENEG 1885
Cdd:COG4717 342 LLDRIEELQELLREA-EELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE-----LKEELEELEEQLEELL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768643 1886 KERLLQQKANRK--MDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRN--LDETEEELQKEKTQKRKYQRE 1957
Cdd:COG4717 416 GELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEE 491
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1287-1889 |
1.47e-08 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 60.48 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1287 LATELRSVNSSRQeNDRRRKQAESQIAELQVKLaEIERARSELQEKCTKLqqEAENITNQLEEA---------ELKASAA 1357
Cdd:COG5022 795 LFIKLQPLLSLLG-SRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSL--KAEVLIQKFGRSlkakkrfslLKKETIY 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1358 VKSASNMESQLTEAQQLLEE-ETRQKLGLSS------------------------KLRQIESEKEALQE-QLEEDDEAKR 1411
Cdd:COG5022 871 LQSAQRVELAERQLQELKIDvKSISSLKLVNleleseiielkkslssdlienlefKTELIARLKKLLNNiDLEEGPSIEY 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1412 NYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELiaqndrldKSKKKIQSELEDATIELEAQR 1491
Cdd:COG5022 951 VKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL--------AELSKQYGALQESTKQLKELP 1022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1492 TKVLELEKKQKNFDKILAEEKAISEQIAQERD-TAEREAREKETKVLSVSRELDEAFDK----IEDLENKRKTLQNELDD 1566
Cdd:COG5022 1023 VEVAELQSASKIISSESTELSILKPLQKLKGLlLLENNQLQARYKALKLRRENSLLDDKqlyqLESTENLLKTINVKDLE 1102
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1567 LANTQGTADKNVhelEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFerDLLAKEEGAEEKRRGLV 1646
Cdd:COG5022 1103 VTNRNLVKPANV---LQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLF--WEANLEALPSPPPFAAL 1177
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1647 KQLRDLETELDEERKqrTAAVASKKKLEGDLKEIETtmemhnKVKEDALKhakklQAQVKDALRDAEEAKAAKEELQALS 1726
Cdd:COG5022 1178 SEKRLYQSALYDEKS--KLSSSEVNDLKNELIALFS------KIFSGWPR-----GDKLKKLISEGWVPTEYSTSLKGFN 1244
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1727 KEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIAN-----NANKGSLMIDEKRRLEARIATLEEELEEEQS 1801
Cdd:COG5022 1245 NLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSllqyiNVGLFNALRTKASSLRWKSATEVNYNSEELD 1324
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1802 NSEVLLDRSRkAQLQIEQL-----TTELANEKSNSQKNENG--RAL--LERQNKELKAKLAEIETAQRTKVKATIatlEA 1872
Cdd:COG5022 1325 DWCREFEISD-VDEELEELiqavkVLQLLKDDLNKLDELLDacYSLnpAEIQNLKSRYDPADKENNLPKEILKKI---EA 1400
|
650
....*....|....*..
gi 386768643 1873 KIANLEEQLENEGKERL 1889
Cdd:COG5022 1401 LLIKQELQLSLEGKDET 1417
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1330-1683 |
1.89e-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: 59.59 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1330 QEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEA--------QQLLEEETRQKLGLSSKLRQIESEKEALQ- 1400
Cdd:COG5185 158 TGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEpsgtvnsiKESETGNLGSESTLLEKAKEIINIEEALKg 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1401 -EQLEEDDEAKRNYERKLAEVTTQMQEIK-KKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQND---RLDKSKKK 1475
Cdd:COG5185 238 fQDPESELEDLAQTSDKLEKLVEQNTDLRlEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkATESLEEQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1476 IQSELEDATIE--LEAQRTKVLEL-EKKQKNFDKILAEEKAISEQIaqERDTAEREAREKETKVLSVSRELDEAFDKI-E 1551
Cdd:COG5185 318 LAAAEAEQELEesKRETETGIQNLtAEIEQGQESLTENLEAIKEEI--ENIVGEVELSKSSEELDSFKDTIESTKESLdE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1552 DLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTE-DAKLRLEVNMQALRSQFERD 1630
Cdd:COG5185 396 IPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMrEADEESQSRLEEAYDEINRS 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 386768643 1631 LLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETT 1683
Cdd:COG5185 476 VRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKD 528
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1117-1680 |
1.91e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.92 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1117 DLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEdleaekaarakaekvrrdLS 1196
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSS------------------LE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1197 EELEALKNELldsldttaAQQELRSKREQELATLKKSLEEEtvnHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKA 1276
Cdd:PRK01156 249 DMKNRYESEI--------KTAESDLSMELEKNNYYKELEER---HMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNI 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1277 KGTLEA--ENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKA 1354
Cdd:PRK01156 318 DAEINKyhAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1355 SAAVKSASNMESQLTEAQQLLEEetrqklgLSSKLRQIESEKEALQEQLeedDEAKRNYERKLAEVTTQMQEIKKKAEED 1434
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQD-------ISSKVSSLNQRIRALRENL---DELSRNMEMLNGQSVCPVCGTTLGEEKS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1435 ADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSE-----------LEDATIELEAQRTKVLELEKKQKN 1503
Cdd:PRK01156 468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEeinksineynkIESARADLEDIKIKINELKDKHDK 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1504 FDKILAEEKAISEQIAQER----------------DTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL 1567
Cdd:PRK01156 548 YEEIKNRYKSLKLEDLDSKrtswlnalavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1568 ANTQGTADKNVHELEKAKRALESQLAELK---AQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEgaeekRRG 1644
Cdd:PRK01156 628 ANNLNNKYNEIQENKILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR-----LES 702
|
570 580 590
....*....|....*....|....*....|....*....
gi 386768643 1645 LVKQLRDLETELDEERKQRTAAVASKKKLE---GDLKEI 1680
Cdd:PRK01156 703 TIEILRTRINELSDRINDINETLESMKKIKkaiGDLKRL 741
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1263-1960 |
1.94e-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: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1263 LENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVkLAEIERARSELqekcTKLQQEaen 1342
Cdd:pfam12128 178 LRHIDKIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQA-IAGIMKIRPEF----TKLQQE--- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1343 iTNQLEEAELKASA---AVKSASNMESQLTEAQQLLEEETRQKLglSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAE 1419
Cdd:pfam12128 250 -FNTLESAELRLSHlhfGYKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAADAAVAKDRSELEA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1420 VTTQ----MQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLD-KSKKKIQSELEDATIELEAQR-TK 1493
Cdd:pfam12128 327 LEDQhgafLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRsKIKEQNNRDIAGIKDKLAKIReAR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1494 VLELEKKQKNFDKIlaeEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTlQNELDDLANTQGT 1573
Cdd:pfam12128 407 DRQLAVAEDDLQAL---ESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENF-DERIERAREEQEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1574 ADKNVHELEKAKRALESQLAElkaQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDL--LAKEEGAEEKRRGLV---KQ 1648
Cdd:pfam12128 483 ANAEVERLQSELRQARKRRDQ---ASEALRQASRRLEERQSALDELELQLFPQAGTLLhfLRKEAPDWEQSIGKVispEL 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1649 L--RDLETELDEERKQRTAAVASkkkLEGDLKEIE--TTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQA 1724
Cdd:pfam12128 560 LhrTDLDPEVWDGSVGGELNLYG---VKLDLKRIDvpEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1725 LSKEAERKVKAL--------------EAEVLQLTEdlaSSERARRAAETERDELAEEIANNANKGSLMIDEKRR--LEAR 1788
Cdd:pfam12128 637 ASREETFARTALknarldlrrlfdekQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEqkREAR 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1789 IAtleeeleEEQSNSEVLLDRSrkaqLQIEQLTTELANEKSNsqknengrallerqnkeLKAKLAEIETAQRTKVKA--- 1865
Cdd:pfam12128 714 TE-------KQAYWQVVEGALD----AQLALLKAAIAARRSG-----------------AKAELKALETWYKRDLASlgv 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1866 ---TIATLEAKIANLEEQLENEGK-------------ERLLQQKANRKMDK-KIKELTMNIEDE-RRHVDQHKEQMDKLN 1927
Cdd:pfam12128 766 dpdVIAKLKREIRTLERKIERIAVrrqevlryfdwyqETWLQRRPRLATQLsNIERAISELQQQlARLIADTKLRRAKLE 845
|
730 740 750
....*....|....*....|....*....|...
gi 386768643 1928 SRIKLLKRNLDETEEELQKEKTQKRKYQRECED 1960
Cdd:pfam12128 846 MERKASEKQQVRLSENLRGLRCEMSKLATLKED 878
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1216-1583 |
2.77e-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: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1216 QQELRSKREQeLATLK---KSLEEETVNHEGVLADMRHKHSQELNSIndqlENLRKAKTVLEKAKgtleaenadlateLR 1292
Cdd:pfam10174 407 QEQLRDKDKQ-LAGLKervKSLQTDSSNTDTALTTLEEALSEKERII----ERLKEQREREDRER-------------LE 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1293 SVNSSRQENdrrrKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQ 1372
Cdd:pfam10174 469 ELESLKKEN----KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1373 QlLEEETRQKLGLSSKLRQIE--------------SEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLA 1438
Cdd:pfam10174 545 N-AEEAVRTNPEINDRIRLLEqevarykeesgkaqAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1439 KELEEGKKRlnKDIEALERQVKEliaQNDRLDKSKkkiQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQI 1518
Cdd:pfam10174 624 KHGQQEMKK--KGAQLLEEARRR---EDNLADNSQ---QLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNL 695
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768643 1519 AQERDTAEREARE-KETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQgtaDKNVHELEK 1583
Cdd:pfam10174 696 RAERRKQLEEILEmKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREK---DRLVHQLKQ 758
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1211-1652 |
2.86e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1211 DTTAAQQELRSKRE-----QELATLKKSLEEETVNHegVLAD-MRHkhSQELNSINDQLENLRKAktvLEKAKGTLEAEN 1284
Cdd:PRK04863 234 DMEAALRENRMTLEairvtQSDRDLFKHLITESTNY--VAADyMRH--ANERRVHLEEALELRRE---LYTSRRQLAAEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1285 ADL---ATELRSVNSSRQENDRRRKQAESQIAELQVKLA---EIERARSELQEKCTKL--QQEA-ENITNQLEEAELKAS 1355
Cdd:PRK04863 307 YRLvemARELAELNEAESDLEQDYQAASDHLNLVQTALRqqeKIERYQADLEELEERLeeQNEVvEEADEQQEENEARAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1356 AAVKSASNMESQLTEAQQLLE----------------EETRQKLGLSS-KLRQIESEKEALQEQLEEDDEAKRNYERKLA 1418
Cdd:PRK04863 387 AAEEEVDELKSQLADYQQALDvqqtraiqyqqavqalERAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLS 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1419 EVttqmQEIKKKAEEDADLAKeleegkkRLNKDIEALE--RQVKELIAQNdrldkSKKKIQSEledatiELEAQRTKVLE 1496
Cdd:PRK04863 467 VA----QAAHSQFEQAYQLVR-------KIAGEVSRSEawDVARELLRRL-----REQRHLAE------QLQQLRMRLSE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1497 LEK---KQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLAntqgt 1573
Cdd:PRK04863 525 LEQrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA----- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1574 adknvhELEKAKRALESQLAELKAQ-NEELEDDLQLTEdaklrlevNMQALRSQfERDLLAKEEGAEEKRRGLVKQLRDL 1652
Cdd:PRK04863 600 ------ARAPAWLAAQDALARLREQsGEEFEDSQDVTE--------YMQQLLER-ERELTVERDELAARKQALDEEIERL 664
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1192-1470 |
3.15e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 59.15 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1192 RRDLSEELEALKNELLDSLDTTAAQQelrsKREQELATLKKSLEEETvnhegvladmrhkhsQELNSINDQLENLRKAKT 1271
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLKQQLAQAP---------------AKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1272 vlEKAKGTLEA-ENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLaeiERARSELQEKCTKLQQeaenITNQLeeA 1350
Cdd:PRK11281 112 --EETRETLSTlSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQP---ERAQAALYANSQRLQQ----IRNLL--K 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1351 ELKASAAVKSAS-----NMESQLTEAQ-----QLLEEETR-QKLG------LSSKLRQIESEKEALQEQLEEddeaKRny 1413
Cdd:PRK11281 181 GGKVGGKALRPSqrvllQAEQALLNAQndlqrKSLEGNTQlQDLLqkqrdyLTARIQRLEHQLQLLQEAINS----KR-- 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1414 eRKLAEVT-TQMQEIKKKAEEDAD--LAKELEegkkrLNKDIEalerqvKELIAQNDRLD 1470
Cdd:PRK11281 255 -LTLSEKTvQEAQSQDEAARIQANplVAQELE-----INLQLS------QRLLKATEKLN 302
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1415-1826 |
3.16e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1415 RKLAEVTTQMQEIKKKAEEDADLAKELEEgkkrLNKDIEALERQVKELIAQNDRLDKSKK--KIQSELEDATIELEAQRT 1492
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1493 KVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKEtkvLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQG 1572
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1573 TADKNVHELEKAKR--ALESQLAELKAqneeleddLQLTEDAKLRLEVNMQALRSQFER----------------DLLAK 1634
Cdd:COG4717 224 ELEEELEQLENELEaaALEERLKEARL--------LLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallfLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1635 EEGAEEKRRGLVKQLRDLEtELDEERKQRTAAV------ASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDA 1708
Cdd:COG4717 296 EKASLGKEAEELQALPALE-ELEEEELEELLAAlglppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1709 LRDAEEAKAAKEELQALskEAERKVKALEAEVLQLTEDLAS--SERARRAAETERDELAEEIANNANKGSLMIDEKRRLE 1786
Cdd:COG4717 375 LLAEAGVEDEEELRAAL--EQAEEYQELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 386768643 1787 ARIATLEEELEEEQSNSEVlldrsRKAQLQIEQLTTELAN 1826
Cdd:COG4717 453 EELAELEAELEQLEEDGEL-----AELLQELEELKAELRE 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1398-1607 |
4.13e-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: 57.85 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1398 ALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQ 1477
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1478 SELEDATIELEAQ--------RTKVLELEKKQKNFDKILAEEKAIsEQIAQERDTAEREAREKETKVLSVSRELDEAFDK 1549
Cdd:COG4942 97 AELEAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVRRLQYL-KYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386768643 1550 IEDLENKRKTLQNELDDLANTQgtaDKNVHELEKAKRALESQLAELKAQNEELEDDLQ 1607
Cdd:COG4942 176 LEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1104-1367 |
4.29e-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: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1104 SDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEesatkatAQKAQRELESQLAEIQEDLEAEka 1183
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA-------LQAEIDKLQAEIAEAEAEIEER-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1184 arakaekvRRDLSEELEALKNE--LLDSLDTTAAQQELrskreqelatlkksleEETVNHEGVLADMRHKHSQELNSIND 1261
Cdd:COG3883 85 --------REELGERARALYRSggSVSYLDVLLGSESF----------------SDFLDRLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1262 QLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAE 1341
Cdd:COG3883 141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
250 260
....*....|....*....|....*.
gi 386768643 1342 NITNQLEEAELKASAAVKSASNMESQ 1367
Cdd:COG3883 221 AAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1058-1298 |
4.93e-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: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1058 RANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLA 1137
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1138 KREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLeaekaarakaekvrRDLSEELEALKNELldsldttAAQQ 1217
Cdd:COG4942 115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL--------------RADLAELAALRAEL-------EAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1218 ELRSKREQELATLKKSLEEETVNHEGVLADMRhkhsQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSS 1297
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
.
gi 386768643 1298 R 1298
Cdd:COG4942 250 A 250
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
893-1549 |
5.51e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 893 KPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLqaeielcAEAEESRSRLMARKQELE 972
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQI-------ADDEKSHSITLKEIERLS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 973 DMMQELETRI---EEEEERVLALGGEKKKLELNIQdleeqleeeeaarqKLQLEKVQLDAKIKKYEEdlaLTDDQNQKLL 1049
Cdd:PRK01156 225 IEYNNAMDDYnnlKSALNELSSLEDMKNRYESEIK--------------TAESDLSMELEKNNYYKE---LEERHMKIIN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1050 KEKKLLEERANDLSQTLAEEEEKAKHLAKLKA---KHEATISELEErLHKDQQQRQESDRSKRKIETEVADLKEQLNERR 1126
Cdd:PRK01156 288 DPVYKNRNYINDYFKYKNDIENKKQILSNIDAeinKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYN 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1127 VQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNel 1206
Cdd:PRK01156 367 SYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSR-- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1207 ldsldtTAAQQELRSKreqeLATLKKSLEEETVNHegvladMRHKHSQELNSINDQLENL-RKAKTVLEKAKgtleaena 1285
Cdd:PRK01156 445 ------NMEMLNGQSV----CPVCGTTLGEEKSNH------IINHYNEKKSRLEEKIREIeIEVKDIDEKIV-------- 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1286 DLATELRSVNSsrqENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITN-QLEEAELKASAAVKSASNM 1364
Cdd:PRK01156 501 DLKKRKEYLES---EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNALAVI 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1365 ESQLTEAQQLLEEETRQKLG-LSSKLRQIESE----KEALQEQLEEDDEAKRNYERKLAEVttqmQEIKKKAEEdadLAK 1439
Cdd:PRK01156 578 SLIDIETNRSRSNEIKKQLNdLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKYNEI----QENKILIEK---LRG 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1440 ELEEGKKRLNKdIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVlelekkqknfDKILAEEKAISEQIA 1519
Cdd:PRK01156 651 KIDNYKKQIAE-IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTI----------EILRTRINELSDRIN 719
|
650 660 670
....*....|....*....|....*....|
gi 386768643 1520 QERDTAEReaREKETKVLSVSRELDEAFDK 1549
Cdd:PRK01156 720 DINETLES--MKKIKKAIGDLKRLREAFDK 747
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1548-1791 |
5.87e-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: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1548 DKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQF 1627
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1628 ErdllakeegaeEKRRGLVKQLRDLETEldeERKQRTAAVASKKklegDLKEIETTMEMHNKVKEDALKHAKKLQAQVKD 1707
Cdd:COG4942 100 E-----------AQKEELAELLRALYRL---GRQPPLALLLSPE----DFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1708 ALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEA 1787
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....
gi 386768643 1788 RIAT 1791
Cdd:COG4942 242 RTPA 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1422-1639 |
6.09e-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: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1422 TQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLEL---- 1497
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1498 --EKKQKNFDKILAEEKAISEQIaqerdtaerearekeTKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTAD 1575
Cdd:COG3883 96 yrSGGSVSYLDVLLGSESFSDFL---------------DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1576 KNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAE 1639
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1058-1670 |
8.05e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1058 RANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKI------ETEVADLKEQLNERRVQVDE 1131
Cdd:PRK04863 493 EAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknlddEDELEQLQEELEARLESLSE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1132 MQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNElldSLD 1211
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE---RDE 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1212 TTAAQQELRSKREQ-------ELATLKKSLE----------------EETVNHEGVLADMRHK-HSQELNSINDQLENLR 1267
Cdd:PRK04863 650 LAARKQALDEEIERlsqpggsEDPRLNALAErfggvllseiyddvslEDAPYFSALYGPARHAiVVPDLSDAAEQLAGLE 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1268 KAKTVLEKAKGTLEA-ENADLATELRSVNSSRQENDRR-------------RKQAESQIAELQVKLAEIERARSELQEKC 1333
Cdd:PRK04863 730 DCPEDLYLIEGDPDSfDDSVFSVEELEKAVVVKIADRQwrysrfpevplfgRAAREKRIEQLRAEREELAERYATLSFDV 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1334 TKLQQeaeniTNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLeeDDEAKRNY 1413
Cdd:PRK04863 810 QKLQR-----LHQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL--SALNRLLP 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1414 ERKLAEVTTQMQEIKKkAEEDADLAKELEEGKKRLNKDIEALERQVKELiaQNDRLDKSKKKIQSELEDATIELEAQRTK 1493
Cdd:PRK04863 883 RLNLLADETLADRVEE-IREQLDEAEEAKRFVQQHGNALAQLEPIVSVL--QSDPEQFEQLKQDYQQAQQTQRDAKQQAF 959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1494 VL-ELEKKQKNFD-----KILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL 1567
Cdd:PRK04863 960 ALtEVVQRRAHFSyedaaEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1568 ANtqgtadknvhELEK-AKRALESQLAELKAQNEELEDDLqltedaklrleVNMQALRSQFERDLLAKEEGAEEkrrgLV 1646
Cdd:PRK04863 1040 KQ----------ELQDlGVPADSGAEERARARRDELHARL-----------SANRSRRNQLEKQLTFCEAEMDN----LT 1094
|
650 660
....*....|....*....|....
gi 386768643 1647 KQLRDLETELDEERKQRTAAVASK 1670
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNAKAGW 1118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1700-1981 |
1.30e-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: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1700 KLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVlQLTEDLASSERARRAAE-----TERDELAEEIANNANK 1774
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQA-EKAERYKELKAELRELElallvLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1775 GSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAE 1854
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1855 IEtAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLK 1934
Cdd:TIGR02168 328 LE-SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 386768643 1935 RNLDETEEELQKEKTQKRKYQRECE-----DMIESQEAMNREINSLKTKLRR 1981
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELER 458
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1743-1981 |
1.52e-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: 57.00 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1743 LTEDLASSERARRAAETERDELaEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSE--------VLLDRSRKAQ 1814
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEEL-EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKekreyegyELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1815 LQIEQLTTELAN-----EKSNSQKNENGRAL--LERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLENegKE 1887
Cdd:TIGR02169 237 RQKEAIERQLASleeelEKLTEEISELEKRLeeIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE--KE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1888 RLLQQKANR--KMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQ 1965
Cdd:TIGR02169 315 RELEDAEERlaKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250
....*....|....*.
gi 386768643 1966 EAMNREINSLKTKLRR 1981
Cdd:TIGR02169 395 EKLKREINELKRELDR 410
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1727-1953 |
1.83e-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: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1727 KEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQsnsEVL 1806
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK---EEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1807 LDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIEtAQRTKVKATIATLEAKIANLEEQLENEGK 1886
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-ADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 1887 ERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRK 1953
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
897-1428 |
4.30e-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: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 897 EVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQ-AEIELCAEAEESRSRLMARKQELEDMM 975
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 976 QELETRIEEEEERVLALGGEKKKLELNiqdleeqleeeeaaRQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLL 1055
Cdd:pfam05483 349 FVVTEFEATTCSLEELLRTEQQRLEKN--------------EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1056 EERandlsQTLAEEEEKAKHLA-KLKAKHEATISELEER---LHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDE 1131
Cdd:pfam05483 415 AED-----EKLLDEKKQFEKIAeELKGKEQELIFLLQARekeIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1132 MQA---QLAKREEELTQ----TLLRIDEESATKATAQKAQRELESQLAEIQEdleAEKAARAKAEKVRRDLSEELEALKN 1204
Cdd:pfam05483 490 LTAhcdKLLLENKELTQeasdMTLELKKHQEDIINCKKQEERMLKQIENLEE---KEMNLRDELESVREEFIQKGDEVKC 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1205 ELLDSLDTTAAQQELRSKREQELATLkksleEETVNHEGVLADMRHKHSQELNSINdqlENLRKAKTVLEKAKGTLEAEN 1284
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKIL-----ENKCNNLKKQIENKNKNIEELHQEN---KALKKKGSAENKQLNAYEIKV 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1285 ADLATELRSVNSSRQE-NDRRRKQAESQIAELQVKLAEIERARSELQEkCTKLQQEAE-----NITNQLEEAELKASAAV 1358
Cdd:pfam05483 639 NKLELELASAKQKFEEiIDNYQKEIEDKKISEEKLLEEVEKAKAIADE-AVKLQKEIDkrcqhKIAEMVALMEKHKHQYD 717
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1359 KSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIK 1428
Cdd:pfam05483 718 KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1305-1488 |
4.60e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.22 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1305 RKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENItnqLEEAELKASAAVKSASNmesqltEAQQLLEE--ETRQK 1382
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAIKEAKK------EADEIIKElrQLQKG 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1383 LGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVT----------TQMQEIKKKAEEDAdlAKELEEGKK-RLN-K 1450
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKvgdevkylslGQKGEVLSIPDDKE--AIVQAGIMKmKVPlS 677
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 386768643 1451 DIEALERQVKELIAQNDRLDKSKKKIQSEL-------EDATIELE 1488
Cdd:PRK00409 678 DLEKIQKPKKKKKKKPKTVKPKPRTVSLELdlrgmryEEALERLD 722
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1297-1768 |
5.83e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1297 SRQENDRRRKQAESqiAELQVKLAEIERARSELQEKCTKLQQEAEnitnQLEEAELKASAAVKSASnmesqltEAQQLLE 1376
Cdd:PRK04863 275 MRHANERRVHLEEA--LELRRELYTSRRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAAS-------DHLNLVQ 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1377 EETRQKlglsSKLRQIESEKEALQEQLEEDdeakrnyerklAEVTTQMQEIKKKAEEDADLA-KELEEGKKRLNKDIEAL 1455
Cdd:PRK04863 342 TALRQQ----EKIERYQADLEELEERLEEQ-----------NEVVEEADEQQEENEARAEAAeEEVDELKSQLADYQQAL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1456 ERQVKELIAQND---RLDKSKKkiQSELEDATIEleaqrtkvlelekkqkNFDKILAEEKAISEQIAQERDTAEREarek 1532
Cdd:PRK04863 407 DVQQTRAIQYQQavqALERAKQ--LCGLPDLTAD----------------NAEDWLEEFQAKEQEATEELLSLEQK---- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1533 etkvLSVSRELDEAFDKIEDLenkrktLQNELDDLANTQgtADKNVHELEKA---KRALESQLAELKAQNEELEDDLQLT 1609
Cdd:PRK04863 465 ----LSVAQAAHSQFEQAYQL------VRKIAGEVSRSE--AWDVARELLRRlreQRHLAEQLQQLRMRLSELEQRLRQQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1610 EDAklrlevnmQALRSQFERDL---LAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTM-E 1685
Cdd:PRK04863 533 QRA--------ERLLAEFCKRLgknLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARApA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1686 MHNKvkEDALKhakKLQAQVKDALRDAEEAKAAKEELQALSKEA-------ERKVKALEAEVLQLTE-DLASSERARRAA 1757
Cdd:PRK04863 605 WLAA--QDALA---RLREQSGEEFEDSQDVTEYMQQLLERERELtverdelAARKQALDEEIERLSQpGGSEDPRLNALA 679
|
490
....*....|.
gi 386768643 1758 ETERDELAEEI 1768
Cdd:PRK04863 680 ERFGGVLLSEI 690
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1098-1358 |
6.17e-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: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1098 QQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQ--LAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQ 1175
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1176 EDLeaekaarakaekvrrdlseeleALKNELLDSLDTTAAQQELRSKR---EQELATLKKSLeeeTVNHEGVLAdmrhkh 1252
Cdd:COG3206 247 AQL----------------------GSGPDALPELLQSPVIQQLRAQLaelEAELAELSARY---TPNHPDVIA------ 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1253 sqelnsINDQLENLRKAktvlekakgtLEAENADLATELRsvnSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEk 1332
Cdd:COG3206 296 ------LRAQIAALRAQ----------LQQEAQRILASLE---AELEALQAREASLQAQLAQLEARLAELPELEAELRR- 355
|
250 260 270
....*....|....*....|....*....|...
gi 386768643 1333 ctkLQQEAEN-------ITNQLEEAELKASAAV 1358
Cdd:COG3206 356 ---LEREVEVarelyesLLQRLEEARLAEALTV 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1451-1669 |
7.17e-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: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1451 DIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTkvlELEKKQKNFDKILAEEKAISEQIAQERDTAEREAR 1530
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA---ELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1531 E--------KETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEEL 1602
Cdd:COG3883 94 AlyrsggsvSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 1603 EDDLQLTEDAKLRLEVNMQALRSQFERdlLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVAS 1669
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAE--LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1154-1373 |
7.56e-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: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1154 SATKATAQKAQRELESQLAEIQEDLEAEKAARAkaekvrrDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKS 1233
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELD-------ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1234 LEEETVNHEGVLADMRHK-----------HSQELNSINDQLENLRK-----AKTV--LEKAKGTLEAENADLATELRSVN 1295
Cdd:COG3883 81 IEERREELGERARALYRSggsvsyldvllGSESFSDFLDRLSALSKiadadADLLeeLKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768643 1296 SSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQ 1373
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1381-1627 |
1.01e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 53.78 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1381 QKLGLSsklrQIESEKEALQ-EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLA-KELEEGKKRLNKDIEALERQ 1458
Cdd:PRK05771 26 HELGVV----HIEDLKEELSnERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSvKSLEELIKDVEEELEKIEKE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1459 VKELIAQNDRLDKSKKKIQSELEDAT----IELEaqrtkvLELEKKQKNFDKILAE--EKAISEQIAQERDTAEREAREK 1532
Cdd:PRK05771 102 IKELEEEISELENEIKELEQEIERLEpwgnFDLD------LSLLLGFKYVSVFVGTvpEDKLEELKLESDVENVEYISTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1533 ETKVLSV----SRELDEAFDKIEDLENKRKTLQNElddlantqGTADKNVHELEKAKRALESQL----AELKAQNEELED 1604
Cdd:PRK05771 176 KGYVYVVvvvlKELSDEVEEELKKLGFERLELEEE--------GTPSELIREIKEELEEIEKEResllEELKELAKKYLE 247
|
250 260
....*....|....*....|...
gi 386768643 1605 DLQLTEDaKLRLEVNMQALRSQF 1627
Cdd:PRK05771 248 ELLALYE-YLEIELERAEALSKF 269
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1366-1643 |
1.43e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1366 SQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGK 1445
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1446 KRLNKDIEALERQVKELiaqndrldkskKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTA 1525
Cdd:COG1340 81 DELNEKLNELREELDEL-----------RKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1526 E--REAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELE 1603
Cdd:COG1340 150 EkaKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 386768643 1604 DDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRR 1643
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1016-1435 |
1.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1016 ARQKLQLEKVQLDAKIKKYEEDLALTDD--QNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLkakhEATISELEER 1093
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1094 LHKDQQQ-RQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLA 1172
Cdd:COG4717 172 LAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1173 EIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEE-ETVNHEGVLADMRHK 1251
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1252 HSQELNSINDQLENLRKAKTVLEKAkgtleaenadlatelrsvnsSRQENDRRRKQAESQIAEL----QVKLAEIERARS 1327
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREA--------------------EELEEELQLEELEQEIAALlaeaGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1328 ELQEKCTKLQQEAENITNQLEEA--ELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKealqEQLEE 1405
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL----EQLEE 467
|
410 420 430
....*....|....*....|....*....|
gi 386768643 1406 DDEakrnYERKLAEVTTQMQEIKKKAEEDA 1435
Cdd:COG4717 468 DGE----LAELLQELEELKAELRELAEEWA 493
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1440-1606 |
1.48e-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: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1440 ELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKilAEE-KAISEQI 1518
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--NKEyEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1519 aqerDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANtqgtadknvhELEKAKRALESQLAELKAQ 1598
Cdd:COG1579 99 ----ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA----------ELDEELAELEAELEELEAE 164
|
....*...
gi 386768643 1599 NEELEDDL 1606
Cdd:COG1579 165 REELAAKI 172
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1216-1482 |
2.32e-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: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1216 QQELRSKREQELATLKKSLEEETVNHEGVLADmrhkhSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATEL---- 1291
Cdd:pfam05667 242 KRKRTKLLKRIAEQLRSAALAGTEATSGASRS-----AQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEApaat 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1292 RSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEE-----AELKASAAVKS-----A 1361
Cdd:pfam05667 317 SSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEElkeqnEELEKQYKVKKktldlL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1362 SNMESQLTEAQQLLEEETRQKLGLSsklRQIESEKEALQEQLEEDDEAKRN----YERKLAEVT---TQMQEIKKKAEED 1434
Cdd:pfam05667 397 PDAEENIAKLQALVDASAQRLVELA---GQWEKHRVPLIEEYRALKEAKSNkedeSQRKLEEIKelrEKIKEVAEEAKQK 473
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 386768643 1435 ADLAKELEEGKKRLNKDI--EALERQVKELIAQndrLDKSKKKIQSELED 1482
Cdd:pfam05667 474 EELYKQLVAEYERLPKDVsrSAYTRRILEIVKN---IKKQKEEITKILSD 520
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1071-1375 |
3.41e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 51.07 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1071 EKAKHLAKLKAKHEATISELEerlhkdQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRI 1150
Cdd:pfam00038 18 DKVRFLEQQNKLLETKISELR------QKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1151 DEESATKataqkaqRELESQLAEIQEDLEAEKAArakaekvRRDLSEELEALKNELLdsldttaaqqELRSKREQELATL 1230
Cdd:pfam00038 92 EDELNLR-------TSAENDLVGLRKDLDEATLA-------RVDLEAKIESLKEELA----------FLKKNHEEEVREL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1231 KKSLEEETVNHE----------GVLADMRHKHSQELNSINDQLENLRKAKTvlekAKGTLEAE-NADlatELRSVNSSRQ 1299
Cdd:pfam00038 148 QAQVSDTQVNVEmdaarkldltSALAEIRAQYEEIAAKNREEAEEWYQSKL----EELQQAAArNGD---ALRSAKEEIT 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768643 1300 ENDRRRKQAESQIAELQVKLAEIERARSELQEkctKLQQEAENITNQLEEAElkaSAAVKSASNMESQLTEAQQLL 1375
Cdd:pfam00038 221 ELRRTIQSLEIELQSLKKQKASLERQLAETEE---RYELQLADYQELISELE---AELQETRQEMARQLREYQELL 290
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
918-1317 |
3.85e-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: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 918 KLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQELETRIEEEEERVLALGGEKK 997
Cdd:pfam12128 584 KLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQ 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 998 KLELNIQdleeqlEEEEAARQKLQLEKVQLDAKIKKYEEDL--ALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKH 1075
Cdd:pfam12128 664 SEKDKKN------KALAERKDSANERLNSLEAQLKQLDKKHqaWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAA 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1076 LAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLnerrvqvdemqAQLAKREEELTQT--------L 1147
Cdd:pfam12128 738 IAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKI-----------ERIAVRRQEVLRYfdwyqetwL 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1148 LRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAekvrRDLSEELEALKNELLDSLDTtaaqqelrskREQEL 1227
Cdd:pfam12128 807 QRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEME----RKASEKQQVRLSENLRGLRC----------EMSKL 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1228 ATLKKSLEEETVNHE-----GVLADMRHKHSQELNSINDQLENLrkaKTVLEKAKGTLEAEN-ADLATELRSVNSSRQEN 1301
Cdd:pfam12128 873 ATLKEDANSEQAQGSigerlAQLEDLKLKRDYLSESVKKYVEHF---KNVIADHSGSGLAETwESLREEDHYQNDKGIRL 949
|
410
....*....|....*...
gi 386768643 1302 DRRRK--QAESQIAELQV 1317
Cdd:pfam12128 950 LDYRKlvPYLEQWFDVRV 967
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1548-1711 |
5.58e-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: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1548 DKIEDLENKRK----TLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRL---EVNM 1620
Cdd:pfam05667 324 ETEEELQQQREeeleELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLpdaEENI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1621 QALRSQFE---RDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQrtaavaSKKKLEgDLKEIETTM---EMHNKVKEDA 1694
Cdd:pfam05667 404 AKLQALVDasaQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDE------SQRKLE-EIKELREKIkevAEEAKQKEEL 476
|
170
....*....|....*..
gi 386768643 1695 LKHakkLQAQVKDALRD 1711
Cdd:pfam05667 477 YKQ---LVAEYERLPKD 490
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1255-1434 |
5.88e-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: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1255 ELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQvklAEIERARSELQEkcT 1334
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLGN--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1335 KLQQEAENITNQLEEAELKASAAvksasnmESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLeedDEAKRNYE 1414
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELE 155
|
170 180
....*....|....*....|
gi 386768643 1415 RKLAEVTTQMQEIKKKAEED 1434
Cdd:COG1579 156 AELEELEAEREELAAKIPPE 175
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1359-1577 |
6.03e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1359 KSASNMESQLTEAQQLLEEETRQK-LGLSSKLRQIESEKEALQEQLEEDDEAKRnyerklaevttQMQEIKKKAEEDAdl 1437
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKqAAEQERLKQLEKERLAAQEQKKQAEEAAK-----------QAALKQKQAEEAA-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1438 AKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSElEDATIELEAQRTKVLELEKKQKnfdkilAEEKAISEQ 1517
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAA-AEAKKKAEAEAAAKAAAEAKKK------AEAEAKKKA 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1518 IAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLEN-KRKTLQNELDDLANtQGTADKN 1577
Cdd:PRK09510 212 AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKaAAAKAAAEVDDLFG-GLDSGKN 271
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1247-1968 |
6.49e-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: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1247 DMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRrkqAESQIAELQVKLAEIERAR 1326
Cdd:pfam10174 88 DLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELR---IETQKQTLGARDESIKKLL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1327 SELQEK--CTKLQQEAENITNQLEEAELKASaavksasNMESQL----TEAQQLLEEETRQklglsSKLRQIESEKEALQ 1400
Cdd:pfam10174 165 EMLQSKglPKKSGEEDWERTRRIAEAEMQLG-------HLEVLLdqkeKENIHLREELHRR-----NQLQPDPAKTKALQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1401 EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEedadlakeleegkkrLNKDIEALERQVKELIAQNDRLDKSK-KKIQSE 1479
Cdd:pfam10174 233 TVIEMKDTKISSLERNIRDLEDEVQMLKTNGL---------------LHTEDREEEIKQMEVYKSHSKFMKNKiDQLKQE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1480 LEDATIELEAQRTKVLELEKKQ---KNFDKILAEEKAISEQIAQ----ERDTAEREAREKETKvlsvsreLDEAFDKIED 1552
Cdd:pfam10174 298 LSKKESELLALQTKLETLTNQNsdcKQHIEVLKESLTAKEQRAAilqtEVDALRLRLEEKESF-------LNKKTKQLQD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1553 LENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQltedaklrlevNMQALRSQFERDLL 1632
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVK-----------SLQTDSSNTDTALT 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1633 AKEEGAEEKRRgLVKQLRDletELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAK-KLQAQVKDALRd 1711
Cdd:pfam10174 440 TLEEALSEKER-IIERLKE---QREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKeHASSLASSGLK- 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1712 aeeakaakeelqalskeAERKVKALEAEVLQLTEDLASSERARRAaeterdelAEEIANNANKGSLMIDEKRRLEARIAT 1791
Cdd:pfam10174 515 -----------------KDSKLKSLEIAVEQKKEECSKLENQLKK--------AHNAEEAVRTNPEINDRIRLLEQEVAR 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1792 LEEELEEEQSNSEVLLDRSRKAQlqieqlttelaNEKSN-SQKNENGRALLERQNKELKAKLAEIETAQRTKVKATIATL 1870
Cdd:pfam10174 570 YKEESGKAQAEVERLLGILREVE-----------NEKNDkDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1871 EAKIANLEEQLENEGKerllqqkanrkmdKKIKELTMNIEDERRHVDQHKEqmdklnsRIKLLKRNLDETEEELQKEKTQ 1950
Cdd:pfam10174 639 EEARRREDNLADNSQQ-------------LQLEELMGALEKTRQELDATKA-------RLSSTQQSLAEKDGHLTNLRAE 698
|
730
....*....|....*...
gi 386768643 1951 KRKYQRECEDMieSQEAM 1968
Cdd:pfam10174 699 RRKQLEEILEM--KQEAL 714
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1060-1982 |
6.76e-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: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1060 NDLSQTLAEEEEKAKHL-------AKLK---AKHEATISELEERLH--------KDQQQRQESDRSKRKIETevADLKEq 1121
Cdd:TIGR01612 751 KDLNKILEDFKNKEKELsnkindyAKEKdelNKYKSKISEIKNHYNdqinidniKDEDAKQNYDKSKEYIKT--ISIKE- 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1122 lNERRVQVDEMQAQlakREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEaekaarakaekvrrdlSEELEA 1201
Cdd:TIGR01612 828 -DEIFKIINEMKFM---KDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEIS----------------DDKLND 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1202 LKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETV--NHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGT 1279
Cdd:TIGR01612 888 YEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKIceNTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDK 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1280 LEAENADLATELR------SVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTK-LQQEAENITNQLEEAEL 1352
Cdd:TIGR01612 968 FDNTLIDKINELDkafkdaSLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEKATNdIEQKIEDANKNIPNIEI 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1353 KASAAVKSASN-MESQLTEAQQLLEEETRQKLGLS--------SKLRQIESEKEALQEQLEEDDEAKR------NYERKL 1417
Cdd:TIGR01612 1048 AIHTSIYNIIDeIEKEIGKNIELLNKEILEEAEINitnfneikEKLKHYNFDDFGKEENIKYADEINKikddikNLDQKI 1127
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1418 AEVTTQMQEIKKKAEEDADLAK----ELEE--GKKRLNKDIEALERQVKELIAQNDR----LDKSKKKIQ--SELEDATI 1485
Cdd:TIGR01612 1128 DHHIKALEEIKKKSENYIDEIKaqinDLEDvaDKAISNDDPEEIEKKIENIVTKIDKkkniYDEIKKLLNeiAEIEKDKT 1207
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1486 ELE---------AQRTKVLELEK----KQKNFDKILAEEKAISE--QIAQERDTAEREAR-----EKETKVLSVSRELDE 1545
Cdd:TIGR01612 1208 SLEevkginlsyGKNLGKLFLEKideeKKKSEHMIKAMEAYIEDldEIKEKSPEIENEMGiemdiKAEMETFNISHDDDK 1287
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1546 AF--------DKIEDLENK-----------------RKTLQNELDDLANTQGTADK---------NVHELEKAKRALE-- 1589
Cdd:TIGR01612 1288 DHhiiskkhdENISDIREKslkiiedfseesdindiKKELQKNLLDAQKHNSDINLylneianiyNILKLNKIKKIIDev 1367
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1590 -SQLAELKAQNEELEDDLQLTED--AKLRLEVNMQALRSQFERDLLAKEegaeekRRGLVKQLRDLETELDEERKQRTAA 1666
Cdd:TIGR01612 1368 kEYTKEIEENNKNIKDELDKSEKliKKIKDDINLEECKSKIESTLDDKD------IDECIKKIKELKNHILSEESNIDTY 1441
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1667 VASKKKLEGDLKEIETTMEMHNKVKEDALKHAKklQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVL---QL 1743
Cdd:TIGR01612 1442 FKNADENNENVLLLFKNIEMADNKSQHILKIKK--DNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKElfeQY 1519
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1744 TEDLasSERARRAAETErdeLAEEIANNANKGSLMIDEKRRLEARIATLEeeleeeqSNSEVLLDRSRKAQLQIEQLTTE 1823
Cdd:TIGR01612 1520 KKDV--TELLNKYSALA---IKNKFAKTKKDSEIIIKEIKDAHKKFILEA-------EKSEQKIKEIKKEKFRIEDDAAK 1587
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1824 laNEKSNSQKNENGRALLERQNKELKakLAEIETAQRTKVKATiATLEAKIANLEEQLENEgkerllQQKANRKMDKKIK 1903
Cdd:TIGR01612 1588 --NDKSNKAAIDIQLSLENFENKFLK--ISDIKKKINDCLKET-ESIEKKISSFSIDSQDT------ELKENGDNLNSLQ 1656
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1904 ELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDEteeelqkektQKRKYQRE-CEDMIESQEAMNREINSLKTKLRRT 1982
Cdd:TIGR01612 1657 EFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQ----------HKKNYEIGiIEKIKEIAIANKEEIESIKELIEPT 1726
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1485-1669 |
1.09e-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: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1485 IELEAQRTKVLELEKKQKNFDKILAEekaiseqIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNEL 1564
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1565 DDLantqgtadKNVHELEkakrALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFErdllAKEEGAEEKRRG 1644
Cdd:COG1579 83 GNV--------RNNKEYE----ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA----ELEAELEEKKAE 146
|
170 180
....*....|....*....|....*
gi 386768643 1645 LVKQLRDLETELDEERKQRTAAVAS 1669
Cdd:COG1579 147 LDEELAELEAELEELEAEREELAAK 171
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1291-1484 |
1.14e-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: 49.37 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1291 LRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAE----LKASAAVKSASNMES 1366
Cdd:pfam09787 39 LDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEeqlaTERSARREAEAELER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1367 QLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLeeddeakrnyerklaevTTQMQEIKKKAEEDADLaKELEEGKK 1446
Cdd:pfam09787 119 LQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQL-----------------TSKSQSSSSQSELENRL-HQLTETLI 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 386768643 1447 RLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDAT 1484
Cdd:pfam09787 181 QKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGT 218
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1081-1234 |
1.30e-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: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1081 AKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATK--A 1158
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKeiE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 1159 TAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSL-DTTAAQQELRSKREQELATLKKSL 1234
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELaELEAELEELEAEREELAAKIPPEL 176
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1192-1946 |
1.34e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1192 RRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHEG-------VLADMRH-----KHSQELNSI 1259
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAasdhlnlVQTALRQqekieRYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1260 NDQLEnlrKAKTVLEKAKGTLEaenadlatelrsvnssrqENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQ- 1338
Cdd:PRK04863 361 EERLE---EQNEVVEEADEQQE------------------ENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1339 ----------------EAENITNQLEEAELKASAA----------VKSASNMESQLTEAQQLLE------------EETR 1380
Cdd:PRK04863 420 vqalerakqlcglpdlTADNAEDWLEEFQAKEQEAteellsleqkLSVAQAAHSQFEQAYQLVRkiagevsrseawDVAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1381 QKLGLSSKLRQIESEKEALQEQ---LEEDDEAKRNYERKLaevttqmQEIKKKAEEDADLAKELEEGKKRLNKDIEALER 1457
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRlseLEQRLRQQQRAERLL-------AEFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1458 QVKELIAQNDRLDKSKKKIQSELEdatiELEAQRTKVLE----LEKKQKNFDKILAEEKAISEQIAQ--ERdtaEREARE 1531
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQ----RLAARAPAWLAaqdaLARLREQSGEEFEDSQDVTEYMQQllER---ERELTV 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1532 KETKVLSVSRELDEafdKIEDLENKRKTLQNELDDLANTQGT-------ADKNVHE-------------------LEKAK 1585
Cdd:PRK04863 646 ERDELAARKQALDE---EIERLSQPGGSEDPRLNALAERFGGvllseiyDDVSLEDapyfsalygparhaivvpdLSDAA 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1586 RALESQlaelkaqnEELEDDLQLTEDaklrlevNMQALRS------QFERDLLAKEEGAEEK-----------RRGLVKQ 1648
Cdd:PRK04863 723 EQLAGL--------EDCPEDLYLIEG-------DPDSFDDsvfsveELEKAVVVKIADRQWRysrfpevplfgRAAREKR 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1649 LRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKedalkhakkLQAQVKDALRDaeeakaakeeLQALSKE 1728
Cdd:PRK04863 788 IEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVA---------FEADPEAELRQ----------LNRRRVE 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1729 AERKVKALEAEVLQLTEDLASSErarraaetERDELAEEIANNANkgsLMIDEkrRLEARIATLEEELEEEQSnSEVLLD 1808
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAK--------EGLSALNRLLPRLN---LLADE--TLADRVEEIREQLDEAEE-AKRFVQ 914
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1809 RSRKAQLQIEQLTTELANEKSNSqknengrALLERQNKELKAKLaeietaQRTKVKA-TIATLEAKIANL--EEQLENEG 1885
Cdd:PRK04863 915 QHGNALAQLEPIVSVLQSDPEQF-------EQLKQDYQQAQQTQ------RDAKQQAfALTEVVQRRAHFsyEDAAEMLA 981
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1886 KERLLQQKANRKMDKKIKELTMNIEDERRHVDQH---KEQMDKLNSRIKLLKRNLDETEEELQK 1946
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLaqyNQVLASLKSSYDAKRQMLQELKQELQD 1045
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1076-1546 |
1.47e-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: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1076 LAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADL-KEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEES 1154
Cdd:pfam07111 106 LAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1155 ATK----ATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDL------SEELEALKNELLDSL-------DTTAAQQ 1217
Cdd:pfam07111 186 AGEakqlAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQvppevhSQTWELERQELLDTMqhlqedrADLQATV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1218 ELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSIndqLENLRKAKTVLEKAKGTLEAENADLATELRSVNSS 1297
Cdd:pfam07111 266 ELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSL---LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1298 RQENDRRRKQAESQIAE-LQVKLAEIERAR---SELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQ 1373
Cdd:pfam07111 343 LQEQVTSQSQEQAILQRaLQDKAAEVEVERmsaKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMT 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1374 LLEEETRQKLGLSSKL----------RQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEE-DADLAKELE 1442
Cdd:pfam07111 423 RVEQAVARIPSLSNRLsyavrkvhtiKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRlDAELQLSAH 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1443 EGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQER 1522
Cdd:pfam07111 503 LIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEK 582
|
490 500
....*....|....*....|....
gi 386768643 1523 dTAEREAREKEtKVLSVSRELDEA 1546
Cdd:pfam07111 583 -VAEVETRLRE-QLSDTKRRLNEA 604
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1346-1496 |
1.52e-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: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1346 QLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTT--Q 1423
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768643 1424 MQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLE 1496
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1401-1703 |
1.55e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1401 EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSEL 1480
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1481 EDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERdtaereaREKETKVLSVSRElDEAFDKIEDLENKRKTL 1560
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLE-------WRQQTEVLSPEEE-KELVEKIKELEKELEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1561 QNElddlantqgtadknvHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSqfERDLLAKEegaee 1640
Cdd:COG1340 153 KKA---------------LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYK--EADELRKE----- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768643 1641 kRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQA 1703
Cdd:COG1340 211 -ADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1112-1373 |
1.55e-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: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1112 ETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEkaarakaekv 1191
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1192 RRDLSEELEALKNellDSLDTTAAQQELRSKreqelatlkkSLEEetvnhegvLADMRHKHSQELNSINDQLENLRKAKT 1271
Cdd:COG3883 85 REELGERARALYR---SGGSVSYLDVLLGSE----------SFSD--------FLDRLSALSKIADADADLLEELKADKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1272 VLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAE 1351
Cdd:COG3883 144 ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250 260
....*....|....*....|..
gi 386768643 1352 LKASAAVKSASNMESQLTEAQQ 1373
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAAAAAS 245
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1059-1613 |
1.56e-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: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1059 ANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQR----QESDRSKRKIE-------------TEVADLKEQ 1121
Cdd:COG3096 538 LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRselrQQLEQLRARIKelaarapawlaaqDALERLREQ 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1122 LNER---RVQVDEMQAQLAKREEELTQTLlriDEESATKATAQKAQRELeSQ--------------------LAEIQEDL 1178
Cdd:COG3096 618 SGEAladSQEVTAAMQQLLEREREATVER---DELAARKQALESQIERL-SQpggaedprllalaerlggvlLSEIYDDV 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1179 EAEKAAR-------AKAEKVRRDLS---EELEALKNELLDSL----------DTTAAQQEL------------------- 1219
Cdd:COG3096 694 TLEDAPYfsalygpARHAIVVPDLSavkEQLAGLEDCPEDLYliegdpdsfdDSVFDAEELedavvvklsdrqwrysrfp 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1220 ------RSKREQELATLKKSLEEETVNHEGVLADmrhkhSQELNSINDQLENLrkaktvleKAKGTLEAENADLATELRS 1293
Cdd:COG3096 774 evplfgRAAREKRLEELRAERDELAEQYAKASFD-----VQKLQRLHQAFSQF--------VGGHLAVAFAPDPEAELAA 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1294 VNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQekctKLQQEA-----ENITNQLEEAELKASAAvKSASNMESQL 1368
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLN----KLLPQAnlladETLADRLEELREELDAA-QEAQAFIQQH 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1369 TEAQQLLEEetrqklgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAdlAKELEEGKKrL 1448
Cdd:COG3096 916 GKALAQLEP-------LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDA--VGLLGENSD-L 985
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1449 NkdiEALERQVKELIAQNDRLDKSKKKIQSELEDATIELE----AQRTKVLELEKKQKNFDKI------LAEEKAISE-Q 1517
Cdd:COG3096 986 N---EKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELgvqadaEAEERARIRrD 1062
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1518 IAQERDTAEREAR-EKETKVLSVSRELDEAFDKIEDLENKRKTL-------------------QNELDDLANTQGTADKN 1577
Cdd:COG3096 1063 ELHEELSQNRSRRsQLEKQLTRCEAEMDSLQKRLRKAERDYKQEreqvvqakagwcavlrlarDNDVERRLHRRELAYLS 1142
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 386768643 1578 VHEL----EKAKRALesQLAElkAQNEELEDDLQLTEDAK 1613
Cdd:COG3096 1143 ADELrsmsDKALGAL--RLAV--ADNEHLRDALRLSEDPR 1178
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1292-1619 |
1.57e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1292 RSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEA 1371
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1372 QQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKD 1451
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1452 IEALERQVKELIAQndRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREARE 1531
Cdd:COG4372 166 LAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1532 KETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTED 1611
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
....*...
gi 386768643 1612 AKLRLEVN 1619
Cdd:COG4372 324 LAKKLELA 331
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1722-1897 |
1.71e-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: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1722 LQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKgslmIDEKRRLEARIATLEEELEEEQS 1801
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE----IEERREELGERARALYRSGGSVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1802 NSEVLL-------------------DRSRKAQLQIEQLTTELANEKSnsqKNENGRALLERQNKELKAKLAEIEtAQRTK 1862
Cdd:COG3883 104 YLDVLLgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKA---ELEAKLAELEALKAELEAAKAELE-AQQAE 179
|
170 180 190
....*....|....*....|....*....|....*
gi 386768643 1863 VKATIATLEAKIANLEEQLENEGKERLLQQKANRK 1897
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1399-1691 |
1.72e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1399 LQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADlakeleegkkRLNKDIEALERQVKELIAQNDRLDKSKKKIQS 1478
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA----------RKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1479 ELEDATIELEAQRTKVLELEKKQKNFDKILaeekaiseqiaqerdtaerEAREKETKVLSVSRELDEAFDKIEDLENKRK 1558
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKVI-------------------KMYEKGGVCPTCTQQISEGPDRITKIKDKLK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1559 TLQNELDDLANTQGTADKNVHELEKAKRALEsqlaELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDllaKEEga 1638
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFNEQSKKLL----ELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDN---AEE-- 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 386768643 1639 eekrrglVKQLRDLETELDEERkqrtaavaSKKKLEGDLKEIETTMEMHNKVK 1691
Cdd:PHA02562 381 -------LAKLQDELDKIVKTK--------SELVKEKYHRGIVTDLLKDSGIK 418
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1267-1441 |
1.76e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1267 RKAKTVLEKAKGTLEAENADLATElrsvnsSRQENDRRRKQAEsqiaelqvklAEIERARSELQEKCTKLQQEAENITNQ 1346
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEALLE------AKEEIHKLRNEFE----------KELRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1347 LEEAELKASAAVKSASNMESQLTEAQQL------LEEETRQKLGLSSKLRQiESEKEALQEQLEEddEAKrnyerklAEV 1420
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKeeeleeLIEEQLQELERISGLTA-EEAKEILLEKVEE--EAR-------HEA 171
|
170 180
....*....|....*....|..
gi 386768643 1421 TTQMQEIKKKAEEDAD-LAKEL 1441
Cdd:PRK12704 172 AVLIKEIEEEAKEEADkKAKEI 193
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1082-1693 |
1.86e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1082 KHEATISELEERLHKDQQ-------QRQESDRSKRKIETEVADLKEQLNERRVQVDEMQA-----QLAKREEELTQTLLR 1149
Cdd:PRK04863 352 RYQADLEELEERLEEQNEvveeadeQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTraiqyQQAVQALERAKQLCG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1150 IDEESATKAtaQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNeLLDSLDTTAAQQELRSK------- 1222
Cdd:PRK04863 432 LPDLTADNA--EDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRK-IAGEVSRSEAWDVARELlrrlreq 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1223 ---------REQELATLKKSLEEETvNHEGVLADMRHKHSQELNSiNDQLENLRKAktvlekakgtLEAENADLATELRS 1293
Cdd:PRK04863 509 rhlaeqlqqLRMRLSELEQRLRQQQ-RAERLLAEFCKRLGKNLDD-EDELEQLQEE----------LEARLESLSESVSE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1294 VNSSRQENDRRRKQAESQIAELqvklAEIERARSELQEKCTKLQQEAenitnqleeaelkaSAAVKSASNMESQLteaQQ 1373
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRL----AARAPAWLAAQDALARLREQS--------------GEEFEDSQDVTEYM---QQ 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1374 LLEEETrqklGLSSKLRQIESEKEALQEQLE--------EDDEAKRNYER----KLAE---------------------- 1419
Cdd:PRK04863 636 LLERER----ELTVERDELAARKQALDEEIErlsqpggsEDPRLNALAERfggvLLSEiyddvsledapyfsalygparh 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1420 --VTTQMQEIKKKAEEDADL--------------------AKELEE----------------------GKKRLNKDIEAL 1455
Cdd:PRK04863 712 aiVVPDLSDAAEQLAGLEDCpedlyliegdpdsfddsvfsVEELEKavvvkiadrqwrysrfpevplfGRAAREKRIEQL 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1456 ERQVKELIAQNDRLDKSKKKIQSELE----------------DATIELEAQRTKVLELEKKQKNFDKilaeekaiSEQIA 1519
Cdd:PRK04863 792 RAEREELAERYATLSFDVQKLQRLHQafsrfigshlavafeaDPEAELRQLNRRRVELERALADHES--------QEQQQ 863
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1520 QERDTAEREAREKETKVLSVSRELDEAF--DKIEDLENKRKTLQNELDDLANTQGTADKnvheLEKAKRALES---QLAE 1594
Cdd:PRK04863 864 RSQLEQAKEGLSALNRLLPRLNLLADETlaDRVEEIREQLDEAEEAKRFVQQHGNALAQ----LEPIVSVLQSdpeQFEQ 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1595 LKAQNEELEDDLQLTeDAKLRLEVNMQALRSQF----ERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASK 1670
Cdd:PRK04863 940 LKQDYQQAQQTQRDA-KQQAFALTEVVQRRAHFsyedAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQY 1018
|
730 740
....*....|....*....|....
gi 386768643 1671 KKLEGDLK-EIETTMEMHNKVKED 1693
Cdd:PRK04863 1019 NQVLASLKsSYDAKRQMLQELKQE 1042
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
943-1178 |
1.95e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 943 LAEQLQAEIELCAEAEESRSRLMARKQELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQL 1022
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1023 EKVQLDAKIKKYEEDLAltddqnqkLLKEKKLLEERANDLSQTLAEEEekAKHLAKLKAKHEATISELEERLHKDQQQRQ 1102
Cdd:COG4942 91 EIAELRAELEAQKEELA--------ELLRALYRLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768643 1103 ESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDL 1178
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
705-732 |
2.16e-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: 2.16e-05
10 20
....*....|....*....|....*...
gi 386768643 705 SHLYKEQLAKLMDTLRNTNPNFVRCIIP 732
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1322-1469 |
2.48e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.44 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1322 IERARSELQEKCTKLqqeaENITNQLEEAELKAsaavksasnmESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQE 1401
Cdd:PRK00409 504 IEEAKKLIGEDKEKL----NELIASLEELEREL----------EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLE 569
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768643 1402 QLEED-----DEAKRNYERKLAEVTTQMQEikkkaEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRL 1469
Cdd:PRK00409 570 EAEKEaqqaiKEAKKEADEIIKELRQLQKG-----GYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEEL 637
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1062-1436 |
2.55e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1062 LSQTLAEE----EEKAKHLAKLKA--KHEATISELEE---RLHK---------------DQQQRQESDRSKRK---IETE 1114
Cdd:PRK10246 459 RNAALNEMrqryKEKTQQLADVKTicEQEARIKDLEAqraQLQAgqpcplcgstshpavEAYQALEPGVNQSRldaLEKE 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1115 VADLKEQLNERRVQVDEMQAQLaKREEELTQTLLRidEESATKATAQKAQRELESQLAeIQEDLEAEKAARAKAEKVRRD 1194
Cdd:PRK10246 539 VKKLGEEGAALRGQLDALTKQL-QRDESEAQSLRQ--EEQALTQQWQAVCASLNITLQ-PQDDIQPWLDAQEEHERQLRL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1195 LSEELEaLKNELldsldttAAQQELRSKREQELATLKKSLEEE------TVNHEGVLADMRHKHSQELNSI---NDQLEN 1265
Cdd:PRK10246 615 LSQRHE-LQGQI-------AAHNQQIIQYQQQIEQRQQQLLTAlagyalTLPQEDEEASWLATRQQEAQSWqqrQNELTA 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1266 LRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLA-EIERARSELQEKCTKLQQEAENIT 1344
Cdd:PRK10246 687 LQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVlEAQRLQKAQAQFDTALQASVFDDQ 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1345 NQLEEAELKASAAvksasnmeSQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQM 1424
Cdd:PRK10246 767 QAFLAALLDEETL--------TQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQL 838
|
410
....*....|....*....
gi 386768643 1425 Q-------EIKKKAEEDAD 1436
Cdd:PRK10246 839 RenttrqgEIRQQLKQDAD 857
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1083-1269 |
2.61e-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: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1083 HEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELtqtllrideeSATKATAQK 1162
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQL----------ATERSARRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1163 AQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELrskrEQELATLKKSLEEETVNHE 1242
Cdd:pfam09787 112 AEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSEL----ENRLHQLTETLIQKQTMLE 187
|
170 180
....*....|....*....|....*..
gi 386768643 1243 GVladmrhkhSQELNSINDQLENLRKA 1269
Cdd:pfam09787 188 AL--------STEKNSLVLQLERMEQQ 206
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1160-1612 |
2.86e-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: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1160 AQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKnELLDSLdttaaQQELRSKREQeLATLKKSLEEETV 1239
Cdd:pfam06160 84 AKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELK-DKYREL-----RKTLLANRFS-YGPAIDELEKQLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1240 NHEGVLADMrhkhsQELNSINDQLEnlrkAKTVLEKAKGTLEAENADLAtelrsvnssrqendrrrkqaesQIAELQVKL 1319
Cdd:pfam06160 157 EIEEEFSQF-----EELTESGDYLE----AREVLEKLEEETDALEELME----------------------DIPPLYEEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1320 -AEIERARSELQEKCTKLQQEAENITNQLEEAELKAsaavksasnMESQLTEAQQLLEEETRQKLglSSKLRQIESEKEA 1398
Cdd:pfam06160 206 kTELPDQLEELKEGYREMEEEGYALEHLNVDKEIQQ---------LEEQLEENLALLENLELDEA--EEALEEIEERIDQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1399 LQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadLAKELEEGKKR--LNKD----IEALERQVKELIAQNDRLDK- 1471
Cdd:pfam06160 275 LYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKE---LKEELERVQQSytLNENelerVRGLEKQLEELEKRYDEIVEr 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1472 --SKKKIQSELEDatieleaqrtkvlELEKKQKNFDKILAEEKAISEQIAQERDtAEREAREketKVLSVSRELDEAFDK 1549
Cdd:pfam06160 352 leEKEVAYSELQE-------------ELEEILEQLEEIEEEQEEFKESLQSLRK-DELEARE---KLDEFKLELREIKRL 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768643 1550 IE---------DLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDA 1612
Cdd:pfam06160 415 VEksnlpglpeSYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATLAEQL 486
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1722-1968 |
3.06e-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: 48.97 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1722 LQALSKEAERKVKALEAEVLQLTEDLASSERARRAaeterdELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQS 1801
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVERRRKLEEAEKARQA------EMDRQAAIYAEQERMAMERERELERIRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1802 NSEVLLDRSRKAQLQIEQLTTELANEKSNsQKNENGRA--LLE----RQNKELKAKLAEIETAQRTKVKATIATLEAKIA 1875
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVR-QELEAARKvkILEeerqRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1876 N------LEEQLENEGKERLLQQKANRKMDK----KIKELTMNIEDERRHV-----DQHKEQMDKLNSRIKLLKRNLDE- 1939
Cdd:pfam17380 446 RemervrLEEQERQQQVERLRQQEEERKRKKleleKEKRDRKRAEEQRRKIlekelEERKQAMIEEERKRKLLEKEMEEr 525
|
250 260 270
....*....|....*....|....*....|...
gi 386768643 1940 ----TEEELQKEKTQKRKYQRECEDMIESQEAM 1968
Cdd:pfam17380 526 qkaiYEEERRREAEEERRKQQEMEERRRIQEQM 558
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1542-1778 |
3.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1542 ELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDL-QLTEDAKLRLEVNM 1620
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1621 QALRSQFERDLLAKEEGAEE--KRRGLVKQLRDLETELDEERKQRTAAVASKKKlegdlkeiettmemhnkvkedalkha 1698
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKA-------------------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1699 kKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLM 1778
Cdd:COG3883 151 -ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1730-1957 |
3.43e-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: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1730 ERKVKALEAEVLQLTEDLassERARRAAETERDELA--EEIANNANKGSLMIDEKRRLEARIATLeeeleeeqsnsevll 1807
Cdd:COG4913 220 EPDTFEAADALVEHFDDL---ERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAAL--------------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1808 dRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLENegke 1887
Cdd:COG4913 282 -RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE---- 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1888 rlLQQKANRkMDKKIKELTMNIEDER----RHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRE 1957
Cdd:COG4913 357 --RERRRAR-LEALLAALGLPLPASAeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1295-1488 |
3.45e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1295 NSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAEnitnQLEEAELKASAAVKSASNMESQLTEAQQL 1374
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK----QAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1375 LEEETRQKLGLSSKlrQIESEKEAlQEQLEEDDEAKRNYERKLAEVTTQ--MQEIKKKAEEDADLAKELEEGKKRLNKDI 1452
Cdd:PRK09510 148 KAEAEAKRAAAAAK--KAAAEAKK-KAEAEAAKKAAAEAKKKAEAEAAAkaAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
|
170 180 190
....*....|....*....|....*....|....*.
gi 386768643 1453 EALERQVKELIAQNDRLDKSKKKIQSELEDATIELE 1488
Cdd:PRK09510 225 AAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1354-1691 |
3.53e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1354 ASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEE 1433
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1434 DADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKA 1513
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1514 ISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLA 1593
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1594 ELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKL 1673
Cdd:COG4372 273 TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
330
....*....|....*...
gi 386768643 1674 EGDLKEIETTMEMHNKVK 1691
Cdd:COG4372 353 NDVLELLSKGAEAGVADG 370
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1061-1441 |
4.04e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1061 DLSQTLAEEEEKAKHLAKLKAKHEatISELEERLHKDQQQRQEsdrskrkIETEVADLKEQLNERRVQVDemqaQLAKRE 1140
Cdd:PRK04778 83 DIEEQLFEAEELNDKFRFRKAKHE--INEIESLLDLIEEDIEQ-------ILEELQELLESEEKNREEVE----QLKDLY 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1141 EELTQTLLrideesATKATAQKAQRELESQLAEIQEDLEAEKAAR-----AKAEKVRRDLSEELEALKN------ELLDS 1209
Cdd:PRK04778 150 RELRKSLL------ANRFSFGPALDELEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQimeeipELLKE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1210 LDTTAAQQ--ELRS---------------KREQELATLKKSLEE-----ETVNHEGVLADMRHKHSqELNSINDQLENLR 1267
Cdd:PRK04778 224 LQTELPDQlqELKAgyrelveegyhldhlDIEKEIQDLKEQIDEnlallEELDLDEAEEKNEEIQE-RIDQLYDILEREV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1268 KAKTVLEKAKGTL-------EAENADLATELRSVNSS----------RQENDRRRKQAESQIAELQVKLAEIERARSELQ 1330
Cdd:PRK04778 303 KARKYVEKNSDTLpdflehaKEQNKELKEEIDRVKQSytlneselesVRQLEKQLESLEKQYDEITERIAEQEIAYSELQ 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1331 EK----------CTKLQQEAENITNQLEEAELKASaavKSASNMESQLTEAQQLLEeetrqKLGL-------SSKLRQIE 1393
Cdd:PRK04778 383 EEleeilkqleeIEKEQEKLSEMLQGLRKDELEAR---EKLERYRNKLHEIKRYLE-----KSNLpglpedyLEMFFEVS 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1394 SEKEALQEQLEEddeAKRNYE---RKLAEVTTQMQEIKKKAEE---DADLAKEL 1441
Cdd:PRK04778 455 DEIEALAEELEE---KPINMEavnRLLEEATEDVETLEEETEElveNATLTEQL 505
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1815-1953 |
4.20e-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: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1815 LQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIEtAQRTKVKATIATLEAKIANLEEQLENEGKERLLQ--- 1891
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-KEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalq 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768643 1892 ------QKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRK 1953
Cdd:COG1579 96 keieslKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
891-1482 |
4.93e-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: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 891 KVKPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQE 970
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 971 LEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEqleeeeaarqklqlEKVQldAKIKKYEEDLALTDDQNQKLLK 1050
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--------------QKEQ--DWNKELKSELKNQEKKLEEIQN 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1051 EKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVD 1130
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1131 EMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSl 1210
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1211 dttaaQQELRSKrEQELatlkKSLEEETVNHEGVLADMRHKHSQELNSINDqlenlrkaktvLEKAKGTLEAENADLATE 1290
Cdd:TIGR04523 488 -----QKELKSK-EKEL----KKLNEEKKELEEKVKDLTKKISSLKEKIEK-----------LESEKKEKESKISDLEDE 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1291 LRSVNSSRQENDRRRKQAESQ--IAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKAsaavksasnmeSQL 1368
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNkeIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI-----------SSL 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1369 TEAQQLLEEETRQklgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKE-LEEGKKR 1447
Cdd:TIGR04523 616 EKELEKAKKENEK---LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDwLKELSLH 692
|
570 580 590
....*....|....*....|....*....|....*
gi 386768643 1448 LNKDIEALERqvkelIAQNDRLDKSKKKIQSELED 1482
Cdd:TIGR04523 693 YKKYITRMIR-----IKDLPKLEEKYKEIEKELKK 722
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
895-1126 |
5.30e-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: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 895 LLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKY----------QQALVEKTTLAEQLQAEI--------ELCAE 956
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEkallkqlaalERRIAALARRIRALEQELaaleaelaELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 957 AEESRSRLMARKQELEDMMQELETRIEEEEERVLalggekkkleLNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEE 1036
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALL----------LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1037 DLALTDDQNQkllkekklleeRANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVA 1116
Cdd:COG4942 162 LAALRAELEA-----------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
250
....*....|
gi 386768643 1117 DLKEQLNERR 1126
Cdd:COG4942 231 RLEAEAAAAA 240
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1127-1438 |
5.69e-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: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1127 VQVDEMQAQLAKREEELTQTL----LRIDEESAtKATAQKAQRELESQLAEI---QEDLEAEKAARAKAE-KVRRD-LSE 1197
Cdd:NF012221 1535 VATSESSQQADAVSKHAKQDDaaqnALADKERA-EADRQRLEQEKQQQLAAIsgsQSQLESTDQNALETNgQAQRDaILE 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1198 ELEALKNEL------LDSLDTTAAQQELRSKREQE------LATLKKSLEEeTVNHEGV-LADMRHKHSQELNSINDQLe 1264
Cdd:NF012221 1614 ESRAVTKELttlaqgLDALDSQATYAGESGDQWRNpfagglLDRVQEQLDD-AKKISGKqLADAKQRHVDNQQKVKDAV- 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1265 nlrkAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAeIERARSELQEKctklQQEAENIT 1344
Cdd:NF012221 1692 ----AKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAA-ANDAQSRGEQD----ASAAENKA 1762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1345 NQleeaelkASAAVKSASNMESqlteaqqllEEETRQKL---GLSSKLRQIESEKEALQeQLEEDDEAKRNyERKLAEVT 1421
Cdd:NF012221 1763 NQ-------AQADAKGAKQDES---------DKPNRQGAagsGLSGKAYSVEGVAEPGS-HINPDSPAAAD-GRFSEGLT 1824
|
330
....*....|....*..
gi 386768643 1422 TQMQEikkkAEEDADLA 1438
Cdd:NF012221 1825 EQEQE----ALEGATNA 1837
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1318-1525 |
6.11e-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: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1318 KLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKL-------------- 1383
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEeaekaadesergrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1384 GLSSKLRQIESEKEALQEQLEE----DDEAKRNYE---RKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALE 1456
Cdd:pfam00261 82 VLENRALKDEEKMEILEAQLKEakeiAEEADRKYEevaRKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768643 1457 RQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTA 1525
Cdd:pfam00261 162 ASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQT 230
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
897-1332 |
6.50e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 897 EVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERK-----YQQALVEKTTLAEQLQAEI-ELCAEAEESRSRLMARKQE 970
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREElekleKLLQLLPLYQELEALEAELaELPERLEELEERLEELREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 971 LEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLK 1050
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1051 EKKLLEER--ANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHkdqqQRQESDRSKRKIETEVADLKEQLNERRVQ 1128
Cdd:COG4717 242 EERLKEARllLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL----LFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1129 VDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDleaekaarakaeKVRRDLSEELEALKNELLD 1208
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE------------ELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1209 SLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADM-RHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADL 1287
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdEEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 386768643 1288 AT--ELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEK 1332
Cdd:COG4717 466 EEdgELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1264-1568 |
6.65e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1264 ENLRKAKTVLEKAKGTLEAENADLA---TELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEA 1340
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1341 ENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKrnYERKLAEV 1420
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE--AEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1421 TTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKK 1500
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768643 1501 QKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLA 1568
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1083-1440 |
7.39e-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: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1083 HEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQvDEMQAQLAKREEELTQTllriDEESATKATAQK 1162
Cdd:pfam09731 47 VLYALGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIP-RQSGVSSEVAEEEKEAT----KDAAEAKAQLPK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1163 AQRELESQLAEIQEDLEAE-----KAARAKAEKVRRDLSEELEALKNELLDSLD------TTAAQQELRSKRE--QELAT 1229
Cdd:pfam09731 122 SEQEKEKALEEVLKEAISKaesatAVAKEAKDDAIQAVKAHTDSLKEASDTAEIsrekatDSALQKAEALAEKlkEVINL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1230 LKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSV---------NSSRQE 1300
Cdd:pfam09731 202 AKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIfpdiipvlkEDNLLS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1301 NDR---------------RRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAEN-ITNQLEEAELKASAAV-KSASN 1363
Cdd:pfam09731 282 NDDlnsliahahreidqlSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEvRAADEAQLRLEFEREReEIRES 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 1364 MESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKE 1440
Cdd:pfam09731 362 YEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEKATSSHSEVEDE 438
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1315-1704 |
7.48e-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: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1315 LQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKsasNMESQLTEAQQLLEEETRQKLGLSSKLRQIES 1394
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRR---ELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1395 EKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadlaKELEegkkrlnkdIEALERQVKELIAQNDRLDKSKK 1474
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLE-----RETE---------LERMKERAKKAGAQRKEEEAERK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1475 KIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKEtkvlSVSRELDEAFDKIEDLE 1554
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE----ALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1555 NKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQlTEDAKLRLEVNMQALRSQ-FERDLLA 1633
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWA-QERETLQQSAEADKDRIEkLSAELQR 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1634 KEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQ 1704
Cdd:pfam07888 330 LEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQR 400
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1849-1967 |
8.43e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1849 KAKLAEIETAQRTKVKAtiATLEAKiaNLEEQLENEGKERLLQQKanRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNS 1928
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE--AKKEAE--AIKKEALLEAKEEIHKLR--NEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110
....*....|....*....|....*....|....*....
gi 386768643 1929 RIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEA 1967
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1637-1914 |
1.16e-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: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1637 GAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMemhnkvkedalkhakklqaqvkdalrdaeeak 1716
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1717 aakeelqalsKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIAnnankgslmidekRRLEARIATLEEEL 1796
Cdd:COG4942 65 ----------AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA-------------ELLRALYRLGRQPP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1797 EEEQSNSEVLLDRSRKAQL---QIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIEtAQRTKVKATIATLEAK 1873
Cdd:COG4942 122 LALLLSPEDFLDAVRRLQYlkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE-EERAALEALKAERQKL 200
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 386768643 1874 IANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERR 1914
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1095-1950 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1095 HKDQQQRQESDRSKRKIETEVADLKEQLnerrVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEI 1174
Cdd:TIGR01612 561 HEIKKELEEENEDSIHLEKEIKDLFDKY----LEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAIDLKKIIENNNAYI 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1175 QEDLEAE--------KAARAKAEKVRRDLSE----ELEALKNEL--------LDSLDTTAAQQELRSKREQELATLKkSL 1234
Cdd:TIGR01612 637 DELAKISpyqvpehlKNKDKIYSTIKSELSKiyedDIDALYNELssivkenaIDNTEDKAKLDDLKSKIDKEYDKIQ-NM 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1235 EEETV--------NHEGVLADM-----RHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADL------ATELRSV- 1294
Cdd:TIGR01612 716 ETATVelhlsnieNKKNELLDIiveikKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELnkykskISEIKNHy 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1295 -------NSSRQENDRRRKQAESQIAELQVK-------LAEIERARSELQEKCTKL----QQEAENITNQLEE-AEL--- 1352
Cdd:TIGR01612 796 ndqinidNIKDEDAKQNYDKSKEYIKTISIKedeifkiINEMKFMKDDFLNKVDKFinfeNNCKEKIDSEHEQfAELtnk 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1353 -KASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQ--EQLEEDDEAKRNYERKLAEVTTQmqEIKK 1429
Cdd:TIGR01612 876 iKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKicENTKESIEKFHNKQNILKEILNK--NIDT 953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1430 KAEEDADLAKELEEGKKRLNKDIEALERQVKELI-----AQNDRLDKSKKKIQSEL---EDATI--ELEAQRTKVLELEK 1499
Cdd:TIGR01612 954 IKESNLIEKSYKDKFDNTLIDKINELDKAFKDASlndyeAKNNELIKYFNDLKANLgknKENMLyhQFDEKEKATNDIEQ 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1500 KQKNFDKILAE-EKAISEQIAQERDTAEREA------------REKETKVLSVSrELDEA-----FDKIEDLENKRKTlq 1561
Cdd:TIGR01612 1034 KIEDANKNIPNiEIAIHTSIYNIIDEIEKEIgkniellnkeilEEAEINITNFN-EIKEKlkhynFDDFGKEENIKYA-- 1110
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1562 NEL----DDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDdlqltedaklrlevnmqalrsqferdlLAKEEG 1637
Cdd:TIGR01612 1111 DEInkikDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED---------------------------VADKAI 1163
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1638 AEEKRRGLVKQLRDLETELDEERKqrtaAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEeaka 1717
Cdd:TIGR01612 1164 SNDDPEEIEKKIENIVTKIDKKKN----IYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEK---- 1235
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1718 akeelqalsKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAE----EIANNANKGSLMIDEK--------RRL 1785
Cdd:TIGR01612 1236 ---------KKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEmetfNISHDDDKDHHIISKKhdenisdiREK 1306
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1786 EARIATLEEELEEEQSNSEVL---LDRSRKAQLQIEQLTTELAN----EKSNSQKN-----ENGRALLERQNKELKAKLA 1853
Cdd:TIGR01612 1307 SLKIIEDFSEESDINDIKKELqknLLDAQKHNSDINLYLNEIANiyniLKLNKIKKiidevKEYTKEIEENNKNIKDELD 1386
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1854 EIETAQRT-KVKATIATLEAKIanleeqlenegkERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKL 1932
Cdd:TIGR01612 1387 KSEKLIKKiKDDINLEECKSKI------------ESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLL 1454
|
970
....*....|....*...
gi 386768643 1933 LKRNLdeteeELQKEKTQ 1950
Cdd:TIGR01612 1455 LFKNI-----EMADNKSQ 1467
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1513-1730 |
1.23e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1513 AISEQIAQERDTAEREAREKETKVLSvsRELDEAFDKIEDLENKRKTL--QNELDDLANTQGTADKNVHELEKAKRALES 1590
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALEFLE--EQLPELRKELEEAEAALEEFrqKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1591 QLAELKAQNEELEDDLQLTEDAKLRLEVN--MQALRSQfERDLLAKEEGAEEK-------RRGLVKQLRDLETELDEERK 1661
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQ-LAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1662 QRTAAVASKKK-LEGDLKEIETTMEMHnkvkEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAE 1730
Cdd:COG3206 313 RILASLEAELEaLQAREASLQAQLAQL----EARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1376-1820 |
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 386768643 1376 EEETRQKLGLSSKLRQiesEKEALQEQLEEDDEAKRNYERKLAEVTtqmqeikkkaEEDADLAKELEEGKKRLNKDIEAL 1455
Cdd:PRK04863 278 ANERRVHLEEALELRR---ELYTSRRQLAAEQYRLVEMARELAELN----------EAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1456 ERQVKEliaqndrldkskKKIQSELEDATIELEAQrtkvlelekkqknfdkilaeeKAISEQIAQERDTAEREAREKETK 1535
Cdd:PRK04863 345 RQQEKI------------ERYQADLEELEERLEEQ---------------------NEVVEEADEQQEENEARAEAAEEE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1536 VLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEE---LEDDLQLTEDA 1612
Cdd:PRK04863 392 VDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEEllsLEQKLSVAQAA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1613 KLRLEVNMQALRSqferdlLAKEEGAEEKRRGLVKQLRDLeteldeeRKQRTAAvASKKKLEGDLKEIETTMEMHNKVKE 1692
Cdd:PRK04863 472 HSQFEQAYQLVRK------IAGEVSRSEAWDVARELLRRL-------REQRHLA-EQLQQLRMRLSELEQRLRQQQRAER 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1693 DALKHAKKLQAQVKDAlrdaeeakaakEELQALSKEAERKVKALEAEVlqltedlaSSERARRAA-ETERDELAEEIANN 1771
Cdd:PRK04863 538 LLAEFCKRLGKNLDDE-----------DELEQLQEELEARLESLSESV--------SEARERRMAlRQQLEQLQARIQRL 598
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768643 1772 ANK------------------GSLMIDEKRRLEARIATLEEELEEEQSNSEVlldRSRKAQL--QIEQL 1820
Cdd:PRK04863 599 AARapawlaaqdalarlreqsGEEFEDSQDVTEYMQQLLERERELTVERDEL---AARKQALdeEIERL 664
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1362-1620 |
1.38e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1362 SNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKEL 1441
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1442 EEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILA--EEKAISEQIA 1519
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1520 QERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQN 1599
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260
....*....|....*....|.
gi 386768643 1600 EELEDDLQLTEDAKLRLEVNM 1620
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEA 287
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
862-1152 |
1.44e-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: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 862 QQLNAIRIIQRNCAAYLKLRNWQWWRLYTKV----KPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQAL 937
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQIsalrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 938 VEKTTLAEQLQAEIElcaEAEESRSRLMARKQELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAAR 1017
Cdd:TIGR02168 778 AEAEAEIEELEAQIE---QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1018 QKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKhlaklkakheatisELEERLHKD 1097
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS--------------ELRRELEEL 920
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 386768643 1098 QQQRQESDRSKRKIETEVADLKEQLNER-RVQVDEMQAQLAKREEELTQTLLRIDE 1152
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1340-1606 |
1.53e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1340 AENITNQLEEAELKAS-AAVKSASNMESQLTEAQQLLEeetrQKLGLSSKLRQIESEKEALQEQLEEDDEakrnyerKLA 1418
Cdd:PRK11281 29 AASNGDLPTEADVQAQlDALNKQKLLEAEDKLVQQDLE----QTLALLDKIDRQKEETEQLKQQLAQAPA-------KLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1419 EVTTQMQEIKKKAEEDA--DLAK-ELEEGKKRLNKDIEALERQVKELIAQNDRLDKSkkkiQSELEDATIELEAQRTKVL 1495
Cdd:PRK11281 98 QAQAELEALKDDNDEETreTLSTlSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL----QTQPERAQAALYANSQRLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1496 ELEKKQKNF------------DKILAEEKAISEQIAQERdtAEREAREKETKVLSVSRELDEAfdKIEDLENKRKTLQNE 1563
Cdd:PRK11281 174 QIRNLLKGGkvggkalrpsqrVLLQAEQALLNAQNDLQR--KSLEGNTQLQDLLQKQRDYLTA--RIQRLEHQLQLLQEA 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 386768643 1564 LDD--LANTQGTAdKNVHELEKAKRALESQL--AELkAQNEELEDDL 1606
Cdd:PRK11281 250 INSkrLTLSEKTV-QEAQSQDEAARIQANPLvaQEL-EINLQLSQRL 294
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1664-1972 |
1.62e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1664 TAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQL 1743
Cdd:PRK10929 19 AATAPDEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1744 TEDLASSErarraaeterdelaeeiannankgslmidekrrLEARIatleeeleeEQSNSEvLLDRSRkaQLQIEQlttE 1823
Cdd:PRK10929 99 PPNMSTDA---------------------------------LEQEI---------LQVSSQ-LLEKSR--QAQQEQ---D 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1824 LANEKSNS------QKNENGRAL--LERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEeqlenegkerLLQQKAN 1895
Cdd:PRK10929 131 RAREISDSlsqlpqQQTEARRQLneIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELE----------LAQLSAN 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1896 RKmdkkiKELTmniedeRRHVDQHKEQMDKLNSRIKLLKRNLD---ETEEELQKEKTQKRKYQreCEDM---IESQEAMN 1969
Cdd:PRK10929 201 NR-----QELA------RLRSELAKKRSQQLDAYLQALRNQLNsqrQREAERALESTELLAEQ--SGDLpksIVAQFKIN 267
|
...
gi 386768643 1970 REI 1972
Cdd:PRK10929 268 REL 270
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1457-1894 |
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 386768643 1457 RQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKvleLEKKQKNFDKILAEEKAISEQIA---QERDTAEREAREKE 1533
Cdd:pfam19220 20 EDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEAL---LAQERAAYGKLRRELAGLTRRLSaaeGELEELVARLAKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1534 TKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLA-NTQGTADKNVHELEKAKrALESQLAELKAQNEELEDDLQLTEDA 1612
Cdd:pfam19220 97 AALREAEAAKEELRIELRDKTAQAEALERQLAAETeQNRALEEENKALREEAQ-AAEKALQRAEGELATARERLALLEQE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1613 KLRLEVNMQALRSQFERdLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKE 1692
Cdd:pfam19220 176 NRRLQALSEEQAAELAE-LTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1693 DALKHAKKLQAQVKDALRDAEEA----KAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAeei 1768
Cdd:pfam19220 255 ARAAATEQLLAEARNQLRDRDEAiraaERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLT--- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1769 annankgslmidekRRLEARIATLeeeleeeqsnsEVLLDRSRKAQLQIEQLTTELANEKsnsqknengrallerqnkel 1848
Cdd:pfam19220 332 --------------KALAAKDAAL-----------ERAEERIASLSDRIAELTKRFEVER-------------------- 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 386768643 1849 kaklaeietaqrtkvkatiATLEAKIANLEEQLENEGKERLLQQKA 1894
Cdd:pfam19220 367 -------------------AALEQANRRLKEELQRERAERALAQGA 393
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1365-1774 |
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 386768643 1365 ESQLTEAQQLL-EEETRQKLGLSSKLRQ--------IESEKEALQEQLEEDDEAKRNYERKLAevTTQMQEIKKKAEEDA 1435
Cdd:pfam18971 383 EDQLTGSQRALsQEEIRNKVDFMEFLAQnntkldnlSEKEKEKFQNEIEDFQKDSKAYLDALG--NDRIAFVSKKDTKHS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1436 DLAKELEEGKkrlnkdieaLERQVKELIAQNDR-LDKSKK-KIQSELE-DATIELEAQRTKvleLEKKQKNFDKILAEEK 1512
Cdd:pfam18971 461 ALITEFNNGD---------LSYTLKDYGKKADKaLDREKNvTLQGSLKhDGVMFVDYSNFK---YTNASKNPNKGVGATN 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1513 AISEQIAQERDTA-------------EREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL--ANTQGTADKN 1577
Cdd:pfam18971 529 GVSHLEAGFNKVAvfnlpdlnnlaitSFVRRNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFnkAVAEAKSTGN 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1578 VHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKR--------------- 1642
Cdd:pfam18971 609 YDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARaiaytqnlkgikrel 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1643 ----RGLVKQLRDLETELDE----ERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKE-----DALKHAKK--------- 1700
Cdd:pfam18971 689 sdklEKISKDLKDFSKSFDEfkngKNKDFSKAEETLKALKGSVKDLGINPEWISKVENlnaalNEFKNGKNkdfskvtqa 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1701 ---LQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETE------RDELAEEIANN 1771
Cdd:pfam18971 769 ksdLENSVKDVIINQKVTDKVDNLNQAVSVAKAMGDFSRVEQVLADLKNFSKEQLAQQAQKNEdfntgkNSELYQSVKNS 848
|
...
gi 386768643 1772 ANK 1774
Cdd:pfam18971 849 VNK 851
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
849-1353 |
2.09e-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: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 849 RGFLARRNYQKRLQQ--LNAIRIIQRNCAAYLKLRNWQWWRLYTKVKPLLEVTKQEEKLVQKEDELKQVREKldtlaknt 926
Cdd:TIGR00618 423 QGQLAHAKKQQELQQryAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA-------- 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 927 QEYERKYQQALVEKTTLaeQLQAEIELCAEAEESRSRLMARKQeledmmqeletrieeeeeRVLALGGEKKKLELNIQDL 1006
Cdd:TIGR00618 495 RLLELQEEPCPLCGSCI--HPNPARQDIDNPGPLTRRMQRGEQ------------------TYAQLETSEEDVYHQLTSE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1007 EEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTddqnqkllkekKLLEERANDLSQTLAEEEEK---AKHLAKLKAKH 1083
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL-----------QNITVRLQDLTEKLSEAEDMlacEQHALLRKLQP 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1084 EATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQaQLAKREEELTQTLLRIDEESATKATaqka 1163
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE-LLASRQLALQKMQSEKEQLTYWKEM---- 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1164 qrelesqLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDttAAQQELRSKREQELATLKKSLEEETVNHEG 1243
Cdd:TIGR00618 699 -------LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARED--ALNQSLKELMHQARTVLKARTEAHFNNNEE 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1244 VLADMrhKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATE-LRSVNSSRQENDRRRKQAESQIAELQVKLAEI 1322
Cdd:TIGR00618 770 VTAAL--QTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
490 500 510
....*....|....*....|....*....|....
gi 386768643 1323 ERARSELQEKCTKLQQ---EAENITNQLEEAELK 1353
Cdd:TIGR00618 848 THQLLKYEECSKQLAQltqEQAKIIQLSDKLNGI 881
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1372-1643 |
2.14e-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: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1372 QQLLEEETRQKLGLSSKLRQIESEKEAL----QEQL----EEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEE 1443
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARQAEMDRQAAiyaeQERMamerERELERIRQEERKRELERIRQEEIAMEISRMRELERLQME 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1444 GKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLEL-EKKQKNFDKILAEEKAISEQIAQER 1522
Cdd:pfam17380 387 RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLeEERAREMERVRLEEQERQQQVERLR 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1523 DTAEREAREK--------------ETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTqgtadknVHELEKAKRAL 1588
Cdd:pfam17380 467 QQEEERKRKKlelekekrdrkraeEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKA-------IYEEERRREAE 539
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 386768643 1589 ESQLAElkaqnEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRR 1643
Cdd:pfam17380 540 EERRKQ-----QEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1589-1984 |
2.84e-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: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1589 ESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLlakEEGAEEKRRGL--VKQLRDLETELDEERKQRTAA 1666
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQL---DRESDRNQELQkrIRLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1667 VASKKKLEgdlkeieTTMEMHNKVKEDALKHAKKLQAQVKDALRD-AEEAKAAKEELQALSKEAERKVKALE------AE 1739
Cdd:pfam05557 78 NRLKKKYL-------EALNKKLNEKESQLADAREVISCLKNELSElRRQIQRAELELQSTNSELEELQERLDllkakaSE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1740 VLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLeARIATLEEELEEEQSNSEVLldrsRKAQLQIEQ 1819
Cdd:pfam05557 151 AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERLREHNKHL----NENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1820 LTTELANEKSNSQKNENGR---ALLERQNKELKAKLAEIE-TAQRTK--------VKATIATLEAKIANLEEQLENEGKE 1887
Cdd:pfam05557 226 LKEEVEDLKRKLEREEKYReeaATLELEKEKLEQELQSWVkLAQDTGlnlrspedLSRRIEQLQQREIVLKEENSSLTSS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1888 RLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSR-------IKLLKRNLDETEEELQKEKT--QKRKYQREC 1958
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRvllltkeRDGYRAILESYDKELTMSNYspQLLERIEEA 385
|
410 420
....*....|....*....|....*.
gi 386768643 1959 EDMIESQEAMNREINSLKTKLRRTGG 1984
Cdd:pfam05557 386 EDMTQKMQAHNEEMEAQLSVAEEELG 411
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1543-1976 |
3.09e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1543 LDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQA 1622
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1623 LRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQR---TAAVASKKKLEG---DLKEIETTMEMHNKVK----- 1691
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiinDPVYKNRNYINDyfkYKNDIENKKQILSNIDaeink 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1692 -EDALKHAKKLQAQVKDALRDAEEAKAAKEEL----------QALSKEAERKVKALEAEVLQLTEDLASSERARRAAETE 1760
Cdd:PRK01156 324 yHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQIlelegyemdyNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEID 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1761 RDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSR-----------KAQLQIEQLTTELANEKS 1829
Cdd:PRK01156 404 PDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgeeKSNHIINHYNEKKSRLEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1830 NSQKNENGRALLERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANrKMDKKIKELTMNI 1909
Cdd:PRK01156 484 KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYE-EIKNRYKSLKLED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1910 EDERRH-------------VDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLK 1976
Cdd:PRK01156 563 LDSKRTswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENK 642
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1491-1704 |
3.17e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1491 RTKVLELEKKqknFDKILAEEKAISEQIAQErdtAEREAREKETKVLS-VSRELDEAFDKIEDLENKrktLQNELDDLAN 1569
Cdd:PRK12704 30 EAKIKEAEEE---AKRILEEAKKEAEAIKKE---ALLEAKEEIHKLRNeFEKELRERRNELQKLEKR---LLQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1570 TQGTADKNVHELEKAKRALESQLAELKAQNEELEddlQLTEDAKLRLEVNMQalrsqferdlLAKEEGAEEkrrglvkQL 1649
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELE---ELIEEQLQELERISG----------LTAEEAKEI-------LL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386768643 1650 RDLETELDEERKQRtaavaskkklegdLKEIEttmemhNKVKEDALKHAKKLQAQ 1704
Cdd:PRK12704 161 EKVEEEARHEAAVL-------------IKEIE------EEAKEEADKKAKEILAQ 196
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1550-1711 |
3.60e-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: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1550 IEDLENKRKTLQNELDDLANTqgTADKNVHELEKAKRALESQLAELKAQNEELEDDLqltEDAKLRLEvnmqalRSQFER 1629
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKE--HEERELTEEEEEIRRLEEQVERLEAEVEELEAEL---EEKDERIE------RLEREL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1630 DLLAKEEGAEEKRRGLVKQLR----DLETELDEERKQRtaavaskKKLEGDLKEIEttmEMHNKVKEDALKHAKKLQAQV 1705
Cdd:COG2433 451 SEARSEERREIRKDREISRLDreieRLERELEEERERI-------EELKRKLERLK---ELWKLEHSGELVPVKVVEKFT 520
|
....*.
gi 386768643 1706 KDALRD 1711
Cdd:COG2433 521 KEAIRR 526
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
927-1669 |
4.13e-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: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 927 QEYERKYQQALVEkttLAEQLQAEIELCAEAEESRSRLMARKQELE-----------------DMMQELETRIEEEeerV 989
Cdd:COG3096 346 QEKIERYQEDLEE---LTERLEEQEEVVEEAAEQLAEAEARLEAAEeevdslksqladyqqalDVQQTRAIQYQQA---V 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 990 LALGGEKKKLELNIQDLEEQLEEEEAARQKLQlekvQLDAKIKKYEEDLALTDDQNQK--------LLKEKKLLEERAND 1061
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQ----QATEEVLELEQKLSVADAARRQfekayelvCKIAGEVERSQAWQ 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1062 LSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADlkeqlnerRVQVDEMQAQLAKREE 1141
Cdd:COG3096 496 TARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA--------AEELEELLAELEAQLE 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1142 ELTQTLlrideesatkATAQKAQRELESQLaeiqEDLEAEKAARAKAEKVRRDLSEELEALKNE----LLDSLDTTAA-Q 1216
Cdd:COG3096 568 ELEEQA----------AEAVEQRSELRQQL----EQLRARIKELAARAPAWLAAQDALERLREQsgeaLADSQEVTAAmQ 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1217 QELRSKRE-----QELATLKKSLEE--ETVNHEGVLADMR----------------------------------HKHS-- 1253
Cdd:COG3096 634 QLLEREREatverDELAARKQALESqiERLSQPGGAEDPRllalaerlggvllseiyddvtledapyfsalygpARHAiv 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1254 -QELNSINDQLENL-----------RKAKTVLEKAKGTLEAENADLAtelrsVNSSRQENDRR--------RKQAESQIA 1313
Cdd:COG3096 714 vPDLSAVKEQLAGLedcpedlylieGDPDSFDDSVFDAEELEDAVVV-----KLSDRQWRYSRfpevplfgRAAREKRLE 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1314 ELQVKLAEIERARSEL---QEKCTKLQQEAEN-ITNQLE-------EAELKASAAvksasnmesQLTEAQQLLEEETRQK 1382
Cdd:COG3096 789 ELRAERDELAEQYAKAsfdVQKLQRLHQAFSQfVGGHLAvafapdpEAELAALRQ---------RRSELERELAQHRAQE 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1383 LGLSSKLRQIESEKEALQ------EQLEEDDEAKRNYErklaevttqmqeikkkAEEDADLAKELEEGKKRLNKDIEALE 1456
Cdd:COG3096 860 QQLRQQLDQLKEQLQLLNkllpqaNLLADETLADRLEE----------------LREELDAAQEAQAFIQQHGKALAQLE 923
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1457 RQVKELiaQNDRLdkSKKKIQSELEDATIELEAQRTKVLELEKKQKNFD--------KILAEEKAISEQIAQERDTAERE 1528
Cdd:COG3096 924 PLVAVL--QSDPE--QFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyedavGLLGENSDLNEKLRARLEQAEEA 999
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1529 AREKETKVLSVSRELDEAFDKIEDL----ENKRKTLQNELDDLANTQGTADKNVHELEKAKRA-LESQLAELKAQNEELE 1603
Cdd:COG3096 1000 RREAREQLRQAQAQYSQYNQVLASLkssrDAKQQTLQELEQELEELGVQADAEAEERARIRRDeLHEELSQNRSRRSQLE 1079
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768643 1604 DDLQLTEdaklrlevnmqalrsqferdllakeegAEekRRGLVKQLRDLETELDEERKQRTAAVAS 1669
Cdd:COG3096 1080 KQLTRCE---------------------------AE--MDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1058-1236 |
4.28e-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: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1058 RANDLSQTLAEEEEKakhLAKLKAKH------------EATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNER 1125
Cdd:COG3206 183 QLPELRKELEEAEAA---LEEFRQKNglvdlseeakllLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1126 R--VQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQL-AEIQEDLEAEKAARAKAEKVRRDLSEELEAL 1202
Cdd:COG3206 260 LqsPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 386768643 1203 KNELldsLDTTAAQQELRS-KREQELA-----TLKKSLEE 1236
Cdd:COG3206 340 EARL---AELPELEAELRRlEREVEVArelyeSLLQRLEE 376
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1224-1640 |
5.46e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1224 EQELATLKKSLEEETvNHEGVLADMRHKHSQELNSINDQLE----------NLRKAKTVLEKAKGTLEA-ENADLATELR 1292
Cdd:PRK10246 215 PEQVQSLTASLQVLT-DEEKQLLTAQQQQQQSLNWLTRLDElqqeasrrqqALQQALAAEEKAQPQLAAlSLAQPARQLR 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1293 SVNSSRQENDRRRKQAESQIAELQVKLAEIERARSEL----QEKCTKLQQEAENITNQLEE--------AELKASAAVKS 1360
Cdd:PRK10246 294 PHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIrhhaAKQSAELQAQQQSLNTWLAEhdrfrqwnNELAGWRAQFS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1361 A-SNMESQLTEAQQLLEEETRQKLGL-----------SSKLRQIESEKEALQEQ---LEEDDEAKRNYERKLAEVTTQMQ 1425
Cdd:PRK10246 374 QqTSDREQLRQWQQQLTHAEQKLNALpaitltltadeVAAALAQHAEQRPLRQRlvaLHGQIVPQQKRLAQLQVAIQNVT 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1426 EIKKKAEEDADLAKELEEGKKRLNKDIEAL---ERQVKELIAQNDRLDKSKKkiqSELEDAT----------IELEAQRT 1492
Cdd:PRK10246 454 QEQTQRNAALNEMRQRYKEKTQQLADVKTIceqEARIKDLEAQRAQLQAGQP---CPLCGSTshpaveayqaLEPGVNQS 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1493 KVLELEKKQKNfdkiLAEE--------KAISEQIAQERDTAEREAREKETkvlsvsreLDEAFDKIEDLENKRKTLQNEL 1564
Cdd:PRK10246 531 RLDALEKEVKK----LGEEgaalrgqlDALTKQLQRDESEAQSLRQEEQA--------LTQQWQAVCASLNITLQPQDDI 598
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 1565 DDLANTQGTADKNVHELEKaKRALESQLAELKAQNEELEDDLQLTEdaklrlevnmQALRSQFER-DLLAKEEGAEE 1640
Cdd:PRK10246 599 QPWLDAQEEHERQLRLLSQ-RHELQGQIAAHNQQIIQYQQQIEQRQ----------QQLLTALAGyALTLPQEDEEA 664
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1555-1906 |
5.83e-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: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1555 NKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDaklRLEVNMQALRSQ-----FER 1629
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASD---HLNLVQTALRQQekierYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1630 DLLAKEEGAEEKrrglVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMhnkvkedalKHAKKLQ-AQVKDA 1708
Cdd:COG3096 355 DLEELTERLEEQ----EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDV---------QQTRAIQyQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1709 LRDAeeakaakeelQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETeRDELAEEIANNankgslmIDEKRRLEAR 1788
Cdd:COG3096 422 LEKA----------RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQ-KLSVADAARRQ-------FEKAYELVCK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1789 IATLEEELEEEQSNSEVLLD-RSRKAQL-QIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETaqrtkVKAT 1866
Cdd:COG3096 484 IAGEVERSQAWQTARELLRRyRSQQALAqRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-----LEEL 558
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 386768643 1867 IATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELT 1906
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA 598
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1722-1882 |
6.37e-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: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1722 LQALSKEAERKVKALEAEVLQLTEDLASSERARRA---------AETERDELAEEIANNANKGSLMIDEKRRLEARIATL 1792
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1793 EEELEEEQSNSEVLLDRSRKAQL--QIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKVKATIATL 1870
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLraQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEAL 325
|
170
....*....|..
gi 386768643 1871 EAKIANLEEQLE 1882
Cdd:COG3206 326 QAREASLQAQLA 337
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1256-1616 |
6.69e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1256 LNSINDQLENLRKAKTV------LEKAKGTLEAENADLATELRSVNSSrqendrrrkqaeSQIAELQvklAEIERARSEL 1329
Cdd:PRK10929 54 LNWLEERKGSLERAKQYqqvidnFPKLSAELRQQLNNERDEPRSVPPN------------MSTDALE---QEILQVSSQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1330 QEKCTKLQQEAEnitnqleeaelKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSS--------KLRQIESEKEALQE 1401
Cdd:PRK10929 119 LEKSRQAQQEQD-----------RAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTpntplaqaQLTALQAESAALKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1402 QLEEDDEAK--RNYERKLAEVTTqmqEIKKKAEEDADLakELEEGKKRLN----KDIE-ALERqvKELIA-QNDRLDKSK 1473
Cdd:PRK10929 188 LVDELELAQlsANNRQELARLRS---ELAKKRSQQLDA--YLQALRNQLNsqrqREAErALES--TELLAeQSGDLPKSI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1474 KKiqseledatiELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDT--AEREarekETKVLSVSRELDEAF-DKI 1550
Cdd:PRK10929 261 VA----------QFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQAlnTLRE----QSQWLGVSNALGEALrAQV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1551 EDLENKRKTLQneLD--------------DLANTQGTADKNVHE----LEKA-KRALESQlaeLKAQNEELED-----DL 1606
Cdd:PRK10929 327 ARLPEMPKPQQ--LDtemaqlrvqrlryeDLLNKQPQLRQIRQAdgqpLTAEqNRILDAQ---LRTQRELLNSllsggDT 401
|
410
....*....|
gi 386768643 1607 QLTEDAKLRL 1616
Cdd:PRK10929 402 LILELTKLKV 411
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1368-1531 |
6.79e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1368 LTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERklaevttqmqEIKKKAEEDADLAKELEEGKKR 1447
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEK----------ELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1448 LNKDIEALERQVKELIAQNDRLDKSKKkiqseledatieleaqrtkvlELEKKQKNFDKILAEEKAISEQIAQErdTAEr 1527
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQ---------------------ELEKKEEELEELIEEQLQELERISGL--TAE- 153
|
....
gi 386768643 1528 EARE 1531
Cdd:PRK12704 154 EAKE 157
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1305-1652 |
7.16e-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: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1305 RKQAESQIAELQVKLAEIERARSE-LQEKCTKLQQEAENITNQLEEAELKASAAVKSASNM---ESQLTEAQQLLEEETR 1380
Cdd:pfam09731 105 EKEATKDAAEAKAQLPKSEQEKEKaLEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSlkeASDTAEISREKATDSA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1381 QKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVK 1460
Cdd:pfam09731 185 LQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1461 ELI------------AQNDRLDKSKKKIQSELEDATIELEAQRTKV-----LELEKKQKNFDKILAE-----EKAISEQI 1518
Cdd:pfam09731 265 SIFpdiipvlkednlLSNDDLNSLIAHAHREIDQLSKKLAELKKREekhieRALEKQKEELDKLAEElsarlEEVRAADE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1519 AQERDTAEREaREKETKVL--SVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKnvheLEKAKRALESQLAELK 1596
Cdd:pfam09731 345 AQLRLEFERE-REEIRESYeeKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEK----VEEERAGRLLKLNELL 419
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768643 1597 AQNEELE---DDLQLTEDAKLR---LEVNMQALRSQFERdllakeEGAEEKRRGLVKQLRDL 1652
Cdd:pfam09731 420 ANLKGLEkatSSHSEVEDENRKaqqLWLAVEALRSTLED------GSADSRPRPLVRELKAL 475
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1441-1981 |
7.38e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1441 LEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIEL-----EAQRTKVLELEKKQKNFD--KILAEEKA 1513
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYnnlksALNELSSLEDMKNRYESEikTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1514 ISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNeLDDLANTQGTADKNVHELE----------K 1583
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSN-IDAEINKYHAIIKKLSVLQkdyndyikkkS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1584 AKRALESQLAELKAQNEELEDDLQLTEDAKLRLE---VNMQALRSQFERDLLAKEEGAEEkrrgLVKQLRDLETELDEER 1660
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEeysKNIERMSAFISEILKIQEIDPDA----IKKELNEINVKLQDIS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1661 KQRTAAVASKKKLEGDLKEIETTMEM---HNK-------VKEDALKHAKKLQAQVKDALRDAEeakaakeelqalsKEAE 1730
Cdd:PRK01156 423 SKVSSLNQRIRALRENLDELSRNMEMlngQSVcpvcgttLGEEKSNHIINHYNEKKSRLEEKI-------------REIE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1731 RKVKALEAEVLQLT---EDLASSERARRAAETERDELAEeiannANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLl 1807
Cdd:PRK01156 490 IEVKDIDEKIVDLKkrkEYLESEEINKSINEYNKIESAR-----ADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDL- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1808 DRSRKAQLQIEQLTTELANEKSNSQKNEngralLERQNKELKAKLAEIETaQRTKVKATIATLEAKIANLEEQLENEGKE 1887
Cdd:PRK01156 564 DSKRTSWLNALAVISLIDIETNRSRSNE-----IKKQLNDLESRLQEIEI-GFPDDKSYIDKSIREIENEANNLNNKYNE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1888 RLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEqmdkLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEA 1967
Cdd:PRK01156 638 IQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE----ITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE 713
|
570
....*....|....
gi 386768643 1968 MNREINSLKTKLRR 1981
Cdd:PRK01156 714 LSDRINDINETLES 727
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1366-1504 |
7.59e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1366 SQLTEAQQLLEEETRQKLGLSSKLRQIE---SEKEALQEQLEEDDEAKrnyERKLAEVTTQMQEIKKKAEEDADLAKELE 1442
Cdd:PRK09039 60 SQIAELADLLSLERQGNQDLQDSVANLRaslSAAEAERSRLQALLAEL---AGAGAAAEGRAGELAQELDSEKQVSARAL 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768643 1443 EGKKRLNKDIEALERQvkeLIAQNDRLDKSKKKIQSelEDATIELEAQR------TKVLELEKKQKNF 1504
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 ... |
1254-1685 |
7.71e-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: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1254 QELNSINDQL----ENLRKAKTVLEKAKGTLEAENADL---ATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERAR 1326
Cdd:pfam05622 3 SEAQEEKDELaqrcHELDQQVSLLQEEKNSLQQENKKLqerLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1327 SELQEKC-------TKLQQEAENITNQLEEAE-LKASAAVKSASNMESQLTEAQQlleEETRQKLG-LSSKLRQI----E 1393
Cdd:pfam05622 83 DDYRIKCeelekevLELQHRNEELTSLAEEAQaLKDEMDILRESSDKVKKLEATV---ETYKKKLEdLGDLRRQVklleE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1394 SEKEALQEQLEEDDEAKR--NYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRL-- 1469
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKanALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLre 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1470 -----------DKSKKKIQSELEDATIELEAQRTKVLELEKKQKnFDKILAEEKAISEQiaQERDTAEREAreketkvlS 1538
Cdd:pfam05622 240 tneelrcaqlqQAELSQADALLSPSSDPGDNLAAEIMPAEIREK-LIRLQHENKMLRLG--QEGSYRERLT--------E 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1539 VSRELDEAFDKIEDLENKRKT-------LQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTED 1611
Cdd:pfam05622 309 LQQLLEDANRRKNELETQNRLanqrileLQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEE 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768643 1612 AKLRLEVNMQALRSQFERDLLAKEE---GAEEKRRGLVKQLRDLETELDEerKQRTAAVASKKKLEGDLKEIETTME 1685
Cdd:pfam05622 389 LEPKQDSNLAQKIDELQEALRKKDEdmkAMEERYKKYVEKAKSVIKTLDP--KQNPASPPEIQALKNQLLEKDKKIE 463
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1306-1551 |
8.07e-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: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1306 KQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITN--QLEEAEL-KASAAVKSASnmeSQLTEAQQLLEEETRQK 1382
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRriQLLEEELeRTEERLAEAL---EKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1383 LGLSSKLRQIESEKEALQEQLEE----DDEAKRNYE---RKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEAL 1455
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEakeiAEEADRKYEevaRKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1456 ERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKkqknfdkilaeekaiseqiaqERDTAEREAREKETK 1535
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEK---------------------EVDRLEDELEAEKEK 219
|
250
....*....|....*.
gi 386768643 1536 VLSVSRELDEAFDKIE 1551
Cdd:pfam00261 220 YKAISEELDQTLAELN 235
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1193-1537 |
8.09e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1193 RDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETvnhegvladmrhkhsQELNSINDQLENLRKAKTV 1272
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN---------------EQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1273 LEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAEL 1352
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1353 KASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAE 1432
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1433 EDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEK 1512
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
330 340
....*....|....*....|....*
gi 386768643 1513 AISEQIAQERDTAEREAREKETKVL 1537
Cdd:COG4372 346 LLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1360-1548 |
9.27e-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: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1360 SASNMESQLTEAQQLLEEEtrqklglsskLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEE-----D 1434
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQA----------IRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAaltkgN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1435 ADLAKELEEGKKRLNKDIEALERQVKEliaQNDRLDKSKKKIQsELEDATIELEAQRTKVLELEKKQKNFDKI------L 1508
Cdd:pfam04012 82 EELAREALAEKKSLEKQAEALETQLAQ---QRSAVEQLRKQLA-ALETKIQQLKAKKNLLKARLKAAKAQEAVqtslgsL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 386768643 1509 AEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFD 1548
Cdd:pfam04012 158 STSSATDSFERIEEKIEEREARADAAAELASAVDLDAKLE 197
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1707-1981 |
9.58e-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: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1707 DALRDAEEAKAAKEELQALSKEaerkVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKR-RL 1785
Cdd:pfam12128 231 QAIAGIMKIRPEFTKLQQEFNT----LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRdEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1786 EARIATLEEELEEEQSNSEVLLDRSRK-AQLQIEQLTTELANEKSNSQKNENgralLERQNKELKAKLAEIETAQRTKVK 1864
Cdd:pfam12128 307 NGELSAADAAVAKDRSELEALEDQHGAfLDADIETAAADQEQLPSWQSELEN----LEERLKALTGKHQDVTAKYNRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1865 ATIATLEAKIANLEEQLENEGKERLLQQKANRK-MDKKIKELTMNIEDERRHVdqhKEQMDKLNSRIKLLKRNLDETEEE 1943
Cdd:pfam12128 383 KIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDdLQALESELREQLEAGKLEF---NEEEYRLKSRLGELKLRLNQATAT 459
|
250 260 270
....*....|....*....|....*....|....*...
gi 386768643 1944 lQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1981
Cdd:pfam12128 460 -PELLLQLENFDERIERAREEQEAANAEVERLQSELRQ 496
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1305-1502 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1305 RKQaESQIAELQVKLAEIERARSELQEKCTKlQQEAENITNQLEE-----------AELKASAAVKSASNMESQLTEAQQ 1373
Cdd:pfam15066 328 RKQ-QMQIQDLQCSNLYLEKKVKELQMKITK-QQVFVDIINKLKEnveeliedkynVILEKNDINKTLQNLQEILANTQK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1374 LLEEetrqklglsSKLrqiesEKEALQEQLEeddEAKRNYERKLAEVTTQMQEIKKKA----EEDADLAKElEEGKKRLN 1449
Cdd:pfam15066 406 HLQE---------SRK-----EKETLQLELK---KIKVNYVHLQERYITEMQQKNKSVsqclEMDKTLSKK-EEEVERLQ 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386768643 1450 KDIEALERqvkeliAQNDRLD--KSKKKIQsELEDATIELEAQRTKVLELEKKQK 1502
Cdd:pfam15066 468 QLKGELEK------ATTSALDllKREKETR-EQEFLSLQEEFQKHEKENLEERQK 515
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1102-1283 |
1.21e-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: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1102 QESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEdleae 1181
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1182 kaarakaekvrrdlSEELEALKNElldsLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSIND 1261
Cdd:COG1579 88 --------------NKEYEALQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|..
gi 386768643 1262 QLENLRKAKTVLEKAKGTLEAE 1283
Cdd:COG1579 150 ELAELEAELEELEAEREELAAK 171
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1295-1465 |
1.21e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.85 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1295 NSSRQENDRRRKQAESQIaELQVKL--AEIERARSELqekctkLQQEAENitnqleeAELKASAAVKSASNMESqltEAQ 1372
Cdd:PTZ00491 666 AAARHQAELLEQEARGRL-ERQKMHdkAKAEEQRTKL------LELQAES-------AAVESSGQSRAEALAEA---EAR 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1373 QLLEEETRQKLGLSSKLRQIEseKEALQEQLEEDDEAKRNYERKLAEVttqmqEIKKkaeedadlAKELEEGK-KRLNKD 1451
Cdd:PTZ00491 729 LIEAEAEVEQAELRAKALRIE--AEAELEKLRKRQELELEYEQAQNEL-----EIAK--------AKELADIEaTKFERI 793
|
170
....*....|....
gi 386768643 1452 IEALERQVKELIAQ 1465
Cdd:PTZ00491 794 VEALGRETLIAIAR 807
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1440-1805 |
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 386768643 1440 ELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILaeekaisEQIA 1519
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-------EELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1520 QERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQN 1599
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1600 EELEDDLQLTEDAKLRLEVNMqalrsqferdLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKE 1679
Cdd:COG4372 167 AALEQELQALSEAEAEQALDE----------LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1680 IETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAET 1759
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 386768643 1760 ERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEV 1805
Cdd:COG4372 317 LLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKG 362
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1365-1609 |
1.35e-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: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1365 ESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEG 1444
Cdd:pfam00261 7 KEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1445 KKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAqrtkvlelekkqknfdkilAEEKAiseqiaqerDT 1524
Cdd:pfam00261 87 ALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLER-------------------AEERA---------EL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1525 AEREAREKETKVLSVSREL-------DEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKA 1597
Cdd:pfam00261 139 AESKIVELEEELKVVGNNLksleaseEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|..
gi 386768643 1598 QNEELEDDLQLT 1609
Cdd:pfam00261 219 KYKAISEELDQT 230
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1287-1532 |
1.63e-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: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1287 LATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENIT--NQLEEAELKASAAVKSASNM 1364
Cdd:pfam15905 78 LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTrvNELLKAKFSEDGTQKKMSSL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1365 ESQLTEAQQLLEEETRQklgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEG 1444
Cdd:pfam15905 158 SMELMKLRNKLEAKMKE---VMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCV 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1445 KKRLNKDIEALeRQVKELIAQNDRLDKSkkkIQSELEDATIELEAQ------RTKVLELEKKQK-NFDKILAEEKAISEQ 1517
Cdd:pfam15905 235 SEQVEKYKLDI-AQLEELLKEKNDEIES---LKQSLEEKEQELSKQikdlneKCKLLESEKEELlREYEEKEQTLNAELE 310
|
250
....*....|....*
gi 386768643 1518 IAQERDTAEREAREK 1532
Cdd:pfam15905 311 ELKEKLTLEEQEHQK 325
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1496-1888 |
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 386768643 1496 ELEKKQKNFDKILAEEKaisEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDdlantqgtad 1575
Cdd:pfam07888 45 ELLQAQEAANRQREKEK---ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE---------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1576 knvhELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKrrglvkqlRDLETE 1655
Cdd:pfam07888 112 ----ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER--------KQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1656 LDEERKQRTAAVASKKKLEGDLKEIET-TMEMHNKVKEDALKHAkklQAQVKDAlrDAEEAKAAKEELQALSKEAERKVK 1734
Cdd:pfam07888 180 LQQTEEELRSLSKEFQELRNSLAQRDTqVLQLQDTITTLTQKLT---TAHRKEA--ENEALLEELRSLQERLNASERKVE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1735 ALEAEVLQLtedlaSSERARRAAETERDEL-AEEIANNANKGSLMIDEKRrleariATLEEELEEEQSNSEVLLDRSRKA 1813
Cdd:pfam07888 255 GLGEELSSM-----AAQRDRTQAELHQARLqAAQLTLQLADASLALREGR------ARWAQERETLQQSAEADKDRIEKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1814 QLQIEQLTTELANEKSNSQKNE--------NGRALLERQNKELKAKLAEIETAQRTK--VKATIATLEAKIANLEEQLEN 1883
Cdd:pfam07888 324 SAELQRLEERLQEERMEREKLEvelgrekdCNRVQLSESRRELQELKASLRVAQKEKeqLQAEKQELLEYIRQLEQRLET 403
|
....*
gi 386768643 1884 EGKER 1888
Cdd:pfam07888 404 VADAK 408
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1198-1583 |
1.76e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1198 ELEALKNELLDSLDTTAAQ-QELRSKREQELATLKKSLEEETVNHEgvladmrhKHSQELNSINDQLENLRKAKTVLEKA 1276
Cdd:PTZ00440 1081 LLEEKVEALLKKIDENKNKlIEIKNKSHEHVVNADKEKNKQTEHYN--------KKKKSLEKIYKQMEKTLKELENMNLE 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1277 KGTL-EAENADLATELRSVNSSRQendrrrkQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKAS 1355
Cdd:PTZ00440 1153 DITLnEVNEIEIEYERILIDHIVE-------QINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDHLTTFEYNAYYDK 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1356 AAVKSAsNMESQLTEAQQLLEEETRqklglSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTT-----QMQEIKKK 1430
Cdd:PTZ00440 1226 ATASYE-NIEELTTEAKGLKGEANR-----STNVDELKEIKLQVFSYLQQVIKENNKMENALHEIKNmyeflISIDSEKI 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1431 AEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVL--ELEKKQKNFDKIL 1508
Cdd:PTZ00440 1300 LKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLEDKQIDDEIKKIEQIkeEISNKRKEINKYL 1379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768643 1509 AEEKAISEQIAQERDTAEREARE----KETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEK 1583
Cdd:PTZ00440 1380 SNIKSNKEKCDLHVRNASRGKDKidflNKHEAIEPSNSKEVNIIKITDNINKCKQYSNEAMETENKADENNDSIIKYEK 1458
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1419-1761 |
2.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1419 EVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLdkskKKIQSELEDATIELEAQRTKVLELE 1498
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL----EELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1499 KKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNV 1578
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1579 HELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDE 1658
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1659 ERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEA 1738
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330 340
....*....|....*....|...
gi 386768643 1739 EVLQLTEDLASSERARRAAETER 1761
Cdd:COG4372 348 VGLLDNDVLELLSKGAEAGVADG 370
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
891-1283 |
2.19e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 891 KVKPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQE 970
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 971 LEDMMQELEtrieeeeervlalggEKKKLElniqdleeqleeeeaarqklQLEKVQLDAKIKKYEEDLALTDDQNQKLLK 1050
Cdd:PTZ00121 1636 EQLKKKEAE---------------EKKKAE--------------------ELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1051 EKKLLEERANdlSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEvadlKEQLNERRVQVD 1130
Cdd:PTZ00121 1681 KKAEEDEKKA--AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED----KKKAEEAKKDEE 1754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1131 EMQ--AQLAKREEELTQTLLRIDE---ESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNE 1205
Cdd:PTZ00121 1755 EKKkiAHLKKEEEKKAEEIRKEKEaviEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKE 1834
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768643 1206 LLDSLDTtaaqQELRSKREQELATLKKSLEEETVNHEGvladmrhKHSQELNSINDQLENLRKAKTVLEKAKGTLEAE 1283
Cdd:PTZ00121 1835 VADSKNM----QLEEADAFEKHKFNKNNENGEDGNKEA-------DFNKEKDLKEDDEEEIEEADEIEKIDKDDIERE 1901
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1274-1426 |
2.28e-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: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1274 EKAKGTLEAENADLATELRsVNSSRQENDRRRKQAESQIAELQVKLAEiERARSELQEKCTKLQQEAENitNQLEEAElK 1353
Cdd:pfam15709 372 EKMREELELEQQRRFEEIR-LRKQRLEEERQRQEEEERKQRLQLQAAQ-ERARQQQEEFRRKLQELQRK--KQQEEAE-R 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768643 1354 ASAAVKSASNMESQLTEAQQLLEEETRQKLgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQE 1426
Cdd:pfam15709 447 AEAEKQRQKELEMQLAEEQKRLMEMAEEER-LEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQE 518
|
|
| rad2 |
TIGR00600 |
DNA excision repair protein (rad2); All proteins in this family for which functions are known ... |
1475-1605 |
2.55e-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: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1475 KIQSELEDATIELEAqrtkVLELEKKQknfdkilAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEafDKIEDLE 1554
Cdd:TIGR00600 651 KEESESDGSFIEVDS----VSSTLELQ-------VPSKSQPTDESEENAENKVASIEGEHRKEIEDLLFDE--SEEDNIV 717
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1555 NKRKTlQNELDDLANTqgTADKNVHELEKAKRALESQLAELKAQNEELEDD 1605
Cdd:TIGR00600 718 GMIEE-EKDADDFKNE--WQDISLEELEALEANLLAEQNSLKAQKQQQKRI 765
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
945-1493 |
2.59e-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: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 945 EQLQAEIELCAEAEESRSRLMARKQELE---DMMQELETRIEEEEER-VLALGGEKKKLELNIQDLEEQLEEEEAARQKL 1020
Cdd:pfam05557 17 EKKQMELEHKRARIELEKKASALKRQLDresDRNQELQKRIRLLEKReAEAEEALREQAELNRLKKKYLEALNKKLNEKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1021 QL-------------EKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLaklkAKHEATI 1087
Cdd:pfam05557 97 SQladarevisclknELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL----AEAEQRI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1088 SELEERLHKDQQQRQESDRSKRKIET--EVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQR 1165
Cdd:pfam05557 173 KELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1166 ELESQLAEIQEdLEAEKAARAKAEKVRRDLSEELEALKN-ELLDSLDTTAAQQELRSKR------EQELATLKKSLEEET 1238
Cdd:pfam05557 253 EKEKLEQELQS-WVKLAQDTGLNLRSPEDLSRRIEQLQQrEIVLKEENSSLTSSARQLEkarrelEQELAQYLKKIEDLN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1239 VNHEgvladmRHKhsqelnsinDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENdRRRKQAESQIAELQVK 1318
Cdd:pfam05557 332 KKLK------RHK---------ALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLL-ERIEEAEDMTQKMQAH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1319 LAEIERARSELQEKCTKLQQEAEniTNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEa 1398
Cdd:pfam05557 396 NEEMEAQLSVAEEELGGYKQQAQ--TLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELE- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1399 lQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAdLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQS 1478
Cdd:pfam05557 473 -RRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEK-LQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRK 550
|
570
....*....|....*
gi 386768643 1479 ELEDAtiELEAQRTK 1493
Cdd:pfam05557 551 ELESA--ELKNQRLK 563
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1311-1535 |
2.82e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1311 QIAELQVKLAeierarSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKL-----GL 1385
Cdd:PRK05771 32 HIEDLKEELS------NERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIekeikEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1386 SSKLRQIESEKEALQEQLEE---------DDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEE------------G 1444
Cdd:PRK05771 106 EEEISELENEIKELEQEIERlepwgnfdlDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvyvvvvV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1445 KKRLNKDIEAL-------------ERQVKELIAQndrLDKSKKKIQSELEDATIELEaqrtkvlelEKKQKNFDKILAEE 1511
Cdd:PRK05771 186 LKELSDEVEEElkklgferleleeEGTPSELIRE---IKEELEEIEKERESLLEELK---------ELAKKYLEELLALY 253
|
250 260
....*....|....*....|....
gi 386768643 1512 kaisEQIAQERDTAEREAREKETK 1535
Cdd:PRK05771 254 ----EYLEIELERAEALSKFLKTD 273
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1089-1483 |
2.85e-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: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1089 ELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQA------QLAKREEELTQTLLRIdeESATKATAQK 1162
Cdd:pfam05622 11 ELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPggkkylLLQKQLEQLQEENFRL--ETARDDYRIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1163 AQrELESQLAEIQ---EDLEAekaarakaekvrrdLSEELEALKNELlDSLDTTAaqqELRSKREQELATLKKSLEEetv 1239
Cdd:pfam05622 89 CE-ELEKEVLELQhrnEELTS--------------LAEEAQALKDEM-DILRESS---DKVKKLEATVETYKKKLED--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1240 nhegvladmrhkhsqelnsindqLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQaesqIAELQVKL 1319
Cdd:pfam05622 147 -----------------------LGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQ----VQELHGKL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1320 AEiERARSE--------LQEKCTKLQQEAENI---------TN------QLEEAELKASAAV--KSASNMESQLTEAQQL 1374
Cdd:pfam05622 200 SE-ESKKADklefeykkLEEKLEALQKEKERLiierdtlreTNeelrcaQLQQAELSQADALlsPSSDPGDNLAAEIMPA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1375 LEEETRQKLGLSSK---LRQIESEKE---ALQEQLEEDDEAKRNYE--------------RKLAEVTTQMQEIKKKAEED 1434
Cdd:pfam05622 279 EIREKLIRLQHENKmlrLGQEGSYRErltELQQLLEDANRRKNELEtqnrlanqrilelqQQVEELQKALQEQGSKAEDS 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 386768643 1435 ADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDA 1483
Cdd:pfam05622 359 SLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEA 407
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1096-1412 |
2.88e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1096 KDQQQRQESDRSK-RKIETEVADLKEQLNERRvqvdemQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEI 1174
Cdd:PLN03229 418 KVNMKKREAVKTPvRELEGEVEKLKEQILKAK------ESSSKPSELALNEMIEKLKKEIDLEYTEAVIAMGLQERLENL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1175 QEDLEAEKAARAKaekVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQ-ELATLKKSLEEETVNHEGVLADMRHK-- 1251
Cdd:PLN03229 492 REEFSKANSQDQL---MHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMlNEFSRAKALSEKKSKAEKLKAEINKKfk 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1252 -------------------HSQELNSINDQLENLRKAktvLEKAKGTLEAEnadLATELRSVNSSRQENDRRRKQAESQI 1312
Cdd:PLN03229 569 evmdrpeikekmealkaevASSGASSGDELDDDLKEK---VEKMKKEIELE---LAGVLKSMGLEVIGVTKKNKDTAEQT 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1313 AELQVKlAEIERARSELQEKCTKLQQEAEnITNQLEEAELKASAAVKSASNMESQLTEAqqlLEEETRQKL-------GL 1385
Cdd:PLN03229 643 PPPNLQ-EKIESLNEEINKKIERVIRSSD-LKSKIELLKLEVAKASKTPDVTEKEKIEA---LEQQIKQKIaealnssEL 717
|
330 340
....*....|....*....|....*..
gi 386768643 1386 SSKLRQIESEKEALQEQLEEDDEAKRN 1412
Cdd:PLN03229 718 KEKFEELEAELAAARETAAESNGSLKN 744
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1280-1628 |
2.97e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1280 LEAENADLATELRSvnsSRQENDRRRKQA----ESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLE-EAELKA 1354
Cdd:pfam00038 23 LEQQNKLLETKISE---LRQKKGAEPSRLyslyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEdELNLRT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1355 SAavksasnmESQLTEAQQLLEEETRQKLGLSSKLrqiesekEALQEQLEEddeAKRNYERKLAEVTTQMQEIKKKAEED 1434
Cdd:pfam00038 100 SA--------ENDLVGLRKDLDEATLARVDLEAKI-------ESLKEELAF---LKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1435 A----DLAKELEEgkkrlnkdieaLERQVKELIAQNdrLDKSKKKIQSELEDATIELEaqrtkvlelekkqKNFDKIlae 1510
Cdd:pfam00038 162 AarklDLTSALAE-----------IRAQYEEIAAKN--REEAEEWYQSKLEELQQAAA-------------RNGDAL--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1511 eKAISEQIAQERDTAEREAREketkvlsvsreldeafdkIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAkraLES 1590
Cdd:pfam00038 213 -RSAKEEITELRRTIQSLEIE------------------LQSLKKQKASLERQLAETEERYELQLADYQELISE---LEA 270
|
330 340 350
....*....|....*....|....*....|....*...
gi 386768643 1591 QLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFE 1628
Cdd:pfam00038 271 ELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1281-1533 |
2.97e-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: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1281 EAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIE----RARSELQEKCTKLQQEAENITNQLEEAELKASA 1356
Cdd:pfam05667 225 EWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATsgasRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1357 AV---KSASNMESQLTEAQQllEEETRQKlglssklrQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEE 1433
Cdd:pfam05667 305 KLqftNEAPAATSSPPTKVE--TEEELQQ--------QREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1434 DADLAKELEEGKKRLNKDIEAL---ERQVKELIAQNDRLDKSKKKIQSELEDATIEL--------EAQRTKVLELEKKqk 1502
Cdd:pfam05667 375 LKEQNEELEKQYKVKKKTLDLLpdaEENIAKLQALVDASAQRLVELAGQWEKHRVPLieeyralkEAKSNKEDESQRK-- 452
|
250 260 270
....*....|....*....|....*....|.
gi 386768643 1503 nfdkiLAEEKAISEQIaqeRDTAErEAREKE 1533
Cdd:pfam05667 453 -----LEEIKELREKI---KEVAE-EAKQKE 474
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1253-1475 |
3.18e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1253 SQELNSINDQLEnlrkaktVLEKAKGTLEAENADLATELRSVNSSRQENDrrrKQAESQIAELQVKLAEIERARSELQEK 1332
Cdd:PHA02562 187 DMKIDHIQQQIK-------TYNKNIEEQRKKNGENIARKQNKYDELVEEA---KTIKAEIEELTDELLNLVMDIEDPSAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1333 CTKLQQEAENITNQLE----EAELKASAAVKSASNmeSQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDE 1408
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEqfqkVIKMYEKGGVCPTCT--QQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1409 AKRNY---ERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIaqNDRLDKSKKK 1475
Cdd:PHA02562 335 QSKKLlelKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV--KTKSELVKEK 402
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1580-1706 |
3.21e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1580 ELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEE 1659
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 386768643 1660 RKQRTAAVASKkklegDLKEIETTMEMHNKVKEDALKHAKKLQAQVK 1706
Cdd:PRK00409 597 QKGGYASVKAH-----ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1439-1568 |
3.27e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 42.36 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1439 KELEEGKKRLNKdiealeRQVKELIAQNDRLDKSKKKIQSELEdatiELEAQRtkvlelekkqknfdkilaeeKAISEQI 1518
Cdd:PRK05431 9 ENPEAVKEALAK------RGFPLDVDELLELDEERRELQTELE----ELQAER--------------------NALSKEI 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1519 AQERDTAER-EAREKETKVLSvsreldeafDKIEDLENKRKTLQNELDDLA 1568
Cdd:PRK05431 59 GQAKRKGEDaEALIAEVKELK---------EEIKALEAELDELEAELEELL 100
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1589-1839 |
3.40e-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: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1589 ESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFErDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVA 1668
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1669 SKKKLEGDLKEIETTMEMHNKvkEDALKHA---KKLQAQVKDALRDaeeakaakeeLQALSKEAERKVKALEAEVLQLTE 1745
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESF--SDFLDRLsalSKIADADADLLEE----------LKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1746 DLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELA 1825
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
250
....*....|....
gi 386768643 1826 NEKSNSQKNENGRA 1839
Cdd:COG3883 242 AAASAAGAGAAGAA 255
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1551-1702 |
3.70e-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: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1551 EDLENKRKTLQNELDDLANT----QGTADKNVHELEKAKRALESQLAELKAQNEELEDdlQLTEDAKLRLEVNMQALRsq 1626
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEakkyQDKAAKVVDKLTDFENQTEKDQTALETLEKALKD--LLTDEGGAIARKEIKDLQ-- 185
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768643 1627 feRDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEmhnkvkeDALKHAKKLQ 1702
Cdd:cd22656 186 --KELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIG-------PAIPALEKLQ 252
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
887-1211 |
3.81e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 887 RLYTKVKPLLEVTKQEEKLVQKEDELK----------QVREKLDTLAKNTQEYERKYQQalVEKTTLAEQLQAEIELCAE 956
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKikaeelkkaeEEKKKVEQLKKKEAEEKKKAEE--LKKAEEENKIKAAEEAKKA 1670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 957 AEESRSRLMARKQELEDMMQELETRIEEEeervlalggEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEE 1036
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAE---------EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1037 DlaltddqnQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKakhEATISelEERLHKDQQQRQESDRSKRKIETEVA 1116
Cdd:PTZ00121 1742 D--------KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK---EAVIE--EELDEEDEKRRMEVDKKIKDIFDNFA 1808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1117 DLKEQLNERRVQVDEmqaqlaKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLS 1196
Cdd:PTZ00121 1809 NIIEGGKEGNLVIND------SKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE 1882
|
330
....*....|....*
gi 386768643 1197 EELEALKNELLDSLD 1211
Cdd:PTZ00121 1883 EIEEADEIEKIDKDD 1897
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1541-1612 |
4.02e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.98 E-value: 4.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386768643 1541 RELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAK---RALESQLAELKAQNEELEDDLQLTEDA 1612
Cdd:PRK05431 21 RGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAE 95
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1197-1607 |
4.11e-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: 42.15 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1197 EELEALKNELLDsLDTTAAQQELRSKR-----EQELATLKKSLEEETVNHegvLADMrhkhSQELNSINDQLE--NLRKA 1269
Cdd:pfam06160 13 DELEERKNELMN-LPVQEELSKVKKLNltgetQEKFEEWRKKWDDIVTKS---LPDI----EELLFEAEELNDkyRFKKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1270 KTVLEKAkgtleaeNADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEE 1349
Cdd:pfam06160 85 KKALDEI-------EELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1350 AELKASAAVksasnmesQLTEAQQLLEEETrqklglssKLRQIESEKEALQEQLEE----DDEAKRNYERKLAEVTTQMQ 1425
Cdd:pfam06160 158 IEEEFSQFE--------ELTESGDYLEARE--------VLEKLEEETDALEELMEDipplYEELKTELPDQLEELKEGYR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1426 EIKKK--AEEDADLAKELEEGKKRLNKDIEALER-QVKELIAQNDRLDKSKKKIQSELEDatiELEAQRtkvlELEKKQK 1502
Cdd:pfam06160 222 EMEEEgyALEHLNVDKEIQQLEEQLEENLALLENlELDEAEEALEEIEERIDQLYDLLEK---EVDAKK----YVEKNLP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1503 NFdkilaeEKAISEQIAQERDTAEREAREKETKVLSvsrelDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELE 1582
Cdd:pfam06160 295 EI------EDYLEHAEEQNKELKEELERVQQSYTLN-----ENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQ 363
|
410 420
....*....|....*....|....*
gi 386768643 1583 KAKRALESQLAELKAQNEELEDDLQ 1607
Cdd:pfam06160 364 EELEEILEQLEEIEEEQEEFKESLQ 388
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1339-1541 |
4.29e-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: 41.28 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1339 EAENITNQLEEAELKASAAVKSASNMESQLTEAQQllEEETRQKLGLSSKLRQIESEKEALQEQLEeddeakrNYERKLA 1418
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKLIASLKEGSG--VEGLDSSTALTLELEELRQERDLLREEIQ-------KLRGQIQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1419 EVTTQMQEIKKKAEEDAD-------LAKELEEGKKRLNKDIEA-LERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQ 1490
Cdd:pfam09787 72 QLRTELQELEAQQQEEAEssreqlqELEEQLATERSARREAEAeLERLQEELRYLEEELRRSKATLQSRIKDREAEIEKL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1491 RTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSR 1541
Cdd:pfam09787 152 RNQLTSKSQSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLER 202
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1348-1536 |
4.36e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.78 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1348 EEAELKASAAVKSASNMESQLT-EAQQLLEEETRQklglSSKLRqieseKEALqeqLEEDDEAKRNYERKLAEVTTQMQE 1426
Cdd:PRK00106 31 EAAELTLLNAEQEAVNLRGKAErDAEHIKKTAKRE----SKALK-----KELL---LEAKEEARKYREEIEQEFKSERQE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1427 IKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEaqrtKVLELEKKQKNfDK 1506
Cdd:PRK00106 99 LKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELE----RVAALSQAEAR-EI 173
|
170 180 190
....*....|....*....|....*....|.
gi 386768643 1507 ILAE-EKAISEQIAQERDTAEREAREKETKV 1536
Cdd:PRK00106 174 ILAEtENKLTHEIATRIREAEREVKDRSDKM 204
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1587-1768 |
4.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1587 ALESQLAELKAQNEELEDDLQltedaklRLEVNMQALRSQFERdllakeegAEEKRRGLVKQLRDLETELDEERKQRtaa 1666
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELA-------ELEDELAALEARLEA--------AKTELEDLEKEIKRLELEIEEVEARI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1667 vaskKKLEGDLKEIETTMEMHNKVKEdaLKHAKKLQAQVKDALRDAEEAK-AAKEELQALSKEAERKVKALEAEVLQLTE 1745
Cdd:COG1579 76 ----KKYEEQLGNVRNNKEYEALQKE--IESLKRRISDLEDEILELMERIeELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|...
gi 386768643 1746 DLASSERARRAAETERDELAEEI 1768
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKI 172
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1210-1512 |
4.67e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.78 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1210 LDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSI---NDQLENLRKAKTVLEKAKGTLEAENAD 1286
Cdd:pfam02029 65 LDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSwekEEKRDSRLGRYKEEETEIREKEYQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1287 LATELRSVNSSRQENDRRRKQAESQ----IAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAE-----LKASAA 1357
Cdd:pfam02029 145 WSTEVRQAEEEGEEEEDKSEEAEEVptenFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEeevtkLKVTTK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1358 VKSASNMESQLTEAQQLLEEETRQKLGlssKLRQIESEKEalqeqlEEDDEAKRnyeRKLAEVTTQMQEIKKKAEEDADL 1437
Cdd:pfam02029 225 RRQGGLSQSQEREEEAEVFLEAEQKLE---ELRRRRQEKE------SEEFEKLR---QKQQEAELELEELKKKREERRKL 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386768643 1438 AKELEEGKKRlnkdiEALERQVKEliaqndrlDKSKKKIQSELEdatieleaqRTKVLELEKKQKNFDKILAEEK 1512
Cdd:pfam02029 293 LEEEEQRRKQ-----EEAERKLRE--------EEEKRRMKEEIE---------RRRAEAAEKRQKLPEDSSSEGK 345
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
900-1259 |
4.93e-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: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 900 KQEEKLVQKEDELKQVREKLDT--LAKNTQEYERKYQQALVEKTTLAEQLQAeieLCAEAEESRSRLMA--RKQELE--D 973
Cdd:pfam07111 255 QEDRADLQATVELLQVRVQSLThmLALQEEELTRKIQPSDSLEPEFPKKCRS---LLNRWREKVFALMVqlKAQDLEhrD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 974 MMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKK 1053
Cdd:pfam07111 332 SVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1054 LLEERandLSQTLAEEEEKAKHLAKLK------AKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRV 1127
Cdd:pfam07111 412 STQIW---LETTMTRVEQAVARIPSLSnrlsyaVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLRE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1128 QVDEMQAQLAKREEELTQTLLRIDEE-SATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNEL 1206
Cdd:pfam07111 489 ERNRLDAELQLSAHLIQQEVGRAREQgEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQEL 568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 386768643 1207 ldsldttAAQQELRSKREQE-LATLKKSLEEETVNHEGVLADMRHKHSQELNSI 1259
Cdd:pfam07111 569 -------TQQQEIYGQALQEkVAEVETRLREQLSDTKRRLNEARREQAKAVVSL 615
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
1018-1173 |
5.18e-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: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1018 QKLQLEKVQLDAKIKKYEEdlalTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKakhlaklkakheatISELEERLHkd 1097
Cdd:pfam10186 29 ARLLSEKDSLKKKVEEALE----GKEEGEQLEDNIGNKKLKLRLLKSEVAISNER--------------LNEIKDKLD-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1098 qQQRQESDRSKRKIETevadLKEQLNERRVQVDEMQAQLAKRE----EELTQTLLRIDEE-SATKATAQKAQRELESQLA 1172
Cdd:pfam10186 89 -QLRREIAEKKKKIEK----LRSSLKQRRSDLESASYQLEERRasqlAKLQNSIKRIKQKwTALHSKTAESRSFLCRELA 163
|
.
gi 386768643 1173 E 1173
Cdd:pfam10186 164 K 164
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1648-1790 |
5.27e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1648 QLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDA------LRDAEEAKAAKEE 1721
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearikkYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768643 1722 LQALSKE---AERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIAnnankgslmiDEKRRLEARIA 1790
Cdd:COG1579 91 YEALQKEiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE----------EKKAELDEELA 152
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1580-1964 |
5.47e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1580 ELEKAKRALESQLAELKAQNE---ELEDDLQlteDAKLRLEVNMQALRSQ-----FERDLLAKEEGAEEKrrglvKQLRD 1651
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEaesDLEQDYQ---AASDHLNLVQTALRQQekierYQADLEELEERLEEQ-----NEVVE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1652 LETE-LDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKvKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQAlskEAE 1730
Cdd:PRK04863 373 EADEqQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQLCGLPDLTADNAEDWLE---EFQ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1731 RKVKALEAEVLQLTEDLASSERARRAAEtERDELAEEIAnnankgslmiDEKRRLEAriatleeeleeEQSNSEVLLD-R 1809
Cdd:PRK04863 449 AKEQEATEELLSLEQKLSVAQAAHSQFE-QAYQLVRKIA----------GEVSRSEA-----------WDVARELLRRlR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1810 SRKAQL-QIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKvkatiATLEAKIANLEEQLENEGKER 1888
Cdd:PRK04863 507 EQRHLAeQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQ-----EELEARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1889 LLQQKANRKMDKKIKELT------MNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMI 1962
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAarapawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI 661
|
..
gi 386768643 1963 ES 1964
Cdd:PRK04863 662 ER 663
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1370-1504 |
5.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1370 EAQQLLEEETrQKL-----GLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAdlAKELEEG 1444
Cdd:PRK00409 506 EAKKLIGEDK-EKLneliaSLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA--QQAIKEA 582
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1445 KKRLNKDIEALERQVKELIAQNDRldKSKKKIQSELEDAtieLEAQRTKVLELEKKQKNF 1504
Cdd:PRK00409 583 KKEADEIIKELRQLQKGGYASVKA--HELIEARKRLNKA---NEKKEKKKKKQKEKQEEL 637
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1145-1330 |
6.11e-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: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1145 QTLLRIDeesatKATAQKAQRELESQLAEIQEDLEAEkaarakaekvrRDLSEELEALKNELLDS-LDTTAAQQELRSKR 1223
Cdd:pfam00529 46 DVLFQLD-----PTDYQAALDSAEAQLAKAQAQVARL-----------QAELDRLQALESELAISrQDYDGATAQLRAAQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1224 EQeLATLKKSLEEETVNHEG--VLADMRHKHSQELNSINDQLENlrkAKTVLEKAKGTLEAENADLAtelRSVNSSRQEN 1301
Cdd:pfam00529 110 AA-VKAAQAQLAQAQIDLARrrVLAPIGGISRESLVTAGALVAQ---AQANLLATVAQLDQIYVQIT---QSAAENQAEV 182
|
170 180
....*....|....*....|....*....
gi 386768643 1302 DRRRKQAESQIAELQvklAEIERARSELQ 1330
Cdd:pfam00529 183 RSELSGAQLQIAEAE---AELKLAKLDLE 208
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1084-1313 |
6.22e-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: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1084 EATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDE-ESATKATAQK 1162
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1163 AQRE----------LESQ----LAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQelrskreQELA 1228
Cdd:COG3883 95 LYRSggsvsyldvlLGSEsfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK-------AELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1229 TLKKSLEEETVNHEGVLADMrhkhSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQA 1308
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQL----SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
....*
gi 386768643 1309 ESQIA 1313
Cdd:COG3883 244 ASAAG 248
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1501-1982 |
6.31e-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: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1501 QKNFDKILAEEKAIS--EQIAQERDTAEREAREKETKVLSVSRELDEAF---DKIEDLENKR-------KTLQNELDDLA 1568
Cdd:TIGR00606 172 KQKFDEIFSATRYIKalETLRQVRQTQGQKVQEHQMELKYLKQYKEKACeirDQITSKEAQLessreivKSYENELDPLK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1569 NTQGTADKNVHELEKakraLESQLAELKAQNEELEDDlqltedaKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQ 1648
Cdd:TIGR00606 252 NRLKEIEHNLSKIMK----LDNEIKALKSRKKQMEKD-------NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1649 LRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNK--VKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALS 1726
Cdd:TIGR00606 321 LVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEhiRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1727 KEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVL 1806
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1807 LDRSRKAQLQIEQLTTELANEKSNSQKNEngRALLERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGK 1886
Cdd:TIGR00606 481 RKAERELSKAEKNSLTETLKKEVKSLQNE--KADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1887 ERLLQQKANRKMDKKIKELTMNieDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQe 1966
Cdd:TIGR00606 559 SDELTSLLGYFPNKKQLEDWLH--SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQ- 635
|
490
....*....|....*.
gi 386768643 1967 AMNREINSLKTKLRRT 1982
Cdd:TIGR00606 636 DEESDLERLKEEIEKS 651
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1191-1354 |
7.03e-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: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1191 VRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEetvnhegvLADMRHKHSQELNSI--NDQLENLRK 1268
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE--------VEARIKKYEEQLGNVrnNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1269 AKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQvklAEIERARSELQEKCTKLQQEAENITNQLE 1348
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREELAAKIP 173
|
....*.
gi 386768643 1349 EAELKA 1354
Cdd:COG1579 174 PELLAL 179
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1068-1351 |
7.16e-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: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1068 EEEEKAKHLAKLKAKHEAT----ISELEeRLHKDQQQRQESDRSkrkiETEVAdlkeqlneRRVQVDEMQAQLAKREEEL 1143
Cdd:pfam17380 354 RQEERKRELERIRQEEIAMeisrMRELE-RLQMERQQKNERVRQ----ELEAA--------RKVKILEEERQRKIQQQKV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1144 TQTLLRIDEESATKATAQKAQRELESQLAEIQEdleaekaarakaekvrrdlsEELEalknelldsldttaAQQELRSKR 1223
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRL--------------------EEQE--------------RQQQVERLR 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1224 EQELATLKKSLEEETVNHEGVLADmrhkhSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDR 1303
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAE-----EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEE 541
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 386768643 1304 RRKQAE----SQIAElQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAE 1351
Cdd:pfam17380 542 RRKQQEmeerRRIQE-QMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1263-1539 |
7.22e-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: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1263 LENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKlAEIERARSELQEKCTKLQQEAEN 1342
Cdd:TIGR00927 627 LGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEGEGEIEAKEAD 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1343 ITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKlglssklrqiESEKEALQEQLEEDDEAKRNYE-RKLAEVT 1421
Cdd:TIGR00927 706 HKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEG----------EGEAEGKHEVETEGDRKETEHEgETEAEGK 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1422 TQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELE---AQRTKVLELE 1498
Cdd:TIGR00927 776 EDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQgeaKQDEKGVDGG 855
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 386768643 1499 KKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSV 1539
Cdd:TIGR00927 856 GGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSL 896
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1841-1952 |
7.52e-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: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1841 LERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLEnegkERLLQQKANRKMDKKIKELtmniederrhvdqhK 1920
Cdd:COG0542 416 LERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELE----ALKARWEAEKELIEEIQEL--------------K 477
|
90 100 110
....*....|....*....|....*....|..
gi 386768643 1921 EQMDKLNSRIKLLKRNLDETEEELQKEKTQKR 1952
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1070-1674 |
7.65e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1070 EEKAKHLAKLKAKHEATISELE-------ERLHKDQQQRQESDRskRKIETEVADLKEQLNERRVQVDEmQAQLAKREEE 1142
Cdd:NF041483 476 EEAARTAEELLTKAKADADELRstataesERVRTEAIERATTLR--RQAEETLERTRAEAERLRAEAEE-QAEEVRAAAE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1143 LTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAA----RAKAEKVRRDLSEELEALKNELLDSLDTTAAQQE 1218
Cdd:NF041483 553 RAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEAladaRAEAERIRREAAEETERLRTEAAERIRTLQAQAE 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1219 LRSKREQELATLKKSleEETVNHEGVLADMRHKHSQELNSINDQLENlrKAKTVLEKAKGTLEAENADLATELrsvNSSR 1298
Cdd:NF041483 633 QEAERLRTEAAADAS--AARAEGENVAVRLRSEAAAEAERLKSEAQE--SADRVRAEAAAAAERVGTEAAEAL---AAAQ 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1299 QENDRRRKQAESQIAELQVKlAEIERARS-----ELQEKCTKLQQEAENITNQL-EEAELKASAAVKSASNMESQLTEAQ 1372
Cdd:NF041483 706 EEAARRRREAEETLGSARAE-ADQERERAreqseELLASARKRVEEAQAEAQRLvEEADRRATELVSAAEQTAQQVRDSV 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1373 QLLEEETRQKL-GLSSKlrqieSEKEALQEQLEEDDEAKRNYERKLAE---VTTQMQEIKKKAEEDADLAKELEegkkrl 1448
Cdd:NF041483 785 AGLQEQAEEEIaGLRSA-----AEHAAERTRTEAQEEADRVRSDAYAErerASEDANRLRREAQEETEAAKALA------ 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1449 nkdiealERQVKELIAQNDRL----DKSKKKIQSELED--ATIELEAQRTKVLELEKKQK-------NFDKILAEEKAIS 1515
Cdd:NF041483 854 -------ERTVSEAIAEAERLrsdaSEYAQRVRTEASDtlASAEQDAARTRADAREDANRirsdaaaQADRLIGEATSEA 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1516 EQI-AQERDTAEREAREKETKVLSVSRELDEAFDK-IEDLENKRKTLQNEL-DDLANTQGTADKNVHELEKAKRALESQL 1592
Cdd:NF041483 927 ERLtAEARAEAERLRDEARAEAERVRADAAAQAEQlIAEATGEAERLRAEAaETVGSAQQHAERIRTEAERVKAEAAAEA 1006
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1593 AELKAQNEELED---DLQLTEDAKLRLEVNMQAlrsqferDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVAS 1669
Cdd:NF041483 1007 ERLRTEAREEADrtlDEARKDANKRRSEAAEQA-------DTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAA 1079
|
....*
gi 386768643 1670 KKKLE 1674
Cdd:NF041483 1080 RKEAE 1084
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1160-1398 |
7.85e-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: 40.82 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1160 AQKAQRELESQLAEIQEDLEAEKAARAkaekvrrdlSEELEALKNELLDSLDttaAQQELRSKREQELATLKKSL---EE 1236
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATD---------DEELEEAKKTIKALLD---DLLKEAKKYQDKAAKVVDKLtdfEN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1237 ETVNHEGVLADMRHKHSQELNSINDQLENLRkaktvLEKAKGTLEAENADLATELRsvnssrqendRRRKQAESQIAELQ 1316
Cdd:cd22656 150 QTEKDQTALETLEKALKDLLTDEGGAIARKE-----IKDLQKELEKLNEEYAAKLK----------AKIDELKALIADDE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1317 VKLAEIERARSELqekcTKLQQEAENITNQLEEAeLKASAAVKSA-SNMESQLTEAQQLLEEETRQKLGLSSKLRQIESE 1395
Cdd:cd22656 215 AKLAAALRLIADL----TAADTDLDNLLALIGPA-IPALEKLQGAwQAIATDLDSLKDLLEDDISKIPAAILAKLELEKA 289
|
...
gi 386768643 1396 KEA 1398
Cdd:cd22656 290 IEK 292
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
1345-1433 |
7.86e-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: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1345 NQLEEAELKASAAVKSASnmesqltEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQM 1424
Cdd:pfam11932 13 ATLDQALDLAEKAVAAAA-------QSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
|
....*....
gi 386768643 1425 QEIKKKAEE 1433
Cdd:pfam11932 86 EEIERTERE 94
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1692-1979 |
8.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1692 EDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETER---DELAEEI 1768
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1769 ANNANKGSLMIDEKRRLEARIATleeeleeeqsnsevLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKEL 1848
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRE--------------LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1849 KAKlaeietaqrTKVKATIATLEAKIANLEEQLE--NEGKERLlqqkanRKMDKKIKELTMNIED-ERRH-----VDQHK 1920
Cdd:PRK03918 307 DEL---------REIEKRLSRLEEEINGIEERIKelEEKEERL------EELKKKLKELEKRLEElEERHelyeeAKAKK 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 386768643 1921 EQMDKLNSRIKllKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKL 1979
Cdd:PRK03918 372 EELERLKKRLT--GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1442-1582 |
8.14e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1442 EEGKKRLNKDIEALErqvkELIAqndRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQE 1521
Cdd:PRK00409 505 EEAKKLIGEDKEKLN----ELIA---SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1522 RDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELE 1582
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1098-1441 |
8.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1098 QQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQED 1177
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1178 LEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHEgvlADMRHKHSQELN 1257
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ---ALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1258 SINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQ 1337
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1338 QEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKL 1417
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330 340
....*....|....*....|....
gi 386768643 1418 AEVTTQMQEIKKKAEEDADLAKEL 1441
Cdd:COG4372 347 LVGLLDNDVLELLSKGAEAGVADG 370
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1857-1946 |
8.55e-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: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1857 TAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRN 1936
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90
....*....|
gi 386768643 1937 LDETEEELQK 1946
Cdd:COG4942 99 LEAQKEELAE 108
|
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
1824-1969 |
8.96e-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: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1824 LANEKSNSQKNENGRALLERQNKELK------AKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGKE--RLLQQKAN 1895
Cdd:smart00806 133 LASSSSAISLANNPDKLNKEQRAELKslqrelAVLRQTHNSFFTEIKESIKDILEKIDKFKSSSLSASGSsnRAYVESSK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1896 RKMD-------KKIKELTMNIEDERRHVDQH-----KEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRK-YQRECEDMI 1962
Cdd:smart00806 213 KKLSedsdsllTKVDDLQDIIEALRKDVAQRgvrpsKKQLETVQKELETARKELKKMEEYIDIEKPIWKKiWEAELDKVC 292
|
....*..
gi 386768643 1963 ESQEAMN 1969
Cdd:smart00806 293 EEQQFLT 299
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
1263-1465 |
9.38e-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: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1263 LENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRR--RKQA--ESQIAELQVKLA-EIERARSELQEKCTKLQ 1337
Cdd:pfam15397 1 IRNRRTSLEELKKHEDFLTKLNLELIKAIQDTEDSTALKVRKllQQYEkfGTIISILEYSNKkQLQQAKAELQEWEEKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768643 1338 QEAENITNQLEEAELKASAA----------------VKSA--SNMESQLteaQQLLEEETRQKLGLSsklRQIESEKEAL 1399
Cdd:pfam15397 81 SKLNKLEQQLEQLNAKIQKTqeelnflstykdkeypVKAVqiANLVRQL---QQLKDSQQDELDELE---EMRRMVLESL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768643 1400 QEQLEEDdeaKRNYERKLAEVT-TQMQE-IKKKAEEDADLAKELEEGKK---RLNKDIEALERQVKELIAQ 1465
Cdd:pfam15397 155 SRKIQKK---KEKILSSLAEKTlSPYQEsLLQKTRDNQVMLKEIEQFREfidELEEEIPKLKAEVQQLQAQ 222
|
|
| |
