|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-781 |
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: 1190.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVANRSMVKNRKTSvdldtstnrIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGK---------KKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd01377 152 HFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHEnKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd01377 232 LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQR-RREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGRE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSvSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd01377 311 WVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQ-YFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKP-MGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKY--VVP 576
Cdd:cd01377 390 FNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNfkKPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 577 EIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIAdvcslsaadstSDTGVFGSRVPKK 656
Cdd:cd01377 470 PKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYE-----------ESGGGGGKKKKKG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 657 GMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQR 736
Cdd:cd01377 539 GSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQR 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 71983975 737 YEkLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd01377 619 YS-ILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-781 |
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: 1038.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVANrSMVKNRKTSVDLDTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAA-SKPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSkYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKS-YAFLSNGSLPVPGVDDYAEFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHEnKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd14911 239 ATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQE-RNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd14911 318 FVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVPEIR 579
Cdd:cd14911 398 FNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 580 SRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDiADVCSLsAADSTSDTGvFGSRVpKKGMF 659
Cdd:cd14911 478 GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD-AEIVGM-AQQALTDTQ-FGART-RKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 660 RTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEk 739
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE- 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 71983975 740 LLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14911 633 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-793 |
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: 1013.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 81 NPPKYDKCEDMSMLTCLNEASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVAD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 161 EAYRSMLQERDDQSILCTGESGAGKTENTKKVIQYLAYVAnrsmvknrktsvdldtSTNRIMGQLEEQLLQANPILEAFG 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS----------------GSNTEVGSVEDQILESNPILEAFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 241 NSKTVKNDNSSRFGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLeDSLSKYK 320
Cdd:smart00242 145 NAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGL-KSPEDYR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 321 FVSNGDS-KLAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQAVLLNDAVAQKIASLLG 399
Cdd:smart00242 224 YLNQGGClTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKEELSNAAELLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 400 VNVTELMRAFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIF 479
Cdd:smart00242 304 VDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 480 ETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGlNLQPTIDLI-DKPMGIMSTLDDVCLFPQGNDQS 558
Cdd:smart00242 383 EVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIeKKPPGILSLLDEECRFPKGTDQT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 559 FVQRLNNTHSQHPKYVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVCSls 638
Cdd:smart00242 462 FLEKLNQHHKKHPHFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAG-- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 639 aadstsdtgvfgsrvpKKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIR 718
Cdd:smart00242 540 ----------------SKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIR 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 719 ICRQGFPTRLPFQEFRQRYeKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFRSGVIAEFEEMRD 793
Cdd:smart00242 604 IRRAGFPYRLPFDEFLQRY-RVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
89-781 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 975.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 89 EDMSMLTCLNEASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQ 168
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 169 ERDDQSILCTGESGAGKTENTKKVIQYLAYVAnrsmvknrktsvdlDTSTNRIMGQLEEQLLQANPILEAFGNSKTVKND 248
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVS--------------GSGSAGNVGRLEEQILQSNPILEAFGNAKTVRNN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 249 NSSRFGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSlSKYKFVSN-GDS 327
Cdd:pfam00063 148 NSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNP-KDYHYLSQsGCY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 328 KLAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFShENKNNDQAVLLNDAVAQKIASLLGVNVTELMR 407
Cdd:pfam00063 227 TIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFK-KERNDEQAVPDDTENLQKAASLLGIDSTELEK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 408 AFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQL 487
Cdd:pfam00063 306 ALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 488 CINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGlNLQPTIDLID-KPMGIMSTLDDVCLFPQGNDQSFVQRLNNT 566
Cdd:pfam00063 386 CINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYST 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 567 HSQHPKYVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVCSLSAADSTSDT 646
Cdd:pfam00063 465 FSKHPHFQKPRLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 647 GVFGsrvpKKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPT 726
Cdd:pfam00063 545 PKRT----KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPN 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 727 RLPFQEFRQRYeKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:pfam00063 621 RITFQEFVQRY-RILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-781 |
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: 949.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVAnrSMVKNRKTsvdldtstNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVA--SSHKGRKD--------HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEdSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd14920 151 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE-GFNNYRFLSNGYIPIPGQQDKDNFQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHEnKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd14920 230 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKE-RNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd14920 309 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPM---GIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVP 576
Cdd:cd14920 389 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 577 -EIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVCSLSAADSTSDTGVFGSRVPK 655
Cdd:cd14920 469 rQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 656 KGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQ 735
Cdd:cd14920 549 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 71983975 736 RYEkLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14920 629 RYE-ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-781 |
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: 890.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVANRSMVKNRKTSVDLDtstnriMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALS------HGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDsLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd14932 155 NFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLED-YSKYRFLSNGNVTIPGQQDKELFA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHEnKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd14932 234 ETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKE-RNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd14932 313 YVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPM---GIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVP 576
Cdd:cd14932 393 FNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 577 -EIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVCSLS--AADSTSDTGVFGSRv 653
Cdd:cd14932 473 kKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDkvAGMGESLHGAFKTR- 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 654 pkKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEF 733
Cdd:cd14932 552 --KGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 71983975 734 RQRYEkLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14932 630 RQRYE-ILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
100-781 |
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: 841.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVAnrSMVKNRKtsvdlDTStnrIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVA--SSHKGKK-----DTS---ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEdSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd14921 151 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLE-GFNNYTFLSNGFVPIPAAQDDEMFQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHEnKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd14921 230 ETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKE-RNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd14921 309 VVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPM---GIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVP 576
Cdd:cd14921 389 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 577 -EIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVCSLSAADSTSDTGVFGSRVPK 655
Cdd:cd14921 469 kQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 656 KGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQ 735
Cdd:cd14921 549 KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 71983975 736 RYEkLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14921 629 RYE-ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-781 |
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: 835.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVANRSMVKNRKtsvdldtstnrimGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ-------------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEdSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd14919 148 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE-PYNKYRFLSNGHVTIPGQQDKDMFQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHEnKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd14919 227 ETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKE-RNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd14919 306 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPM---GIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVP 576
Cdd:cd14919 386 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 577 -EIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVCSLSAADSTSDTGVFGSRVPK 655
Cdd:cd14919 466 kQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTR 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 656 KGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQ 735
Cdd:cd14919 546 KGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 71983975 736 RYEkLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14919 626 RYE-ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1351 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 823.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 36 WVPSEKDGFALGAVIGEPHADGTIDIEL-METGERQRVSSDDCQ--KPNPPKYDKCEDMSMLTCLNEASVLHNLKQRYFS 112
Cdd:COG5022 13 WIPDEEKGWIWAEIIKEAFNKGKVTEEGkKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 113 NLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGESGAGKTENTKKV 192
Cdd:COG5022 93 GQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 193 IQYLAYVANrsmvknrktsvdldtSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVHFDSTGCISGANI 272
Cdd:COG5022 173 MQYLASVTS---------------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 273 EFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSlSKYKFVSNG-DSKLAGVDDGAEMKETLNAMSIMGLN 351
Cdd:COG5022 238 ETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNP-KDYIYLSQGgCDKIDGIDDAKEFKITLDALKTIGID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 352 DEEIGGILRVVSAVMLFGNLEFSHEnkNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRDLVHRAQSVDQVN 431
Cdd:COG5022 317 EEEQDQIFKILAAILHIGNIEFKED--RNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 432 FSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSvSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQE 511
Cdd:COG5022 395 AIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 512 YLDEGLEWKFLDFgLNLQPTIDLIDK--PMGIMSTLDDVCLFPQGNDQSFVQRLNNT--HSQHPKYVVPEIRSRSdFAVV 587
Cdd:COG5022 474 YVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSNPKFKKSRFRDNK-FVVK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 588 HYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADvcslsaadstsdtgvfgsrVPKKGMFRTVSQLYK 667
Cdd:COG5022 552 HYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN-------------------IESKGRFPTLGSRFK 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 668 EQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEkLLAPDVNP 747
Cdd:COG5022 613 ESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYR-ILSPSKSW 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 748 AG----FMDGKNAVYRIVQYLEVDANLFRIGQSKIFFRSGVIAEFEEMRDQKLSALIESFQAQCRGWLGRRVMVRRREQE 823
Cdd:COG5022 692 TGeytwKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRI 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 824 VAIKILQRNGLAWMRLREWQWWRLLTKVKPLLEVTNKDELIAEREQELKVTAEKLRRSEVFISDYKQqmeKMDEERLVLK 903
Cdd:COG5022 772 KKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEV---EFSLKAEVLI 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 904 TRLdaessERAEIFEERSRMAARrdelEGILEEVSKRLEIEEQKAKKADSESRKLTEMVrhlEENLEDEersrQKLLLEK 983
Cdd:COG5022 849 QKF-----GRSLKAKKRFSLLKK----ETIYLQSAQRVELAERQLQELKIDVKSISSLK---LVNLELE----SEIIELK 912
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 984 NSIESRLKEleaqglELEDSGNKLSKEKKALEER-CEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHN 1062
Cdd:COG5022 913 KSLSSDLIE------NLEFKTELIARLKKLLNNIdLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVRE 986
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1063 AETAR------RAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISirndEELAARQQLeREIREIRAQLDDAIEE 1136
Cdd:COG5022 987 GNKANselknfKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIIS----SESTELSIL-KPLQKLKGLLLLENNQ 1061
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1137 TNkekaARQKAEKARRD--MAEELESYKQELEESNDKTVLHSQLKAKrdeeyahlQKQLEETVKSSEEVVEEM-KAQNQK 1213
Cdd:COG5022 1062 LQ----ARYKALKLRREnsLLDDKQLYQLESTENLLKTINVKDLEVT--------NRNLVKPANVLQFIVAQMiKLNLLQ 1129
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1214 KIEELNETIDQL---KRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSlmEKDH-KMREMQSNLDDLM 1289
Cdd:COG5022 1130 EISKFLSQLVNTlepVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYD--EKSKlSSSEVNDLKNELI 1207
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1290 AKLSKMNNELE-SIQKAKSADETLNSNLLKK--NASLDMQLSELTEASEEDRRTRaTLNNKIRQL 1351
Cdd:COG5022 1208 ALFSKIFSGWPrGDKLKKLISEGWVPTEYSTslKGFNNLNKKFDTPASMSNEKLL-SLLNSIDNL 1271
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-781 |
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: 821.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVAnrSMVKNRKTSvdldtstnRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVA--SSPKGRKEP--------GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEdSLSKYKFVSNGDSKLAGvDDGAEMK 339
Cdd:cd14930 151 NFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PCSHYRFLTNGPSSSPG-QERELFQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHEnKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd14930 229 ETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRE-RNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd14930 308 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPM---GIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVP 576
Cdd:cd14930 388 FNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 577 E-IRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVCSLSAADSTSDtGVFGSRvPK 655
Cdd:cd14930 468 RhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGD-GPPGGR-PR 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 656 KGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQ 735
Cdd:cd14930 546 RGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 71983975 736 RYEkLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14930 626 RYE-ILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-781 |
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: 821.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVANRSMVKNRKTSVDLDTstnrimGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSH------GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDsLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd15896 155 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLEN-YNNYRFLSNGNVTIPGQQDKDLFT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHEnKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd15896 234 ETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKE-RHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd15896 313 YVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPM---GIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVP 576
Cdd:cd15896 393 FNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 577 -EIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVCSLSAADSTSDT-GVFGSRvp 654
Cdd:cd15896 473 kKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMpGAFKTR-- 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 655 kKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFR 734
Cdd:cd15896 551 -KGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 71983975 735 QRYEkLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd15896 630 QRYE-ILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-781 |
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: 813.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKR-KEMPPHIFAVADEAYRSMLQERDDQSILCT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 179 GESGAGKTENTKKVIQYLAYVANRSMVKNRKTSVDLdtstnrimgqlEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIR 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSASSI-----------EQQILQSNPILEAFGNAKTVRNDNSSRFGKFIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 259 VHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKF----VSNGDSKLAGVDD 334
Cdd:cd00124 150 LQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 335 GAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSH-ENKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPK 413
Cdd:cd00124 230 AEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEdEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 414 IKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRT-RQQSVSFIGILDIAGFEIFETNSFEQLCINYT 492
Cdd:cd00124 310 IKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTdAAESTSFIGILDIFGFENFEVNSFEQLCINYA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 493 NEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLID-KPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHP 571
Cdd:cd00124 390 NEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDFPDN-QDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 572 KYVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSkeslivdmwkdiadvcslsaadstsdtgvfgs 651
Cdd:cd00124 469 RFFSKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG-------------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 652 rvpkkgmfrtvSQlYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQ 731
Cdd:cd00124 517 -----------SQ-FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFD 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 71983975 732 EFRQRYeKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd00124 585 EFLKRY-RILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-781 |
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: 736.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVANRSMVKNRKTSvdldtstnriMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKS----------KGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd14909 151 HFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKnNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd14909 231 LTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGR-EEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd14909 310 FVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH------SQHPKY 573
Cdd:cd14909 389 FNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHlgksapFQKPKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 574 VVPEIRSrSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDiadvcslSAADSTSDTGVFGSRV 653
Cdd:cd14909 469 PKPGQQA-AHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-------HAGQSGGGEQAKGGRG 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 654 PKKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEF 733
Cdd:cd14909 541 KKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 71983975 734 RQRYeKLLAPDVNPAGfMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14909 621 KMRY-KILNPAGIQGE-EDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
100-781 |
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: 734.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVANRSMVKNRKTSvdldTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQ----FLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd14927 157 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKnNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd14927 237 ATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQR-EEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd14927 316 YVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH-SQHPKYVVPEI 578
Cdd:cd14927 395 FNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPRP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 579 ----RSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIadVCSLSAADSTSDTgvfGSRVP 654
Cdd:cd14927 475 dkkrKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY--VGSDSTEDPKSGV---KEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 655 KKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFR 734
Cdd:cd14927 550 KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 71983975 735 QRYeKLLAPDVNP-AGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14927 630 QRY-RILNPSAIPdDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
101-781 |
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: 701.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLAYVANRSMVKNRKTSvdldtstnRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKDS--------KMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMKE 340
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 341 TLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKnNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRDL 420
Cdd:cd14913 234 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQR-EEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 421 VHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLF 500
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 501 NNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH------SQHPKYV 574
Cdd:cd14913 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgksnnFQKPKVV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 575 vpEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADvcslSAADSTSDTGvfgsrVP 654
Cdd:cd14913 472 --KGRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFAT----ADADSGKKKV-----AK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 655 KKG-MFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEF 733
Cdd:cd14913 541 KKGsSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 71983975 734 RQRYEKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14913 621 KQRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
100-781 |
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: 697.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVANRSmvknrKTSVDLDtstnrimGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTG-----KQSSDGK-------GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd14934 149 HFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKnNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd14934 229 ITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPR-EEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd14934 308 FVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH-SQHPKYVVPE- 577
Cdd:cd14934 387 FNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKg 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 578 ---IRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSkESLIVDMWKDiadvcslsaadstSDTGVFGSRVP 654
Cdd:cd14934 467 gkgKGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKS-SLGLLALLFK-------------EEEAPAGSKKQ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 655 KKG-MFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEF 733
Cdd:cd14934 533 KRGsSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEF 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 71983975 734 RQRYEkLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14934 613 KQRYQ-VLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-781 |
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: 685.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVAnrSMVKNRKTsvdldtstnriMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIA--AMIESKKK-----------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGlSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd14929 148 HFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSG-KKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFShENKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd14929 227 ATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFK-QKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRL------NNTHSQHPKy 573
Cdd:cd14929 385 FNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLfdnhfgKSVHFQKPK- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 574 vVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDiaDVCSLSAADstsdtgvFGSRV 653
Cdd:cd14929 464 -PDKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN--YISTDSAIQ-------FGEKK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 654 PKKGM-FRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQE 732
Cdd:cd14929 534 RKKGAsFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYAD 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 71983975 733 FRQRYeKLLAPDVNP-AGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14929 614 FKQRY-CILNPRTFPkSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
858-1934 |
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: 660.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 858 TNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEV 937
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 938 SKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEER 1017
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1018 CEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMR 1097
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1098 KESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKTVLHSQ 1177
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1178 LKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASAR 1257
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1258 LEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEED 1337
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1338 RRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERAD 1417
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1418 MAE--QARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALV 1495
Cdd:pfam01576 561 LEEkaAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1496 LSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEV 1575
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1576 NMQAMRSEFERQLASREEDEDDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQL 1655
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1656 RKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEV-SSLRASSFS 1734
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIaSGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1735 NEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQQLQDAENT 1814
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1815 AVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQLE 1894
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|
gi 71983975 1895 DTEAERDRLTNKLKDERRRAEEMTDLNETLSRDVSLLKQR 1934
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
101-781 |
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: 660.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYF-SNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVanrsmvknrktsvdldTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATV----------------GGSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd01380 146 LFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHEnkNNDQAVLLNDAVAQKIA-SLLGVNVTELMRAFLKPKIKVQR 418
Cdd:cd01380 226 ETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKAT--RNDSASISPDDEHLQIAcELLGIDESQLAKWLCKRKIVTRS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 419 DLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSV-SFIGILDIAGFEIFETNSFEQLCINYTNEKLQ 497
Cdd:cd01380 304 EVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 498 QLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPK--YVV 575
Cdd:cd01380 384 QQFNQHVFKLEQEEYVKEEIEWSFIDFYDN-QPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 576 PEIrSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKEslivdmwkdiadvcslsaadstsdtgvfgsrvpk 655
Cdd:cd01380 463 PRF-SNTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------------- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 656 kgMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQ 735
Cdd:cd01380 508 --RKKTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFS 585
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 71983975 736 RYeKLLAP--DVNPagfMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd01380 586 RY-RVLLPskEWLR---DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
101-781 |
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: 649.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLAYVAnrsMVKNRKTSvdlDTSTNRimGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIA---AIGDRSKK---DQTPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMKE 340
Cdd:cd14917 154 FGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 341 TLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKnNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRDL 420
Cdd:cd14917 234 TDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQR-EEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 421 VHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLF 500
Cdd:cd14917 313 VTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 501 NNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH------SQHPKYV 574
Cdd:cd14917 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlgksnnFQKPRNI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 575 vpEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIAdvcslsAADSTSDTGvfGSRVP 654
Cdd:cd14917 472 --KGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYA------GADAPIEKG--KGKAK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 655 KKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFR 734
Cdd:cd14917 542 KGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 71983975 735 QRYeKLLAPDVNPAG-FMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14917 622 QRY-RILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
101-781 |
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: 644.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLAYVANRSMVKNrktsvdlDTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKK-------EQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMKE 340
Cdd:cd14923 155 FGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 341 TLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNnDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRDL 420
Cdd:cd14923 235 TDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQRE-EQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 421 VHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLF 500
Cdd:cd14923 314 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 501 NNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH------SQHPKYV 574
Cdd:cd14923 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgksnnFQKPKPA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 575 vpEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIAdvcslsAADSTSDTGVFGSRVP 654
Cdd:cd14923 473 --KGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYA------GAEAGDSGGSKKGGKK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 655 KKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFR 734
Cdd:cd14923 545 KGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFK 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 71983975 735 QRYEKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14923 625 QRYRILNASAIPEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
101-781 |
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: 636.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLAYVAnrsMVKNRKTSVDLDTSTnrimGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIA---AIGDRSKKENPNANK----GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMKE 340
Cdd:cd14916 155 FGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 341 TLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKnNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRDL 420
Cdd:cd14916 235 TDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQR-EEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 421 VHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLF 500
Cdd:cd14916 314 VTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 501 NNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH------SQHPKYV 574
Cdd:cd14916 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHlgksnnFQKPRNV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 575 vpEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIAdvcslsAADsTSDTGVFGSRVP 654
Cdd:cd14916 473 --KGKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYA------SAD-TGDSGKGKGGKK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 655 KKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFR 734
Cdd:cd14916 544 KGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 71983975 735 QRYeKLLAPDVNPAG-FMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14916 624 QRY-RILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-781 |
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: 634.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLAYVANRSMVKNRktsvdlDTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKE------EITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMKE 340
Cdd:cd14912 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 341 TLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKnNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRDL 420
Cdd:cd14912 236 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQR-EEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 421 VHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLF 500
Cdd:cd14912 315 VTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 501 NNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH------SQHPKYV 574
Cdd:cd14912 394 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgksanFQKPKVV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 575 vpEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWkdiadvcslSAADSTSDTGVFGSrvP 654
Cdd:cd14912 474 --KGKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF---------SGAQTAEGASAGGG--A 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 655 KKG------MFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRL 728
Cdd:cd14912 541 KKGgkkkgsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 71983975 729 PFQEFRQRYEKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14912 621 LYADFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-781 |
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: 631.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLAYVANRSmvknrktsvdlDTSTNRIMgqleEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGS-----------ESEVERVK----DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMKE 340
Cdd:cd01378 147 FDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 341 TLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNdqAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQ--- 417
Cdd:cd01378 227 VLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGN--AAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGggg 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 418 RDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQ 497
Cdd:cd01378 305 RSVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 498 QLFNNTMFVREQQEYLDEGLEWKFLDFgLNLQPTIDLID-KPMGIMSTLDDVCLFP-QGNDQSFVQRLNNTHSQHPKYVV 575
Cdd:cd01378 385 QIFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFEC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 576 PEIR---SRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADvcslsaADSTsdtgvfgSR 652
Cdd:cd01378 464 PSGHfelRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------LDSK-------KR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 653 VPkkgmfrTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQE 732
Cdd:cd01378 531 PP------TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEK 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 71983975 733 FRQRYeKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd01378 605 FLERY-KLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
101-781 |
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: 630.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLAYVAnrsMVKNRKTSvdlDTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIA---VTGEKKKE---EATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMKE 340
Cdd:cd14910 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 341 TLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKnNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRDL 420
Cdd:cd14910 236 TDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQR-EEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 421 VHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLF 500
Cdd:cd14910 315 VTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 501 NNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH------SQHPKYV 574
Cdd:cd14910 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgksnnFQKPKPA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 575 VPEIRSRsdFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKdiadvcSLSAADSTSDTGVFGSRvp 654
Cdd:cd14910 474 KGKVEAH--FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFS------GAAAAEAEEGGGKKGGK-- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 655 KKG-MFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEF 733
Cdd:cd14910 544 KKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 71983975 734 RQRYEKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14910 624 KQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
102-781 |
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: 626.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 102 VLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGES 181
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 182 GAGKTENTKKVIQYLAYVANRSMVKNRKTSvdldtstnRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVHF 261
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESG--------KMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 262 DSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMKET 341
Cdd:cd14918 155 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 342 LNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKnNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRDLV 421
Cdd:cd14918 235 DSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQR-EEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 422 HRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14918 314 TKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 502 NTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH------SQHPKYVv 575
Cdd:cd14918 393 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlgksanFQKPKVV- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 576 pEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADvcslSAADSTSDTGvfgsrVPK 655
Cdd:cd14918 472 -KGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYAS----AEADSGAKKG-----AKK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 656 KG-MFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFR 734
Cdd:cd14918 542 KGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFK 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 71983975 735 QRYEKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14918 622 QRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
101-781 |
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: 621.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLAYVAnrsMVKNRKTSvdlDTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIA---VTGEKKKE---EAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMKE 340
Cdd:cd14915 156 FGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 341 TLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKnNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRDL 420
Cdd:cd14915 236 TDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQR-EEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 421 VHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLF 500
Cdd:cd14915 315 VTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 501 NNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH------SQHPKYV 574
Cdd:cd14915 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgksnnFQKPKPA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 575 vpEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKdiadvcSLSAADSTSDTGVFGSRvp 654
Cdd:cd14915 474 --KGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFS------GGQTAEAEGGGGKKGGK-- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 655 KKG-MFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEF 733
Cdd:cd14915 544 KKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 71983975 734 RQRYEKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14915 624 KQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-781 |
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: 607.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLAYVANRSmvknrktsvdldtstnrimGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNH-------------------SWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKG--LSKVQREHYLLEDsLSKYKFVS-NGDSKLAGVDDGAE 337
Cdd:cd14883 143 FDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGE-PEDYHYLNqSGCIRIDNINDKKD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 338 MKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQ 417
Cdd:cd14883 222 FDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 418 RDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSvSFIGILDIAGFEIFETNSFEQLCINYTNEKLQ 497
Cdd:cd14883 302 GNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLH 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 498 QLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLIDK-PMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVP 576
Cdd:cd14883 381 KFFNHYVFKLEQEEYEKEGINWSHIVFTDN-QECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 577 EIR-SRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWK--DIADVCSLSAADSTSDTgvfgSRV 653
Cdd:cd14883 460 DRRrWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypDLLALTGLSISLGGDTT----SRG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 654 PKKGMfRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEF 733
Cdd:cd14883 536 TSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEF 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 71983975 734 RQRYeKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14883 615 VDRY-LCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
100-781 |
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: 606.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVAnrsmvknrktsvdldtstnrimGQ---LEEQLLQANPILEAFGNSKTVKNDNSSRFGKF 256
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS----------------------GQhswIEQQILEANPILEAFGNAKTIRNDNSSRFGKY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 257 IRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSlSKYKFVSNGDS-KLAGVDDG 335
Cdd:cd01381 139 IDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDA-SDYYYLTQGNClTCEGRDDA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 336 AEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQAVLLNDAVA-QKIASLLGVNVTELMRAFLKPKI 414
Cdd:cd01381 218 AEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDNLDASEVRDPPNlERAAKLLEVPKQDLVDALTTRTI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 415 KVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVS--FIGILDIAGFEIFETNSFEQLCINYT 492
Cdd:cd01381 298 FTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 493 NEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLI-DKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHP 571
Cdd:cd01381 378 NENLQQFFVRHIFKLEQEEYDKEGINWQHIEFVDN-QDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 572 KYVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDiadvcSLSAADSTSdtgvfgS 651
Cdd:cd01381 457 NYLKPKSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNE-----DISMGSETR------K 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 652 RVPkkgmfrTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQ 731
Cdd:cd01381 526 KSP------TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFE 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 71983975 732 EFRQRYeKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd01381 600 EFVERY-RVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-781 |
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: 604.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 179 GESGAGKTENTKKVIQYLAYVANRSMVKNRktSVdldtstnrimgqlEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIR 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGR--SV-------------EQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 259 VHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSlSKYKFVSNGDS-KLAGVDDGAE 337
Cdd:cd01384 146 IQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDP-KQFHYLNQSKCfELDGVDDAEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 338 MKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFShENKNNDQAVLLNDAV---AQKIASLLGVNVTELMRAFLKPKI 414
Cdd:cd01384 225 YRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFS-KGEEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 415 KVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNE 494
Cdd:cd01384 304 VTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIG-QDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 495 KLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLID-KPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKY 573
Cdd:cd01384 383 KLQQHFNQHVFKMEQEEYTKEEIDWSYIEFVDN-QDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 574 VVPEiRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLivdmwkdiadVCSLSAADSTSDTgvfgsrv 653
Cdd:cd01384 462 SKPK-LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPF----------VAGLFPPLPREGT------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 654 pKKGM-FRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQE 732
Cdd:cd01384 524 -SSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEE 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 71983975 733 FRQRYeKLLAPDVnPAGFMDGKNAVYRIVQYLEVDAnlFRIGQSKIFFR 781
Cdd:cd01384 603 FLDRF-GLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
101-781 |
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: 587.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKckKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLAYVANRSmvknrktsvdldtstnrimGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGS-------------------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLeDSLSKYKFVSNGDS-KLAGVDDGAEMK 339
Cdd:cd01383 141 FDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLNQSNClTIDGVDDAKKFH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFsHENKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRD 419
Cdd:cd01383 220 ELKEALDTVGISKEDQEHIFQMLAAVLWLGNISF-QVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 420 LVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQL 499
Cdd:cd01383 299 KIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQH 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 FNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLID-KPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYvvpEI 578
Cdd:cd01383 379 FNRHLFKLEQEEYELDGIDWTKVDFEDN-QECLDLIEkKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCF---KG 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 579 RSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIvdmwKDIADVCSLSAADSTSDTGVFGSRVPKkgm 658
Cdd:cd01383 455 ERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLP----QLFASKMLDASRKALPLTKASGSDSQK--- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 659 fRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYE 738
Cdd:cd01383 528 -QSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYG 606
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 71983975 739 KLLAPDVNPAGfmDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd01383 607 FLLPEDVSASQ--DPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-781 |
7.83e-174 |
|
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: 544.37 E-value: 7.83e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVANrsmvknrktsvdldtSTNRImgqlEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAG---------------STNGV----EQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLskVQREHYLLEDSlSKYKFVSNGDS-KLAGVDDGAEM 338
Cdd:cd14872 142 HFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSS-AAYGYLSLSGCiEVEGVDDVADF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 339 KETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQ--AVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKV 416
Cdd:cd14872 219 EEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVsgSTVANRDVLKEVATLLGVDAATLEEALTSRLMEI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 417 Q-----RDLVHRAQSVDQVNfsvgAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINY 491
Cdd:cd14872 299 KgcdptRIPLTPAQATDACD----ALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 492 TNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLIDK-PMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQH 570
Cdd:cd14872 375 TNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDFIDN-QPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 571 PKYVVPEIR-SRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKdiadvcsLSAADSTSdtgvf 649
Cdd:cd14872 454 STFVYAEVRtSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP-------PSEGDQKT----- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 650 gSRVPKKGMFRtvsqlykEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLP 729
Cdd:cd14872 522 -SKVTLGGQFR-------KQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYS 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 71983975 730 FQEFRQRYeKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14872 594 HERFLKRY-RFLVKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
100-781 |
3.10e-172 |
|
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: 540.50 E-value: 3.10e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAyvanrSMVKNRKTSVdldtstnrimgqlEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd01387 81 ESGSGKTEATKLIMQYLA-----AVNQRRNNLV-------------TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDStGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd01387 143 FFEG-GVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEF-SHENKNNDQAVLL-NDAVAQKIASLLGVNVTELMRAFLKPKIKVQ 417
Cdd:cd01387 222 RLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFhKRQLRHGQEGVSVgSDAEIQWVAHLLQISPEGLQKALTFKVTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 418 RDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSfIGILDIAGFEIFETNSFEQLCINYTNEKLQ 497
Cdd:cd01387 302 RERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-IAILDIFGFEDLSENSFEQLCINYANENLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 498 QLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLI-DKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVP 576
Cdd:cd01387 381 YYFNKHVFKLEQEEYIREQIDWTEIAFADN-QPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 577 EIRSRsDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVcslsaADSTSDTGVFGSRVPKK 656
Cdd:cd01387 460 RMPLP-EFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQ-----TDKAPPRLGKGRFVTMK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 657 GMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQR 736
Cdd:cd01387 534 PRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDR 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 71983975 737 YEKLLA-PDVNPAGFmDGKNAVYRIVQYLeVDANLFRIGQSKIFFR 781
Cdd:cd01387 614 YRCLVAlKLPRPAPG-DMCVSLLSRLCTV-TPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
100-781 |
3.64e-165 |
|
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: 521.04 E-value: 3.64e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYT-DTIaEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILC 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSsETI-KSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 178 TGESGAGKTENTKKVIQYLAYvanrsmvkNRKTSVdldtstnrimGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFI 257
Cdd:cd01382 80 SGESGAGKTESTKYILRYLTE--------SWGSGA----------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 258 RVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHyLLEDSLskykfvsngdsklagVDDGAE 337
Cdd:cd01382 142 EIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREK-LLKDPL---------------LDDVGD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 338 MKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFShENKNNDQAVLLNDAVAQK----IASLLGVNVTEL-----MRA 408
Cdd:cd01382 206 FIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFE-ENGSDSGGGCNVKPKSEQsleyAAELLGLDQDELrvsltTRV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 409 FLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLdrTRQQSVSFIGILDIAGFEIFETNSFEQLC 488
Cdd:cd01382 285 MQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCI--PFETSSYFIGVLDIAGFEYFEVNSFEQFC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 489 INYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLID-KPMGIMSTLDDVCLFPQGNDQSFVQRLNNTH 567
Cdd:cd01382 363 INYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEYVDN-QDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 568 SQHPKYVVP---------EIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADvcslS 638
Cdd:cd01382 442 KNHFRLSIPrksklkihrNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTN----N 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 639 AADSTSDTGvfgsrvpkKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIR 718
Cdd:cd01382 518 NKDSKQKAG--------KLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLD 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 719 ICRQGFPTRLPFQEFRQRYEKLLAPDV---NPAGFMdgkNAVYRIVQYLEVDanlFRIGQSKIFFR 781
Cdd:cd01382 590 LMQGGFPSRTSFHDLYNMYKKYLPPKLarlDPRLFC---KALFKALGLNEND---FKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
100-781 |
1.67e-164 |
|
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: 519.72 E-value: 1.67e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQ----ERDDQS 174
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 175 ILCTGESGAGKTENTKKVIQYLAYVANRSMVKNRKTSVDLDTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFG 254
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 255 KFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNgDSKLAGVDD 334
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGE-CSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 335 GAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHEnknNDQAVLLNDAVAQ---KIASLLGVNVTELMRAFLK 411
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE---NDTTVLEDATTLQslkLAAELLGVNEDALEKALLT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 412 PKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTrQQSVSFIGILDIAGFEIFETNSFEQLCINY 491
Cdd:cd14890 317 RQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSP-DDKWGFIGVLDIYGFEKFEWNTFEQLCINY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 492 TNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLID-----KPmGIMSTLDDVCLFPQGN-DQSFVQRLNN 565
Cdd:cd14890 396 ANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDN-QACLELIEgkvngKP-GIFITLDDCWRFKGEEaNKKFVSQLHA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 566 TH-------------SQHPKYVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLivdmwkdia 632
Cdd:cd14890 474 SFgrksgsggtrrgsSQHPHFVHPKFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI--------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 633 dvcslsaaDSTSdtgvfgsrvpkkgmfrtVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNG 712
Cdd:cd14890 545 --------REVS-----------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSG 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 713 VLEGIRICRQGFPTRLPFQEFRQRYEKLLaPDVNpagfmDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14890 600 MMEAIQIRQQGFALREEHDSFFYDFQVLL-PTAE-----NIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-779 |
1.11e-163 |
|
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: 517.03 E-value: 1.11e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQF------KCKKRKEMPPHIFAVADEAYRSMLQERD-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 172 --DQSILCTGESGAGKTENTKKVIQYLAYVANRSmvKNRKTSVDLDTSTNRImgqleeqlLQANPILEAFGNSKTVKNDN 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSAT--THGQNATERENVRDRV--------LESNPILEAFGNARTNRNNN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 250 SSRFGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSL-SKYKFVSNGDSK 328
Cdd:cd14901 151 SSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 329 LAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQAVLLNDAVAQKIASLLGVNVTELMRA 408
Cdd:cd14901 231 RDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 409 FLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLD-RTRQQSVSFIGILDIAGFEIFETNSFEQL 487
Cdd:cd14901 311 LCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAySESTGASRFIGIVDIFGFEIFATNSLEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 488 CINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFglnlqPTIDLI-----DKPMGIMSTLDDVCLFPQGNDQSFVQR 562
Cdd:cd14901 391 CINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PNNDACvamfeARPTGLFSLLDEQCLLPRGNDEKLANK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 563 LNNTHSQHPKYVVPEI-RSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLivdmwkdiadvcsLSAad 641
Cdd:cd14901 466 YYDLLAKHASFSVSKLqQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF-------------LSS-- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 642 stsdtgvfgsrvpkkgmfrTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICR 721
Cdd:cd14901 531 -------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISR 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71983975 722 QGFPTRLPFQEFRQRYEkLLAPDVNPAGFMDGKNAVYRIVQYLEVDANL-----FRIGQSKIF 779
Cdd:cd14901 592 SGYPVRFPHDAFVHTYS-CLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
100-781 |
1.03e-162 |
|
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: 514.97 E-value: 1.03e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP---------IYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQER 170
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 171 DDQSILCTGESGAGKTENTKKVIQYL----AYVANRSMVKNRKTSVDldtSTNRIMGQLEEQLLQANPILEAFGNSKTVK 246
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsQQEQNSEEVLTLTSSIR---ATSKSTKSIEQKILSCNPILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 247 NDNSSRFGKFIRVHFD-STGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVS-- 323
Cdd:cd14907 158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRYDYlk 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 324 -NGDSKLAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEF--SHENKNNDQAVLlNDAVAQKIASLLGV 400
Cdd:cd14907 238 kSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddSTLDDNSPCCVK-NKETLQIIAKLLGI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 401 NVTELMRAFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSL-------DRTRQQSVSFIGILDI 473
Cdd:cd14907 317 DEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 474 AGFEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKF--LDFGLNlQPTIDLIDK-PMGIMSTLDDVCL 550
Cdd:cd14907 397 FGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDN-QDVIDLLDKpPIGIFNLLDDSCK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 551 FPQGNDQSFVQRLNNTHSQHPKYVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKD 630
Cdd:cd14907 476 LATGTDEKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 631 IADvcslsaadstSDTGVFGSRVPKKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRC 710
Cdd:cd14907 556 EDG----------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71983975 711 NGVLEGIRICRQGFPTRLPFQEFRQRYEKLLapdvnpagfmdgKNAVYrivqylevdanlfriGQSKIFFR 781
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLLK------------KNVLF---------------GKTKIFMK 669
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
100-781 |
8.10e-162 |
|
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: 8.10e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEM---PPHIFAVADEAYRSMLQER----DD 172
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 173 QSILCTGESGAGKTENTKKVIQYLAYVAnrsmvKNRKTSVDLDTSTNrIMGQLEEQLLQANPILEAFGNSKTVKNDNSSR 252
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATAS-----KLAKGASTSKGAAN-AHESIEECVLLSNLILEAFGNAKTIRNDNSSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 253 FGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSlSKYKFVSNGDS-KLAG 331
Cdd:cd14892 155 FGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPA-ESFLFLNQGNCvEVDG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 332 VDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQAVLLNDAVA-QKIASLLGVNVTELMRAFL 410
Cdd:cd14892 234 VDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvAKAAGLLGVDAAELMFKLV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 411 KPKIKVQR-DLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQS---------VSFIGILDIAGFEIFE 480
Cdd:cd14892 314 TQTTSTARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGVtggaasptfSPFIGILDIFGFEIMP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 481 TNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLIDK-PMGIMSTLDD-VCLFPQGNDQS 558
Cdd:cd14892 394 TNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDN-QDCLDLIQKkPLGLLPLLEEqMLLKRKTTDKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 559 FVQRLNNTH-SQHPKYVVPEIRSrSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKEslivdmwkdiadvcsl 637
Cdd:cd14892 473 LLTIYHQTHlDKHPHYAKPRFEC-DEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK---------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 638 saadstsdtgvfgsrvpkkgmFRTvsqlykeQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGI 717
Cdd:cd14892 536 ---------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 718 RICRQGFPTRLPFQEFRQRYEKLLAPDVNPAGFMDGKNAVYRIVQYLEV-----DANLFRIGQSKIFFR 781
Cdd:cd14892 588 RIRREGFPIRRQFEEFYEKFWPLARNKAGVAASPDACDATTARKKCEEIvaralERENFQLGRTKVFLR 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-744 |
4.92e-161 |
|
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: 510.39 E-value: 4.92e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQFKcKKRKEMPPHIFAVADEAYRSMLQERDDQSILCT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 179 GESGAGKTENTKKVIQYLAYVANRSmVKNRKTsvdldtstnrimgqLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIR 258
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSED-IKKRSL--------------VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 259 VHFD---------STGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKY------KFVS 323
Cdd:cd14888 145 LQFSklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLakgadaKPIS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 324 NGDSK-----------------LAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFShENKNNDQAVLL 386
Cdd:cd14888 225 IDMSSfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFE-NNEACSEGAVV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 387 NDAVAQ---KIASLLGVNVTELMRAFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQ 463
Cdd:cd14888 304 SASCTDdleKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 464 SVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLI-DKPMGIM 542
Cdd:cd14888 384 SLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDN-QDCVDLLqEKPLGIF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 543 STLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVpeIRSRSD-FAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKE 621
Cdd:cd14888 463 CMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDV--VKTDPNsFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 622 SLIVDMWKDIadvcsLSAADSTSdtgvfgsrvPKKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNA 701
Cdd:cd14888 541 PFISNLFSAY-----LRRGTDGN---------TKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDR 606
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 71983975 702 HLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEKLLAPD 744
Cdd:cd14888 607 ISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLNGE 649
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
100-781 |
9.77e-158 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 500.86 E-value: 9.77e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCT 178
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 179 GESGAGKTENTKKVIQYLAYVANRSmvknrktsvdLDTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIR 258
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQS----------LELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 259 VHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSlSKYKFVS-NGDSKLAGVDDGAE 337
Cdd:cd14873 151 LNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTP-ENYHYLNqSGCVEDKTISDQES 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 338 MKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFShenkNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQ 417
Cdd:cd14873 230 FREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI----TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 418 RDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLdrTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQ 497
Cdd:cd14873 306 GEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 498 QLFNNTMFVREQQEYLDEGLEWKFLDFGLNLQpTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVPE 577
Cdd:cd14873 384 EYFNKHIFSLEQLEYSREGLVWEDIDWIDNGE-CLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 578 IRSRsDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKdiaDVCSLSAADStsdtgvfgsrvPKKG 657
Cdd:cd14873 463 VAVN-NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFE---HVSSRNNQDT-----------LKCG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 658 MFR---TVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFR 734
Cdd:cd14873 528 SKHrrpTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFY 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 71983975 735 QRYeKLLAPDVNPAGFMDGKNAVyrIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14873 608 KRY-KVLMRNLALPEDVRGKCTS--LLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
100-781 |
4.23e-156 |
|
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: 495.75 E-value: 4.23e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKK-RKEMPPHIFAVADEAYRSMLQERDDQSILCT 178
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 179 GESGAGKTENTKKVIQYLAYVanrsmvknrktsvdldtsTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIR 258
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKL------------------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 259 VHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSlSKYKFVSNGDSKLAGVDDGAEM 338
Cdd:cd14897 143 LHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDP-DCHRILRDDNRNRPVFNDSEEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 339 K-------ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFShENKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLK 411
Cdd:cd14897 222 EyyrqmfhDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFI-PDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALIS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 412 PKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSL----DRTRQQSVSFIGILDIAGFEIFETNSFEQL 487
Cdd:cd14897 301 NVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 488 CINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLI-DKPMGIMSTLDDVCLFPQGNDQSFVQRLNNT 566
Cdd:cd14897 381 CINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYHDN-DDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNKY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 567 HSQHPKYvVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWkdiadvcslsaadstsdt 646
Cdd:cd14897 460 CGESPRY-VASPGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF------------------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 647 gvfgsrvpkkgmfrtvSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPT 726
Cdd:cd14897 521 ----------------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 727 RLPFQEFRQRYeKLLAPDVNPAGFMDGKNAVyRIVQYLEVDAnlFRIGQSKIFFR 781
Cdd:cd14897 585 RIKYEDFVKRY-KEICDFSNKVRSDDLGKCQ-KILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
100-781 |
4.23e-155 |
|
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: 494.97 E-value: 4.23e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVANrsmvKNRKTSVdldtstnrimgqlEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTALSQ----KGYGSGV-------------EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSlSKYKFVSNGDSK-LAGVDDGAEM 338
Cdd:cd01385 144 NYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQP-EDYHYLNQSDCYtLEGEDEKYEF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 339 KETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQAVLL-NDAVAQKIASLLGVNVTELMRAFLKPKIKVQ 417
Cdd:cd01385 223 ERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAYHRDESVTVgNPEVLDIISELLRVKEETLLEALTTKKTVTV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 418 RDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSL---DRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNE 494
Cdd:cd01385 303 GETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 495 KLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNLQpTIDLID-KPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKY 573
Cdd:cd01385 383 HLQYYFNQHIFKLEQEEYKKEGISWHNIEYTDNTG-CLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 574 VVPEIRSRSdFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDM----------WKDI----------AD 633
Cdd:cd01385 462 EKPQVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrWAVLrafframaafRE 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 634 VCSLSAADSTSDTGVFGSRVPKKGMFR-------TVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLD 706
Cdd:cd01385 541 AGRRRAQRTAGHSLTLHDRTTKSLLHLhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLR 620
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 707 QLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEKLLapdvnPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd01385 621 QLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLL-----PKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-781 |
3.07e-151 |
|
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: 483.12 E-value: 3.07e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 179 GESGAGKTENTKKVIQYLAYVANrsmvknrktsvDLDTSTNRimgqleeQLLQANPILEAFGNSKTVKNDNSSRFGKFIR 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG-----------GLNDSTIK-------KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 259 VHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGlSKVQREHYLLEDSLSKYKFvSNGDSKLAGVDDGAEM 338
Cdd:cd14903 143 LQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLAS-PDVEERLFLDSANECAYTG-ANKTIKIEGMSDRKHF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 339 KETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEF-SHENKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQ 417
Cdd:cd14903 221 ARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIqSKPNDDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 418 RDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSvSFIGILDIAGFEIFETNSFEQLCINYTNEKLQ 497
Cdd:cd14903 301 GDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMA-NHIGVLDIFGFEHFKHNSFEQFCINYANEKLQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 498 QLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYV-VP 576
Cdd:cd14903 380 QKFTQDVFKTVQIEYEEEGIRWAHIDFADN-QDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIeFP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 577 EIrSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIAdvcSLSAADSTSDTGVFGSRVPKK 656
Cdd:cd14903 459 RT-SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKV---ESPAAASTSLARGARRRRGGA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 657 GMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQR 736
Cdd:cd14903 535 LTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDK 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 71983975 737 YEKLLapDVNPAGFMDGKNAVYRIVQYLEVDA-NLFRIGQSKIFFR 781
Cdd:cd14903 615 FWLFL--PEGRNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
101-781 |
2.00e-149 |
|
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: 477.15 E-value: 2.00e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLayvanrsmvknrktsVDLDTSTNRimgQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd01379 82 SGAGKTESANLLVQQL---------------TVLGKANNR---TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQR-EHYLLEDSLSKYKFVSNGDSKLAGVDDGA--- 336
Cdd:cd01379 144 FTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNSGnre 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 337 EMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSH---ENKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPK 413
Cdd:cd01379 224 KFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEvesNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 414 IKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVS--FIGILDIAGFEIFETNSFEQLCINY 491
Cdd:cd01379 304 VVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDEplSIGILDIFGFENFQKNSFEQLCINI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 492 TNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTID-LIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQH 570
Cdd:cd01379 384 ANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEDN-RPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 571 PkYVVPEiRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVdmwkdiadvcslsaadstsdtgvfg 650
Cdd:cd01379 463 Y-YWRPK-SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 651 srvpkkgmfRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPF 730
Cdd:cd01379 516 ---------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILF 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 71983975 731 QEFRQRYeKLLAPDVNPAGFMDGKNAVyRIVQYLEVDAnlFRIGQSKIFFR 781
Cdd:cd01379 587 ADFLKRY-YFLAFKWNEEVVANRENCR-LILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-781 |
5.16e-141 |
|
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: 454.75 E-value: 5.16e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 102 VLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSML----QERDDQSILC 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 178 TGESGAGKTENTKKVIQYLAYVAnrsmvknrktsvdldtstnRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFI 257
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC-------------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 258 RVHFDStGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSlSKYKFVSNG-DSKLAGVDDGA 336
Cdd:cd14889 144 QLRFRN-GHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDP-GKYRYLNNGaGCKREVQYWKK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 337 EMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFshENKNNDQAVLLNDAVA--QKIASLLGVNVTELMRAFLKPKI 414
Cdd:cd14889 222 KYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGwlKAAAGQFGVSEEDLLKTLTCTVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 415 KVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSF--IGILDIAGFEIFETNSFEQLCINYT 492
Cdd:cd14889 300 FTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVELreIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 493 NEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDL-IDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHP 571
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITYKDN-KPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 572 KYVVPEIRSRSdFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIvdmwkdiadvcSLSAADSTSDTGVFGS 651
Cdd:cd14889 459 YYGKSRSKSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLL-----------SVLFTATRSRTGTLMP 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 652 RVPK---------KGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQ 722
Cdd:cd14889 527 RAKLpqagsdnfnSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRRE 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 723 GFPTRLPFQEFRQRYEKLLAPDVNPAgfmdGKNAVYRIVQYLEVDAnlFRIGQSKIFFR 781
Cdd:cd14889 607 GFSWRPSFAEFAERYKILLCEPALPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
81-831 |
6.47e-140 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 457.57 E-value: 6.47e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 81 NPPKYDkceDMSMLTCLNEASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYT-DTIAEQFKCKKRKEMPPHIFAVA 159
Cdd:PTZ00014 94 DPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTnDWIRRYRDAKDSDKLPPHVFTTA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 160 DEAYRSMLQERDDQSILCTGESGAGKTENTKKVIQYLAYVANRSMvknrktsvDLDTStNRIMGqleeqllqANPILEAF 239
Cdd:PTZ00014 171 RRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNM--------DLKIQ-NAIMA--------ANPVLEAF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 240 GNSKTVKNDNSSRFGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEdSLSKY 319
Cdd:PTZ00014 234 GNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLK-SLEEY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 320 KFVSNGDSKLAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKN--NDQAVLLND--AVAQKIA 395
Cdd:PTZ00014 313 KYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGglTDAAAISDEslEVFNEAC 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 396 SLLGVNVTELMRAFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVsFIGILDIAG 475
Cdd:PTZ00014 393 ELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 476 FEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGN 555
Cdd:PTZ00014 472 FEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGT 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 556 DQSFVQRLNNTHSQHPKYVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVC 635
Cdd:PTZ00014 552 DEKFVSSCNTNLKNNPKYKPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEK 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 636 SLSAadstsdtgvfgsrvpkKGMFRTvSQlYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLE 715
Cdd:PTZ00014 632 GKLA----------------KGQLIG-SQ-FLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILE 693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 716 GIRICRQGFPTRLPFQEFRQRYEKLLAPDVNPAGfMDGKNAVYRIVQYLEVDANLFRIGQSKIFFRSGVIAEFEEMRDQK 795
Cdd:PTZ00014 694 ALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSS-LDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREK 772
|
730 740 750
....*....|....*....|....*....|....*....
gi 71983975 796 LSA---LIESFQAqcrgwLGRRVMvRRREQEVAIKILQR 831
Cdd:PTZ00014 773 LAAwepLVSVLEA-----LILKIK-KKRKVRKNIKSLVR 805
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
101-737 |
3.85e-139 |
|
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: 448.22 E-value: 3.85e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP------------IYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQ 168
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPglyssdtmakylLSFEARSSSTRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 169 ERD----DQSILCTGESGAGKTENTKKVIQYLAYVANrsmvKNRKTSVDLDTSTNRImgqlEEQLLQANPILEAFGNSKT 244
Cdd:cd14900 82 GLNgvmsDQSILVSGESGSGKTESTKFLMEYLAQAGD----NNLAASVSMGKSTSGI----AAKVLQTNILLESFGNART 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 245 VKNDNSSRFGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLedslskykfvsn 324
Cdd:cd14900 154 LRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKRDMY------------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 325 gdsklagvddgaemKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQAVLLNDAVAQKI------ASLL 398
Cdd:cd14900 222 --------------RRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSSIwsrdaaATLL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 399 GVNVTELMRAFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLN---KSLDR-TRQQSVSFIGILDIA 474
Cdd:cd14900 288 SVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNaflKMDDSsKSHGGLHFIGILDIF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 475 GFEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLID-KPMGIMSTLDDVCLFPQ 553
Cdd:cd14900 368 GFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDN-QDCVNLISqRPTGILSLIDEECVMPK 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 554 GNDQSFVQRLNNTHSQHPKYVVPEI-RSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDvlktskeslivdmwkdia 632
Cdd:cd14900 447 GSDTTLASKLYRACGSHPRFSASRIqRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVD------------------ 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 633 dvcslsaadstsdtgvfgsrvpkkgMFRTVSQlYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNG 712
Cdd:cd14900 509 -------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNG 562
|
650 660
....*....|....*....|....*
gi 71983975 713 VLEGIRICRQGFPTRLPFQEFRQRY 737
Cdd:cd14900 563 VMEAVRVARAGFPIRLLHDEFVARY 587
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-741 |
5.48e-136 |
|
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: 442.79 E-value: 5.48e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP---------IYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQ-E 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdlysesqlnAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 170 RDDQSILCTGESGAGKTENTKKVIQYLAyvanrsMVKNRKTSVDLDTSTNRIMGQleeQLLQANPILEAFGNSKTVKNDN 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLT------SVGRDQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 250 SSRFGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDS-----LSKYkFVSN 324
Cdd:cd14902 152 SSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGgkyelLNSY-GPSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 325 GDSKLAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQAVL--LNDAVAQKIASLLGVNV 402
Cdd:cd14902 231 ARKRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVtaASRFHLAKCAELMGVDV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 403 TELMRAFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLD--------RTRQQSVSFIGILDIA 474
Cdd:cd14902 311 DKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 475 GFEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQG 554
Cdd:cd14902 391 GFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 555 NDQSFVQRLNNTHSQhpkyvvpeirsRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDiadv 634
Cdd:cd14902 471 SNQALSTKFYRYHGG-----------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGAD---- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 635 csLSAADSTSDTGVFGSRVPKKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVL 714
Cdd:cd14902 536 --ENRDSPGADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVL 613
|
650 660
....*....|....*....|....*..
gi 71983975 715 EGIRICRQGFPTRLPFQEFRQRYEKLL 741
Cdd:cd14902 614 EAVRIARHGYSVRLAHASFIELFSGFK 640
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-781 |
1.43e-135 |
|
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: 439.09 E-value: 1.43e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRY-FSNLY-YTYSGLFCVVINPYKRI--PIYTDTIAEQFKckkrkEMPPHIFAVADEAYRSM--LQERD-D 172
Cdd:cd14891 1 AGILHNLEERSkLDNQRpYTFMANVLIAVNPLRRLpePDKSDYINTPLD-----PCPPHPYAIAEMAYQQMclGSGRMqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 173 QSILCTGESGAGKTENTKKVIQYLAyvaNRSMV--KNRKTSVDLDTSTNRIMGQ-LEEQLLQANPILEAFGNSKTVKNDN 249
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLT---TRAVGgkKASGQDIEQSSKKRKLSVTsLDERLMDTNPILESFGNAKTLRNHN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 250 SSRFGKFIRVHFDSTGC-ISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSK 328
Cdd:cd14891 153 SSRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 329 LAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQAVLLNDAVAQKI---ASLLGVNVTEL 405
Cdd:cd14891 233 DDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEALataAELLGVDEEAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 406 MRAFLkpkikvQRDLVHRAQ------SVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRqQSVSFIGILDIAGFEIF 479
Cdd:cd14891 313 EKVIT------QREIVTRGEtftikrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDP-DPLPYIGVLDIFGFESF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 480 ET-NSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGlewkfLDFGLNLQP----TIDLI-DKPMGIMSTLDDVCLFPQ 553
Cdd:cd14891 386 ETkNDFEQLLINYANEALQATFNQQVFIAEQELYKSEG-----IDVGVITWPdnreCLDLIaSKPNGILPLLDNEARNPN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 554 GNDQSFVQRLNNTHSQHPKYVVPEIRS-RSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKeslivdmwkdia 632
Cdd:cd14891 461 PSDAKLNETLHKTHKRHPCFPRPHPKDmREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA------------ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 633 dvcslsaadstsdtgvfgsrvpkkgmfrtvsqLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNG 712
Cdd:cd14891 529 --------------------------------KFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSG 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 713 VLEGIRICRQGFPTRLPFQEFRQRYEKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14891 577 ILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-781 |
7.95e-134 |
|
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: 435.49 E-value: 7.95e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFK---------CKKRKEMPPHIFAVADEAYRSMLQE- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqegllrsqgIESPQALGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 170 RDDQSILCTGESGAGKTENTKKVIQYLAYVANRSMVknrktsVDLDTSTNRiMGQLEEQLLQANPILEAFGNSKTVKNDN 249
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEG------APNEGEELG-KLSIMDRVLQSNPILEAFGNARTLRNDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 250 SSRFGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSK-------YKFV 322
Cdd:cd14908 154 SSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGglqlpneFHYT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 323 SNGDS-KLAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFshENKNNDQAVLL----NDAVAQKIASL 397
Cdd:cd14908 234 GQGGApDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEF--ESKEEDGAAEIaeegNEKCLARVAKL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 398 LGVNVTELMRAFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSV-SFIGILDIAGF 476
Cdd:cd14908 312 LGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 477 EIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLID-KPMGIMSTLDDVCLFPQ-G 554
Cdd:cd14908 392 ECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDN-QDCLDTIQaKKKGILTMLDDECRLGIrG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 555 NDQSFVQRL--------NNTHSQHPKYVVPEI-RSRSDFAVVHYAGRVDYQSE-GWRVKNMDplnenviDVLKTSKEsli 624
Cdd:cd14908 471 SDANYASRLyetylpekNQTHSENTRFEATSIqKTKLIFAVRHFAGQVQYTVEtTFCEKNKD-------EIPLTADS--- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 625 vdmwkdiadvcslsaadstsdtgvfgsrvpkkgMFRTvSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLV 704
Cdd:cd14908 541 ---------------------------------LFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRV 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 705 LDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEKLLA--PDVNPAGFMDGKNAVYRIVQYLEVD--------------- 767
Cdd:cd14908 587 TEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPliPEVVLSWSMERLDPQKLCVKKMCKDlvkgvlspamvsmkn 666
|
730
....*....|....*.
gi 71983975 768 --ANLFRIGQSKIFFR 781
Cdd:cd14908 667 ipEDTMQLGKSKVFMR 682
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-779 |
1.99e-132 |
|
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: 430.18 E-value: 1.99e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFK-CKKRKEMPPHIFAVADEAYRSMLQERDDQSILCT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRdAPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 179 GESGAGKTENTKKVIQYLAYVANRSMvknrktsvdldtsTNRImgqlEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIR 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKSGNM-------------DLRI----QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 259 VHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDsLSKYKFVSNGDSKLAGVDDGAEM 338
Cdd:cd14876 144 LDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 339 KETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKN--NDQAVLLND--AVAQKIASLLGVNVTELMRAFLKPKI 414
Cdd:cd14876 223 EEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQgvDDAAAISNEslEVFKEACSLLFLDPEALKRELTVKVT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 415 KVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVsFIGILDIAGFEIFETNSFEQLCINYTNE 494
Cdd:cd14876 303 KAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 495 KLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNLqPTID-LIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKY 573
Cdd:cd14876 382 MLQKNFIDIVFERESKLYKDEGIPTAELEYTSNA-EVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 574 VVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIadvcslsaadsTSDTGVFGsrv 653
Cdd:cd14876 461 KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV-----------VVEKGKIA--- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 654 pkKGMFrTVSQLYKeQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEF 733
Cdd:cd14876 527 --KGSL-IGSQFLK-QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 71983975 734 RQRYeKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIF 779
Cdd:cd14876 603 LYQF-KFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-781 |
9.43e-132 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 428.04 E-value: 9.43e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLayvanrsmvknrkTSVDLDTSTNRIMgQLEEQLlqanPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL-------------SSLYQDQTEDRLR-QPEDVL----PILESFGHAKTILNANASRFGQVLRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDStGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd14896 143 HLQH-GVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEF-SHENKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQR 418
Cdd:cd14896 222 GLLKALQGLGLCAEELTAIWAVLAAILQLGNICFsSSERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 419 DLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQ-QSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQ 497
Cdd:cd14896 302 GRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEaESDATIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 498 QLFNNTMFVREQQEYLDEGLEWKFLDfGLNLQPTIDLI-DKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVP 576
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 577 EIrSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVCSLSAADSTsdtgvFGSRvpkk 656
Cdd:cd14896 461 QL-PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKPT-----LASR---- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 657 gmfrtvsqlYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQR 736
Cdd:cd14896 531 ---------FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLAR 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 71983975 737 YEKLLAPDVNPAGFMDGKNAVyrIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14896 602 FGALGSERQEALSDRERCGAI--LSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-743 |
1.76e-130 |
|
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: 425.13 E-value: 1.76e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 179 GESGAGKTENTKKVIQYLAYVANrsmvknrktsvDLDTSTnrimgqlEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIR 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG-----------GRKDKT-------IAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 259 VHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLS-KYKFVSNGDSKLAGVDDGAE 337
Cdd:cd14904 143 LQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQyQYLGDSLAQMQIPGLDDAKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 338 MKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNdqAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQ 417
Cdd:cd14904 223 FASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENG--SRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 418 RDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQ 497
Cdd:cd14904 301 NESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 498 QLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQR--------LNNTHSQ 569
Cdd:cd14904 381 QKFTTDVFKTVEEEYIREGLQWDHIEYQDN-QGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKirtnhqtkKDNESID 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 570 HPKYvvpeirSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDiadvcslsaADSTSDTGVF 649
Cdd:cd14904 460 FPKV------KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS---------SEAPSETKEG 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 650 GSRVPKKGMFRTVSQlYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLP 729
Cdd:cd14904 525 KSGKGTKAPKSLGSQ-FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLT 603
|
650
....*....|....
gi 71983975 730 FQEFRQRYEKLLAP 743
Cdd:cd14904 604 PKELATRYAIMFPP 617
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
100-741 |
8.74e-121 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 399.74 E-value: 8.74e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQFK-CKKRKEMPPHIFAVADEAYRSMLQERDDQSILC 177
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKdINQNKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 178 TGESGAGKTENTKKVIQYLAYVANRSMVKNrktsvdldTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFI 257
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQN--------NNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 258 RVHFDST-GCISGANIEFYLLEKSRVLKQAPNER-SFHIFYQLLKGLSKVQREHYLLEDSLSKYKFV------------- 322
Cdd:cd14906 153 KIEFRSSdGKIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLdarddvissfksq 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 323 -SNGDSKLAGVDDGAE----MKETLNAMSImglNDEEIGGILRVVSAVMLFGNLEFsHENKNNDQAVLLNDAVAQKIAS- 396
Cdd:cd14906 233 sSNKNSNHNNKTESIEsfqlLKQSMESMSI---NKEQCDAIFLSLAAILHLGNIEF-EEDSDFSKYAYQKDKVTASLESv 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 397 --LLGVNVTELMRAFLKPKIKVQ-RDLVH-RAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQ--------- 463
Cdd:cd14906 309 skLLGYIESVFKQALLNRNLKAGgRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSndlaggsnk 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 464 -SVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFgLNLQPTIDLID-KPMGI 541
Cdd:cd14906 389 kNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 542 MSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVPEIrSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKE 621
Cdd:cd14906 468 LSLLDDECIMPKGSEQSLLEKYNKQYHNTNQYYQRTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 622 SLIvdmwkdiadvCSLSAADSTSDTgvfgSRVPKKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNA 701
Cdd:cd14906 547 FLK----------KSLFQQQITSTT----NTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNN 612
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 71983975 702 HLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEKLL 741
Cdd:cd14906 613 VHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
101-742 |
3.05e-119 |
|
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: 394.70 E-value: 3.05e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSM---LQE----RDDQ 173
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYDLHKYREEMPGWTALPPHVFSIAEGAYRSLrrrLHEpgasKKNQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 174 SILCTGESGAGKTENTKKVIQYLAYVAnrsmvknRKTSVDLDTSTNRIMGQleEQLLQANPILEAFGNSKTVKNDNSSRF 253
Cdd:cd14895 82 TILVSGESGAGKTETTKFIMNYLAESS-------KHTTATSSSKRRRAISG--SELLSANPILESFGNARTLRNDNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 254 GKFIRVHF-----DSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLS-KVQREHYLLEDSLSKYKFVSNGD- 326
Cdd:cd14895 153 GKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAAdDMKLELQLELLSAQEFQYISGGQc 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 327 -SKLAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEF--------SHENKNNDQAVLLNDAVAQKIA-- 395
Cdd:cd14895 233 yQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFvassedegEEDNGAASAPCRLASASPSSLTvq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 396 -------SLLGVNVTELMRAFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQ----- 463
Cdd:cd14895 313 qhldivsKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFAlnpnk 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 464 -----SVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLID-K 537
Cdd:cd14895 393 aankdTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 538 PMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVpeirSRSD-----FAVVHYAGRVDYQSEGWRVKNMDPLNENV 612
Cdd:cd14895 472 PSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSA----SRTDqadvaFQIHHYAGAVRYQAEGFCEKNKDQPNAEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 613 IDVLKTSKESLIVDMWKDIAdvCSLSAADSTSDTGVFGSRVPKKGMfrTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNH 692
Cdd:cd14895 548 FSVLGKTSDAHLRELFEFFK--ASESAELSLGQPKLRRRSSVLSSV--GIGSQFKQQLASLLDVVQQTQTHYIRCIKPND 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 71983975 693 EKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEKLLA 742
Cdd:cd14895 624 ESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA 673
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
100-740 |
1.03e-115 |
|
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: 383.05 E-value: 1.03e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQFKCKKR-KEMPPHIFAVADEAYRSMLQERD--DQSI 175
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 176 LCTGESGAGKTENTKKVIQYLAYVANRSmvknrkTSVDldtsTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGK 255
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASP------TSWE----SHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 256 FIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSlSKYKFVSNGDSKLAgvDDG 335
Cdd:cd14880 151 FIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEG-AAFSWLPNPERNLE--EDC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 336 AEMkeTLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQAVLLNDA--VAQKIASLLGVNVTELMRAFLKPK 413
Cdd:cd14880 228 FEV--TREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkeSVRTSALLLKLPEDHLLETLQIRT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 414 IKV--QRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINY 491
Cdd:cd14880 306 IRAgkQQQVFKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 492 TNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLID-KPMGIMSTLDDVCLFPQGNDQSFVQ-RLNNTHSQ 569
Cdd:cd14880 386 ANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDN-QTCLDLIEgSPISICSLINEECRLNRPSSAAQLQtRIESALAG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 570 HPKYVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDiadvcslSAADSTSDTGVF 649
Cdd:cd14880 465 NPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPA-------NPEEKTQEEPSG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 650 GSRVPkkgmFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLP 729
Cdd:cd14880 538 QSRAP----VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVS 613
|
650
....*....|.
gi 71983975 730 FQEFRQRYEKL 740
Cdd:cd14880 614 HQNFVERYKLL 624
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
100-741 |
1.13e-113 |
|
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: 379.05 E-value: 1.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQF----------KCKKRKEMPPHIFAVADEAYRSMLQ 168
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 169 ERDDQSILCTGESGAGKTENTKKVIQYLAyVANRSMVKNRKTSVDLDTSTNRIMGQLEEQLLQANPILEAFGNSKTVKND 248
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 249 NSSRFGKFIRVHF-DSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKG----LSKVQREHYLLEDSLSKYKFVS 323
Cdd:cd14899 160 NSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 324 NG--DSKLAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEF---SHENKNN---DQAVLLNDAVA---- 391
Cdd:cd14899 240 QSlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiPHKGDDTvfaDEARVMSSTTGafdh 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 392 -QKIASLLGVNVTELMRAFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRT---------- 460
Cdd:cd14899 320 fTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgades 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 461 ----RQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGlNLQPTIDLID 536
Cdd:cd14899 400 dvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 537 -KPMGIMSTLDDVCLFPQGNDQSFVQRLN---NTHSQHPKY-VVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNEN 611
Cdd:cd14899 479 hRPIGIFSLTDQECVFPQGTDRALVAKYYlefEKKNSHPHFrSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCES 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 612 VIDVLKTSKESLIVDMWKDIADVCSLSAADSTSDTGVFGSRVPKKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPN 691
Cdd:cd14899 559 AAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKPN 638
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 71983975 692 HEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEKLL 741
Cdd:cd14899 639 DSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRRVL 688
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
100-781 |
2.11e-113 |
|
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: 376.15 E-value: 2.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQFKCKKRK-----EMPPHIFAVADEAYRSMLQERDDQ 173
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 174 SILCTGESGAGKTENTKKVIQYLAYVANrsmvknrktsvdldTSTNRImgqlEEQLLQANPILEAFGNSKTVKNDNSSRF 253
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHS--------------TSSTDV----QSLILGSNPLLESFGNAKTLRNNNSSRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 254 GKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEdSLSKYKFVSNGDSKLA-GV 332
Cdd:cd14886 143 GKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFK-SLESYNFLNASKCYDApGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 333 DDGAEMKETLNAMSIMgLNDEEIGGILRVVSAVMLFGNLEFSHENKN--NDQAVLLNDAVAQKIASLLGVNVTELMRAFL 410
Cdd:cd14886 222 DDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgvINAAKISNDEDFGKMCELLGIESSKAAQAII 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 411 KPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNkSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCIN 490
Cdd:cd14886 301 TKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLN-EIIQFDADARPWIGILDIYGFEFFERNTYEQLLIN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 491 YTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNLQpTIDLIDKP-MGIMSTLDDVCLFPQGNDQSFVQRLnNTHSQ 569
Cdd:cd14886 380 YANERLQQYFINQVFKSEIQEYEIEGIDHSMITFTDNSN-VLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKIK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 570 HPKYvVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIAdvcslsaadstSDTGVF 649
Cdd:cd14886 458 NNSF-IPGKGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIP-----------NEDGNM 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 650 gsrvpkKGMFrtVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLP 729
Cdd:cd14886 526 ------KGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDT 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 71983975 730 FQEFRQRYEKLL--APDVNPAGfMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14886 598 FEEFFHRNKILIshNSSSQNAG-EDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
100-781 |
1.47e-110 |
|
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: 369.33 E-value: 1.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVANRSmvkNRKTSVdldtstnrimgqleEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSV---GGVLSV--------------EKLNAALTVLEAFGNVRTALNGNATRFSQLFSL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGV-DDGAEM 338
Cdd:cd01386 144 DFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKqKAAAAF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 339 KETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNdQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIK--V 416
Cdd:cd01386 224 SKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAG-RKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSggP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 417 QRDLVHRAQSVDQVNFSVG----------AIAKASYERLFRWLVHRLNKSLdRTRQQSVSFIGILDIAGFEIFETN---- 482
Cdd:cd01386 303 QQSTTSSGQESPARSSSGGpkltgvealeGFAAGLYSELFAAVVSLINRSL-SSSHHSTSSITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 483 --SFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDK---------------PMGIMSTL 545
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 546 DDVCLFPQGNDQSFVQRLnntHSQHPKYVVPEIRS-------RSDFAVVHYAGR--VDYQSEGW-RVKNMDPLNENVIDV 615
Cdd:cd01386 462 DEEALYPGSSDDTFLERL---FSHYGDKEGGKGHSllrrsegPLQFVLGHLLGTnpVEYDVSGWlKAAKENPSAQNATQL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 616 LKTSKeslivdmwkdiadvcSLSAAdstsdtgvfgsrVPKKGMFrtvSQLyKEQLARLMSTLNNTNPHFVRCIIPNHE-K 694
Cdd:cd01386 539 LQESQ---------------KETAA------------VKRKSPC---LQI-KFQVDALIDTLRRTGLHFVHCLLPQHNaG 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 695 KHG-----------VLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEkLLAPDVN-----PAGFMDGKNAVY 758
Cdd:cd01386 588 KDErstsspaagdeLLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQ-VLAPPLTkklglNSEVADERKAVE 666
|
730 740
....*....|....*....|...
gi 71983975 759 RIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd01386 667 ELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
100-781 |
9.89e-109 |
|
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: 362.98 E-value: 9.89e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRyFSNLYYTYS--GLFCVVINPYKRIPIYTDTIAEQF-KCKKRKEMPPHIFAVADEAYRSM-LQERDDQSI 175
Cdd:cd14875 1 ATLLHCIKER-FEKLHQQYSlmGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 176 LCTGESGAGKTENTKKVIqylAYVANRSMVKNRktsvdlDTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGK 255
Cdd:cd14875 80 VISGESGSGKTENAKMLI---AYLGQLSYMHSS------NTSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 256 FIRVHFDST-GCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKL-AGVD 333
Cdd:cd14875 151 YIKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrRGVD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 334 -----DGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFshENKNNDQAVLLNDAVAQKIASLLGVNVTELMRA 408
Cdd:cd14875 231 gktldDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEF--ESDQNDKAQIADETPFLTACRLLQLDPAKLREC 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 409 FLkpkIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLD-RTRQQSVSFIGILDIAGFEIFETNSFEQL 487
Cdd:cd14875 309 FL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 488 CINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRL-NNT 566
Cdd:cd14875 386 CINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLwDQW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 567 HSQHPKYVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVdmwkdiadvcSLSAADSTSDT 646
Cdd:cd14875 466 ANKSPYFVLPKSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIR----------TLLSTEKGLAR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 647 gvfgsrvpKKgmfRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPT 726
Cdd:cd14875 536 --------RK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPV 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983975 727 RLPFQEFrQRYEKLLAPDvNPAGFMDGKNAVYRIVQYLEVDANLFR-------IGQSKIFFR 781
Cdd:cd14875 605 RRPIEQF-CRYFYLIMPR-STASLFKQEKYSEAAKDFLAYYQRLYGwakpnyaVGKTKVFLR 664
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-781 |
1.67e-96 |
|
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: 326.59 E-value: 1.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIpiytDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYlaYVanrSMVKNRKtsvdldtstnrimgQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14937 77 ESGSGKTEASKLVIKY--YL---SGVKEDN--------------EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEdSLSKYKFVSNGDSKLAGVDDGAEMK 339
Cdd:cd14937 138 ELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIR-SENEYKYIVNKNVVIPEIDDAKDFG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 340 ETLNAMSIMGLNDEEiGGILRVVSAVMLFGNLEFSHENK----NNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIK 415
Cdd:cd14937 217 NLMISFDKMNMHDMK-DDLFLTLSGLLLLGNVEYQEIEKggktNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 416 VQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSvSFIGILDIAGFEIFETNSFEQLCINYTNEK 495
Cdd:cd14937 296 IANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELN-NYIGILDIFGFEIFSKNSLEQLLINIANEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 496 LQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNlQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVV 575
Cdd:cd14937 375 IHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYAS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 576 PEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVCSLsaadstsdtgvfgsrvpk 655
Cdd:cd14937 454 TKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESL------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 656 kGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRIcRQGFPTRLPFQEFRQ 735
Cdd:cd14937 516 -GRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLS 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 71983975 736 RYEKLLAPDVNPAGFMDgKNAVYRIVQYlEVDANLFRIGQSKIFFR 781
Cdd:cd14937 594 YFEYLDYSTSKDSSLTD-KEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
100-740 |
3.67e-95 |
|
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: 323.31 E-value: 3.67e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKC---KKRKEMPPHIFAVADEAYRSMLQERDDQSIL 176
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSssgQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 177 CTGESGAGKTENTKKVIQYLAYVAnrsmvknrktsvdldtSTNRIMgqLEEQLLQANPILEAFGNSKTVKNDNSSRFGKF 256
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRA----------------SSSRTT--FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 257 IRVHF-DSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSkvQREHYLLE-DSLSKYKFVSNGDSKLAGVDD 334
Cdd:cd14878 143 FELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLS--AEEKYGLHlNNLCAHRYLNQTMREDVSTAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 335 GAEMKETL----NAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENkNNDQAVLLNDAVAQKIASLLGVNVTELMRAFL 410
Cdd:cd14878 221 RSLNREKLavlkQALNVVGFSSLEVENLFVILSAILHLGDIRFTALT-EADSAFVSDLQLLEQVAGMLQVSTDELASALT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 411 KPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSL---DRTRQQSVSFIGILDIAGFEIFETNSFEQL 487
Cdd:cd14878 300 TDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 488 CINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTID-LIDKPMGIMSTLDDVCLFPQGNDQSFVQRL--- 563
Cdd:cd14878 380 CVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKLqsl 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 564 ---NNTHSQHPKYV-----VPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKdiadvC 635
Cdd:cd14878 460 lesSNTNAVYSPMKdgngnVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ-----S 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 636 SLSaadstsdtgvfgsrvpkkgmfrTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLE 715
Cdd:cd14878 535 KLV----------------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLE 592
|
650 660
....*....|....*....|....*
gi 71983975 716 GIRICRQGFPTRLPFQEFRQRYEKL 740
Cdd:cd14878 593 MVKIFRYGYPVRLSFSDFLSRYKPL 617
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
97-780 |
6.79e-92 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 313.72 E-value: 6.79e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 97 LNEASVLHNLKQRYFSNLYYTY---SGLfcVVINPYKRIPIYTDTIAEQFKCKKRKEM-------PPHIFAVADEAYRSM 166
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGSEYYDTTsgskeplPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 167 LQERDDQSILCTGESGAGKTENTKKVIQYLayvanrsmvknrktsVDLdTSTNRIMGQLEEQLLQANPILEAFGNSKTVK 246
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQL---------------LRL-SSHSKKGTKLSSQISAAEFVLDSFGNAKTLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 247 NDNSSRFGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGD 326
Cdd:cd14879 143 NPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 327 SKL---AGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHEN-KNNDQAVLLNDAVAQKIASLLGVNV 402
Cdd:cd14879 223 HPLplgPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHeGGEESAVVKNTDVLDIVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 403 TELmRAFLKPKIKvqrdLVHR---------AQSVDQVNfsvgAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDI 473
Cdd:cd14879 303 EDL-ETSLTYKTK----LVRKelctvfldpEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 474 AGFEIFET---NSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEwkfldfgLNLQPTID-------LIDKPMGIMS 543
Cdd:cd14879 374 PGFQNRSStggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVS-------VPATSYFDnsdcvrlLRGKPGGLLG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 544 TLDDVCL-FPQGNDQSFVQRLNNTHSQHPKYVVPEI----RSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNenvidvlkt 618
Cdd:cd14879 447 ILDDQTRrMPKKTDEQMLEALRKRFGNHSSFIAVGNfatrSGSASFTVNHYAGEVTYSVEGFLERNGDVLS--------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 619 skeslivdmwkdiADVCSLsaadstsdtgvfgsrvpkkgmFRTVSQLyKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGV 698
Cdd:cd14879 518 -------------PDFVNL---------------------LRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNS 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 699 LNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYekllAPDVNPAGFMDGKNAVYRIVQYLEVDanlFRIGQSKI 778
Cdd:cd14879 563 FDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERY----KSTLRGSAAERIRQCARANGWWEGRD---YVLGNTKV 635
|
..
gi 71983975 779 FF 780
Cdd:cd14879 636 FL 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-781 |
3.05e-91 |
|
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: 314.28 E-value: 3.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFS--------NLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERD 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 172 DQSILCTGESGAGKTENTKKVIQYLAYVANRsmvknRKTSvdlDTSTnrimgqLEEQLLQANPILEAFGNSKTVKNDNSS 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDR-----RHGA---DSQG------LEARLLQSGPVLEAFGNAHTVLNANSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 252 RFGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKG--LSKVQrehylleDSLSKYkfvsnGDSKL 329
Cdd:cd14887 147 RFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAavAAATQ-------KSSAGE-----GDPES 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 330 AGVDdgaemkETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEF--SHENKNNDQAVLL-----NDAVAQKIASLL---- 398
Cdd:cd14887 215 TDLR------RITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFttDQEPETSKKRKLTsvsvgCEETAADRSHSSevkc 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 399 ---GVNVTELMRAFLK---------PKIKVQRDL--------VHRAQS---VDQVNFSVGAIAKASYERLFRWLVHRLNK 455
Cdd:cd14887 289 lssGLKVTEASRKHLKtvarllglpPGVEGEEMLrlalvsrsVRETRSffdLDGAAAARDAACKNLYSRAFDAVVARINA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 456 SLDRTRQQS-------------VSFIGILDIAGFEIFET---NSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEW 519
Cdd:cd14887 369 GLQRSAKPSesdsdedtpsttgTQTIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQ 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 520 KFLDFGLNLQP------------TIDLIDKP--------------MGIMSTLDD-VCLFP---QGNDQS--FVQRLNNTH 567
Cdd:cd14887 449 NQDCSAFPFSFplastltsspssTSPFSPTPsfrsssafatspslPSSLSSLSSsLSSSPpvwEGRDNSdlFYEKLNKNI 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 568 SQHPKY--VVPEI-RSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNeNVIDVLKTSKESLIvdmwkdiadvcSLSAADSTS 644
Cdd:cd14887 529 INSAKYknITPALsRENLEFTVSHFACDVTYDARDFCRANREATS-DELERLFLACSTYT-----------RLVGSKKNS 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 645 DTGVFGSRVpkkgmfRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGF 724
Cdd:cd14887 597 GVRAISSRR------STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGF 670
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 71983975 725 PTRLPFQEFRQRYEKLLAPDVNPAgfMDGKNAVYRIVQYLEVDANLFRIGQSKIFFR 781
Cdd:cd14887 671 PCRLPYVELWRRYETKLPMALREA--LTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-740 |
3.15e-84 |
|
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: 289.10 E-value: 3.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYtDTIAEQFKCKKRKEmpPHIFAVADEAYRSMLQErDDQSILCTGE 180
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGA-GAMKAYLKNYSHVE--PHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLayvanrsmvknrktsVDLDTSTNRImgqlEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd14898 78 SGSGKTENAKLVIKYL---------------VERTASTTSI----EKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDstGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLL--KGLSkvqrehyLLEDSLSKYKFVSNgdsKLAGVDDGAEM 338
Cdd:cd14898 139 FD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCasKRLN-------IKNDFIDTSSTAGN---KESIVQLSEKY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 339 KETLNAMSIMGLNDeeIGGILRVVSAVMLFGNLEFSHENKnndqAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQR 418
Cdd:cd14898 207 KMTCSAMKSLGIAN--FKSIEDCLLGILYLGSIQFVNDGI----LKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 419 DLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSfigILDIAGFEIFETNSFEQLCINYTNEKLQQ 498
Cdd:cd14898 281 ETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERSIS---VLDIFGFEIFESNGLDQLCINWTNEKIQN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 499 LFNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDlIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNthsqhpkYVVPEI 578
Cdd:cd14898 358 DFIKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRD-FEKPCGLMDLISEESFNAWGNVKNLLVKIKK-------YLNGFI 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 579 RSRSDFAVV--HYAGRVDYQSEGWRVKNMDPLNenvidvLKTSKESLIVDmwkdiadvcslsaadstsdtgvfgsrvpkK 656
Cdd:cd14898 430 NTKARDKIKvsHYAGDVEYDLRDFLDKNREKGQ------LLIFKNLLIND-----------------------------E 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 657 GMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQR 736
Cdd:cd14898 475 GSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEER 554
|
....
gi 71983975 737 YEKL 740
Cdd:cd14898 555 YRIL 558
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-745 |
3.60e-82 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 286.42 E-value: 3.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQFKCKKRKE-------MPPHIFAVADEAYRSMLQERD 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 172 DQSILCTGESGAGKTENTKKVIQYLAYVANRSMVKNRktsvdldtstnrimgqlEEQLLQANPILEAFGNSKTVKNDNSS 251
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTER-----------------IDKLIYINNILESMSNATTIKNNNSS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 252 RFGKFIRVHFDS---------TGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQR---------EHY-LL 312
Cdd:cd14884 144 RCGRINLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLarrnlvrncGVYgLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 313 EDSLSKYKFVSNGD----------SKLAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFshenknndq 382
Cdd:cd14884 224 NPDESHQKRSVKGTlrlgsdsldpSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAY--------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 383 avllndavaQKIASLLGVNVTELMRAFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSL--DRT 460
Cdd:cd14884 295 ---------KAAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkCKE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 461 RQQSV---------SFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFlDFGLNLQPT 531
Cdd:cd14884 366 KDESDnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCS-DVAPSYSDT 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 532 IDLIDKpmgIMSTLDDV-----CLFPQGNDQSFVQRLNNTHSQHPK------YVVPEIRSRSD---------FAVVHYAG 591
Cdd:cd14884 445 LIFIAK---IFRRLDDItklknQGQKKTDDHFFRYLLNNERQQQLEgkvsygFVLNHDADGTAkkqnikkniFFIRHYAG 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 592 RVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIvdmwkdiadvcslsaadstSDTGVFGsrvpKKGMFRTVSQLYKEQLA 671
Cdd:cd14884 522 LVTYRINNWIDKNSDKIETSIETLISCSSNRFL-------------------REANNGG----NKGNFLSVSKKYIKELD 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983975 672 RLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEKLLAPDV 745
Cdd:cd14884 579 NLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKEQIAKEL 652
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
101-781 |
6.94e-78 |
|
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: 272.38 E-value: 6.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGE 180
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 181 SGAGKTENTKKVIQYLAYVANrsmvKNRKTSvdldtstnrimgqleEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVH 260
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGD----GNRGAT---------------GRVESSIKAILALVNAGTPLNADSTRCILQYQLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 261 FDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQR--EHYLLEDSLSKYKFV--SNGDSKLAGVDDGA 336
Cdd:cd14882 143 FGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlkEYNLKAGRNYRYLRIppEVPPSKLKYRRDDP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 337 E-----MKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFShenKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLK 411
Cdd:cd14882 223 EgnverYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFR---QNGGYAELENTEIASRVAELLRLDEKKFMWALTN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 412 PKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTR-----QQSVSfigILDIAGFEIFETNSFEQ 486
Cdd:cd14882 300 YCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRavfgdKYSIS---IHDMFGFECFHRNRLEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 487 LCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVClfPQGNDQSFV-QRLNN 565
Cdd:cd14882 377 LMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDAS--RSCQDQNYImDRIKE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 566 THSQHPKYVvpeirSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDiadvcslsaadstsd 645
Cdd:cd14882 455 KHSQFVKKH-----SAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 646 tgvfgSRVPKkgmFRTVSQLYKEQLARLMSTL----NNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICR 721
Cdd:cd14882 515 -----SQVRN---MRTLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQ 586
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 722 QGFPTRLPFQEFRQRYeKLLAPDVNPAGFMDGKNAvyRIVqYLEVDANLFRIGQSKIFFR 781
Cdd:cd14882 587 KGFSYRIPFQEFLRRY-QFLAFDFDETVEMTKDNC--RLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-743 |
4.75e-77 |
|
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: 269.68 E-value: 4.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-----IYTDTIAEQfkckkrkempPHIFAVADEAYRSMLQERDDQSI 175
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVGnpltlTSTRSSPLA----------PQLLKVVQEAVRQQSETGYPQAI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 176 LCTGESGAGKTENTKKVIQYLAYVANrsmvknrktsvdldtstnrimGQLE----EQLLQANPILEAFGNSKTVKNDNSS 251
Cdd:cd14881 72 ILSGTSGSGKTYASMLLLRQLFDVAG---------------------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 252 RFGKFIRVHFdSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLED-SLSKYKFVSNGDSKLA 330
Cdd:cd14881 131 RIGHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGySPANLRYLSHGDTRQN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 331 GVDDGAEMKETLNAMSIMGLndeEIGGILRVVSAVMLFGNLEFsHENKNNDQAVLlNDAVAQKIASLLGVNVTELMRAFL 410
Cdd:cd14881 210 EAEDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQF-IDGGGLEVDVK-GETELKSVAALLGVSGAALFRGLT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 411 KPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNkSLDR-----TRQQSVSFIGILDIAGFEIFETNSFE 485
Cdd:cd14881 285 TRTHNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRAN-SLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 486 QLCINYTNEKLQQLFNNTMFVREQQEYLDEG----LEWKFLDfglNLqPTIDLIDK-PMGIMSTLDDVCLfPQGNDQSFV 560
Cdd:cd14881 364 HLCINLCAETMQHFYNTHIFKSSIESCRDEGiqceVEVDYVD---NV-PCIDLISSlRTGLLSMLDVECS-PRGTAESYV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 561 QRLNNTHSQHPKYVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLktSKESlivdmwkdiadvCSlsaa 640
Cdd:cd14881 439 AKIKVQHRQNPRLFEAKPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVF--YKQN------------CN---- 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 641 dstsdtgvFGsrvpkkgmFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRIC 720
Cdd:cd14881 501 --------FG--------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLM 564
|
650 660
....*....|....*....|...
gi 71983975 721 RQGFPTRLPFQEFRQRYeKLLAP 743
Cdd:cd14881 565 AGGYPHRMRFKAFNARY-RLLAP 586
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
100-781 |
3.88e-70 |
|
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: 249.40 E-value: 3.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 100 ASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFkckkrkemppHIFAVADEAYRSMLQERDD-QSILCT 178
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 179 GESGAGKTENTKKVIQYLAYVANRSMVKNRKTSVDldtstnrimgqleeqllqanPILEAFGNSKTVKNDNSSRFGKFIR 258
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIE--------------------SVFKSFGCAKTLKNDEATRFGCSID 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 259 VHFDSTgCISGANIEFYL-LEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDsLSKYKFVSNGDSKLAGVDDGAE 337
Cdd:cd14874 131 LLYKRN-VLTGLNLKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKG-LQKFFYINQGNSTENIQSDVNH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 338 MKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEF-SHENKNNDQAVLL--NDAVAQKIASLLGVNVTELMrAFLKPKI 414
Cdd:cd14874 209 FKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFrTKRNPNVEQDVVEigNMSEVKWVAFLLEVDFDQLV-NFLLPKS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 415 KVQRDLvhraqSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVsfIGILDIAGFEIFETNSFEQLCINYTNE 494
Cdd:cd14874 288 EDGTTI-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 495 KLQQLFNNTMFVREQQEYLDEGLEWKF-LDFGLNLQPTIDLI-DKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPK 572
Cdd:cd14874 361 RIENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 573 YVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKdiadvcslSAADSTSDtgvfgsr 652
Cdd:cd14874 441 YGKARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE--------SYSSNTSD------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 653 vpkkgMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQE 732
Cdd:cd14874 506 -----MIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTT 580
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 71983975 733 FRQRYEKLLAPDVnpAGFMDGKNAVYRIVQYLEVD-ANLFRIGQSKIFFR 781
Cdd:cd14874 581 FARQYRCLLPGDI--AMCQNEKEIIQDILQGQGVKyENDFKIGTEYVFLR 628
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
101-781 |
2.87e-67 |
|
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: 241.92 E-value: 2.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIP-IYTDTIAEQFKckKRKEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLayvanrsmvknrkTSVDLDTSTnrimgQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRV 259
Cdd:cd14905 80 ESGSGKSENTKIIIQYL-------------LTTDLSRSK-----YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 260 HFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDsLSKYKFVSNGDS-KLAGVDDGAEM 338
Cdd:cd14905 142 FYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGD-INSYHYLNQGGSiSVESIDDNRVF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 339 KETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDqavLLNDAVAQKIASLLGVNVTELMRAFLKpkikvqr 418
Cdd:cd14905 221 DRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGKTE---VKDRTLIESLSHNITFDSTKLENILIS------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 419 dlvHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTrqQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQ 498
Cdd:cd14905 291 ---DRSMPVNEAVENRDSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 499 LFNNTMFVREQQEYLDEGLEWKF-LDFGLNlQPTIDLIDKpmgIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVvpe 577
Cdd:cd14905 366 IYLQTVLKQEQREYQTERIPWMTpISFKDN-EESVEMMEK---IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFG--- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 578 iRSRSDFAVVHYAGRVDYQSEGWRVKNMDP-------LNENVIDVLKTSKESlIVDMWKDIADVCSLSAADSTSDTGVF- 649
Cdd:cd14905 439 -KKPNKFGIEHYFGQFYYDVRGFIIKNRDEilqrtnvLHKNSITKYLFSRDG-VFNINATVAELNQMFDAKNTAKKSPLs 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 650 --------GSRVPKK-------------------------GMFRTVSQLYKeqlarlmsTLNNTNP--HFVRCIIPNHEK 694
Cdd:cd14905 517 ivkvllscGSNNPNNvnnpnnnsgggggggnsgggsgsggSTYTTYSSTNK--------AINNSNCdfHFIRCIKPNSKK 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 695 KHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEKLlapdvnpagFMDGKNAVYRIVQYLEVDANL---- 770
Cdd:cd14905 589 THLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFF---------FQNQRNFQNLFEKLKENDINIdsil 659
|
730
....*....|....
gi 71983975 771 ---FRIGQSKIFFR 781
Cdd:cd14905 660 pppIQVGNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-740 |
2.87e-65 |
|
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: 237.56 E-value: 2.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 103 LHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTdTIAEQFKCKKRKEM-----------PPHIFAVADEAYRSMLQERD 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYT-PDHMQAYNKSREQTplyekdtvndaPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 172 DQSILCTGESGAGKTENTKKVIQYLAYVANRSMVKNRKTSvdldtsTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSS 251
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEG------ASGVLHPIGQQILHAFTILEAFGNAATRQNRNSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 252 RFGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSK--VQREHYLLEDSLSKYKFVSNGDSKL 329
Cdd:cd14893 157 RFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMNKCVNEFVMLKQADPLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 330 AGVD-DGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEF-------SHENKNNDQAVLLNDAVAQK-------I 394
Cdd:cd14893 237 TNFAlDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQSCALKdpaqillA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 395 ASLLGV------NVTELMRAFLKPKIKVQRDLvhRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSL----DRTRQQS 464
Cdd:cd14893 317 AKLLEVepvvldNYFRTRQFFSKDGNKTVSSL--KVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 465 VSF----IGILDIAGFEIFET--NSFEQLCINYTNEKLQQLF-NNTMFVR------EQQEYLDEGLEWKFLDFGLNLQPT 531
Cdd:cd14893 395 IVInsqgVHVLDMVGFENLTPsqNSFDQLCFNYWSEKVHHFYvQNTLAINfsfledESQQVENRLTVNSNVDITSEQEKC 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 532 IDLI-DKPMGIMSTLDDVCLFPQGNDQSFVQRL-------------NNTHSQHPKYVVPEIRSRSDFAVVHYAGRVDYQS 597
Cdd:cd14893 475 LQLFeDKPFGIFDLLTENCKVRLPNDEDFVNKLfsgneavgglsrpNMGADTTNEYLAPSKDWRLLFIVQHHCGKVTYNG 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 598 EGWRVKNMDPLNENVIDVLKTSKESLI-----VDMWKDIADVCSLSAADSTSDTGVFGSRVPKKGMFRTVS-----QLYK 667
Cdd:cd14893 555 KGLSSKNMLSISSTCAAIMQSSKNAVLhavgaAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNITdsaatDVYN 634
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71983975 668 EQLArLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEKL 740
Cdd:cd14893 635 QADA-LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNV 706
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
101-779 |
3.00e-57 |
|
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: 213.16 E-value: 3.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 101 SVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKR-KEMPPHIFAVADEAYRSMLQERDDQSILCTG 179
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCiEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 180 ESGAGKTENTKKVIQYLAYVA--NRSMVKNRKTSVDLDT---STNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFG 254
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgSRRLPTNLNDQEEDNIhneENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 255 KFIRVHFDSTGcISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDsLSKYKFVSNGDSKLAGVDD 334
Cdd:cd14938 162 KFCTIHIENEE-IKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKN-IENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 335 GAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEF-----------------------SHENK-NNDQAVLLNDAV 390
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIvkafrkksllmgknqcgqninyeTILSElENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 391 AQKI--ASLLGVNVTELMRAFLKPKIkVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSV--S 466
Cdd:cd14938 320 KNLLlaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNINIntN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 467 FIGILDIAGFEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTID-LIDKPMG-IMST 544
Cdd:cd14938 399 YINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNlLVGPTEGsLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 545 LDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVPE--IRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKEs 622
Cdd:cd14938 479 LENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDdiTGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN- 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 623 livdmwKDIADVCSLSAADSTSDTGVFGSRVPKKGMFRTVSQLY--KEQLA---------RLMSTLNNTNPHFVRCIIPN 691
Cdd:cd14938 558 ------EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYdtKNQMAvsllrnnltELEKLQETTFCHFIVCMKPN 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 692 HEKKH-GVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEKLLApdvnpagfmDGKNAVYRIVQYLEVDANL 770
Cdd:cd14938 632 ESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYE 702
|
....*....
gi 71983975 771 FRIGQSKIF 779
Cdd:cd14938 703 WMIGNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-265 |
5.37e-52 |
|
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: 181.00 E-value: 5.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 122 FCVVINPYKRIPIYTDT-IAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGESGAGKTENTKKVIQYLAYVA 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 201 NRSMVKNRKTSVDLDTStnrIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVHFDSTG 265
Cdd:cd01363 81 FNGINKGETEGWVYLTE---ITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
906-1768 |
1.38e-31 |
|
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: 135.57 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 906 LDAESSERAEIFEER---SRMAARRDE--------------LEGILEEVSKRLEIEEQKAKKADsESRKLTEMVRHLEEN 968
Cdd:TIGR02168 150 IEAKPEERRAIFEEAagiSKYKERRKEterklertrenldrLEDILNELERQLKSLERQAEKAE-RYKELKAELRELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 969 LedeersrqkLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLideVERSKQLVKAKARLEATVAE 1048
Cdd:TIGR02168 229 L---------LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV---SELEEEIEELQKELYALANE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1049 IND---ELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIRE 1125
Cdd:TIGR02168 297 ISRleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1126 IRAQLDDAieetnkeKAARQKAEKARRDMAEELESYKQELEESNDktvlhsqlkakrdeeyaHLQKQLEETVKSSEEVVE 1205
Cdd:TIGR02168 377 LEEQLETL-------RSKVAQLELQIASLNNEIERLEARLERLED-----------------RRERLQQEIEELLKKLEE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1206 EMKAQNQKKIEELNETIDQLkrqkisadkakssaESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSnl 1285
Cdd:TIGR02168 433 AELKELQAELEELEEELEEL--------------QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER-- 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1286 ddlmaklskMNNELESIQKAKSAdETLNSNLLkknASLDMQLSELTEASEEDRRTRATLnnkirqLEEDL-AVAVEARDD 1364
Cdd:TIGR02168 497 ---------LQENLEGFSEGVKA-LLKNQSGL---SGILGVLSELISVDEGYEAAIEAA------LGGRLqAVVVENLNA 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1365 ALDAQEKIeKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDK-----AERAKKKAIQEAED 1439
Cdd:TIGR02168 558 AKKAIAFL-KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllGGVLVVDDLDNALE 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1440 VQKELT----------DVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQ 1509
Cdd:TIGR02168 637 LAKKLRpgyrivtldgDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1510 LEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQLa 1589
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK- 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1590 sreededDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDV 1669
Cdd:TIGR02168 796 -------EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1670 TEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLrassfsNEEKRRLEAKVIDLE 1749
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL------ELRLEGLEVRIDNLQ 942
|
890 900
....*....|....*....|
gi 71983975 1750 DQLDEEASAN-ELAQEKVRK 1768
Cdd:TIGR02168 943 ERLSEEYSLTlEEAEALENK 962
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
850-1755 |
3.69e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 134.88 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 850 KVKPLLEVTNKDELIAERE-----QELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEErsrma 924
Cdd:PTZ00121 1028 KIEELTEYGNNDDVLKEKDiidedIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEE----- 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 925 ARRDElEGILEEVSKRLEieeqkAKKADSESRKLTEmVRHLEENLEDEERSRQKlllEKNSIESRLKELEAQGLELedsg 1004
Cdd:PTZ00121 1103 AKKTE-TGKAEEARKAEE-----AKKKAEDARKAEE-ARKAEDARKAEEARKAE---DAKRVEIARKAEDARKAEE---- 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1005 NKLSKEKKALEErcedlsSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRhNAETARRAAETQLREEQESCLEK 1084
Cdd:PTZ00121 1169 ARKAEDAKKAEA------ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAEEAKKDAEE 1241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1085 TRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIR-------AQLDDAIEETNKEKAARQKAEKARRdmAEE 1157
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKkaeekkkADEAKKAEEKKKADEAKKKAEEAKK--ADE 1319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1158 LESYKQELEESNDKTVLHSQLKAKRDEeyahLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKR---QKISADK 1234
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEAKKAAE----AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeEKKKADE 1395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1235 AKSSAESDNENfRAELSNIASARLEAEK-KRKAAETSLMEKDHKMREMQSNLDDLMAKLS---KMNNELESIQKAKSADE 1310
Cdd:PTZ00121 1396 AKKKAEEDKKK-ADELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEeakKAEEAKKKAEEAKKADE 1474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1311 tlnsnlLKKNASLDMQLSELTEASEEDRRTRATLNNK--IRQLEEDLAVAVEAR--DDALDAQEKieKEVKEVKSllAEA 1386
Cdd:PTZ00121 1475 ------AKKKAEEAKKADEAKKKAEEAKKKADEAKKAaeAKKKADEAKKAEEAKkaDEAKKAEEA--KKADEAKK--AEE 1544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1387 RKKLDEENRevmeelrkKKEKELSAEKERADMAEQARDKAERAKKKAiQEAEDVQKELTDVVAATREMERKMRKFDQQLA 1466
Cdd:PTZ00121 1545 KKKADELKK--------AEELKKAEEKKKAEEAKKAEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1467 EErnntllaqqERDMAHQMLRDAETKALV--LSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYEL---EKT 1541
Cdd:PTZ00121 1616 EE---------AKIKAEELKKAEEEKKKVeqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaEED 1686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1542 KRRLDEELSRAEQQIIELEDALQLADDARSRVEvnmQAMRSEFERQL----ASREEDEDDRK-------KGLTSKIRNLT 1610
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE---ELKKAEEENKIkaeeAKKEAEEDKKKaeeakkdEEEKKKIAHLK 1763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1611 EelESEQRARQAAIANKKKIESQISELTEKNEASL-RQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKR 1689
Cdd:PTZ00121 1764 K--EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVdKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNM 1841
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1690 ARASEDEIKRLTADIQAVSSSKRKAEAErdelieevSSLRASSFSNEEKRRLEAKVIDLEDQLDEE 1755
Cdd:PTZ00121 1842 QLEEADAFEKHKFNKNNENGEDGNKEAD--------FNKEKDLKEDDEEEIEEADEIEKIDKDDIE 1899
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
106-721 |
1.01e-30 |
|
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: 132.17 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 106 LKQRYFSNLYYTYSGLFCV-VINPYKRI------PIYTDTIAEQFKCKKRKE--MPPHIFAVADEAY------------- 163
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 164 -------RSMLQERDDQSILCtGESGAGKTENTKKVIQYLAYVANRSMVK-----------NRKTSVDLDTSTNRIMGQL 225
Cdd:cd14894 87 pstissnRSMTEGRGQSLFLC-GESGSGKTELAKDLLKYLVLVAQPALSKgseetckvsgsTRQPKIKLFTSSTKSTIQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 226 ----------------------------------------------------------------EEQL------------ 229
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 230 ----LQANPILEAFGNSKTVKNDNSSRFGKF--IRVHFDSTGC---ISGANIEFYLLEKSRVLKQA------PNERSFHI 294
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 295 FYQLLKGLSK------VQREHYLLEDSLSKYKFVSNGDSKLAGV--------DDGAEMKETLNAMSIMGLNDEEIGGILR 360
Cdd:cd14894 326 LYAMVAGVNAfpfmrlLAKELHLDGIDCSALTYLGRSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 361 VVSAVMLFGNLEFSHENKNNDQAVLLNDAV--AQKIASLLGV-NVTELMRAFLKPKIKVQR--DLVHRAQSVDQVNFSVG 435
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTGALnaPQKVVELLELgSVEKLERMLMTKSVSLQStsETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 436 AIAKASYERLFRWLVHRLNK-------SLDRTRQQ---------SVSFIGILDIAGFEIFETNSFEQLCINYTNEKLqql 499
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEatkmsalSTDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 500 fnntmFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQS----------FVQRL---NNT 566
Cdd:cd14894 563 -----YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNaqqeekrnklFVRNIydrNSS 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 567 HSQHPKYVVPEIRSRS-------DFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVcslsA 639
Cdd:cd14894 638 RLPEPPRVLSNAKRHTpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQL----G 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 640 ADSTSDTGVFGSRVPKKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRI 719
Cdd:cd14894 714 WSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEI 793
|
..
gi 71983975 720 CR 721
Cdd:cd14894 794 CR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
925-1664 |
1.64e-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: 132.10 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 925 ARRDELEGILEEVSKRLEIEEQKAKKADSESrkltEMVRHLEENLEDEERSRQKLLLEKNSiesRLKELEAQGLELEDSG 1004
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKL----EELRLEVSELEEEIEELQKELYALAN---EISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1005 NKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEK 1084
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1085 TRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREirAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQE 1164
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1165 LEESNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAQNQ---------------KKIEELNETIDQLKRQK 1229
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdEGYEAAIEAALGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1230 I---SADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMReMQSNLDDLMAKLSK-MNNELESIQKA 1305
Cdd:TIGR02168 550 VvveNLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLG-VAKDLVKFDPKLRKaLSYLLGGVLVV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1306 KSADETLN-SNLLKKNASLDMQLSEL-------TEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVK 1377
Cdd:TIGR02168 629 DDLDNALElAKKLRPGYRIVTLDGDLvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1378 EVKSLLAEARKKLDEENREVmeelrkkkekelSAEKERADMAEQARDKAErakkkaiQEAEDVQKELTdvvaatrEMERK 1457
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQI------------SALRKDLARLEAEVEQLE-------ERIAQLSKELT-------ELEAE 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1458 MRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYE 1537
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1538 LEKTKRRLDEELSRAEQQI-------IELEDALQLADDARSRVEVNMQAMRSEFErQLASREEDEDDRKKGLTSKIRNLT 1610
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIeeleeliEELESELEALLNERASLEEALALLRSELE-ELSEELRELESKRSELRRELEELR 921
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 71983975 1611 EELESEQRARQAAianKKKIESQISELTEKNEASLRQIEDLSRQLRKAQLGWKD 1664
Cdd:TIGR02168 922 EKLAQLELRLEGL---EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
864-1460 |
5.94e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.59 E-value: 5.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 864 IAEREQELKVTAEKLRRSEVF--ISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRL 941
Cdd:COG1196 211 KAERYRELKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 942 EIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDL 1021
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1022 SSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESE 1101
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1102 LSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKqELEESNDKTVLHSQLKAK 1181
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGLAGAVAVL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1182 RDEEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQ----LKRQKISADKAKSSAESDNENFRAELSNIASAR 1257
Cdd:COG1196 530 IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratfLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1258 LEAEKKRKAAETSLMEkdhkmremQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEED 1337
Cdd:COG1196 610 EADARYYVLGDTLLGR--------TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1338 RRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERAD 1417
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983975 1418 mAEQARDKAERAKKK----------AIQEAE--------------DVQKELTDVVAATREMERKMRK 1460
Cdd:COG1196 762 -LEELERELERLEREiealgpvnllAIEEYEeleerydflseqreDLEEARETLEEAIEEIDRETRE 827
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
838-1619 |
6.67e-29 |
|
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: 126.71 E-value: 6.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 838 RLREWQWWRLLTKVKPLL-EVTNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEI 916
Cdd:TIGR02168 221 ELRELELALLVLRLEELReELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 917 FEERSRMAARRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQ 996
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 997 GL-------ELEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLvkAKARLEATVAEINDELEKEKQQRHNAETARRA 1069
Cdd:TIGR02168 381 LEtlrskvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELER 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1070 AETQLREEQESclektrkAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLD-------------DAIEE 1136
Cdd:TIGR02168 459 LEEALEELREE-------LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKnqsglsgilgvlsELISV 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1137 TNKEKAARQKAEKARRDMA--EELESYKQE---LEESNDKTVLHSQLKAKRD--------------EEYAHLQKQLEETV 1197
Cdd:TIGR02168 532 DEGYEAAIEAALGGRLQAVvvENLNAAKKAiafLKQNELGRVTFLPLDSIKGteiqgndreilkniEGFLGVAKDLVKFD 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1198 KSSEEVVEEM-----------KAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNiASARLEAEKKRKA 1266
Cdd:TIGR02168 612 PKLRKALSYLlggvlvvddldNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRR-EIEELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1267 AETslmekdhkmREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNN 1346
Cdd:TIGR02168 691 EKI---------AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1347 KIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQAR--D 1424
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERrlE 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1425 KAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKK 1504
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1505 DIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYE-LEKTKRRLDEELSRAEQQIIELEDALQladdarSRVEVNMQAMrSE 1583
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENKIK------ELGPVNLAAI-EE 994
|
810 820 830
....*....|....*....|....*....|....*.
gi 71983975 1584 FerqlasreEDEDDRKKGLTSKIRNLTEELESEQRA 1619
Cdd:TIGR02168 995 Y--------EELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1023-1847 |
7.87e-28 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 123.71 E-value: 7.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1023 SRLIDEVERSKQLVKAKARLEATVAEindELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESEL 1102
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAE---EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1103 SQISIRNDEELAARQQLEREIREIR-AQLDDAIEETNKEKAARqKAEKARRdmAEELESYKQEleesndktvlhsqlkaK 1181
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRkAEELRKAEDARKAEAAR-KAEEERK--AEEARKAEDA----------------K 1224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1182 RDEEYahlqKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENfraelsniasarlEAE 1261
Cdd:PTZ00121 1225 KAEAV----KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK-------------KAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1262 KKRKAAETSLMEKDHKMREMQSNlddlmAKLSKMNNELesiqKAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTR 1341
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKK-----AEEAKKADEA----KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1342 ATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERAD---- 1417
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADeakk 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1418 MAEQARdKAERAKKKAiQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTllAQQERDMAHQMLRDAETKALVLS 1497
Cdd:PTZ00121 1439 KAEEAK-KADEAKKKA-EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK--AEEAKKKADEAKKAAEAKKKADE 1514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1498 NELSEKKDIVDQLEKDKRTLKLEidnlASTKDDAGKNVYELEKTKR-RLDEELSRAEQQIIELEDalqlADDARSRVEVN 1576
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKAD----EAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEED----KNMALRKAEEA 1586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1577 MQAMRSEFERQLASREEDeddrKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLR 1656
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEE----KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1657 KAQLGWK--DLQLDVTEARAAMEDalagQRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDEliEEVSSLRASsfs 1734
Cdd:PTZ00121 1663 AAEEAKKaeEDKKKAEEAKKAEED----EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA--EEENKIKAE--- 1733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1735 nEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLA-MERSVCERTESDKIALERANRDLKQQLQ---- 1809
Cdd:PTZ00121 1734 -EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAvIEEELDEEDEKRRMEVDKKIKDIFDNFAniie 1812
|
810 820 830
....*....|....*....|....*....|....*....
gi 71983975 1810 -DAENTAVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQ 1847
Cdd:PTZ00121 1813 gGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEK 1851
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1116-1916 |
2.10e-27 |
|
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: 122.09 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1116 RQQLEREIREIR---AQLDDAIEETNKE-KAARQKAEKArrdmaEELESYKQELEESnDKTVLHSQLKAKRDEeyahlQK 1191
Cdd:TIGR02168 174 RKETERKLERTRenlDRLEDILNELERQlKSLERQAEKA-----ERYKELKAELREL-ELALLVLRLEELREE-----LE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1192 QLEETVKSSEEVVEEMKAQnqkkIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSL 1271
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1272 MEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSAdetlnsnLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQL 1351
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1352 EEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDE-ENREVMEELRKKKEKELSAEKERADMAEQAR--DKAER 1428
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEelREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1429 AKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVd 1508
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1509 qLEKDKRTLKLEIDNLAstKDDAGKNVYeLEKTKRRLDEELSRAEQQIIELEDALQLADD---ARSRVEVNMQAMRSEFe 1585
Cdd:TIGR02168 551 -VVENLNAAKKAIAFLK--QNELGRVTF-LPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvkFDPKLRKALSYLLGGV- 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1586 rQLASREEDEDDRKKGLTSKIRNLTEELE----------SEQRARQAAIANKKKIEsqisELTEKNEASLRQIEDLSRQL 1655
Cdd:TIGR02168 626 -LVVDDLDNALELAKKLRPGYRIVTLDGDlvrpggvitgGSAKTNSSILERRREIE----ELEEKIEELEEKIAELEKAL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1656 RKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRassfsn 1735
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE------ 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1736 EEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQQLQDAE--- 1812
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSedi 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1813 ----------NTAVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQ 1882
Cdd:TIGR02168 855 eslaaeieelEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
810 820 830
....*....|....*....|....*....|....*...
gi 71983975 1883 NARIRQLRTQL----EDTEAERDRLTNKLKDERRRAEE 1916
Cdd:TIGR02168 935 EVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARR 972
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
947-1622 |
1.46e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 118.89 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 947 KAKKADSEsRKLTEMvrhlEENLEdeersRQKLLLEknSIESRLKELEAQgleledsgnklsKEK----KALEERCEDLS 1022
Cdd:COG1196 171 KERKEEAE-RKLEAT----EENLE-----RLEDILG--ELERQLEPLERQ------------AEKaeryRELKEELKELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1023 SRLIdeVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESEL 1102
Cdd:COG1196 227 AELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1103 SQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEEsndktvLHSQLKAKR 1182
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1183 DEEYAHLQKQLEETVKSSEEVVEEmkAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEK 1262
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQL--EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1263 KRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEedrrtra 1342
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL------- 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1343 tlnnkiRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQA 1422
Cdd:COG1196 530 ------IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1423 RDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSE 1502
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1503 KKDIVDQLEKDKRTLKLEidnlastkddagknvyeLEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRS 1582
Cdd:COG1196 684 LAERLAEEELELEEALLA-----------------EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 71983975 1583 EFERQLASREEDEDDRKKgltskirnLTEELESEQRARQA 1622
Cdd:COG1196 747 LLEEEALEELPEPPDLEE--------LERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
868-1524 |
1.69e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.42 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 868 EQELKVTAEKLRRSEVFISDYKQQMEKMDEERlvlktrldaessERAEIFEERSRMAARRDELEGILEEVSKRLEIEEqk 947
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLERQA------------EKAERYRELKEELKELEAELLLLKLRELEAELEE-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 948 akkadsesrkltemvrhLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLID 1027
Cdd:COG1196 244 -----------------LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1028 EVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISI 1107
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1108 RNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEEsndktvlhsqlkakRDEEYA 1187
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE--------------AAEEEA 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1188 HLQKQLEETvksseevvEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAA 1267
Cdd:COG1196 453 ELEEEEEAL--------LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1268 ETSLMEKDHKmrEMQSNLDDLMAKLSKmNNELESIQKAKSADETLNSNLLKKNASLdmQLSELTEASEEDRRTRATLNNK 1347
Cdd:COG1196 525 AVAVLIGVEA--AYEAALEAALAAALQ-NIVVEDDEVAAAAIEYLKAAKAGRATFL--PLDKIRARAALAAALARGAIGA 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1348 IRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDKAE 1427
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1428 RAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDI- 1506
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEp 759
|
650 660
....*....|....*....|
gi 71983975 1507 --VDQLEKDKRTLKLEIDNL 1524
Cdd:COG1196 760 pdLEELERELERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
954-1766 |
5.99e-25 |
|
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: 114.01 E-value: 5.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 954 ESRKLTEMVRHLEENLEDEERSRQKLllekNSIESRLKELEAQGLELEDSGNKLSKEKKALEeRCEDLSSRLID--EVER 1031
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREyeGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1032 SKQLVKAKARLEATVAEInDELEKEKQQRhnaetarraaETQLREEQESCLEKTRKAEELTNQLMRK-ESELSQISIRND 1110
Cdd:TIGR02169 229 LKEKEALERQKEAIERQL-ASLEEELEKL----------TEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1111 EELAARQQLEREIREIRAQLDDAIEEtnkekaaRQKAEKARRDMAEELESYKQELEESN-DKTVLHSQLKAKRDEeYAHL 1189
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEER-------LAKLEAEIDKLLAEIEELEREIEEERkRRDKLTEEYAELKEE-LEDL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1190 QKQLEETVKSSEEVVEEMKaQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAET 1269
Cdd:TIGR02169 370 RAELEEVDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1270 SLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADEtlnsnllKKNASLDMQLSELTEASEEDRRTRATLNNKIR 1349
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ-------RELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1350 ----------QLEEDLAVAVEAR----------DDALDAQEKIE--KEVKEVKSLLAEARKKLDEEnrevmeelrkkKEK 1407
Cdd:TIGR02169 522 gvhgtvaqlgSVGERYATAIEVAagnrlnnvvvEDDAVAKEAIEllKRRKAGRATFLPLNKMRDER-----------RDL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1408 ELSAEKERADMAE---QARDKAERAKKKAIQEAEDVQkeltDVVAATREMER-KMRKFDQQLAEERNNTLLAQQERDMAH 1483
Cdd:TIGR02169 591 SILSEDGVIGFAVdlvEFDPKYEPAFKYVFGDTLVVE----DIEAARRLMGKyRMVTLEGELFEKSGAMTGGSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1484 QMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDAL 1563
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1564 QLADDARSRVEVNMQAMRSEFERQLAS----REEDEDDRKKGLTSKIRNLTEELESEQRARQaaiankkKIESQISELte 1639
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDlhklEEALNDLEARLSHSRIPEIQAELSKLEEEVS-------RIEARLREI-- 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1640 knEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAgqrDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERD 1719
Cdd:TIGR02169 818 --EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 71983975 1720 ELIEEVSSLRassfsnEEKRRLEAKVIDLEDQLDEEASANELAQEKV 1766
Cdd:TIGR02169 893 ELEAQLRELE------RKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
911-1792 |
5.89e-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: 110.54 E-value: 5.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 911 SERAEIFEERSRMAARRDELEGILEEVSK---RLEIEEQKAKKADSESRKLtemvrhleenledEERSRQKLLLEKNSIE 987
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQqleRLRREREKAERYQALLKEK-------------REYEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 988 SRLKELEAQGLELEDSGNKLSKEKKALEERCEDLsSRLIDEVERskqlvKAKARLEATVAEINDELEKEKQQRHNAETAR 1067
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEI-EQLLEELNK-----KIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1068 RAAETQLREEQesclEKTRKAEEltnQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKA 1147
Cdd:TIGR02169 311 AEKERELEDAE----ERLAKLEA---EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1148 EKARRDMAEELESYKQELEESNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAQnQKKIEELNETIDQLKR 1227
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1228 QKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKA-K 1306
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAiE 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1307 SADETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLnNKIRQLEEDLAV-----AVEARDDALDAQEKIEKEVKEV-- 1379
Cdd:TIGR02169 543 VAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPL-NKMRDERRDLSIlsedgVIGFAVDLVEFDPKYEPAFKYVfg 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1380 KSLLAEARkkldEENREVMEELRKKKEKELSAEKERAdMAEQARDKAERAKKKAIQEAedvqkELTDVVAATREMERKMR 1459
Cdd:TIGR02169 622 DTLVVEDI----EAARRLMGKYRMVTLEGELFEKSGA-MTGGSRAPRGGILFSRSEPA-----ELQRLRERLEGLKRELS 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1460 KFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELE 1539
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1540 KTKRRLDEEL-----SRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERqLASREEDEDDRKKGLTSKIRNLTEELE 1614
Cdd:TIGR02169 772 EDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1615 SEQRARQAAIANKKKIESQISELteknEASLRQIEDlsrqlrkaqlGWKDLQLDVTEARAAMEDALAGQRDAEKRARASE 1694
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEEL----EAALRDLES----------RLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1695 DEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRASSFSNEEKRRLEAKVIDLEDqldeeasANELAQ---EKVRKSQQ 1771
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP-------VNMLAIqeyEEVLKRLD 989
|
890 900
....*....|....*....|..
gi 71983975 1772 QLEQMTADLAMER-SVCERTES 1792
Cdd:TIGR02169 990 ELKEKRAKLEEERkAILERIEE 1011
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
890-1655 |
1.17e-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: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 890 QQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRLEIEEQKAKKadsesrKLTEMVRHLEENL 969
Cdd:pfam01576 292 KQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQ------KHTQALEELTEQL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 970 EDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEI 1049
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1050 NDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQ 1129
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1130 LDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKTVLHSQLKAKRDEEYAHL------QKQ----LEETVKS 1199
Cdd:pfam01576 526 LSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLlvdldhQRQlvsnLEKKQKK 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1200 SEEVVEEMKAQNQKKIEELNETIDQ----------LKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKkrkaaet 1269
Cdd:pfam01576 606 FDQMLAEEKAISARYAEERDRAEAEareketralsLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGK------- 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1270 SLMEKDHKMREMQSNLDDLMAKLSKMNNELesiQKAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTratLNNKIR 1349
Cdd:pfam01576 679 NVHELERSKRALEQQVEEMKTQLEELEDEL---QATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQ---LVKQVR 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1350 QLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERA---DMAEQARDK- 1425
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAsrdEILAQSKESe 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1426 -------------------AERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQML 1486
Cdd:pfam01576 833 kklknleaellqlqedlaaSERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL 912
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1487 RDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLAStkddagkNVYELEKT-KRRLDEELSRAEQQIIELEDalQL 1565
Cdd:pfam01576 913 RKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKA-------KLQEMEGTvKSKFKSSIAALEAKIAQLEE--QL 983
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1566 ADDARSRVEVNMQAMRSEF-----------ERQLASREEDEDDRkkgLTSKIRNLTEELESEQRARQAAIANKKKIESQI 1634
Cdd:pfam01576 984 EQESRERQAANKLVRRTEKklkevllqvedERRHADQYKDQAEK---GNSRMKQLKRQLEEAEEEASRANAARRKLQREL 1060
|
810 820
....*....|....*....|.
gi 71983975 1635 SELTEKNEASLRQIEDLSRQL 1655
Cdd:pfam01576 1061 DDATESNESMNREVSTLKSKL 1081
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1332-1934 |
4.52e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1332 EASEEDRRTRATLN-NKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVmeelrkkkekelS 1410
Cdd:COG1196 217 ELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL------------E 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1411 AEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAE 1490
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1491 TKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDdagknvyELEKTKRRLDEELSRAEQQIIELEDALQLADDAR 1570
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE-------ELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1571 SRVEVNMQAMRSEFERQLASREEDEDDRKKGLTSkiRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIED 1650
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEE--AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1651 LSRQLRKAQLGwKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEikrltadiQAVSSSKRKAEAERDELIEEVSSLRA 1730
Cdd:COG1196 516 LAGLRGLAGAV-AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--------AAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1731 SSFSNEEKRRLEAKVIDLEDQLDEEASANELAQEkvrksqqqleqmtaDLAMERSVCERTESDKIALERANRDLKQQLQD 1810
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGD--------------TLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1811 AENTAVARLRTqinvaEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLR 1890
Cdd:COG1196 653 GEGGSAGGSLT-----GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 71983975 1891 TQLEDTEAERDRLTNKLKDERRRAEEMTDLN----ETLSRDVSLLKQR 1934
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEppdlEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1247-1894 |
7.09e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1247 RAEL-SNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDM 1325
Cdd:COG1196 195 LGELeRQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1326 QLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMeelrkkk 1405
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE------- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1406 ekelsAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEernntlLAQQERDMAHQM 1485
Cdd:COG1196 348 -----EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE------LEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1486 LRdAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLAStkddagknvyELEKTKRRLDEELSRAEQQIIELEDALQL 1565
Cdd:COG1196 417 ER-LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE----------EEEALLELLAELLEEAALLEAALAELLEE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1566 ADDARSRVEVNMQAMRSEFERQLASREEDEDDRKKGLTSKIRNLTEELESEQRARQAAIAnkkkieSQISELTEKNEASL 1645
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA------AALQNIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1646 RQIEDLSRQLRKAQLGwkDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRltadiqavsssKRKAEAERDELIEEV 1725
Cdd:COG1196 560 AAAIEYLKAAKAGRAT--FLPLDKIRARAALAAALARGAIGAAVDLVASDLREA-----------DARYYVLGDTLLGRT 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1726 SSLRASSFSNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQmtadlamersvcertesdKIALERANRDLK 1805
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE------------------AEAELEELAERL 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1806 QQLQDAENTAVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNAR 1885
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
....*....
gi 71983975 1886 IRQLRTQLE 1894
Cdd:COG1196 769 LERLEREIE 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
861-1655 |
9.72e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 106.69 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 861 DELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEER------LVLKTRL-DAESSERA----EIFEERSRMAARRDE 929
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKrEYEGYELLkekeALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 930 LEGILEEVSKRLeieEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEknsIESRLKELEAQGLELEDSGNKLSK 1009
Cdd:TIGR02169 249 LEEELEKLTEEI---SELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE---LEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1010 EKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAE 1089
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1090 ELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETnkeKAARQKAEKARRDMAEELESYKQELEESN 1169
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI---KKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1170 DktvLHSQLKAKRdEEYAHLQKQ---LEETVKSSEEVVEEMKAqnqkKIEELNETIDQLKRQKISADKAKSSAESDNENF 1246
Cdd:TIGR02169 480 R---VEKELSKLQ-RELAEAEAQaraSEERVRGGRAVEEVLKA----SIQGVHGTVAQLGSVGERYATAIEVAAGNRLNN 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1247 -RAELSNIASARLEAEKKRKAAETSLMEKDhKMREMQSNLD--------DLMAKLSKMNNELESIQKAKSADETLNSNL- 1316
Cdd:TIGR02169 552 vVVEDDAVAKEAIELLKRRKAGRATFLPLN-KMRDERRDLSilsedgviGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIe 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1317 ----LKKNASLDMQLSELTEASEE----DRRTRATLNNKIRQLEEDLAVAveARDDALDAQ-EKIEKEVKEVKSLLAEAR 1387
Cdd:TIGR02169 631 aarrLMGKYRMVTLEGELFEKSGAmtggSRAPRGGILFSRSEPAELQRLR--ERLEGLKRElSSLQSELRRIENRLDELS 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1388 KKLDEENREVMEELRKKKEKELSAEKERADMAEQARD--KAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQL 1465
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1466 AEERNNTLlaQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRL 1545
Cdd:TIGR02169 789 SHSRIPEI--QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1546 DEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEfERQLASREEDEDDRKKGLTSKIRNLTEELESEQRARQAAI- 1624
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERK-IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEe 945
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 71983975 1625 ------------ANKKKIESQISELTEKNEASLRQIEDLSRQL 1655
Cdd:TIGR02169 946 ipeeelsledvqAELQRVEEEIRALEPVNMLAIQEYEEVLKRL 988
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1105-1938 |
1.21e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 103.30 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1105 ISIRNDEELAARQQLEREIREiRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKTVLHSQLKAKRDE 1184
Cdd:PTZ00121 1024 FNIEKIEELTEYGNNDDVLKE-KDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEE 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1185 EYAHLQKQLEETVKSSEEvveEMKAQNQKKIEELNETIDQLKRQ---KISADKAKSSAESDNENFRAELSNIASARLEAE 1261
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEA---KKKAEDARKAEEARKAEDARKAEearKAEDAKRVEIARKAEDARKAEEARKAEDAKKAE 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1262 KKRKAAETSLMEKDHKMREMQSnlddlmAKLSKMNNELESIQKAKSADETLNSNLLKKnasldmqLSELTEASEEDRRTR 1341
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARK------AEAARKAEEERKAEEARKAEDAKKAEAVKK-------AEEAKKDAEEAKKAE 1246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1342 ATLNNK-IRQLEEDLAVAVEARDDALDAQE--------KIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAE 1412
Cdd:PTZ00121 1247 EERNNEeIRKFEEARMAHFARRQAAIKAEEarkadelkKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1413 KERAdmAEQARDKAERAKKKAiqeaedvqkeltdvVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAET- 1491
Cdd:PTZ00121 1327 AKKK--ADAAKKKAEEAKKAA--------------EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEk 1390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1492 -KALVLSNELSEKKDIVDQLEKdkrtlkleidnlastKDDAGKNVYELEKTKrrldEELSRAEQQIIELEDALQlADDAR 1570
Cdd:PTZ00121 1391 kKADEAKKKAEEDKKKADELKK---------------AAAAKKKADEAKKKA----EEKKKADEAKKKAEEAKK-ADEAK 1450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1571 SRVEvnmQAMRSEFERQLASREEDEDDRKKGltskirnlTEELESEQRARQAAIANKKKIEsqisELTEKNEASLRqied 1650
Cdd:PTZ00121 1451 KKAE---EAKKAEEAKKKAEEAKKADEAKKK--------AEEAKKADEAKKKAEEAKKKAD----EAKKAAEAKKK---- 1511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1651 lSRQLRKAQLGWKDLQLDVTEARAAMEDAlagqRDAEKRARAseDEIKRlTADIQAVSSSKRKAEAERDELIEEVSSLRA 1730
Cdd:PTZ00121 1512 -ADEAKKAEEAKKADEAKKAEEAKKADEA----KKAEEKKKA--DELKK-AEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1731 SSFSNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQqleqmtadlamersvCERTESDKIALERANRDLKQQLQD 1810
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE---------------LKKAEEEKKKVEQLKKKEAEEKKK 1648
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1811 AENTAVARLRTQINVAEakvsslEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLR 1890
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAE------EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK 1722
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 71983975 1891 TQLEDTEAERDRLTNKLKDERRRAEEMTDLNETLSRDVSLLKQRETTA 1938
Cdd:PTZ00121 1723 KAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
858-1658 |
1.48e-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: 102.84 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 858 TNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEV 937
Cdd:TIGR02169 198 QQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 938 SKRLE---IEEQKAKKAD-----SESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSK 1009
Cdd:TIGR02169 278 NKKIKdlgEEEQLRVKEKigeleAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1010 EKKALEERCEDLSSRLideverskqlvkakARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAE 1089
Cdd:TIGR02169 358 EYAELKEELEDLRAEL--------------EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1090 ELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESN 1169
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1170 DK--------TVLHSQLKA---------KRDEEYA---------HLQKQLEETVKSSEEVVEEMKAQNQKKIE--ELNET 1221
Cdd:TIGR02169 504 ERvrggraveEVLKASIQGvhgtvaqlgSVGERYAtaievaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATflPLNKM 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1222 IDQLKRQKISA-----DKAKSSAESDNEN-------FRAEL--SNIASARLEAEKKRKAA-ETSLMEKDHKM-------R 1279
Cdd:TIGR02169 584 RDERRDLSILSedgviGFAVDLVEFDPKYepafkyvFGDTLvvEDIEAARRLMGKYRMVTlEGELFEKSGAMtggsrapR 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1280 EMQSNLDDLMAKLSKMNNELESIQKAKSAdetlnsnLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAV 1359
Cdd:TIGR02169 664 GGILFSRSEPAELQRLRERLEGLKRELSS-------LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1360 EARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREvmeelrkkkekelsAEKERADMAEQARDKAERAKKKAIQEAED 1439
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSELKELEARIEELEED--------------LHKLEEALNDLEARLSHSRIPEIQAELSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1440 VQKELTDVVAATREMERKMRK--FDQQLAEERNNTLLAQQE-----RDMAHQMLRDAETKALVLSNELSEKKDIVDQLEK 1512
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRltLEKEYLEKEIQELQEQRIdlkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1513 DKRTLKLEIDNLASTKDdagknvyELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQLasre 1592
Cdd:TIGR02169 883 RLGDLKKERDELEAQLR-------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL---- 951
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71983975 1593 eDEDDRKKgltsKIRNLTEELESEQRARQAAIANKKKIESQISELTEK-------NEASLRQIEDLSRQLRKA 1658
Cdd:TIGR02169 952 -SLEDVQA----ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKrakleeeRKAILERIEEYEKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1296-1963 |
4.00e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 101.76 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1296 NNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKE 1375
Cdd:PTZ00121 1055 NHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR 1134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1376 VKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQK------------- 1442
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKaeaarkaeeerka 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1443 ------ELTDVVAATREME--RKMRKFDQQLAEERNNTLLAQ-QERDMAHQMLRDAETKAlvlsnELSEKKDIVDQLEKD 1513
Cdd:PTZ00121 1215 eearkaEDAKKAEAVKKAEeaKKDAEEAKKAEEERNNEEIRKfEEARMAHFARRQAAIKA-----EEARKADELKKAEEK 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1514 KRTLKLEIDNLASTKDDAGKNVYElektKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQLASREE 1593
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1594 DEDDRKKglTSKIRNLTEELESEQRARQAAIANKKKIES--QISELTEKNEASLRQIEDLSR---QLRKAQlgwkDLQLD 1668
Cdd:PTZ00121 1366 AEAAEKK--KEEAKKKADAAKKKAEEKKKADEAKKKAEEdkKKADELKKAAAAKKKADEAKKkaeEKKKAD----EAKKK 1439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1669 VTEARAAMEDALAGQ--RDAEKRARASE-----DEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRASSFSNEEKRRL 1741
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEeaKKAEEAKKKAEeakkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1742 EAKVIDLEDQLDEEASANELAQ-EKVRKSQQQLEQMTADLAMERsvcERTESDKIALERANRDLKQQlQDAENTAVARLR 1820
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKaEEKKKADELKKAEELKKAEEK---KKAEEAKKAEEDKNMALRKA-EEAKKAEEARIE 1595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1821 TQINVAEAKVSSLEQQLSLEEQDKMR--QGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQLEDTEA 1898
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1899 ERDRLtNKLKDERRRAEEMTDLNETLSRDVSLLKQRETTARRTPGLIGHRESRRFGSNTSLARDE 1963
Cdd:PTZ00121 1676 KAEEA-KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1139-1933 |
3.31e-20 |
|
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: 98.59 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1139 KEKAARQKAEKARRDMAEELESYKQELEESNdKTVLHSQLKAKRDEEYAHLQKQLEETVKSSeeVVEEMKAQNqKKIEEL 1218
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELE-RQLKSLERQAEKAERYKELKAELRELELAL--LVLRLEELR-EELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1219 NETIDQLKRQKISADKAKSSAESDNENFRAELSniasarleaekkrkaaetslmEKDHKMREMQSNLDDLMAKLSKMNNE 1298
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVS---------------------ELEEEIEELQKELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1299 LESIQKAKsadETLNSNLLKKNASLDMQLSELTEASEEDRRTRA---TLNNKIRQLEEDLAVAVEARDDALDAQEKIEKE 1375
Cdd:TIGR02168 304 KQILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEkleELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1376 VKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREME 1455
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1456 RKMRKFDQQLAEernntllaqqerdmAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGknv 1535
Cdd:TIGR02168 461 EALEELREELEE--------------AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG--- 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1536 yelektkrRLDEELSRAEQQIIELEDALqlADDARSRVEVNMQAMRSEFERQLASREED----EDDRKKGltSKIRNLTE 1611
Cdd:TIGR02168 524 --------VLSELISVDEGYEAAIEAAL--GGRLQAVVVENLNAAKKAIAFLKQNELGRvtflPLDSIKG--TEIQGNDR 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1612 ELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLS---RQLRKAQLGWKDLQLDVTEARAamEDALAGQRDAEK 1688
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDnalELAKKLRPGYRIVTLDGDLVRP--GGVITGGSAKTN 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1689 RAR-ASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLrassfsNEEKRRLEAKVIDLEDQLDEEASANELAQEKVR 1767
Cdd:TIGR02168 670 SSIlERRREIEELEEKIEELEEKIAELEKALAELRKELEEL------EEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1768 KSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQQLQDAENTaVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQ 1847
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAANL 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1848 GRTLRRMETKMAEMQQMLEEEKRQ-------GESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKLKDERRRAEEMTDL 1920
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQieelsedIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
810
....*....|...
gi 71983975 1921 NETLSRDVSLLKQ 1933
Cdd:TIGR02168 903 LRELESKRSELRR 915
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1252-1938 |
8.41e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.06 E-value: 8.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1252 NIASARLEAEKKRKAAETSLMEKDHKMR--EMQSNLDDLMAKLskMNNELESIQKAKSADETLNSNLLKKNASLDMQLSE 1329
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAERyqALLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1330 LTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQ----EKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKK 1405
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEiaslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1406 EKELSAEKERAD-MAEQARDKAERAKKKaiQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQ 1484
Cdd:TIGR02169 343 REIEEERKRRDKlTEEYAELKEELEDLR--AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1485 MLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQ 1564
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1565 LAddarsrvevnmqamrSEFERQLASREEDEDDRKKGLTSKIRNLTEELESEQRARQAAIANKKK---------IESQIS 1635
Cdd:TIGR02169 501 AS---------------EERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNnvvveddavAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1636 ELTEKNEAS-----LRQIEDLSRQLRK-AQLGWKDLQLDVTE------------------------ARAAMEDA----LA 1681
Cdd:TIGR02169 566 LLKRRKAGRatflpLNKMRDERRDLSIlSEDGVIGFAVDLVEfdpkyepafkyvfgdtlvvedieaARRLMGKYrmvtLE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1682 GQ---------------RDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRASsfSNEEKRRLEAKVI 1746
Cdd:TIGR02169 646 GElfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE--LSDASRKIGEIEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1747 DLEDQLDEEASANELA---QEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQQLQDAE----------- 1812
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLeelEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelskl 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1813 NTAVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQ 1892
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 71983975 1893 LEDTEAERDRLTNKLKDERRRAEEmtdLNETLSRDVSLLKQRETTA 1938
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEE---LEAQIEKKRKRLSELKAKL 926
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
852-1736 |
8.93e-20 |
|
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: 96.96 E-value: 8.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 852 KPLLEVTN--KDELIAEREQELKVTAEKLRRSEvfisDYKQQMEKMDEERLVLKTRLDAESSERAEifeersrmaaRRDE 929
Cdd:pfam02463 176 KKLIEETEnlAELIIDLEELKLQELKLKEQAKK----ALEYYQLKEKLELEEEYLLYLDYLKLNEE----------RIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 930 LEGILEEVSKRLEIEEQKAKKADsesrkltEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSK 1009
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEE-------EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1010 EKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQesclEKTRKAE 1089
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES----ERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1090 ELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEE--TNKEKAARQKAEKARRDMAEELESYKQELEE 1167
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEEsiELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1168 SNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNEtIDQLKRQKISADKAKSSAESDNENFR 1247
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR-IISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1248 AELSNIASARLEAEKKRKAAETSLmEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQL 1327
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTEL-PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGI 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1328 SELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEK 1407
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1408 ELSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLR 1487
Cdd:pfam02463 709 KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1488 DAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLAD 1567
Cdd:pfam02463 789 EEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1568 DARSRvevnmqamrsefERQLASREEDEDDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQ 1647
Cdd:pfam02463 869 LQELL------------LKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEE 936
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1648 IEDLSRQ--LRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQavsssKRKAEAERDELIEEV 1725
Cdd:pfam02463 937 PEELLLEeaDEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE-----KERLEEEKKKLIRAI 1011
|
890
....*....|.
gi 71983975 1726 SSLRASSFSNE 1736
Cdd:pfam02463 1012 IEETCQRLKEF 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1618 |
1.82e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.91 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 849 TKVKPLLEvtnkDELIAEREQELKVTAEkLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRD 928
Cdd:TIGR02169 279 KKIKDLGE----EEQLRVKEKIGELEAE-IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 929 ELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLS 1008
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1009 KEKKALEERCEDLSSRLIDEVERSKQLVKAKA-------RLEATVAEINDELEKEKQQRHNAETARRAAETQLRE--EQE 1079
Cdd:TIGR02169 434 AKINELEEEKEDKALEIKKQEWKLEQLAADLSkyeqelyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGgrAVE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1080 SCLEKTRKA-EELTNQLMRKESELsQISIrndeELAARQQLEREIREiraqlDDAIEETNKEKAARQKAEKARRDMAEEL 1158
Cdd:TIGR02169 514 EVLKASIQGvHGTVAQLGSVGERY-ATAI----EVAAGNRLNNVVVE-----DDAVAKEAIELLKRRKAGRATFLPLNKM 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1159 ESYKQELEESNDKTVLHSQLKAKR-DEEYAHLQKQ-LEETVksseeVVEEMKAQNQKKIEELNETIDQLKRQKISADKAK 1236
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAVDLVEfDPKYEPAFKYvFGDTL-----VVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGG 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1237 SSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEkdhKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNL 1316
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS---ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1317 LKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDD--ALDAQEKIEKEVKEVKSLLAEaRKKLDEEN 1394
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDleARLSHSRIPEIQAELSKLEEE-VSRIEARL 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1395 REVMEELRKKKEKELSAEKERADMAEQARDKAERaKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEernntll 1474
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD------- 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1475 AQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKdDAGKNVYELEKTKRRLDEELSRAEQ 1554
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEE 965
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1555 QIIELEDalqladdarsrveVNMQAMRsEFERQLASREEDEDDRKKGLTSK--IRNLTEELESEQR 1618
Cdd:TIGR02169 966 EIRALEP-------------VNMLAIQ-EYEEVLKRLDELKEKRAKLEEERkaILERIEEYEKKKR 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
855-1548 |
2.38e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 95.51 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 855 LEVTNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGIL 934
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 935 EEVSKRLEieEQKAKKADSESRkltemVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKAL 1014
Cdd:TIGR02168 354 ESLEAELE--ELEAELEELESR-----LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1015 EERCEdlSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQ------ESCLEKTRKA 1088
Cdd:TIGR02168 427 LKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENLEGF 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1089 EELTNQLMRKESELS--------QISIRNDEELA-------ARQQLEREIREIRAQLDDAIEETNKEKAA--------RQ 1145
Cdd:TIGR02168 505 SEGVKALLKNQSGLSgilgvlseLISVDEGYEAAieaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTflpldsikGT 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1146 KAEKARRDMAEELESYKQ---ELEESNDK---------------------TVLHSQLKAK-------------------- 1181
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGvakDLVKFDPKlrkalsyllggvlvvddldnaLELAKKLRPGyrivtldgdlvrpggvitgg 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1182 ----------RDEEYAHLQKQ---LEETVKSSEEVVEEMKAQN---QKKIEELNETIDQLKRQKISADKAKSSAESDNEN 1245
Cdd:TIGR02168 665 saktnssileRRREIEELEEKieeLEEKIAELEKALAELRKELeelEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1246 FRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDM 1325
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1326 QLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEenrevmeelrkkk 1405
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL------------- 891
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1406 ekelsAEKERADMAEQARDkAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLlaqqerDMAHQM 1485
Cdd:TIGR02168 892 -----LRSELEELSEELRE-LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL------EEAEAL 959
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1486 LRDAETKALVLSNELSEKKDIVDQL-------EKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEE 1548
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
925-1468 |
3.20e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 94.75 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 925 ARRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQK---LLLEKNSIESRLKELEAQGLELE 1001
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1002 DSGNKLSKEKKALEERCEDLSS------RLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAE--TQ 1073
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEelKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1074 LREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEElaARQQLEREIREI---RAQLDDAIEETNKEKAARQKAEKA 1150
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELekaKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1151 RRDMAEELESYK-------QELEESNDKTVLhsqlkakrdEEYAHLQKQLEETVKSSEEVVEEMKAqNQKKIEELNETID 1223
Cdd:PRK03918 424 LKKAIEELKKAKgkcpvcgRELTEEHRKELL---------EEYTAELKRIEKELKEIEEKERKLRK-ELRELEKVLKKES 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1224 QLKRQKISADKAKSsAESDNENFRAElsniasarlEAEKKRKAAETsLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQ 1303
Cdd:PRK03918 494 ELIKLKELAEQLKE-LEEKLKKYNLE---------ELEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELKKKLAELE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1304 KAKSADETLNSNLLKKNAS--------LDMQLSELTEASEEDRRTRATlNNKIRQLEEDLAVAVEARDDALDAQEKIEKE 1375
Cdd:PRK03918 563 KKLDELEEELAELLKELEElgfesveeLEERLKELEPFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKR 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1376 VKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDKAER------AKKKAIQEAEDVQKELTDVVA 1449
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKtleklkEELEEREKAKKELEKLEKALE 721
|
570
....*....|....*....
gi 71983975 1450 ATREMERKMRKFDQQLAEE 1468
Cdd:PRK03918 722 RVEELREKVKKYKALLKER 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
855-1397 |
2.98e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 855 LEVTNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGIL 934
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 935 EEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKAL 1014
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1015 EERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAEtARRAAETQLREEQESCLEKTRKAEELTNQ 1094
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA-ARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1095 LMRKESELSQISIRNDEELAAR----QQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESND 1170
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1171 KTVLHSQLKAKRDEEYAHLQKQLEETVkSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAEL 1250
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRT-LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1251 SNIASARLEAEKKRKAAETSLMEKDHKMREMQsnlddlmAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSEL 1330
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELA-------EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1331 TEASEEDRRTRATLNNKIRQLEEDL----AV---------AVEARDDALDAQ-EKIEKEVKEvkslLAEARKKLDEENRE 1396
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIealgPVnllaieeyeELEERYDFLSEQrEDLEEARET----LEEAIEEIDRETRE 827
|
.
gi 71983975 1397 V 1397
Cdd:COG1196 828 R 828
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
860-1376 |
9.63e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 9.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 860 KDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDE-------ERLVLKTRLDAESSERAEIFEERSRMAARRDELEG 932
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElkkaaaaKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 933 ILEEVSKRLEIEE--QKAKKADsESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSK- 1009
Cdd:PTZ00121 1452 KAEEAKKAEEAKKkaEEAKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKa 1530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1010 -EKKALEERCEDLSSRLIDEVERSKQLVKAKARLEatVAEINDELEKEKQQRHNAETARRAAETQL-------REEQESC 1081
Cdd:PTZ00121 1531 eEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEEAKKAEEARIeevmklyEEEKKMK 1608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1082 LEKTRKAEE--LTNQLMRKESE----LSQISIRNDEELAARQQLEREIREIRAQlddAIEETNKEKAARQKAEKARRDMA 1155
Cdd:PTZ00121 1609 AEEAKKAEEakIKAEELKKAEEekkkVEQLKKKEAEEKKKAEELKKAEEENKIK---AAEEAKKAEEDKKKAEEAKKAEE 1685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1156 EELESYKQELEESNDKTVLHsQLKAKRDEEyahlqKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKisADKA 1235
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAE-ELKKKEAEE-----KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE--EEKK 1757
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1236 KSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMN---NELESIQKAKSADETL 1312
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlviNDSKEMEDSAIKEVAD 1837
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1313 NSNLLKKNA-SLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEV 1376
Cdd:PTZ00121 1838 SKNMQLEEAdAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
862-1313 |
2.17e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.50 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 862 ELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEErlvlKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRL 941
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR----LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 942 EIEEQKAKKADSESRKLTEMVRH-----------LEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKE 1010
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLkkrltgltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1011 KKaleeRCEdLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAetarRAAETQLREEqesclEKTRKAEE 1090
Cdd:PRK03918 435 KG----KCP-VCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL----RELEKVLKKE-----SELIKLKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1091 LTNQLMRKESELSQIsirNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEEsnd 1170
Cdd:PRK03918 501 LAEQLKELEEKLKKY---NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE--- 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1171 ktvLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAqnQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAEL 1250
Cdd:PRK03918 575 ---LLKELEELGFESVEELEERLKELEPFYNEYLELKDA--EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1251 SNIASARLEAEKKRKAAETSLMEKDH-----KMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLN 1313
Cdd:PRK03918 650 EELEKKYSEEEYEELREEYLELSRELaglraELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1349-1913 |
3.01e-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: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1349 RQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSL--LAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDKA 1426
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIELLepIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1427 ERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFD----QQLAEERNNTLLAQQERDMAHQMLRDAeTKALVLSNELSE 1502
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELEERERRRARLEAL-LAALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1503 kkdivDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDAlqladdaRSRVEVNMQAMRS 1582
Cdd:COG4913 380 -----EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR-------KSNIPARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1583 EFERQLASREED-----------EDDRK------KGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASL 1645
Cdd:COG4913 448 ALAEALGLDEAElpfvgelievrPEEERwrgaieRVLGGFALTLLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1646 RQIEDLSRQLRKaqlgwkdLQLDVTEARAAMEDALAGQRDAEKRARASE--DEIKRLTADIQaVSSSKRKAEAERDELIE 1723
Cdd:COG4913 528 RPRLDPDSLAGK-------LDFKPHPFRAWLEAELGRRFDYVCVDSPEElrRHPRAITRAGQ-VKGNGTRHEKDDRRRIR 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1724 EVSSLrasSFSNEEKR-RLEAKVIDLEDQLDEeasanelAQEKVRKSQQQLEQMTADLAMERSVCERTES--DKIALERA 1800
Cdd:COG4913 600 SRYVL---GFDNRAKLaALEAELAELEEELAE-------AEERLEALEAELDALQERREALQRLAEYSWDeiDVASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1801 NRDLKQQLQ--DAENTAVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESN--- 1875
Cdd:COG4913 670 IAELEAELErlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElra 749
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 71983975 1876 -------RQAVDRQNARIR-QLRTQLEDTEAERDRLTNKLKDERRR 1913
Cdd:COG4913 750 lleerfaAALGDAVERELReNLEERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1277-1941 |
2.92e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.03 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1277 KMREMQSNLDDLMAKLSKMNNELESIQK-AKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEdl 1355
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERqAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEE-- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1356 avaVEARDDALDAQ-EKIEKEVKEVKSLLAEARKKLDEENREV--MEELRKKKEKELSAEKERADMAEQARDKAERAKKK 1432
Cdd:TIGR02168 258 ---LTAELQELEEKlEELRLEVSELEEEIEELQKELYALANEIsrLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1433 AIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEK 1512
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1513 DKRTLKLEIDNLASTKDDAgknvyELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEferqlasre 1592
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEA-----ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA--------- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1593 EDEDDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIE------SQISELTEKNEASLrqiedlsrqlrKAQLGwKDLQ 1666
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvlSELISVDEGYEAAI-----------EAALG-GRLQ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1667 LDVTEARAAMEDALAGQRDAEKRARA-------SEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRASSFSN---- 1735
Cdd:TIGR02168 549 AVVVENLNAAKKAIAFLKQNELGRVTflpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvv 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1736 -------EEKRRLEAK--VIDLEDQL----------DEEASANELAQEK-VRKSQQQLEQMTADLAMERSVCERTESDKI 1795
Cdd:TIGR02168 629 ddldnalELAKKLRPGyrIVTLDGDLvrpggvitggSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1796 ALERANRDLKQQLQDaentavarLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESN 1875
Cdd:TIGR02168 709 ELEEELEQLRKELEE--------LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1876 RQAVDRQNARIRQLRTQLEDTEAERDRLTNKLKDERRRAEEMTDLNETLSRDVSLLKQRETTARRT 1941
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1000-1655 |
4.86e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 81.26 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1000 LEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINdELEKEkqqrhnaetarraaETQLREEQE 1079
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-EISSE--------------LPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1080 SCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDaIEETNKEKAARQKAEKARRDMAEELE 1159
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1160 SYKQELEESndktvlhSQLKAKRDEEYAHLQKQLEEtVKSSEEVVEEMKaqnqKKIEELNETIDQLKRQKISADKAKSSA 1239
Cdd:PRK03918 304 EYLDELREI-------EKRLSRLEEEINGIEERIKE-LEEKEERLEELK----KKLKELEKRLEELEERHELYEEAKAKK 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1240 EsDNENFRAELSNIASARLEAE-KKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELEsiqKAKSADETLNSnllk 1318
Cdd:PRK03918 372 E-ELERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVCGR---- 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1319 knasldmqlsELTEASEEDRRTRATLnnKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEarKKLDEENREVM 1398
Cdd:PRK03918 444 ----------ELTEEHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL--KELAEQLKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1399 EELRKKKEKELSAEKERADMAEQARDKAE---RAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLA 1475
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKgeiKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1476 QQERdmaHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRaeqq 1555
Cdd:PRK03918 590 LEER---LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE---- 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1556 iieledalqladdarsRVEVNMQAMRSEFERQLASREEDEdDRKKGLTSKIRNLTEELESEQRARQaAIANKKKIESQIS 1635
Cdd:PRK03918 663 ----------------ELREEYLELSRELAGLRAELEELE-KRREEIKKTLEKLKEELEEREKAKK-ELEKLEKALERVE 724
|
650 660
....*....|....*....|....*...
gi 71983975 1636 ELTEK--------NEASLRQIEDLSRQL 1655
Cdd:PRK03918 725 ELREKvkkykallKERALSKVGEIASEI 752
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
860-1389 |
1.10e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 860 KDELIAEREQELKVTAEKLRRSEvfisdykQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSK 939
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKAD-------EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 940 RLEIEE--QKAKKADSESRKLTEMVRHLEENLEDEERSR----QKLLLEKNSIESRLKELEAQGLELEDSGN-KLSKEKK 1012
Cdd:PTZ00121 1485 ADEAKKkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKadeaKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKK 1564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1013 ALEE--RCEDLSSRLIDEVERSKQLVKAKARLEATVAEIN-----DELEKEKQQRHNAETARRAAETQLREEQ--ESCLE 1083
Cdd:PTZ00121 1565 KAEEakKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEkkmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQlkKKEAE 1644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1084 KTRKAEELTN----------QLMRKESElsqiSIRNDEELAARQQLEREireiraqlddAIEETNKEKAARQKAEKARRD 1153
Cdd:PTZ00121 1645 EKKKAEELKKaeeenkikaaEEAKKAEE----DKKKAEEAKKAEEDEKK----------AAEALKKEAEEAKKAEELKKK 1710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1154 MAEELESYKQELEESNDKTVLHSQLKAKRDEEyahlQKQLEETVKSSEE--VVEEMKAQNQKKIEELNETIDQLKRQKIS 1231
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEED----KKKAEEAKKDEEEkkKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1232 ADKAKSSAESDN--ENFRAELSNIASArleaekkrkAAETSLMEKDHKMREMqSNLDDLMAKLSKMNNELESIQKAKSAD 1309
Cdd:PTZ00121 1787 EEDEKRRMEVDKkiKDIFDNFANIIEG---------GKEGNLVINDSKEMED-SAIKEVADSKNMQLEEADAFEKHKFNK 1856
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1310 ETLNSNLLKKNASLDMQ---LSELTEASEEDRRTRATLNNKIRQLEEDLAVA---VEARDDALDAQEKIEKEVKEVKSLL 1383
Cdd:PTZ00121 1857 NNENGEDGNKEADFNKEkdlKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAgknNDIIDDKLDKDEYIKRDAEETREEI 1936
|
....*.
gi 71983975 1384 AEARKK 1389
Cdd:PTZ00121 1937 IKISKK 1942
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
865-1350 |
1.68e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 865 AEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEE-------RSRMAARRDELEGILEEV 937
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadAEAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 938 SKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEER 1017
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1018 CEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMR 1097
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELED 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1098 KESELSQISIRNdEELAARQQLEREIREIRAQLDDA---IEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKTVL 1174
Cdd:PRK02224 487 LEEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1175 HSQLKAKRDEEYAHLQKQLEETVKSSEEVVE--EMKAQNQKKIEELNETIDQLKRQKisaDKAKSSAESDNENFRAELSN 1252
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLERIRTllAAIADAEDEIERLREKREALAELN---DERRERLAEKRERKRELEAE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1253 IASARLE-AEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKknasldmqLSELT 1331
Cdd:PRK02224 643 FDEARIEeAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEA--------LEALY 714
|
490
....*....|....*....
gi 71983975 1332 EASEEDRRTRATLNNKIRQ 1350
Cdd:PRK02224 715 DEAEELESMYGDLRAELRQ 733
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1040-1378 |
1.78e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 79.72 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1040 ARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQL 1119
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1120 EREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKTVLHSQ-----------------LKAKR 1182
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanlrerleslerriaATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1183 DEEYAHLQKQLEETVKSSEEVVEEMkaqnQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEK 1262
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEEL----EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1263 KRKAAETSLMEKDHKMREMQSNLDDLMAKLS-KMNNELESIQKAKSADETLNSNLLKKNASLDMQLSEL----TEASEED 1337
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEY 995
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 71983975 1338 RRTRATLNNKIRQLEEdlavAVEARDDALDAQEKIEKEVKE 1378
Cdd:TIGR02168 996 EELKERYDFLTAQKED----LTEAKETLEEAIEEIDREARE 1032
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1646-1944 |
1.95e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1646 RQIEDLSRQLRKAQ----LGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDEL 1721
Cdd:COG1196 200 RQLEPLERQAEKAEryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1722 IEEVSSLRAssfsneEKRRLEAKVIDLEDQLDeeasaneLAQEKVRKSQQQLEQMTADLAmersvcertesdkiALERAN 1801
Cdd:COG1196 280 ELELEEAQA------EEYELLAELARLEQDIA-------RLEERRRELEERLEELEEELA--------------ELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1802 RDLKQQLQDAENTAVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDR 1881
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71983975 1882 QNARIRQLRTQLEDTEAERDRLTNKLKDERRRAEEMTDLNETLSRDVSLLKQRETTARRTPGL 1944
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1042-1690 |
2.91e-14 |
|
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: 79.11 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1042 LEATVAEI--NDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQIS--IRNDEELAARQ 1117
Cdd:pfam12128 198 VKSMIVAIleDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHfgYKSDETLIASR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1118 Q---------LEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESndktvlhsqlkakRDEEYAH 1188
Cdd:pfam12128 278 QeerqetsaeLNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDA-------------DIETAAA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1189 LQKQLEETVKSSEEVVEEMKAQ--NQKKIEELNETIDQLKRQKISADKAKSSAESDNEnfraelsniasaRLEAEKKRKA 1266
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALtgKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKI------------REARDRQLAV 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1267 AETSLMEKDHKMREmqsnldDLMAKLSKMNNELESIqkaKSADETLNSNLLKKNASLD--MQLSELTEASEEDRRTRATL 1344
Cdd:pfam12128 413 AEDDLQALESELRE------QLEAGKLEFNEEEYRL---KSRLGELKLRLNQATATPEllLQLENFDERIERAREEQEAA 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1345 NNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLD-----------------EEN------REVMEEL 1401
Cdd:pfam12128 484 NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFpqagtllhflrkeapdwEQSigkvisPELLHRT 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1402 RKKKEKELSAEK------------------ERADMAEQARDKAERAkKKAIQEAEDVQKELTD-VVAATREMERKMRKFD 1462
Cdd:pfam12128 564 DLDPEVWDGSVGgelnlygvkldlkridvpEWAASEEELRERLDKA-EEALQSAREKQAAAEEqLVQANGELEKASREET 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1463 QQLAEERNNTLLAQQERDmAHQMLRDAETKALVLSNELSEKKdiVDQLEKDKRTLKLEI-DNLASTKDDAGKNVYELEKT 1541
Cdd:pfam12128 643 FARTALKNARLDLRRLFD-EKQSEKDKKNKALAERKDSANER--LNSLEAQLKQLDKKHqAWLEEQKEQKREARTEKQAY 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1542 KRRLDEELSRAEQQIIELEDALQLADDARsrvevnMQAMRSEFERQLASREEDEdDRKKGLTSKIRNLTEELESEQRARQ 1621
Cdd:pfam12128 720 WQVVEGALDAQLALLKAAIAARRSGAKAE------LKALETWYKRDLASLGVDP-DVIAKLKREIRTLERKIERIAVRRQ 792
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 1622 AAIANKKKIESQISELTEKNEASLRQIEdlsRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRA 1690
Cdd:pfam12128 793 EVLRYFDWYQETWLQRRPRLATQLSNIE---RAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRL 858
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1368-1914 |
9.39e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 77.08 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1368 AQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMaEQARDKAERAKKKAIQEAEDVQKELTDV 1447
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM-QMERDAMADIRRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1448 VaatREMErKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKdivdqLEKDKRTLKLEIDNLAST 1527
Cdd:pfam15921 151 V---HELE-AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKK-----IYEHDSMSTMHFRSLGSA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1528 kddagknvyeLEKTKRRLDEELSRAEQQIIELEDALQ-LADDARSRVEVNMQAMRSEFErQLASREEDEddrkkgltskI 1606
Cdd:pfam15921 222 ----------ISKILRELDTEISYLKGRIFPVEDQLEaLKSESQNKIELLLQQHQDRIE-QLISEHEVE----------I 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1607 RNLTEELESeqrARQAAIANKKKIESQISELTEKNEASLRQIEDLSR-------QLRKAQLGWKD----LQLDVTEARAA 1675
Cdd:pfam15921 281 TGLTEKASS---ARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLEStvsqlrsELREAKRMYEDkieeLEKQLVLANSE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1676 MEDALAGQRDAEKRARASEDEIKRLTADIQ------AVSSSKRKAEAERD--ELIEEVSSLRASSFSNEEKRRLEAKVID 1747
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLLADLHkrekelSLEKEQNKRLWDRDtgNSITIDHLRRELDDRNMEVQRLEALLKA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1748 LED----QLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANR---DLKQQLQDAE------NT 1814
Cdd:pfam15921 438 MKSecqgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKEraieatNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1815 AVARLRTQINVAEAKVSSLEQQ---------------LSLEEQDK----MRQ------------GRTLRRMETKMAEMQQ 1863
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEgdhlrnvqtecealkLQMAEKDKvieiLRQqienmtqlvgqhGRTAGAMQVEKAQLEK 597
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 71983975 1864 MLEEEKRQGESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKlKDERRRA 1914
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNA-GSERLRA 647
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1255-1754 |
1.92e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.23 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1255 SARLEAEKKRKAAETSLMEKDHKM-----REMQSNLDDLMAKLSKMNNELESIQK----AKSADETLNSNL------LKK 1319
Cdd:PRK02224 173 DARLGVERVLSDQRGSLDQLKAQIeekeeKDLHERLNGLESELAELDEEIERYEEqreqARETRDEADEVLeeheerREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1320 NASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVME 1399
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1400 ELRKKKEKELSAEKERADM------AEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFD----------- 1462
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDAddleerAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvdlgnaed 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1463 --QQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNE------------------LSEKKDIVDQLEKDKRTLKLEID 1522
Cdd:PRK02224 413 flEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1523 NLAStKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQ------LASREEDED 1596
Cdd:PRK02224 493 EVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKreaaaeAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1597 DRKKGLTSKIRNLTEELESEQRAR--QAAIANkkkIESQISELTEKNEAsLRQIEDLSRQL------RKAQLGWKDLQLD 1668
Cdd:PRK02224 572 EEVAELNSKLAELKERIESLERIRtlLAAIAD---AEDEIERLREKREA-LAELNDERRERlaekreRKRELEAEFDEAR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1669 VTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSkrkaeaerdelIEEVSSLRassfsnEEKRRLEAKVIDL 1748
Cdd:PRK02224 648 IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENE-----------LEELEELR------ERREALENRVEAL 710
|
....*.
gi 71983975 1749 EDQLDE 1754
Cdd:PRK02224 711 EALYDE 716
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
870-1392 |
1.97e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 75.83 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 870 ELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRLEIEEQKAK 949
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 950 KADSESRKL----------TEMVRHLEENLEDEERSRQKLlleKNSIESRLKELEAQGLELEDSGNKLS-------KEKK 1012
Cdd:TIGR04523 191 KIKNKLLKLelllsnlkkkIQKNKSLESQISELKKQNNQL---KDNIEKKQQEINEKTTEISNTQTQLNqlkdeqnKIKK 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1013 ALEERCEDL--SSRLIDEVErsKQLVKAKARLEATVAEINDELEKE-KQQRHNAETARRAAETQLRE---------EQES 1080
Cdd:TIGR04523 268 QLSEKQKELeqNNKKIKELE--KQLNQLKSEISDLNNQKEQDWNKElKSELKNQEKKLEEIQNQISQnnkiisqlnEQIS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1081 CLEKTRKAEELTN-----QLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDaIEETNKEKAAR-QKAEKARRDM 1154
Cdd:TIGR04523 346 QLKKELTNSESENsekqrELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN-QEKLNQQKDEQiKKLQQEKELL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1155 AEELESYKQELEESND-----------KTVLHSQLKAKRDeeyaHLQKQLEETVKSSEEVVEEMKaQNQKKIEELNETID 1223
Cdd:TIGR04523 425 EKEIERLKETIIKNNSeikdltnqdsvKELIIKNLDNTRE----SLETQLKVLSRSINKIKQNLE-QKQKELKSKEKELK 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1224 QLKRQKIsadkaKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQ 1303
Cdd:TIGR04523 500 KLNEEKK-----ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELK 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1304 KAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLL 1383
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
....*....
gi 71983975 1384 AEARKKLDE 1392
Cdd:TIGR04523 655 KEIRNKWPE 663
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
786-1223 |
2.74e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 786 AEFEEMRDQKLSALIESFQAqcrgwlgRRVMVRRREQEVAIKILQRNGLAwMRLREwqwwrlltKVKPLLE-VTNKDELI 864
Cdd:PRK02224 302 AGLDDADAEAVEARREELED-------RDEELRDRLEECRVAAQAHNEEA-ESLRE--------DADDLEErAEELREEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 865 AEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRLEIE 944
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 945 EQ--KAKKA-----DSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQgLELEDSGNKLSKEKKALEER 1017
Cdd:PRK02224 446 EAllEAGKCpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEEL 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1018 CEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKekqQRHNAETARRAAET------QLREEQEScLEKTR----K 1087
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE---AEEEAEEAREEVAElnsklaELKERIES-LERIRtllaA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1088 AEELTNQLMRKESELSQISIRNDEElaaRQQLeREIREIRAQLDDAIEETNKEKAA--RQKAEKARRDMAEELEsykqEL 1165
Cdd:PRK02224 601 IADAEDEIERLREKREALAELNDER---RERL-AEKRERKRELEAEFDEARIEEARedKERAEEYLEQVEEKLD----EL 672
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1166 EESNDKtvLHSQLKA-----KRDEEYAHLQKQLEETVKSSEEVVEE--------------MKAQNQKKIEE-LNETID 1223
Cdd:PRK02224 673 REERDD--LQAEIGAvenelEELEELRERREALENRVEALEALYDEaeelesmygdlraeLRQRNVETLERmLNETFD 748
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1075-1729 |
3.58e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 75.06 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1075 REEQESCLEKtrKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKaarqkaekarrDM 1154
Cdd:TIGR04523 31 QDTEEKQLEK--KLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK-----------DK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1155 AEELESykqELEESNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMKaQNQKKIEELNETIDQLKRQKISADK 1234
Cdd:TIGR04523 98 INKLNS---DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIK-KKEKELEKLNNKYNDLKKQKEELEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1235 AKSSAESDNENFRAELSNIASARLEAEKKRkaaeTSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNS 1314
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLELLL----SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1315 N-------LLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQ-----EKIEKEVKEVKSL 1382
Cdd:TIGR04523 250 NtqtqlnqLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1383 LAEARKKLDEENREVmeelRKKKEKELSAEKERADMAEQARDKaERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFD 1462
Cdd:TIGR04523 330 ISQNNKIISQLNEQI----SQLKKELTNSESENSEKQRELEEK-QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1463 QQLAEERNNTLLAQQERDMAHQMLRDaetkalvLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTK 1542
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIER-------LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1543 RRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFErQLASREEDEDDRKKGLTSKIRNLTEELESEQRARqa 1622
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS-SLKEKIEKLESEKKEKESKISDLEDELNKDDFEL-- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1623 aiaNKKKIESQISELTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTA 1702
Cdd:TIGR04523 555 ---KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
650 660
....*....|....*....|....*..
gi 71983975 1703 DIQAVSSSKrkaeaerDELIEEVSSLR 1729
Cdd:TIGR04523 632 IIKNIKSKK-------NKLKQEVKQIK 651
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
977-1665 |
5.07e-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: 74.67 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 977 QKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKE 1056
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1057 KQQRHNAETARRAAETQLREEQEsclektrKAEELTNQLMRKESELSQISIRNDEelaarqqLEREIREIRAQLDDAIEE 1136
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKK-------NIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1137 TNKEKAARQKAEKARRDMAEELESYKQELEESNDKTVLHSQLKAKrdeeyahlQKQLEETVKSSEEVVEEMKAQNQKKIE 1216
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ--------NNQLKDNIEKKQQEINEKTTEISNTQT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1217 ELNETIDQLKRQKISADKAKSSAESDNE---NFRAELSNIASaRLEAEKKRKAAETS------LMEKDHKMREMQSNLDD 1287
Cdd:TIGR04523 254 QLNQLKDEQNKIKKQLSEKQKELEQNNKkikELEKQLNQLKS-EISDLNNQKEQDWNkelkseLKNQEKKLEEIQNQISQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1288 LMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLavavearddald 1367
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI------------ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1368 aqekieKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQardkaERAKKKAIQEAEDVQKELTDv 1447
Cdd:TIGR04523 401 ------QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ-----DSVKELIIKNLDNTRESLET- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1448 vaATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLAS- 1526
Cdd:TIGR04523 469 --QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDe 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1527 -TKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDAlqladdarsrvevnmqamRSEFERQLASREEDEDDRKKGL--- 1602
Cdd:TIGR04523 547 lNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKK------------------QEEKQELIDQKEKEKKDLIKEIeek 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71983975 1603 TSKIRNLTEELESeqrarqaAIANKKKIESQISELTEKNEASLRQIEDLSRQLRKAQLGWKDL 1665
Cdd:TIGR04523 609 EKKISSLEKELEK-------AKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1184-1981 |
5.49e-13 |
|
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: 74.77 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1184 EEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASaRLEAEK- 1262
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH-ELEAAKc 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1263 -KRKAAETSLMEKDhKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKN--ASLDMQLSEL-TEASeedr 1338
Cdd:pfam15921 160 lKEDMLEDSNTQIE-QLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSlgSAISKILRELdTEIS---- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1339 rtraTLNNKIRQLEEDLAvAVEArddalDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADM 1418
Cdd:pfam15921 235 ----YLKGRIFPVEDQLE-ALKS-----ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1419 AEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSN 1498
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1499 ELSEK-KDIVDQLEKDKRTL------KLEIDNLASTKDDAGKNVYELEKTKRRLDEELS-RAEQQIIELE---DALQLAD 1567
Cdd:pfam15921 385 DLHKReKELSLEKEQNKRLWdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQgknESLEKVS 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1568 DARSRVEVNMQAMRSEFERQLASREEDEDDRKKgltskIRNLTEELESEQRARQAAIANKKKIESQIS-ELTEkneasLR 1646
Cdd:pfam15921 465 SLTAQLESTKEMLRKVVEELTAKKMTLESSERT-----VSDLTASLQEKERAIEATNAEITKLRSRVDlKLQE-----LQ 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1647 QIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDAlagqRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVS 1726
Cdd:pfam15921 535 HLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL----RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1727 SLRASSfsNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQ 1806
Cdd:pfam15921 611 ILKDKK--DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE 688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1807 QLQDAENtavaRLRTQINVAEAKVSSLEQQL-SLEEQD--------KMRQGRTLRRMETKMAEMQ-QMLEEEKRQGESNR 1876
Cdd:pfam15921 689 EMETTTN----KLKMQLKSAQSELEQTRNTLkSMEGSDghamkvamGMQKQITAKRGQIDALQSKiQFLEEAMTNANKEK 764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1877 QAVDRQNARIRQlrtQLEDTEAERDRLTNKLK----DERRRAEEMTDLNETLSRDVSLLKQRETTARRTpgligHRESRR 1952
Cdd:pfam15921 765 HFLKEEKNKLSQ---ELSTVATEKNKMAGELEvlrsQERRLKEKVANMEVALDKASLQFAECQDIIQRQ-----EQESVR 836
|
810 820 830
....*....|....*....|....*....|..
gi 71983975 1953 FGSNTSLARDEFRGSALTNEMSPSDR---PAS 1981
Cdd:pfam15921 837 LKLQHTLDVKELQGPGYTSNSSMKPRllqPAS 868
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1243-1925 |
9.60e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 74.22 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1243 NENFRAELSNIAsarLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESiqkaksADETLNsnlLKKNAs 1322
Cdd:PRK04863 277 HANERRVHLEEA---LELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA------ASDHLN---LVQTA- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1323 ldmqlselTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEK---IEKEVKEVKSLLAEARKKLDEENRevme 1399
Cdd:PRK04863 344 --------LRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARaeaAEEEVDELKSQLADYQQALDVQQT---- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1400 elrkkkekelsaekeRADMAEQARDKAERAK-------------KKAIQEAEDVQKELTDvvaATREMERKMR------- 1459
Cdd:PRK04863 412 ---------------RAIQYQQAVQALERAKqlcglpdltadnaEDWLEEFQAKEQEATE---ELLSLEQKLSvaqaahs 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1460 KFDQQLAEERNntLLAQQERDMAHQMLRDAETkalvlsnELSEKKDIVDQLEKDKRTLK-LEID-----NLASTKDDAGK 1533
Cdd:PRK04863 474 QFEQAYQLVRK--IAGEVSRSEAWDVARELLR-------RLREQRHLAEQLQQLRMRLSeLEQRlrqqqRAERLLAEFCK 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1534 NVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFER----------------QLASREEDEDD 1597
Cdd:PRK04863 545 RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRlaarapawlaaqdalaRLREQSGEEFE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1598 RKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLRKAQLGwkDLQLDVTEARAAME 1677
Cdd:PRK04863 625 DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVLLS--EIYDDVSLEDAPYF 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1678 DALAGQ-------RDAEKRARASE------DEIKRLTADIQAVSSSKRKAEA-ERDELIEEVS-SLRASSFSNEE---KR 1739
Cdd:PRK04863 703 SALYGParhaivvPDLSDAAEQLAgledcpEDLYLIEGDPDSFDDSVFSVEElEKAVVVKIADrQWRYSRFPEVPlfgRA 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1740 RLEAKVIDLEDQLDEEASANELAQEKVRKSQ---QQLEQMTA----------------DLAMERSVCERTESDkiaLERA 1800
Cdd:PRK04863 783 AREKRIEQLRAEREELAERYATLSFDVQKLQrlhQAFSRFIGshlavafeadpeaelrQLNRRRVELERALAD---HESQ 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1801 NRDLKQQLQDAEN--TAVARLRTQINVAE-----AKVSSLEQQLSLEEQDKM---RQGRTLRRMETKMAEMQ---QMLEE 1867
Cdd:PRK04863 860 EQQQRSQLEQAKEglSALNRLLPRLNLLAdetlaDRVEEIREQLDEAEEAKRfvqQHGNALAQLEPIVSVLQsdpEQFEQ 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1868 EKRQGESNRQAVDRQNARIR-----------------------------QLRTQLEDTEAERDRLTNKLkdeRRRAEEMT 1918
Cdd:PRK04863 940 LKQDYQQAQQTQRDAKQQAFaltevvqrrahfsyedaaemlaknsdlneKLRQRLEQAEQERTRAREQL---RQAQAQLA 1016
|
....*..
gi 71983975 1919 DLNETLS 1925
Cdd:PRK04863 1017 QYNQVLA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
860-1172 |
3.62e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 860 KDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSK 939
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 940 RLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERsrqkllleknsiesRLKELEAQGLELEDSGNKLSKEKKALEERCE 1019
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATER--------------RLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1020 DLSSRLideversKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKE 1099
Cdd:TIGR02168 870 ELESEL-------EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1100 SELSQISIRNDEELAA--------RQQLEREIREIRAQLD-------DAIEETNKEKAARQKAEKARRDMAEELESYKQE 1164
Cdd:TIGR02168 943 ERLSEEYSLTLEEAEAlenkieddEEEARRRLKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
....*...
gi 71983975 1165 LEESNDKT 1172
Cdd:TIGR02168 1023 IEEIDREA 1030
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1080-1892 |
3.74e-12 |
|
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: 72.07 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1080 SCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELE 1159
Cdd:pfam15921 37 TIIENTSSTGTFTQIPIFPKYEVELDSPRKIIAYPGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1160 SYKQELEESNDKTVlhsQLKAKRDEEYAHLQKQLEETVKSseevVEEMKAQNQKKIEELNETIDQLKRQKISadkakssa 1239
Cdd:pfam15921 117 TKLQEMQMERDAMA---DIRRRESQSQEDLRNQLQNTVHE----LEAAKCLKEDMLEDSNTQIEQLRKMMLS-------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1240 esdNENFRAELSNIASARLEAEKKRKAAETSLMEKDHK---------MREMQSNLDDLMAKLSKMNNELESIqkaKSADE 1310
Cdd:pfam15921 182 ---HEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRslgsaiskiLRELDTEISYLKGRIFPVEDQLEAL---KSESQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1311 TLNSNLLKKNASLDMQL-----SELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAE 1385
Cdd:pfam15921 256 NKIELLLQQHQDRIEQLiseheVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELRE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1386 ARKKLDEENREVMEELRKKKEKELSAEKERADMAeqardkaerakkkaiQEAEDVQKELTDVVAATREMERKMrkfdqQL 1465
Cdd:pfam15921 336 AKRMYEDKIEELEKQLVLANSELTEARTERDQFS---------------QESGNLDDQLQKLLADLHKREKEL-----SL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1466 AEERNNTLLaqqERDMAHQMLRDAetkalvLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDA--GKNvYELEKTKR 1543
Cdd:pfam15921 396 EKEQNKRLW---DRDTGNSITIDH------LRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAiqGKN-ESLEKVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1544 RLDEELSRAE--QQIIELEDALQLADDARSRVEVNMQAMRSEFERQLASREEDEDDRKKGLTSKIRNLtEELESEQRARQ 1621
Cdd:pfam15921 466 LTAQLESTKEmlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL-QHLKNEGDHLR 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1622 AAIANKKKIESQISELTEKNEASLRQIEDLSR------------QLRKAQLGWK--DLQLDVTEARAAMEDALAGQRDAE 1687
Cdd:pfam15921 545 NVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamQVEKAQLEKEinDRRLELQEFKILKDKKDAKIRELE 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1688 KRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRASSFSNEE-----KRRLEAKVIDLEDQLDEEASANELA 1762
Cdd:pfam15921 625 ARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyevlKRNFRNKSEEMETTTNKLKMQLKSA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1763 QEKVRKSQQQLEQMTADLAMERSVCERTESdKIALERANRD-LKQQLQDAENTAVARLRTQINVAEAKvSSLEQQLSLEE 1841
Cdd:pfam15921 705 QSELEQTRNTLKSMEGSDGHAMKVAMGMQK-QITAKRGQIDaLQSKIQFLEEAMTNANKEKHFLKEEK-NKLSQELSTVA 782
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1842 QDKMRQGRTL-------RRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQ 1892
Cdd:pfam15921 783 TEKNKMAGELevlrsqeRRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
846-1598 |
7.31e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 846 RLLTKVKPLLEVTNKDELIAER---EQELKVTAEKLRrsEVF--ISDYKQQMEKMDEERLVLkTRLDAESSERAEIFEER 920
Cdd:COG4913 195 RLLHKTQSFKPIGDLDDFVREYmleEPDTFEAADALV--EHFddLERAHEALEDAREQIELL-EPIRELAERYAAARERL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 921 SRMAARRDELEgiLEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIE-SRLKELEAQGLE 999
Cdd:COG4913 272 AELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1000 LEDSGNKLSKEKKALEERCEDLSSRLIDEverskqlvkaKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQE 1079
Cdd:COG4913 350 LERELEERERRRARLEALLAALGLPLPAS----------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1080 sclEKTRKAEELtNQLMRKESELSQisirndEELAARQQLEREIREIRAQLD----------------DAIE-------- 1135
Cdd:COG4913 420 ---ELRELEAEI-ASLERRKSNIPA------RLLALRDALAEALGLDEAELPfvgelievrpeeerwrGAIErvlggfal 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1136 ----ETNKEKAARQKAEkaRRDMAEELESYKQELEESNDKTV------LHSQLKAKRDEEYAHLQKQLEET-----VKSS 1200
Cdd:COG4913 490 tllvPPEHYAAALRWVN--RLHLRGRLVYERVRTGLPDPERPrldpdsLAGKLDFKPHPFRAWLEAELGRRfdyvcVDSP 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1201 EEVVEEMKA------------------------------QNQKKIEELNETIDQLKR--QKISADKAKSSAESDNENFRA 1248
Cdd:COG4913 568 EELRRHPRAitragqvkgngtrhekddrrrirsryvlgfDNRAKLAALEAELAELEEelAEAEERLEALEAELDALQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1249 ELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAklskmnnelesiqkaksadetlnsnllkknasLDMQLS 1328
Cdd:COG4913 648 EALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAA--------------------------------LEEQLE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1329 ELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKlDEENREVMEELRKKKEKE 1408
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA-AALGDAVERELRENLEER 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1409 LSAEKERadmAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREmerkmrkFDQQLAEERNNTLLAQQERdmahqmlrd 1488
Cdd:COG4913 775 IDALRAR---LNRAEEELERAMRAFNREWPAETADLDADLESLPE-------YLALLDRLEEDGLPEYEER--------- 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1489 aeTKALVLSNELSEKKDIVDQLEKDKRTLKLEIDN----LASTKDDAGKnVYELEkTKRRLDEELSRAEQQIIELEDALQ 1564
Cdd:COG4913 836 --FKELLNENSIEFVADLLSKLRRAIREIKERIDPlndsLKRIPFGPGR-YLRLE-ARPRPDPEVREFRQELRAVTSGAS 911
|
810 820 830
....*....|....*....|....*....|....
gi 71983975 1565 LADDARSrvEVNMQAMRSEFERqLASREEDEDDR 1598
Cdd:COG4913 912 LFDEELS--EARFAALKRLIER-LRSEEEESDRR 942
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
927-1554 |
9.01e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 9.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 927 RDELEGILEEVSKRLEIEEQKAKKA-----DSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELE 1001
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHErlnglESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1002 DSGNKLS---KEKKALEERCEDLSSRLIDEVERSKQLVkAKARLEA----TVAEINDELEKEKQQRHNAETARRAAETQL 1074
Cdd:PRK02224 262 DLRETIAeteREREELAEEVRDLRERLEELEEERDDLL-AEAGLDDadaeAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1075 REEQESCLEKTRKAEELTNQLMRKESELsqisirnDEELaarQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARrdm 1154
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAEL-------ESEL---EEAREAVEDRREEIEELEEEIEELRERFGDAPVDL--- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1155 aEELESYKQELEESNDKtvLHSQLkakrdeeyahlqKQLEETVKSSEEVVEEmkaqnqkkieelnetidqlKRQKISADK 1234
Cdd:PRK02224 408 -GNAEDFLEELREERDE--LRERE------------AELEATLRTARERVEE-------------------AEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1235 AKSSAESDNENFRAElsniasarleaekkrkaaetSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNS 1314
Cdd:PRK02224 454 CPECGQPVEGSPHVE--------------------TIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIER 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1315 nLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDlavAVEARDDALDAQEKIEKEVKEVKSLlaEARKKLDEEN 1394
Cdd:PRK02224 514 -LEERREDLEELIAERRETIEEKRERAEELRERAAELEAE---AEEKREAAAEAEEEAEEAREEVAEL--NSKLAELKER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1395 REVMEELRkkkekelsaekERADMAEQARDKAE--RAKKKAIQEAEDVQKEltdvvaatREMERKMRKfdQQLAEERNNT 1472
Cdd:PRK02224 588 IESLERIR-----------TLLAAIADAEDEIErlREKREALAELNDERRE--------RLAEKRERK--RELEAEFDEA 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1473 LL--AQQERDMAHQMLRDAETKalvlsneLSEKKDIVDQLEKDKRTLKLEIDNLASTKDDagknVYELEKTKRRLDEELS 1550
Cdd:PRK02224 647 RIeeAREDKERAEEYLEQVEEK-------LDELREERDDLQAEIGAVENELEELEELRER----REALENRVEALEALYD 715
|
....
gi 71983975 1551 RAEQ 1554
Cdd:PRK02224 716 EAEE 719
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1625-1940 |
1.96e-11 |
|
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: 69.70 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1625 ANKKKIESQIsELTEKNeasLRQIEDLSRQLRKAqlgWKDLQLdvtEARAAmedalagQRDAEKRARASEDEIKRLTADI 1704
Cdd:TIGR02168 172 ERRKETERKL-ERTREN---LDRLEDILNELERQ---LKSLER---QAEKA-------ERYKELKAELRELELALLVLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1705 QAVSSSKRKAEAERDELIEEVSSLRAssfsneEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLAMER 1784
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTA------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1785 SVCERTESDKIALERANRDLKQQLQDAEnTAVARLRTQINVAEAKVSSLEQQLSLEEQDkmrqgrtLRRMETKMAEMQQM 1864
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELA-EELAELEEKLEELKEELESLEAELEELEAE-------LEELESRLEELEEQ 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1865 LEEEKRQGESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKLKDERRRAEEmTDLNETLSRDVSLLKQRETTARR 1940
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE-AELKELQAELEELEEELEELQEE 455
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
857-1890 |
5.26e-11 |
|
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: 68.54 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 857 VTNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTrLDAESSERAEIFEERSRMAARRDELEGILE- 935
Cdd:TIGR01612 553 AKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINK-LKLELKEKIKNISDKNEYIKKAIDLKKIIEn 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 936 --------------EVSKRLEIEEQKAKKADSESRKL---------TEMVRHLEENLEDEERSRQKLLLEKNSIE---SR 989
Cdd:TIGR01612 632 nnayidelakispyQVPEHLKNKDKIYSTIKSELSKIyeddidalyNELSSIVKENAIDNTEDKAKLDDLKSKIDkeyDK 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 990 LKELEAQGLEL-----EDSGNKLSK-----EKKALEERCEDLSSRLIDEVERSKQLvkakARLEATVAEINDELEKEKQq 1059
Cdd:TIGR01612 712 IQNMETATVELhlsniENKKNELLDiiveiKKHIHGEINKDLNKILEDFKNKEKEL----SNKINDYAKEKDELNKYKS- 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1060 rhnaetarRAAETQLREEQESCLEKTRKAEELTNQLMRKESeLSQISIRNDEelaarqqLEREIREIRAQLDDAIEETNK 1139
Cdd:TIGR01612 787 --------KISEIKNHYNDQINIDNIKDEDAKQNYDKSKEY-IKTISIKEDE-------IFKIINEMKFMKDDFLNKVDK 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1140 ----EKAARQKAEKARRDMAEELESYKQELEES---------NDKTVLHSQLKAKRDEEYAHLQ--KQLEETVK---SSE 1201
Cdd:TIGR01612 851 finfENNCKEKIDSEHEQFAELTNKIKAEISDDklndyekkfNDSKSLINEINKSIEEEYQNINtlKKVDEYIKiceNTK 930
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1202 EVVEEMKAQNQKKIEELNETIDQLKR-----------------------QKISADKAKSSAESDN-------ENFRAELS 1251
Cdd:TIGR01612 931 ESIEKFHNKQNILKEILNKNIDTIKEsnlieksykdkfdntlidkinelDKAFKDASLNDYEAKNnelikyfNDLKANLG 1010
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1252 NIASARLEAEKKRKAAETSLMEKdhKMREMQSNLDDL-MAKLSKMNNELESIQKAKSAD-ETLNSNLLKK---------- 1319
Cdd:TIGR01612 1011 KNKENMLYHQFDEKEKATNDIEQ--KIEDANKNIPNIeIAIHTSIYNIIDEIEKEIGKNiELLNKEILEEaeinitnfne 1088
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1320 -----------------------------------NASLDMQLSELTEASEEDRRTRATLNNKIRQLeEDLAVAVEARDD 1364
Cdd:TIGR01612 1089 ikeklkhynfddfgkeenikyadeinkikddiknlDQKIDHHIKALEEIKKKSENYIDEIKAQINDL-EDVADKAISNDD 1167
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1365 ALDAQEKIEKEVKEVksllaEARKKLDEENREVMEELRKKKEKELSAEKERA-------DMAEQARDKAERAKKKA---I 1434
Cdd:TIGR01612 1168 PEEIEKKIENIVTKI-----DKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGinlsygkNLGKLFLEKIDEEKKKSehmI 1242
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1435 QEAEDVQKELTDVVAATREMERKMRKFDQQLAEErnNTLLAQQERDMAHQM--------LRDAETKALVLSNELSEKKDI 1506
Cdd:TIGR01612 1243 KAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEM--ETFNISHDDDKDHHIiskkhdenISDIREKSLKIIEDFSEESDI 1320
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1507 VDQlekdKRTLK--------------------------LEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELE 1560
Cdd:TIGR01612 1321 NDI----KKELQknlldaqkhnsdinlylneianiyniLKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIK 1396
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1561 DalqladdarsrvEVNMQAMRSEFERQLASREEDeddrkkGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEK 1640
Cdd:TIGR01612 1397 D------------DINLEECKSKIESTLDDKDID------ECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKN 1458
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1641 NEASLRQIEDLSRQlrKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEiKRLTadiqavssskRKAEAERDE 1720
Cdd:TIGR01612 1459 IEMADNKSQHILKI--KKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKN-KELF----------EQYKKDVTE 1525
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1721 LIEEVSSLRASSFSNEEKRRLEA---KVIDLEDQLDEEASANELAQEKVRKSQqqleqmtadLAMERSVCERTESDKIAL 1797
Cdd:TIGR01612 1526 LLNKYSALAIKNKFAKTKKDSEIiikEIKDAHKKFILEAEKSEQKIKEIKKEK---------FRIEDDAAKNDKSNKAAI 1596
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1798 eranrDLKQQLQDAENT--AVARLRTQINVAEAKVSSLEQQLSLEEQDKmrQGRTLRRMETKMAEMQQMLE---EEKRQG 1872
Cdd:TIGR01612 1597 -----DIQLSLENFENKflKISDIKKKINDCLKETESIEKKISSFSIDS--QDTELKENGDNLNSLQEFLEslkDQKKNI 1669
|
1210
....*....|....*...
gi 71983975 1873 ESNRQAVDRQNARIRQLR 1890
Cdd:TIGR01612 1670 EDKKKELDELDSEIEKIE 1687
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
967-1684 |
5.68e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.82 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 967 ENLEDEERSRQKLLLEKNSIESRLKELEAqglELEDSGNKLSKEKKALEERcedlsSRLIDEVERSKQlvKAKARLEATV 1046
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEA---ELKQKENKLQENRKIIEAQ-----RKAIQELQFENE--KVSLKLEEEI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1047 AEINDELEKEKQQRHNA----ETARRAAETQLREEQESclEKTRKAE-ELTNQLMRKESELSQISIRNDEelaARQQLER 1121
Cdd:pfam05483 141 QENKDLIKENNATRHLCnllkETCARSAEKTKKYEYER--EETRQVYmDLNNNIEKMILAFEELRVQAEN---ARLEMHF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1122 EIREIRAQLDDAIEETNKEKAARQK-----------AEKARRDMAEELESYKQELEESNDKTVLHSQLKAKRDEEYAHLQ 1190
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKqvsllliqiteKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1191 KQLEETVKSSEEVVEEMKAQnQKKIEELNETIDQLKRQKIS----ADKAKSSAESDNENFRAELSNIASARLEAEKKRKA 1266
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKAL-EEDLQIATKTICQLTEEKEAqmeeLNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1267 AETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLnsnlLKKNASLDMQLSELTEASEEDRRTRATLNN 1346
Cdd:pfam05483 375 NEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKL----LDEKKQFEKIAEELKGKEQELIFLLQAREK 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1347 KIRQLEEDLAVAVEArddaldaQEKIEKEVKEVKSLLAEARKKldeeNREVMEELRKKKEKELSAEKERADMAEQARDKA 1426
Cdd:pfam05483 451 EIHDLEIQLTAIKTS-------EEHYLKEVEDLKTELEKEKLK----NIELTAHCDKLLLENKELTQEASDMTLELKKHQ 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1427 ERAKKKAIQEAEDVQKeltdvVAATREMERKMRKFDQQLAEErnntllAQQERDMAHQMLRDAETKALVLSNELSEKKDI 1506
Cdd:pfam05483 520 EDIINCKKQEERMLKQ-----IENLEEKEMNLRDELESVREE------FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQ 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1507 VDQLEKDKRTLKLEIDNlastkddAGKNVYELEKTKRRLDEELSRAEQQIIELEDALqladdarSRVEVNMQAMRSEFER 1586
Cdd:pfam05483 589 MKILENKCNNLKKQIEN-------KNKNIEELHQENKALKKKGSAENKQLNAYEIKV-------NKLELELASAKQKFEE 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1587 QLASREEDEDDRKkgltSKIRNLTEELESEQRARQAAIANKKKI----ESQISELTEKNEASLRQIEDLSRQlRKAQLG- 1661
Cdd:pfam05483 655 IIDNYQKEIEDKK----ISEEKLLEEVEKAKAIADEAVKLQKEIdkrcQHKIAEMVALMEKHKHQYDKIIEE-RDSELGl 729
|
730 740
....*....|....*....|...
gi 71983975 1662 WKDLQLDVTEARAAMEDALAGQR 1684
Cdd:pfam05483 730 YKNKEQEQSSAKAALEIELSNIK 752
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1206-1423 |
8.42e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.94 E-value: 8.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1206 EMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNL 1285
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1286 DDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEED----RRTRATLNNKIRQLEEDLAVAVEA 1361
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQaeelRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1362 RDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQAR 1423
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1413-1936 |
9.35e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 9.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1413 KERADMAEQARDKAERAKKKAIQEAED--VQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAE 1490
Cdd:PRK02224 168 RERASDARLGVERVLSDQRGSLDQLKAqiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1491 tkalvlsnelsEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELS--------------RAEQQI 1556
Cdd:PRK02224 248 -----------ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDdllaeaglddadaeAVEARR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1557 IELEDALQLADDARSRVEVNMQAMRSEFERqLASREEDEDDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISE 1636
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAES-LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1637 LTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDAlagqRDAEKRARASEDEIKRLTADiQAVSSS------ 1710
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA----RERVEEAEALLEAGKCPECG-QPVEGSphveti 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1711 ------KRKAEAERDELIEEVSSL-----RASSFSNEEKR--RLEAKVIDLEDQLDE---EASANELAQEKVRKSQQQLE 1774
Cdd:PRK02224 471 eedrerVEELEAELEDLEEEVEEVeerleRAEDLVEAEDRieRLEERREDLEELIAErreTIEEKRERAEELRERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1775 QmTADLAMERSVCERTESDKIALERANRDLKQQLQDAENTAVARLRTQ---INVAEAKVSSLEQQLS-LEEQDKMRQGRT 1850
Cdd:PRK02224 551 A-EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLlaaIADAEDEIERLREKREaLAELNDERRERL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1851 LRRMETKmAEMQQMLEEEKRqgESNRQAVDRQNARIRQLRTQLEDTEAERDRL-------TNKLKDERRRAEEMTDLNET 1923
Cdd:PRK02224 630 AEKRERK-RELEAEFDEARI--EEAREDKERAEEYLEQVEEKLDELREERDDLqaeigavENELEELEELRERREALENR 706
|
570
....*....|...
gi 71983975 1924 LSRDVSLLKQRET 1936
Cdd:PRK02224 707 VEALEALYDEAEE 719
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1009-1636 |
9.89e-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: 67.30 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1009 KEKKALEERCEDLSSRL----IDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQEsCLEK 1084
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL-LKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1085 TRKAEELTNQL-----MRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELE 1159
Cdd:TIGR00618 266 RARIEELRAQEavleeTQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1160 SYKQELEESNDKTVLHSQLKAKRDeeyaHLQKQLEETvksseevvEEMKAQNQKKiEELNETIDQLKRQKISADKAKSSA 1239
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHEVATSIRE----ISCQQHTLT--------QHIHTLQQQK-TTLTQKLQSLCKELDILQREQATI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1240 ESDNENFRAELSNIASARLEAEKKRKAAE----------TSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSAD 1309
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKKQQELQQRYAElcaaaitctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1310 ETLNSNLLKKNASLDMQLSELTEA------SEEDRRTRATLNNKIRQLEEDLAvAVEARDDALDAQEKIEKEVKEVKSLL 1383
Cdd:TIGR00618 493 LARLLELQEEPCPLCGSCIHPNPArqdidnPGPLTRRMQRGEQTYAQLETSEE-DVYHQLTSERKQRASLKEQMQEIQQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1384 AEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQ 1463
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1464 QLaeernnTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLkleidnlaSTKDDAGKNVYELEKTKR 1543
Cdd:TIGR00618 652 QL------TLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML--------AQCQTLLRELETHIEEYD 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1544 RLDEELSRAEQQIIEledALQLADDARSRVevnMQAMRSEFERQLASREEDEDDRKKGLTSKIRNLTE------ELESEQ 1617
Cdd:TIGR00618 718 REFNEIENASSSLGS---DLAAREDALNQS---LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAElshlaaEIQFFN 791
|
650
....*....|....*....
gi 71983975 1618 RARQAAIANKKKIESQISE 1636
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQ 810
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
856-1446 |
1.60e-10 |
|
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: 66.79 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 856 EVTNKDELIAEREQELKVTAEKLRrsEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEI--------------FEERS 921
Cdd:pfam12128 266 GYKSDETLIASRQEERQETSAELN--QLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELealedqhgafldadIETAA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 922 RMAARRDELEGILEEVSKRLEIEEQKAKKADSESRKL-----TEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQ 996
Cdd:pfam12128 344 ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRrskikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 997 -GLELEDSGNKLSKEKKALEERCEDLSSRLiDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAET--- 1072
Cdd:pfam12128 424 lREQLEAGKLEFNEEEYRLKSRLGELKLRL-NQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKrrd 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1073 ----QLREEQESCLEKTRKAEELTNQL----------MRKESELSQISI----------RND------------------ 1110
Cdd:pfam12128 503 qaseALRQASRRLEERQSALDELELQLfpqagtllhfLRKEAPDWEQSIgkvispellhRTDldpevwdgsvggelnlyg 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1111 -----------EELAARQQLEREIREIRAQLDDA---IEETNKEKA-ARQKAEKARRDMAEELESYKQELEESNDKTVLH 1175
Cdd:pfam12128 583 vkldlkridvpEWAASEEELRERLDKAEEALQSArekQAAAEEQLVqANGELEKASREETFARTALKNARLDLRRLFDEK 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1176 SQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNEnfraelsNIAS 1255
Cdd:pfam12128 663 QSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQL-------ALLK 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1256 ARLEAEKKRKAAETSLMEKDHKmREMQS------NLDDLMAKLSKMNNELESI----QKAKSADETLNSNLLKKNASLDM 1325
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWYK-RDLASlgvdpdVIAKLKREIRTLERKIERIavrrQEVLRYFDWYQETWLQRRPRLAT 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1326 QLSELTEASEEdrrTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAE-ARKKLDEENREVmeelrkk 1404
Cdd:pfam12128 815 QLSNIERAISE---LQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKlATLKEDANSEQA------- 884
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 71983975 1405 kekeLSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTD 1446
Cdd:pfam12128 885 ----QGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAD 922
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
861-1381 |
1.69e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 66.68 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 861 DELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEE-----RLVLKTRLDAESSeraeIFEERSRMAARRDELEGILE 935
Cdd:pfam15921 270 EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQarnqnSMYMRQLSDLEST----VSQLRSELREAKRMYEDKIE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 936 EVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLedeersrQKLL--LEKNSIESRLKELEAQGLELEDSGNKLSKE--K 1011
Cdd:pfam15921 346 ELEKQLVLANSELTEARTERDQFSQESGNLDDQL-------QKLLadLHKREKELSLEKEQNKRLWDRDTGNSITIDhlR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1012 KALEERCEdlssrlidEVERSKQLVKA-----KARLEATVAEI---NDELEK----EKQQRHNAETARRAAEtQLREEQE 1079
Cdd:pfam15921 419 RELDDRNM--------EVQRLEALLKAmksecQGQMERQMAAIqgkNESLEKvsslTAQLESTKEMLRKVVE-ELTAKKM 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1080 SCLEKTRKAEELTNQLMRKE-------SELSQISIRNDEELAARQQLEREIREIRaqlddaieetnkekAARQKAEKARR 1152
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKEraieatnAEITKLRSRVDLKLQELQHLKNEGDHLR--------------NVQTECEALKL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1153 DMAEE---LESYKQELEESNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEvVEEMKAQNQKKIEELNETIDQLKRQK 1229
Cdd:pfam15921 556 QMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE-FKILKDKKDAKIRELEARVSDLELEK 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1230 ISADKAKSS---AESDNENFRAELSN-IASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKA 1305
Cdd:pfam15921 635 VKLVNAGSErlrAVKDIKQERDQLLNeVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNT 714
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1306 KSADETLNSNLLKKNASLDMQLSelteaseEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKS 1381
Cdd:pfam15921 715 LKSMEGSDGHAMKVAMGMQKQIT-------AKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVAT 783
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
856-1298 |
1.84e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 856 EVTNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEG--- 932
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEErae 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 933 ILEEVSKRLEIEEQKAKKA-----------DSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQ----- 996
Cdd:PRK02224 360 ELREEAAELESELEEAREAvedrreeieelEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATlrtar 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 997 ------------------GLELEDSGNKLSKEKKalEERCEDLSSRLIDEVERSKQLVKAKARLEATVaEINDELEKEKQ 1058
Cdd:PRK02224 440 erveeaealleagkcpecGQPVEGSPHVETIEED--RERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEE 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1059 QRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREireiRAQLDDAIEETN 1138
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK----LAELKERIESLE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1139 KEKAARQKAEKARRDmAEELESYKQELEESNDKTvlHSQLKAKRDEeyahlQKQLEETVksSEEVVEEMKAQNQ---KKI 1215
Cdd:PRK02224 593 RIRTLLAAIADAEDE-IERLREKREALAELNDER--RERLAEKRER-----KRELEAEF--DEARIEEAREDKEraeEYL 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1216 EELNETIDQLKRQKISADKAKSSAESDNENfRAELSNiasaRLEAEKKRKAAETSLMEkdhKMREMQSNLDDLMAKLSKM 1295
Cdd:PRK02224 663 EQVEEKLDELREERDDLQAEIGAVENELEE-LEELRE----RREALENRVEALEALYD---EAEELESMYGDLRAELRQR 734
|
...
gi 71983975 1296 NNE 1298
Cdd:PRK02224 735 NVE 737
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
885-1241 |
2.17e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.92 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 885 ISDYKQQ--MEKMDEERLvlktrldaesseRAEIfEERSRMAARRDELEGilEEVSKRLEIEEQKAKKADSEsRKLTEMV 962
Cdd:pfam17380 284 VSERQQQekFEKMEQERL------------RQEK-EEKAREVERRRKLEE--AEKARQAEMDRQAAIYAEQE-RMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 963 RHLEE-NLEDEERSRQKLLLEKNSIE-SRLKELEAQGLELEDSGNKLSKEKKALEERcedlssrLIDEVERSKQLVKAKA 1040
Cdd:pfam17380 348 RELERiRQEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKV-------KILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1041 RLEatvaeindelekekQQRHNAETARRAAETQLREEQESCLEKTRKaeeltnqlmrkeselsqisirndEELAARQQLE 1120
Cdd:pfam17380 421 EME--------------QIRAEQEEARQREVRRLEEERAREMERVRL-----------------------EEQERQQQVE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1121 ReIREIRAQLDDAIEETNKEKAARQKAEKARRDMAE-ELESYKQE-LEESNDKTVLHSQLKAKRDEEYAHLQKQLEETVK 1198
Cdd:pfam17380 464 R-LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEkELEERKQAmIEEERKRKLLEKEMEERQKAIYEEERRREAEEER 542
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 71983975 1199 SSEEVVEE--------MKAQNQKKIEELNETIDQLKRQKISADKAKSSAES 1241
Cdd:pfam17380 543 RKQQEMEErrriqeqmRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1062-1912 |
3.14e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 65.74 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1062 NAETARRAAETQLREEQESCLEKTRKAEELTnqlmrkeselsqisirndeelAARQQLEREireiraqLDDAIEETNKEK 1141
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELS---------------------ARESDLEQD-------YQAASDHLNLVQ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1142 AARQKAEKarrdmaeeLESYKQELEESNDKTVLHSQLKAKRDEEYAHLQKQLEETvkssEEVVEEMKAQnqkkIEELNET 1221
Cdd:COG3096 341 TALRQQEK--------IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAA----EEEVDSLKSQ----LADYQQA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1222 IDQLKRQKIS---ADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQ---SNLDDLMAKLSKM 1295
Cdd:COG3096 405 LDVQQTRAIQyqqAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKI 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1296 NNELESIQKAKSADETLN-----SNLLKKNASLDMQLSELTEASEEDRRTRATLNnkirQLEEDLAVAVEARDDALDAQE 1370
Cdd:COG3096 485 AGEVERSQAWQTARELLRryrsqQALAQRLQQLRAQLAELEQRLRQQQNAERLLE----EFCQRIGQQLDAAEELEELLA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1371 KIEKEVKEVKSLLAEARkkldeENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQkELTDVVAA 1450
Cdd:COG3096 561 ELEAQLEELEEQAAEAV-----EQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQ-EVTAAMQQ 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1451 TREMERKMRKFDQQLAEERNNtlLAQQERDMAH-------QMLRDAETKALVLSNELSEKKDI----------------- 1506
Cdd:COG3096 635 LLEREREATVERDELAARKQA--LESQIERLSQpggaedpRLLALAERLGGVLLSEIYDDVTLedapyfsalygparhai 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1507 -VDQLEKDKRTLkleiDNLASTKDDagknVYELEKTKRRLDEELSRAEqqiiELEDALQladdarsrVEVNMQAMRSE-- 1583
Cdd:COG3096 713 vVPDLSAVKEQL----AGLEDCPED----LYLIEGDPDSFDDSVFDAE----ELEDAVV--------VKLSDRQWRYSrf 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1584 -----FERqlASREEdeddrkkgltsKIRNLTEELESEQRARQAAIANKKKIEsqiseltekneaslRQIEDLSRQLRKA 1658
Cdd:COG3096 773 pevplFGR--AAREK-----------RLEELRAERDELAEQYAKASFDVQKLQ--------------RLHQAFSQFVGGH 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1659 QLGWKD------LQLdVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSS-----KRKAEAERDELIEEVSS 1727
Cdd:COG3096 826 LAVAFApdpeaeLAA-LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQanllaDETLADRLEELREELDA 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1728 LR-ASSFSNEEKRRLEAkvidLEDQLD----EEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTE---SDKIALER 1799
Cdd:COG3096 905 AQeAQAFIQQHGKALAQ----LEPLVAvlqsDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyEDAVGLLG 980
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1800 ANRD----LKQQLQDAEnTAVARLRTQINVAEAKVSSLEQQL-SLEEQDKMRQgRTLRRMETKMAEMQQMLE---EEKRQ 1871
Cdd:COG3096 981 ENSDlnekLRARLEQAE-EARREAREQLRQAQAQYSQYNQVLaSLKSSRDAKQ-QTLQELEQELEELGVQADaeaEERAR 1058
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 71983975 1872 GESNR--QAVDRQNARIRQLRTQLEDTEAERDRLTNKLKDERR 1912
Cdd:COG3096 1059 IRRDElhEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAER 1101
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1122-1935 |
3.15e-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: 65.84 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1122 EIREIRAQLDDAIEETNKEKAaRQKAEKARRDMAEELESYKQELEESNDKTVLHSQLKAKRDEEYAHLQKQlEETVKSSE 1201
Cdd:TIGR00606 167 EGKALKQKFDEIFSATRYIKA-LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS-REIVKSYE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1202 EVVEEMKaQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRaelsniasarLEAEKKRKAAETSLMEKDH----K 1277
Cdd:TIGR00606 245 NELDPLK-NRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELE----------LKMEKVFQGTDEQLNDLYHnhqrT 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1278 MREMQSNLDDLMAKLSKMNNELESIQKAKSA----------------DETLNSNLLKKNASLDMQLSELTEASEEDRRTR 1341
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRLLNQEKTEllveqgrlqlqadrhqEHIRARDSLIQSLATRLELDGFERGPFSERQIK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1342 ATLNNKIRQLEEDLAVAVEARDD-------ALDAQEKIEKEVKEVKSLLAEARKKLDEENREVmeELRKKKEKELSAEKE 1414
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADlqskerlKQEQADEIRDEKKGLGRTIELKKEILEKKQEEL--KFVIKELQQLEGSSD 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1415 RADMAEQARDKAERAKKKAIQEA--EDVQKELTDVVAATREMERKMRKFDQQLAE------ERNNTLLAQQERDMAHQML 1486
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnhhttTRTQMEMLTKDKMDKDEQI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1487 RDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALqla 1566
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL--- 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1567 ddarsrvevnmqamrseFErqlASREEDEDdrkkgltSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLR 1646
Cdd:TIGR00606 629 -----------------FD---VCGSQDEE-------SDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCP 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1647 QIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRarasEDEIKRLTADIQAVSSSKRKAEAERDELIEEVS 1726
Cdd:TIGR00606 682 VCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKR----RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1727 SLRASSFSNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLAmersvcerTESDKIALERANRDLKQ 1806
Cdd:TIGR00606 758 RDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQA--------AKLQGSDLDRTVQQVNQ 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1807 QLQDAENtavaRLRTQINVAE--AKVSSLEQQLSLEEQDKMRQGRTLR-RMETKMAEMQQM---LEEEKRQGESNRQAVD 1880
Cdd:TIGR00606 830 EKQEKQH----ELDTVVSKIElnRKLIQDQQEQIQHLKSKTNELKSEKlQIGTNLQRRQQFeeqLVELSTEVQSLIREIK 905
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1881 RQNARIRQLRTQLEDTEAERDRLTNKLKDERRRAE-EMTDLNETLSRDVSLLKQRE 1935
Cdd:TIGR00606 906 DAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIE 961
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
856-1279 |
4.19e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 856 EVTNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERlVLKTRLDAESSERA------------EIFEERSRM 923
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE-RLKKRLTGLTPEKLekeleelekakeEIEEEISKI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 924 AARRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEmvRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDS 1003
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE--EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1004 GNKLSK---------EKKALEERCEDLSSRLIDEVERSKQLVKAKAR-LEATVAEINDELEKEKQqrhnAETARRAAETQ 1073
Cdd:PRK03918 489 LKKESEliklkelaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIkLKGEIKSLKKELEKLEE----LKKKLAELEKK 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1074 LREEQESCLEKTRKAEEL----TNQLMRKESELSQISIRNDEELAARQQLEREIREI---RAQLDDAIEETNKEKAarqK 1146
Cdd:PRK03918 565 LDELEEELAELLKELEELgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKELkklEEELDKAFEELAETEK---R 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1147 AEKARRDMAEELESY-KQELEESNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAQNQKK--IEELNETID 1223
Cdd:PRK03918 642 LEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKkeLEKLEKALE 721
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1224 QLKRQKISADKAKSSAEsdnENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMR 1279
Cdd:PRK03918 722 RVEELREKVKKYKALLK---ERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1326-1926 |
6.96e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1326 QLSELTEASEEDRRTRATLNnKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKK 1405
Cdd:COG4913 236 DLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1406 EKELSAEKERADMAEQARDKAERAKKKAIQ-EAEDVQKELTDVVAATREMERKMRKFDQQLAEERNnTLLAQQERdmAHQ 1484
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLErEIERLERELEERERRRARLEALLAALGLPLPASAE-EFAALRAE--AAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1485 MLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLAStkddaGKNVY--ELEKTKRRLDEELSRAEQ-------- 1554
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER-----RKSNIpaRLLALRDALAEALGLDEAelpfvgel 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1555 -QIIELEDALQLA-------------------DDARSRVEVNMQAMRSEFER--QLASREEDEDDRKKGLTSKI------ 1606
Cdd:COG4913 467 iEVRPEEERWRGAiervlggfaltllvppehyAAALRWVNRLHLRGRLVYERvrTGLPDPERPRLDPDSLAGKLdfkphp 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1607 -----RNL------------TEELESEQRA-----------------RQAAIA--------NKKKI---ESQISELTEKN 1641
Cdd:COG4913 547 frawlEAElgrrfdyvcvdsPEELRRHPRAitragqvkgngtrhekdDRRRIRsryvlgfdNRAKLaalEAELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1642 EASLRQIEDLSRQLRKAQlgwkdlqldvteARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSK---RKAEAER 1718
Cdd:COG4913 627 AEAEERLEALEAELDALQ------------ERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1719 DELIEEVSSLRassfsnEEKRRLEAKVIDLEDQLDEeasanelAQEKVRKSQQQLEQMTADLAMErsvcertesdkiALE 1798
Cdd:COG4913 695 EELEAELEELE------EELDELKGEIGRLEKELEQ-------AEEELDELQDRLEAAEDLARLE------------LRA 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1799 RANRDLKQQLQDA-ENTAVARLRTQINVAEAKVSSLEQQLsleeQDKMRQGRTLRRMETK--------MAEMQQMLEEEK 1869
Cdd:COG4913 750 LLEERFAAALGDAvERELRENLEERIDALRARLNRAEEEL----ERAMRAFNREWPAETAdldadlesLPEYLALLDRLE 825
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1870 RQGesnrqaVDRQNARIRQLRTqlEDTEAERDRLTNKLKDERRRAEE-MTDLNETLSR 1926
Cdd:COG4913 826 EDG------LPEYEERFKELLN--ENSIEFVADLLSKLRRAIREIKErIDPLNDSLKR 875
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
904-1395 |
7.51e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 904 TRLDAESSERAEIFEERSRMAARRDELEgileEVSKRLEIEEQKAKKADSESRKLTEMVRHLE--ENLEDEERSRQKLLL 981
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 982 EKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSsrlIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRH 1061
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1062 NAETARRAAETQLREEQEscLEKTRKAEELTNQLmrkeSELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEK 1141
Cdd:COG4717 224 ELEEELEQLENELEAAAL--EERLKEARLLLLIA----AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1142 AARQKAEKARRDMAEELESYKQELEEsndktvLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNET 1221
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEE------LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1222 IDQLKRQkisadkakssAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDlmaklskmnneles 1301
Cdd:COG4717 372 IAALLAE----------AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-------------- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1302 iqkaksadetlnSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAvEARDDALDAQEKIEKEVKEVKS 1381
Cdd:COG4717 428 ------------EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA-ELLQELEELKAELRELAEEWAA 494
|
490 500
....*....|....*....|
gi 71983975 1382 L------LAEARKKLDEENR 1395
Cdd:COG4717 495 LklalelLEEAREEYREERL 514
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
910-1551 |
1.13e-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: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 910 SSERAEIFEERS-RMAARRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEK-NSIE 987
Cdd:pfam12128 274 IASRQEERQETSaELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQlPSWQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 988 SRLKELEAQGLELEDSGNKLSKEKKALE----ERCEDLSSRLIDEVERSKQlvkAKARLEATVAEINDELEKEKQQRHNA 1063
Cdd:pfam12128 354 SELENLEERLKALTGKHQDVTAKYNRRRskikEQNNRDIAGIKDKLAKIRE---ARDRQLAVAEDDLQALESELREQLEA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1064 etarraAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREireiRAQLDDAIEETNKEKAA 1143
Cdd:pfam12128 431 ------GKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAA----NAEVERLQSELRQARKR 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1144 RQKAEKARRDMAEELESYKQELEEsndktvLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEmkaqnqkkieelnetiD 1223
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDE------LELQLFPQAGTLLHFLRKEAPDWEQSIGKVISP----------------E 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1224 QLKRQKISADKAKSSAESDNENF-------RAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMN 1296
Cdd:pfam12128 559 LLHRTDLDPEVWDGSVGGELNLYgvkldlkRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1297 NELESIQKAKsadetlnsnllkKNASLDMQLSELTEASEEDRRTRATlnnkirqlEEDLAVAVEARDDaLDAQEKIEKev 1376
Cdd:pfam12128 639 REETFARTAL------------KNARLDLRRLFDEKQSEKDKKNKAL--------AERKDSANERLNS-LEAQLKQLD-- 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1377 KEVKSLLAEARKKLdEENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQE--AEDVQKELTDVVAATReM 1454
Cdd:pfam12128 696 KKHQAWLEEQKEQK-REARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETwyKRDLASLGVDPDVIAK-L 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1455 ERKMRKFDQQLAE-ERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGK 1533
Cdd:pfam12128 774 KREIRTLERKIERiAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEK 853
|
650
....*....|....*...
gi 71983975 1534 NVYELEKTKRRLDEELSR 1551
Cdd:pfam12128 854 QQVRLSENLRGLRCEMSK 871
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1331-1572 |
1.15e-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: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1331 TEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELS 1410
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1411 AEKERADMAEQARD--KAERAKKKAI----QEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQ 1484
Cdd:COG4942 99 LEAQKEELAELLRAlyRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1485 MLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDnlastkddagknvyELEKTKRRLDEELSRAEQQIIELEDALQ 1564
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELA--------------ELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*...
gi 71983975 1565 LADDARSR 1572
Cdd:COG4942 245 AAGFAALK 252
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1058-1869 |
1.33e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.82 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1058 QQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIReiraqlddAIEET 1137
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIER--------YQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1138 NKEKAARQKAEKARRDMAEELESYKQELEESNdktvlhsqlkakrdEEYAHLQKQLEEtVKSSEEVVEEMKAQNQKKIEE 1217
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARAEAAE--------------EEVDELKSQLAD-YQQALDVQQTRAIQYQQAVQA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1218 LNETIDQLKRQKISADKAKSSAESdnenFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKlskmnn 1297
Cdd:PRK04863 423 LERAKQLCGLPDLTADNAEDWLEE----FQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRS------ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1298 elESIQKAKSADETLNS--NLLKKNASLDMQLSELteasEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKE 1375
Cdd:PRK04863 493 --EAWDVARELLRRLREqrHLAEQLQQLRMRLSEL----EQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEAR 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1376 VKEVKSLLAEARkkldeENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQkELTDVVAATREME 1455
Cdd:PRK04863 567 LESLSESVSEAR-----ERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ-DVTEYMQQLLERE 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1456 RKMRKFDQQLAEERNNTL-----LAQQERDMAHQMLRDAETKALVLSNELSEkkDI--------------------VDQL 1510
Cdd:PRK04863 641 RELTVERDELAARKQALDeeierLSQPGGSEDPRLNALAERFGGVLLSEIYD--DVsledapyfsalygparhaivVPDL 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1511 EKDKRTLKleidnlasTKDDAGKNVYELEKTKRRLDEELSRAEqqiiELEDAL--QLAD----------------DARSR 1572
Cdd:PRK04863 719 SDAAEQLA--------GLEDCPEDLYLIEGDPDSFDDSVFSVE----ELEKAVvvKIADrqwrysrfpevplfgrAAREK 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1573 VEVNMQAMRSEFERQLASREEDEDDRKKGLTSKIRNLT------------EELESEQRARQAAIANKKKIESQISELTEK 1640
Cdd:PRK04863 787 RIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQ 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1641 NEASLRQIEDLSRQLRKAQLGWKD-LQLDVTEARAAMEDALAGQRDAEKRA-------------RASEDEIKRLTADIQA 1706
Cdd:PRK04863 867 LEQAKEGLSALNRLLPRLNLLADEtLADRVEEIREQLDEAEEAKRFVQQHGnalaqlepivsvlQSDPEQFEQLKQDYQQ 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1707 VSSSKRKAEAERDELIEEVSslRASSFSNEEKRRLEAKVIDLEDQLDEEASANELAQ----EKVRKSQQQLEQMTADLAM 1782
Cdd:PRK04863 947 AQQTQRDAKQQAFALTEVVQ--RRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERtrarEQLRQAQAQLAQYNQVLAS 1024
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1783 ERSVCERTESDKIALERANRDLKQQL-QDAENTAVAR---LRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKM 1858
Cdd:PRK04863 1025 LKSSYDAKRQMLQELKQELQDLGVPAdSGAEERARARrdeLHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDY 1104
|
890
....*....|.
gi 71983975 1859 AEMQQMLEEEK 1869
Cdd:PRK04863 1105 HEMREQVVNAK 1115
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1279-1934 |
1.71e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1279 REMQSNLDDLMaKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEEDR-----RTRATLNNKIRQLEE 1353
Cdd:PRK02224 149 SDRQDMIDDLL-QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERlngleSELAELDEEIERYEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1354 DLAVAVEARDDA---LDAQEKIEKEVKEVKSLLAEARKKLDEenrevmeelrkkkekelsAEKERADMAEQARDKAERAk 1430
Cdd:PRK02224 228 QREQARETRDEAdevLEEHEERREELETLEAEIEDLRETIAE------------------TEREREELAEEVRDLRERL- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1431 kkaiqeaEDVQKELTDVVAatremERKMRKFDQQLAEERNNTLlaQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQL 1510
Cdd:PRK02224 289 -------EELEEERDDLLA-----EAGLDDADAEAVEARREEL--EDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1511 EKDKRTLKLEIDNLASTKDDAGKNVyelekTKRRldEELSRAEQQIIELEDALQLADDARSRVEvnmqamrsEFERQLAS 1590
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAV-----EDRR--EEIEELEEEIEELRERFGDAPVDLGNAE--------DFLEELRE 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1591 REEDEDDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLrkaqlgwkdlqLDVT 1670
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAEL-----------EDLE 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1671 EARAAMEDALagqrDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRassfsnEEKRRLEAKVidleD 1750
Cdd:PRK02224 489 EEVEEVEERL----ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR------ERAAELEAEA----E 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1751 QLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALE---------RANRDLKQQLQDAENTAVARLRT 1821
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAdaedeierlREKREALAELNDERRERLAEKRE 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1822 QINVAEAKVSslEQQLSLEEQDKMRQGRTLRRMETKMAEmqqmLEEEKRQGESNRQAVDRQNARIRQLRTqledteaERD 1901
Cdd:PRK02224 635 RKRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDE----LREERDDLQAEIGAVENELEELEELRE-------RRE 701
|
650 660 670
....*....|....*....|....*....|...
gi 71983975 1902 RLTNKLKDERRRAEEMTDLNETLSRDVSLLKQR 1934
Cdd:PRK02224 702 ALENRVEALEALYDEAEELESMYGDLRAELRQR 734
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
855-1297 |
1.71e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.12 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 855 LEVTNKDELIAERE---QELKVTAEKLR--RSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDE 929
Cdd:TIGR04523 274 KELEQNNKKIKELEkqlNQLKSEISDLNnqKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 930 LEgiLEEVSKRLEIEEQKAKkadsesrkltemVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSK 1009
Cdd:TIGR04523 354 SE--SENSEKQRELEEKQNE------------IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1010 EKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLreeqesclektrkaE 1089
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL--------------E 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1090 ELTNQLMRKESELSQISIRNdeelaarQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESN 1169
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEK-------KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1170 DKTVLHSqlKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAQNQ---KKIEELNETIDQLKRQkisadkaKSSAESDNENF 1246
Cdd:TIGR04523 559 LEKEIDE--KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdliKEIEEKEKKISSLEKE-------LEKAKKENEKL 629
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 71983975 1247 RAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNN 1297
Cdd:TIGR04523 630 SSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIE 680
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
874-1277 |
1.82e-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: 62.82 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 874 TAEKLRRSEvfisdyKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRLEIEEQKAKKADS 953
Cdd:pfam05483 360 SLEELLRTE------QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 954 ESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELED----------SGNKLSKEKKALEERCEDLSS 1023
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklknieltaHCDKLLLENKELTQEASDMTL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1024 RLIDEVErskQLVKAKARLEATVAEINDELEKEKQQRHNAETARRaaetqlreeqesclEKTRKAEELTNQLMRKESELS 1103
Cdd:pfam05483 514 ELKKHQE---DIINCKKQEERMLKQIENLEEKEMNLRDELESVRE--------------EFIQKGDEVKCKLDKSEENAR 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1104 QISIRNDEELAARQQLEREIREIRAQLDDA---IEETNKEKAARQK---AEKARRDMAE--------ELESYKQELEESN 1169
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQENKALKKkgsAENKQLNAYEikvnklelELASAKQKFEEII 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1170 DKTVLHSQLKAKRDE----EYAHLQKQLEETVKSSEEV--------------VEEMKAQNQKKIEELNETIDQLKRQKIS 1231
Cdd:pfam05483 657 DNYQKEIEDKKISEEklleEVEKAKAIADEAVKLQKEIdkrcqhkiaemvalMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1232 ADKAKSSAESDNENFRAELSNIaSARLEAEK------KRKAAETSLMEKDHK 1277
Cdd:pfam05483 737 QSSAKAALEIELSNIKAELLSL-KKQLEIEKeekeklKMEAKENTAILKDKK 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1430-1941 |
1.92e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1430 KKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQ 1509
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1510 LEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLD-EELSRAEQQIIELEDALQLADDARSRvevnmqamrseFERQL 1588
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRAR-----------LEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1589 ASREEDEDDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSR----------QLRKA 1658
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksniparllALRDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1659 ---QLGWKDLQL-------DVTEA----RAAMEDALAGQR-----DAEKRARASE--DEIK-RLTADIQAVSSSKRKAEA 1716
Cdd:COG4913 449 laeALGLDEAELpfvgeliEVRPEeerwRGAIERVLGGFAltllvPPEHYAAALRwvNRLHlRGRLVYERVRTGLPDPER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1717 ER---DELIEEVSSlRASSFSNEEKRRLE-----AKViDLEDQLDEEASAneLAQEKVRKSQQQLEQM-TADLAMERSVC 1787
Cdd:COG4913 529 PRldpDSLAGKLDF-KPHPFRAWLEAELGrrfdyVCV-DSPEELRRHPRA--ITRAGQVKGNGTRHEKdDRRRIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1788 ERTESDKIAleranrDLKQQLQDAEnTAVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKmAEMQQmLEE 1867
Cdd:COG4913 605 GFDNRAKLA------ALEAELAELE-EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAE-LEA 675
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983975 1868 EKRQGESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKLKDERRRAEEMTDLNETLSRDVSLLKQRETTARRT 1941
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
924-1146 |
4.82e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 924 AARRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEds 1003
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1004 gNKLSKEKKALEERCED-------------LSSRLIDEVERSKQLVKAKAR-LEATVAEINDELEKEKQQRHNAETARRA 1069
Cdd:COG4942 97 -AELEAQKEELAELLRAlyrlgrqpplallLSPEDFLDAVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983975 1070 AETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQK 1146
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
876-1614 |
5.40e-09 |
|
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: 61.60 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 876 EKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSER-----------------AEIFEERSRMAARRDELEGI----- 933
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSReivksyeneldplknrlKEIEHNLSKIMKLDNEIKALksrkk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 934 -LEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKK 1012
Cdd:TIGR00606 280 qMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRH 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1013 ALEERCED-----LSSRL-IDEVERS-------KQLVKAKARLEATVAEINDELEKEKQQRhnaETARRAAETQLREEQE 1079
Cdd:TIGR00606 360 QEHIRARDsliqsLATRLeLDGFERGpfserqiKNFHTLVIERQEDEAKTAAQLCADLQSK---ERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1080 SCLE----KTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKArrDMA 1155
Cdd:TIGR00606 437 GLGRtielKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA--DLD 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1156 EELESYKQELEESNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEM-----KAQNQKKIEELNETIDQLKRQKI 1230
Cdd:TIGR00606 515 RKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfpnKKQLEDWLHSKSKEINQTRDRLA 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1231 SADKAKSSAESDNENFRAElsniasarleaEKKRKAAETSLMEKDHKM---REMQSNLDDLMAKLSKMNNELESIQKAKS 1307
Cdd:TIGR00606 595 KLNKELASLEQNKNHINNE-----------LESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQRAMLAGATA 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1308 ADETLNSNLLKKNASldmqlseLTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEAR 1387
Cdd:TIGR00606 664 VYSQFITQLTDENQS-------CCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1388 KKLDEENREVMEELRKKKEKELSAEKERADMAEQarDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAE 1467
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ--ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1468 ERNNTLLAQQERdmAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVyeleKTKRRLDE 1547
Cdd:TIGR00606 815 LQGSDLDRTVQQ--VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL----QRRQQFEE 888
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983975 1548 ELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQLASREEDeddrKKGLTSKIRNLTEELE 1614
Cdd:TIGR00606 889 QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS----NKKAQDKVNDIKEKVK 951
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1078-1775 |
6.49e-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: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1078 QESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKaarqkaEKARRDMAEE 1157
Cdd:pfam05483 66 KDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFEN------EKVSLKLEEE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1158 LESYKQELEESNDKTVLHSQLK---AKRDEEYAHLQKQLEET----------VKSSEEVVEEMKAQNQKKIEELNETIDQ 1224
Cdd:pfam05483 140 IQENKDLIKENNATRHLCNLLKetcARSAEKTKKYEYEREETrqvymdlnnnIEKMILAFEELRVQAENARLEMHFKLKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1225 lKRQKISADKAKSSAESDNENFRAELSNIASArlEAEKKRKAAETSLMEKDHKMREMQ-------SNLDDLMAKLSKMNN 1297
Cdd:pfam05483 220 -DHEKIQHLEEEYKKEINDKEKQVSLLLIQIT--EKENKMKDLTFLLEESRDKANQLEektklqdENLKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1298 ELE----SIQKAKSADETLNSNLLKKNASLdMQLSELTEAS-EEDRRTRATLNNKIRQLEedlAVAVEARDDALDAQEKI 1372
Cdd:pfam05483 297 ELEdikmSLQRSMSTQKALEEDLQIATKTI-CQLTEEKEAQmEELNKAKAAHSFVVTEFE---ATTCSLEELLRTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1373 EKEVKEVKSLLAEARKKldeeNREVMEELRKKKEKELSAEKERADMAEqaRDKAERAKKKAIQEAEDVQKELTDVVAATR 1452
Cdd:pfam05483 373 EKNEDQLKIITMELQKK----SSELEEMTKFKNNKEVELEELKKILAE--DEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1453 EMERKMRKFDQQL-----AEERNNTLLAQQERDMAHQMLRDAETKA----LVLSNE--LSEKKDIVDQLEKDKRtlklEI 1521
Cdd:pfam05483 447 AREKEIHDLEIQLtaiktSEEHYLKEVEDLKTELEKEKLKNIELTAhcdkLLLENKelTQEASDMTLELKKHQE----DI 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1522 DNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQLASREEDEDDRKKG 1601
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1602 LTSKIRNLtEELESEQRA-RQAAIANKKKI---ESQISELTEKNEASLRQIEDLS----RQLRKAQLGWKDLQLDVTEAR 1673
Cdd:pfam05483 603 IENKNKNI-EELHQENKAlKKKGSAENKQLnayEIKVNKLELELASAKQKFEEIIdnyqKEIEDKKISEEKLLEEVEKAK 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1674 AAMEDALAGQRDAEKRArasEDEIKRLTADIQAVSSSKRKAEAERDELI-------EEVSSLRASsfSNEEKRRLEAKVI 1746
Cdd:pfam05483 682 AIADEAVKLQKEIDKRC---QHKIAEMVALMEKHKHQYDKIIEERDSELglyknkeQEQSSAKAA--LEIELSNIKAELL 756
|
730 740
....*....|....*....|....*....
gi 71983975 1747 DLEDQLDEEASANELAQEKVRKSQQQLEQ 1775
Cdd:pfam05483 757 SLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1447-1940 |
7.33e-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: 61.39 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1447 VVAATREMERKMRKFDQQLAEErnNTLLAQQERDMahQMLRDAETKAL-VLSNELSEKKDIVDQLEKDKRT-LKLEIDNL 1524
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAEL--NQLLRTLDDQW--KEKRDELNGELsAADAAVAKDRSELEALEDQHGAfLDADIETA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1525 ASTKDDAGKNVYELEKTKRRLDEeLSRAEQQIIELEDALQLADDAR-----SRVEVNMQAMRSEFERQLASREEDEDDRK 1599
Cdd:pfam12128 343 AADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKYNRRRSKIKEQnnrdiAGIKDKLAKIREARDRQLAVAEDDLQALE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1600 KGLTSKIRNLTEELESEQRARQAAIANKKKIESQI---SELTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAM 1676
Cdd:pfam12128 422 SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRR 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1677 EDALAGQRDAEKRA--RASEDEIKRLTADIQAVS--------------SSKRKAEAE---RDELIEEVSSLRASSFSNEE 1737
Cdd:pfam12128 502 DQASEALRQASRRLeeRQSALDELELQLFPQAGTllhflrkeapdweqSIGKVISPEllhRTDLDPEVWDGSVGGELNLY 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1738 KRRLEAKVID------LEDQLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESD-KIALERANRDL------ 1804
Cdd:pfam12128 582 GVKLDLKRIDvpewaaSEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFaRTALKNARLDLrrlfde 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1805 KQQLQDAENTAVARLRTQINV------AEAKVSSLEQQLSLEEQDkmrqgRTLRRMETKMAEMQQMLEEEKrqgesnrqa 1878
Cdd:pfam12128 662 KQSEKDKKNKALAERKDSANErlnsleAQLKQLDKKHQAWLEEQK-----EQKREARTEKQAYWQVVEGAL--------- 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1879 vdrqNARIRQLRTQLEDTEAERDRLTNKLKDERRRAEEMTDLNEtlSRDVSLLKQRETTARR 1940
Cdd:pfam12128 728 ----DAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDP--DVIAKLKREIRTLERK 783
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1026-1657 |
9.28e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 60.69 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1026 IDEVERSKQLVKAKAR-LEATVAEINDEleKEKQQRHNAETARRAAETQLREEQESCLEKTRKA-EELTNQLMRKESELS 1103
Cdd:PRK01156 161 INSLERNYDKLKDVIDmLRAEISNIDYL--EEKLKSSNLELENIKKQIADDEKSHSITLKEIERlSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1104 QISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMA----EELESYKQELEESNDKTVLHSQLK 1179
Cdd:PRK01156 239 SALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVyknrNYINDYFKYKNDIENKKQILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1180 AKRdEEYAHLQKQLEETVKSSEEVVEEmkaqnQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLE 1259
Cdd:PRK01156 319 AEI-NKYHAIIKKLSVLQKDYNDYIKK-----KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAF 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1260 AEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNnelESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEEDRR 1339
Cdd:PRK01156 393 ISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLN---QRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNH 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1340 TRATLNNKIRQLEEDLavavearddaldaqEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKEradma 1419
Cdd:PRK01156 470 IINHYNEKKSRLEEKI--------------REIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARAD----- 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1420 eqardkaerakkkaIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLaqqeRDMAHQMLRDAETkalvLSNE 1499
Cdd:PRK01156 531 --------------LEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWL----NALAVISLIDIET----NRSR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1500 LSEKKDIVDQLEKDKRTLKLEIDNLASTkddagknvyeLEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEvnmqa 1579
Cdd:PRK01156 589 SNEIKKQLNDLESRLQEIEIGFPDDKSY----------IDKSIREIENEANNLNNKYNEIQENKILIEKLRGKID----- 653
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1580 mrsEFERQLASREEDEDDrKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLRK 1657
Cdd:PRK01156 654 ---NYKKQIAEIDSIIPD-LKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLES 727
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1115-1795 |
1.11e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1115 ARQQLE--REIREIRAQLDDAIEETN-----KEKAARQKAEKARRDMAEELESYKQELEESNDKTVLHSQLKAKRDEEYA 1187
Cdd:COG4913 247 AREQIEllEPIRELAERYAAARERLAeleylRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1188 HLQKQLEEtvkSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAA 1267
Cdd:COG4913 327 ELEAQIRG---NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1268 ETSLmekdhkmREMQSNLDDLMAKLSKMNNELESIQKAKSadeTLNSNLLKKNASLDMQLS----------ELTEASEED 1337
Cdd:COG4913 404 EEAL-------AEAEAALRDLRRELRELEAEIASLERRKS---NIPARLLALRDALAEALGldeaelpfvgELIEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1338 RRTRATLNNKIRQLEEDLAVAVEARDDALDA-----------QEKIEKEVKEVKSLLAEAR---KKLD-EEN------RE 1396
Cdd:COG4913 474 ERWRGAIERVLGGFALTLLVPPEHYAAALRWvnrlhlrgrlvYERVRTGLPDPERPRLDPDslaGKLDfKPHpfrawlEA 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1397 VMEELRKKKEKELSAEKERADMA----EQARDKAERAKK---KAIQEA----EDVQKELTDVVAATREMERKMRKFDQQL 1465
Cdd:COG4913 554 ELGRRFDYVCVDSPEELRRHPRAitraGQVKGNGTRHEKddrRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERL 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1466 aEERNNTLLAQQERDMAHQMLRD---AETKALVLSNELSEKKDIVDQLEKDK---RTLKLEIDNLASTKDDAGKNVYELE 1539
Cdd:COG4913 634 -EALEAELDALQERREALQRLAEyswDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELK 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1540 KTKRRLDEELSRAEQQIIELEDALQLADDARSrvevnmQAMRSEFERQL--ASREEDEDDRKKGLTSKIRNLTEELE-SE 1616
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAEDLAR------LELRALLEERFaaALGDAVERELRENLEERIDALRARLNrAE 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1617 QRARQAAIANKKKIESQISELTEkNEASLRQIEDLSRQLRkaqlgwkdlQLDVTEARAAMEDALagqrdaekrARASEDE 1696
Cdd:COG4913 787 EELERAMRAFNREWPAETADLDA-DLESLPEYLALLDRLE---------EDGLPEYEERFKELL---------NENSIEF 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1697 IKRLTADIqavssskRKAEAERDELIEEV-SSLRASSFSNEEKRRLEAK------VIDLEDQLDEEASANELAQEKVRKS 1769
Cdd:COG4913 848 VADLLSKL-------RRAIREIKERIDPLnDSLKRIPFGPGRYLRLEARprpdpeVREFRQELRAVTSGASLFDEELSEA 920
|
730 740
....*....|....*....|....*..
gi 71983975 1770 Q-QQLEQMTADLAMERSVCERTESDKI 1795
Cdd:COG4913 921 RfAALKRLIERLRSEEEESDRRWRARV 947
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
791-1310 |
1.47e-08 |
|
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: 60.13 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 791 MRDQKLSALIESFQAQCRGWLGRRVMVRRREQEVAIKIlqrnglawmrlrewqwwrllTKVKPLLEVTNkdELIAEREQE 870
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV--------------------SSLTAQLESTK--EMLRKVVEE 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 871 LKVTAEKLRRSEVFISDYKQQMEkmDEERLVLKTrldaesseRAEIFEERSRMAARRDELEGILEEVS--KRLEIEEQKA 948
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQ--EKERAIEAT--------NAEITKLRSRVDLKLQELQHLKNEGDhlRNVQTECEAL 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 949 KKADSESRKLTEMVRHLEENLE----DEERSRQKLLLEKNSIEsrlKELEAQGLELEDSgnKLSKEKKalEERCEDLSSR 1024
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIENMTqlvgQHGRTAGAMQVEKAQLE---KEINDRRLELQEF--KILKDKK--DAKIRELEAR 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1025 LID-EVERSKQLVKAKARLEATvaeinDELEKEKQQRHNAETARRAAETQLREEQESCLEKTR-KAEEL---TN----QL 1095
Cdd:pfam15921 627 VSDlELEKVKLVNAGSERLRAV-----KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRnKSEEMettTNklkmQL 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1096 MRKESELSQI-----SIRNDEELAAR--QQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEE- 1167
Cdd:pfam15921 702 KSAQSELEQTrntlkSMEGSDGHAMKvaMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTv 781
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1168 SNDKTVLHSQLKAKRDEEyahlqKQLEETVKSSEEVVEEMK---AQNQKKIEELNETIDQLKRQ-KISADKAKSSAESDN 1243
Cdd:pfam15921 782 ATEKNKMAGELEVLRSQE-----RRLKEKVANMEVALDKASlqfAECQDIIQRQEQESVRLKLQhTLDVKELQGPGYTSN 856
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71983975 1244 ENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMR------EMQSNLDDLMAKLSKMNNELESIQKAKSADE 1310
Cdd:pfam15921 857 SSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHSRKtnalkeDPTRDLKQLLQELRSVINEEPTVQLSKAEDK 929
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
855-1376 |
1.80e-08 |
|
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: 59.74 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 855 LEVTNKDELIAEREQELKVTAEKLRRSEVFisDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGIL 934
Cdd:pfam05483 186 MDLNNNIEKMILAFEELRVQAENARLEMHF--KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 935 EEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLK-----------ELEAQGLELEDS 1003
Cdd:pfam05483 264 EESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticqlteEKEAQMEELNKA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1004 GNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQeSCLE 1083
Cdd:pfam05483 344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDE-KLLD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1084 KTRKAEELTNQLMRKESELSQIsirndeelaaRQQLEREIREIRAQLddaieetNKEKAARQKAEKARRDMAEELESYK- 1162
Cdd:pfam05483 423 EKKQFEKIAEELKGKEQELIFL----------LQAREKEIHDLEIQL-------TAIKTSEEHYLKEVEDLKTELEKEKl 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1163 --QELEESNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMkaqnQKKIEELNETIDQLKRQkisadkakssAE 1240
Cdd:pfam05483 486 knIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM----LKQIENLEEKEMNLRDE----------LE 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1241 SDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQ--------KAKSADETL 1312
Cdd:pfam05483 552 SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHqenkalkkKGSAENKQL 631
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983975 1313 NSNLLKKNaSLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEV 1376
Cdd:pfam05483 632 NAYEIKVN-KLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEI 694
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1326-1913 |
1.94e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1326 QLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQ--------EKIEKEVKEVKSLLAEARKKLDE----- 1392
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARleall 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1393 --------ENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQ 1464
Cdd:COG4913 369 aalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1465 LAEErnntlLAQQERDM-----------AHQMLRDAETKAL--------VLSNELSEKKDIVDQLEKDKR--TLKLEIDN 1523
Cdd:COG4913 449 LAEA-----LGLDEAELpfvgelievrpEEERWRGAIERVLggfaltllVPPEHYAAALRWVNRLHLRGRlvYERVRTGL 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1524 LASTKDDAGKN--VYELE----KTKRRLDEELSRaEQQIIELEDALQLADDARSrveVNMQAMRSeferQLASREEdEDD 1597
Cdd:COG4913 524 PDPERPRLDPDslAGKLDfkphPFRAWLEAELGR-RFDYVCVDSPEELRRHPRA---ITRAGQVK----GNGTRHE-KDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1598 RKKGL---------TSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEAsLRQIEDLSRqlrkAQLGWKDLQLD 1668
Cdd:COG4913 595 RRRIRsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA-LQRLAEYSW----DEIDVASAERE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1669 VTEARAAMEDALAGQRD----------AEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSL----RASSFS 1734
Cdd:COG4913 670 IAELEAELERLDASSDDlaaleeqleeLEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlaRLELRA 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1735 NEEKRRLEAKVIDLEDQLDEEASAN-ELAQEKVRKSQQQLEQM------------------TADLAMERSVCERTESDki 1795
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLEERiDALRARLNRAEEELERAmrafnrewpaetadldadLESLPEYLALLDRLEED-- 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1796 ALERANRDLKQQLQDAENTAVARLRTQInvaEAKVSSLEQQL-----SLEEQDkMRQGRTLR-----RMETKMAEMQQML 1865
Cdd:COG4913 828 GLPEYEERFKELLNENSIEFVADLLSKL---RRAIREIKERIdplndSLKRIP-FGPGRYLRlearpRPDPEVREFRQEL 903
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 71983975 1866 EEEKRQG-ESNRQAVDRQNARIRQLRTQLEDTEAERDRL-TNKLKDERRR 1913
Cdd:COG4913 904 RAVTSGAsLFDEELSEARFAALKRLIERLRSEEEESDRRwRARVLDVRNH 953
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1347-1941 |
2.52e-08 |
|
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: 59.60 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1347 KIRQLEEDLAVAvearddaldaqekIEKEVKEvksllaEARKKLDEENREvmeeLRKKKEKELSAEKERADMAEQARDKA 1426
Cdd:pfam02463 154 RRLEIEEEAAGS-------------RLKRKKK------EALKKLIEETEN----LAELIIDLEELKLQELKLKEQAKKAL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1427 ERAKKKAIQEAEdvqkELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSN-ELSEKKD 1505
Cdd:pfam02463 211 EYYQLKEKLELE----EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEkEKKLQEE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1506 IVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFE 1585
Cdd:pfam02463 287 ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1586 RQLASREEDEDDRKKG--LTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLRKAQLGWK 1663
Cdd:pfam02463 367 KLEQLEEELLAKKKLEseRLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKL 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1664 DLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRASSFSNEEKRRLEA 1743
Cdd:pfam02463 447 TEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1744 KVIDLEDQldEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQQLQDAE------NTAVA 1817
Cdd:pfam02463 527 AHGRLGDL--GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSiavleiDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1818 RLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQLEDTE 1897
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 71983975 1898 AERDRLTNKLKDERRRAEEMTDLNETLSRDVSLLKQRETTARRT 1941
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQ 728
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
906-1657 |
2.57e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.21 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 906 LDAESSERAEIFEErsrmaarrdeLEGiLEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEErsrQKLLLEKNS 985
Cdd:TIGR00618 158 LKAKSKEKKELLMN----------LFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMP---DTYHERKQV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 986 IESRLKELEAQGLELEDSGNKLSKEKKALEERcedlssrlideVERSKQLVKAKARLEatvaEINDELEKEKQQRHNAET 1065
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQEEQ-----------LKKQQLLKQLRARIE----ELRAQEAVLEETQERINR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1066 ARRAAetQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIR---EIRAQLDDAIEETNKEKA 1142
Cdd:TIGR00618 289 ARKAA--PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllqTLHSQEIHIRDAHEVATS 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1143 ARQKAEKARRDMaEELESYKQELEESNDKTVLHSQLKAKRDEEYAhlqKQLEETVKSSEEVVEEMKAQNQKKIEELNETI 1222
Cdd:TIGR00618 367 IREISCQQHTLT-QHIHTLQQQKTTLTQKLQSLCKELDILQREQA---TIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1223 DQLKRQKiSADKAKSSAESDNENFRA------ELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMN 1296
Cdd:TIGR00618 443 CAAAITC-TAQCEKLEKIHLQESAQSlkereqQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDID 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1297 NeLESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTRatlnNKIRQLEEDLAVAVEARDDALDAQEKIEKEV 1376
Cdd:TIGR00618 522 N-PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM----QEIQQSFSILTQCDNRSKEDIPNLQNITVRL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1377 KEVKSLLAEARKKLDEENREVMEELrkkkekelsaeKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMER 1456
Cdd:TIGR00618 597 QDLTEKLSEAEDMLACEQHALLRKL-----------QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1457 KMRKFDQQLAEERNNTLLAQQERDMAHQMLRDA-ETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNV 1535
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1536 YELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFE---RQLASREED-EDDRKKGLtsKIRNLTE 1611
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREedtHLLKTLEAEiGQEIPSDE--DILNLQC 823
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 71983975 1612 ELESEQRAR-QAAIANKKKIESQISELTEKNEASLRQIEDLSRQLRK 1657
Cdd:TIGR00618 824 ETLVQEEEQfLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
925-1196 |
3.71e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 925 ARRDELEGILEEVSKRLEIEEQKAKK-----ADSESRKLTEMV------RHLEENLEDEERSRQKLLlekNSIESRLKEL 993
Cdd:COG3206 111 GEEASREAAIERLRKNLTVEPVKGSNvieisYTSPDPELAAAVanalaeAYLEQNLELRREEARKAL---EFLEEQLPEL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 994 EAQgleLEDSGNKLSKEKKaleercedlSSRLIDEVERSKQLVkakarleATVAEINDELEKEKQQRHNAETARRAAETQ 1073
Cdd:COG3206 188 RKE---LEEAEAALEEFRQ---------KNGLVDLSEEAKLLL-------QQLSELESQLAEARAELAEAEARLAALRAQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1074 LRE--EQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKE-KAARQKAEKA 1150
Cdd:COG3206 249 LGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASlEAELEALQAR 328
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 71983975 1151 RRDMAEELESYKQELEESNDKTVLHSQLKAKRD---EEYAHLQKQLEET 1196
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELRRLEREVEvarELYESLLQRLEEA 377
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1062-1912 |
4.49e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1062 NAETARRAAE--TQLREEQESCLEKTRKAEELTNQLMRKESELSqisirndeelAARQQLEREIREIRAQLddaieetNK 1139
Cdd:PRK04863 277 HANERRVHLEeaLELRRELYTSRRQLAAEQYRLVEMARELAELN----------EAESDLEQDYQAASDHL-------NL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1140 EKAARQKAEKarrdmaeeLESYKQELEESNDKTVLHSQLKAKRDEEYAHLQKQLEETvkssEEVVEEMKAQ---NQKKIE 1216
Cdd:PRK04863 340 VQTALRQQEK--------IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAA----EEEVDELKSQladYQQALD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1217 ELNETIDQLkRQKISA-DKAKS----------SAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNL 1285
Cdd:PRK04863 408 VQQTRAIQY-QQAVQAlERAKQlcglpdltadNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1286 DDLMAKlskmnnelESIQKAKSADETLNS--NLLKKNASLDMQLSELteasEEDRRTRATLNNKIRQLEEDLAVAVEARD 1363
Cdd:PRK04863 487 GEVSRS--------EAWDVARELLRRLREqrHLAEQLQQLRMRLSEL----EQRLRQQQRAERLLAEFCKRLGKNLDDED 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1364 DALDAQEKIEKEVKEVKSLLAEARkkldeENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQkE 1443
Cdd:PRK04863 555 ELEQLQEELEARLESLSESVSEAR-----ERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ-D 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1444 LTDVVAATREMERKMRKFDQQLAEERNNTL-----LAQQERDMAHQMLRDAETKALVLSNELSEkkDI------------ 1506
Cdd:PRK04863 629 VTEYMQQLLERERELTVERDELAARKQALDeeierLSQPGGSEDPRLNALAERFGGVLLSEIYD--DVsledapyfsaly 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1507 --------VDQLEKDKRTLKleidnlasTKDDAGKNVYELEKTKRRLDEELSRAEqqiiELEDAL--QLAD--------- 1567
Cdd:PRK04863 707 gparhaivVPDLSDAAEQLA--------GLEDCPEDLYLIEGDPDSFDDSVFSVE----ELEKAVvvKIADrqwrysrfp 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1568 -------DARSRVEVNMQAMRSEFERQLASREEDEDDRKKGLTSKIRNLT------------EELESEQRARQAAIANKK 1628
Cdd:PRK04863 775 evplfgrAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGshlavafeadpeAELRQLNRRRVELERALA 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1629 KIESQISELTEKNEASLRQIEDLSRQLRKAQLGWKD-LQLDVTEARAAMEDALAGQRDAEKRARASEdEIKRLTADIQAV 1707
Cdd:PRK04863 855 DHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADEtLADRVEEIREQLDEAEEAKRFVQQHGNALA-QLEPIVSVLQSD 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1708 SSSKRKAEAERDELIEEVSSLRASSFSNEE--KRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLamers 1785
Cdd:PRK04863 934 PEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQL----- 1008
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1786 vcertesdkialeranRDLKQQLQDAeNTAVARLRTQINVAEAKVSSLEQqlsleeqdkmrqgrtlrrmetkmaEMQQM- 1864
Cdd:PRK04863 1009 ----------------RQAQAQLAQY-NQVLASLKSSYDAKRQMLQELKQ------------------------ELQDLg 1047
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1865 ------LEEEKRQGESNRQAVDRQN-ARIRQLRTQLEDTEAERDRLTNKLKDERR 1912
Cdd:PRK04863 1048 vpadsgAEERARARRDELHARLSANrSRRNQLEKQLTFCEAEMDNLTKKLRKLER 1102
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
843-1424 |
4.65e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.44 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 843 QWWRLLTKVKPLLEVTNKDELIAEREQElkvtAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSR 922
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLEETQE----RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 923 MAARRDE------LEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKnSIESRLKELEAQ 996
Cdd:TIGR00618 333 HVKQQSSieeqrrLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC-KELDILQREQAT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 997 GLELEDSGNKLSKEKKALEERCEDLSSRL-----------------IDEVERSKQLVKAKARLEATVAEINdELEKEKQQ 1059
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAHAKKQQELQQRYAelcaaaitctaqcekleKIHLQESAQSLKEREQQLQTKEQIH-LQETRKKA 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1060 RHNAETARRAAETQLREEQESCLEK-----------TRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRa 1128
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNParqdidnpgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ- 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1129 qlDDAIEETNKEKAARQKAEKARRdMAEELESYKQELEESNDKTVLHSQ-LKAKRDEEYAHLQKQLEETVKSSEEVVEEM 1207
Cdd:TIGR00618 570 --QSFSILTQCDNRSKEDIPNLQN-ITVRLQDLTEKLSEAEDMLACEQHaLLRKLQPEQDLQDVRLHLQQCSQELALKLT 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1208 KAQN------QKKIEELNETIDQLKRQKISADKAKSSAEsdnENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREM 1281
Cdd:TIGR00618 647 ALHAlqltltQERVREHALSIRVLPKELLASRQLALQKM---QSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEI 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1282 QSNLDDLMAKLSKMNNELESIQ-----------KAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQ 1350
Cdd:TIGR00618 724 ENASSSLGSDLAAREDALNQSLkelmhqartvlKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKT 803
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1351 LEEDLAVAVEARDDALDAQ-EKIEKEVKEVKSLLAEARKKLDEENREvMEELRKKKEKELSAEKERADMAEQARD 1424
Cdd:TIGR00618 804 LEAEIGQEIPSDEDILNLQcETLVQEEEQFLSRLEEKSATLGEITHQ-LLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1554-1915 |
7.54e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.83 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1554 QQIIELEDALQLADDARSRVEVNMQAMRSEFERQLASREEDEDDRKKGLTSKIRnlteELESEQRARQAAIANKKKIESQ 1633
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRR----KLEEAEKARQAEMDRQAAIYAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1634 ISELTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEkrarasedeikRLTADIQAVSSSKRK 1713
Cdd:pfam17380 339 QERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNE-----------RVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1714 AEAERDELIEEVSSLRASSFSNEEKRRLEAKVIDledqlDEEASANELAQEKVRKSQQQLE---QMTADLAMERSVCERT 1790
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE-----EERAREMERVRLEEQERQQQVErlrQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1791 ESDKIALERANRDLKQQLQDAENTAVARLRTQINVAEAKVSslEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKR 1870
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEME--ERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRK 560
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 71983975 1871 QGESnrqavdrqnarirqlRTQLEDTEAERDRLTNKLKDERRRAE 1915
Cdd:pfam17380 561 ATEE---------------RSRLEAMEREREMMRQIVESEKARAE 590
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1247-1916 |
9.32e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1247 RAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNsnllKKNASLDMQ 1326
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELE----KELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1327 LSELTEASEEDRRTRATLNNKIRQLEEDLAvavearddaldAQEKIEKEVKEVKSLLAEARKKLDEENRevmeelrkkke 1406
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVK-----------ELKELKEKAEEYIKLSEFYEEYLDELRE----------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1407 kelsAEKERADMAEQARDKAERakkkaIQEAEDVQKELTDVVAATREMERKMRKFdqqlaeernntllaqqerdmahqml 1486
Cdd:PRK03918 312 ----IEKRLSRLEEEINGIEER-----IKELEEKEERLEELKKKLKELEKRLEEL------------------------- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1487 rdaETKALvlsnELSEKKDIVDQLEKDKRTLK-LEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQL 1565
Cdd:PRK03918 358 ---EERHE----LYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1566 ADDARSRVEVnmqamrseferqlASREEDEDDRKKGL---TSKIRNLTEELESEQRARQAAIANKKKIESQISELTE--K 1640
Cdd:PRK03918 431 LKKAKGKCPV-------------CGRELTEEHRKELLeeyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliK 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1641 NEASLRQIEDLSRQLRKAQLgwKDLQLDVTEARAAMEDAlagqRDAEKRARASEDEIKRLtadiQAVSSSKRKAEAERDE 1720
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYNL--EELEKKAEEYEKLKEKL----IKLKGEIKSLKKELEKL----EELKKKLAELEKKLDE 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1721 LIEEVSSLrassfsneeKRRLEAKVIDLEDQLDEEAsanelaqekvrksqQQLEQMTADLAMERSVCERTESDKIALERA 1800
Cdd:PRK03918 568 LEEELAEL---------LKELEELGFESVEELEERL--------------KELEPFYNEYLELKDAEKELEREEKELKKL 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1801 NRDLKQQLQDaentaVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQ-QMLEEEKRQGESNRQAV 1879
Cdd:PRK03918 625 EEELDKAFEE-----LAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAElEELEKRREEIKKTLEKL 699
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 71983975 1880 DRQNARIRQLRTQLEDTEAERDRLTN---KLKDERRRAEE 1916
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEElreKVKKYKALLKE 739
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1283-1884 |
1.10e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1283 SNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDmqlSELTEASEEDRRTRATLNNKIRQLEEdlavavear 1362
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLS---IEYNNAMDDYNNLKSALNELSSLEDM--------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1363 ddaldaQEKIEKEVKEVKSLLA---EARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDKAERAK--KKAIQEA 1437
Cdd:PRK01156 251 ------KNRYESEIKTAESDLSmelEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSniDAEINKY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1438 EDVQKELTDVVAATREMERKMRKFDqqlaeERNNTLLAQQERDMAHQ-MLRDAETKALVLSNELSEKKDIVDQLEKDKRT 1516
Cdd:PRK01156 325 HAIIKKLSVLQKDYNDYIKKKSRYD-----DLNNQILELEGYEMDYNsYLKSIESLKKKIEEYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1517 LKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLAdDARSRVEVNMQAMRSEFERQLAsreEDED 1596
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEML-NGQSVCPVCGTTLGEEKSNHII---NHYN 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1597 DRKKGLTSKIRnlteELESEQRARQAAIANKKKIESQI-SELTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAA 1675
Cdd:PRK01156 476 EKKSRLEEKIR----EIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1676 ME-------DALAGQRDAEKRARASEDEIkrltaDIQAVSSSKRKAEAERDELIE-----EVSSLRASSFSNEEKRRLEA 1743
Cdd:PRK01156 552 KNrykslklEDLDSKRTSWLNALAVISLI-----DIETNRSRSNEIKKQLNDLESrlqeiEIGFPDDKSYIDKSIREIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1744 KVIDLEDQLDeEASANELAQEKVRKsqqQLEQMTADLAMERSVCERTESDKIALERANRDLKQ---QLQDAeNTAVARLR 1820
Cdd:PRK01156 627 EANNLNNKYN-EIQENKILIEKLRG---KIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKsrkALDDA-KANRARLE 701
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983975 1821 TQINVAEAKVSSLEQQLSLEEqdkmrqgRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNA 1884
Cdd:PRK01156 702 STIEILRTRINELSDRINDIN-------ETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSA 758
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1013-1239 |
1.17e-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: 56.31 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1013 ALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELT 1092
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1093 NQLMRKESELSQ-----------------ISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRdma 1155
Cdd:COG4942 97 AELEAQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1156 EELESYKQELEESNDKTvlhSQLKAKRDEEYAHLQKQLEETvksseevvEEMKAQNQKKIEELNETIDQLKRQKISADKA 1235
Cdd:COG4942 174 AELEALLAELEEERAAL---EALKAERQKLLARLEKELAEL--------AAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....
gi 71983975 1236 KSSA 1239
Cdd:COG4942 243 TPAA 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1632-1938 |
1.20e-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: 57.39 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1632 SQISELTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALagqRDAEKRARASEDEIKRLTADIQAVSSSK 1711
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE---RYQALLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1712 RKAEAERDELIEEVSSLRASSFSNEEkrRLEAKVIDLEDqldEEASANELAQEKVRKSQQQLEQMTADLAmersvcerte 1791
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEK--RLEEIEQLLEE---LNKKIKDLGEEEQLRVKEKIGELEAEIA---------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1792 sdkiALERANRDLKQQLQDAENTaVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQ 1871
Cdd:TIGR02169 305 ----SLERSIAEKERELEDAEER-LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983975 1872 GESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKLkdeRRRAEEMTDLNETLSRDVSLLKQRETTA 1938
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEEL---QRLSEELADLNAAIAGIEAKINELEEEK 443
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1494-1935 |
1.24e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1494 LVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRV 1573
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1574 EVNMQAMRSEFER--QLASREEDEDDRKKGLTSKI-------RNLTEELESEQRARQAAIANKKKIESQISELTEKNEAS 1644
Cdd:TIGR04523 186 QKNIDKIKNKLLKleLLLSNLKKKIQKNKSLESQIselkkqnNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1645 LRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDaLAGQRDaekrarasEDEIKRLTADIQAVSSSKRKAEAERDELIEE 1724
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD-LNNQKE--------QDWNKELKSELKNQEKKLEEIQNQISQNNKI 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1725 VSSLrassfsneekrrlEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKialeranRDL 1804
Cdd:TIGR04523 337 ISQL-------------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-------NDL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1805 KQQLQDAENTAvARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNA 1884
Cdd:TIGR04523 397 ESKIQNQEKLN-QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 71983975 1885 RIRQLRTQLEDTEAERDRLTNKLKDERRRAEEMTDLNETLSRDVSLLKQRE 1935
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1255-1593 |
1.35e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.67 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1255 SARLEAEKKRKAAETSL-MEKDHKMREMQSNlddlmaklskmnNELESIQKAKSADETLNSNLLKKNASLDMQLS-ELTE 1332
Cdd:pfam17380 285 SERQQQEKFEKMEQERLrQEKEEKAREVERR------------RKLEEAEKARQAEMDRQAAIYAEQERMAMERErELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1333 ASEEDRRTRatlNNKIRQleEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARK-KLDEENREVMEELRKKKEKELSA 1411
Cdd:pfam17380 353 IRQEERKRE---LERIRQ--EEIAMEISRMRELERLQMERQQKNERVRQELEAARKvKILEEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1412 EKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQlAEERNNTLLAQQERdmahqmlrdaet 1491
Cdd:pfam17380 428 EQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE-KEKRDRKRAEEQRR------------ 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1492 kaLVLSNELSEKKDIVDQLEKDKRTLKLEIdnlastkDDAGKNVYELEktKRRLDEELSRAEQQIIE---LEDALQLADD 1568
Cdd:pfam17380 495 --KILEKELEERKQAMIEEERKRKLLEKEM-------EERQKAIYEEE--RRREAEEERRKQQEMEErrrIQEQMRKATE 563
|
330 340
....*....|....*....|....*..
gi 71983975 1569 ARSRVEvnmqAMRSEFE--RQLASREE 1593
Cdd:pfam17380 564 ERSRLE----AMEREREmmRQIVESEK 586
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
869-1227 |
1.48e-07 |
|
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: 56.77 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 869 QELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSrmaarrdELEGILEEVSKRLEIEEQKA 948
Cdd:pfam12128 576 GELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLV-------QANGELEKASREETFARTAL 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 949 KKADSESRKLTEMVRHLEENLEDEERSRQKllleknSIESRLKELEAQGLELEDSGNKLSKEKK--ALEERCEDLSSRLI 1026
Cdd:pfam12128 649 KNARLDLRRLFDEKQSEKDKKNKALAERKD------SANERLNSLEAQLKQLDKKHQAWLEEQKeqKREARTEKQAYWQV 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1027 DEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQL------REEQESCLEKTRKAEELTNQLMRKES 1100
Cdd:pfam12128 723 VEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIaklkreIRTLERKIERIAVRRQEVLRYFDWYQ 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1101 ElsQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEEL--ESYKQELEESNDKTVLHSQL 1178
Cdd:pfam12128 803 E--TWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLseNLRGLRCEMSKLATLKEDAN 880
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 71983975 1179 KAKRDEEYAHLQKQLEETVKSSEEVVEEMkaqnQKKIEELNETIDQLKR 1227
Cdd:pfam12128 881 SEQAQGSIGERLAQLEDLKLKRDYLSESV----KKYVEHFKNVIADHSG 925
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1493-1741 |
1.89e-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: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1493 ALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSR 1572
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1573 VEVNMQAMRsefeRQLASREEDEDDR-----KKGLTSKIRNLTEELESEQRARQAAIAnkKKIESQISELTEKNEASLRQ 1647
Cdd:COG4942 88 LEKEIAELR----AELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAVRRLQYL--KYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1648 IEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSS 1727
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|....
gi 71983975 1728 LRASSFSNEEKRRL 1741
Cdd:COG4942 242 RTPAAGFAALKGKL 255
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
864-1837 |
1.95e-07 |
|
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: 56.60 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 864 IAEREQELKVTAEKLRRSEVFisdYKQQMEKMDE-----ERLVLKTRLDAESSERAEIFEE------RSRMAARRDELEG 932
Cdd:TIGR01612 394 IAKQRAIFFYNAKKLKHLEIL---YKHQEDILNNfhktiERLIFEKPDPNNNNIFKDDFDEfnkpipKSKLKALEKRFFE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 933 ILEEVSKRLEIEEQKAKKADSES---------RKLTEMVRHLEENLEDEERSRQKLLLEknsIESRLKELEAQGLE--LE 1001
Cdd:TIGR01612 471 IFEEEWGSYDIKKDIDENSKQDNtvklilmrmKDFKDIIDFMELYKPDEVPSKNIIGFD---IDQNIKAKLYKEIEagLK 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1002 DSGNKLSKEKKALEErcedLSSRLIDEVERSKQLVKAKARLEATVAEINDELekekqqrhnaeTARRAAETQLREEQESC 1081
Cdd:TIGR01612 548 ESYELAKNWKKLIHE----IKKELEEENEDSIHLEKEIKDLFDKYLEIDDEI-----------IYINKLKLELKEKIKNI 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1082 LEKtrkaeeltNQLMRKESELSQISIRND---EELA--ARQQLEREIREiraqlDDAIEETNKEKAArQKAEKARRDMAE 1156
Cdd:TIGR01612 613 SDK--------NEYIKKAIDLKKIIENNNayiDELAkiSPYQVPEHLKN-----KDKIYSTIKSELS-KIYEDDIDALYN 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1157 ELESYKQE--LEESNDKTVLhSQLKAKRDEEYAHLQKQLEETVKSSEEVVE-----------EMKAQNQKKI-EELNETI 1222
Cdd:TIGR01612 679 ELSSIVKEnaIDNTEDKAKL-DDLKSKIDKEYDKIQNMETATVELHLSNIEnkknelldiivEIKKHIHGEInKDLNKIL 757
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1223 DQL--KRQKISADKAKSSAESDNEN-FRAELSNIAS---------------ARLEAEKKRKAAETSLMEKDHKMR---EM 1281
Cdd:TIGR01612 758 EDFknKEKELSNKINDYAKEKDELNkYKSKISEIKNhyndqinidnikdedAKQNYDKSKEYIKTISIKEDEIFKiinEM 837
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1282 QSNLDDLMAKLSKM----NNELESIQ-------------KAKSADETLNSNLLKKNASLDMqLSELTEASEEDRRTRATL 1344
Cdd:TIGR01612 838 KFMKDDFLNKVDKFinfeNNCKEKIDseheqfaeltnkiKAEISDDKLNDYEKKFNDSKSL-INEINKSIEEEYQNINTL 916
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1345 ---NNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVK--------------SLLAEARKKLDE------------ENR 1395
Cdd:TIGR01612 917 kkvDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKesnlieksykdkfdNTLIDKINELDKafkdaslndyeaKNN 996
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1396 EVMeelRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVvaatremERKMRKFDQQLAEERNNtLLA 1475
Cdd:TIGR01612 997 ELI---KYFNDLKANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNI-------EIAIHTSIYNIIDEIEK-EIG 1065
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1476 QQERDMAHQMLRDAETKALVLsNELSEK-----------------KDIVDQLEKDKRTLKLEIDnlastkddagKNVYEL 1538
Cdd:TIGR01612 1066 KNIELLNKEILEEAEINITNF-NEIKEKlkhynfddfgkeenikyADEINKIKDDIKNLDQKID----------HHIKAL 1134
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1539 EKTKRRLDEELSRAEQQIIELEDalqLADDARSrvevnmqamrseferqlasreedeDDRKKGLTSKIRNLTEELESEQR 1618
Cdd:TIGR01612 1135 EEIKKKSENYIDEIKAQINDLED---VADKAIS------------------------NDDPEEIEKKIENIVTKIDKKKN 1187
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1619 ARQaaiaNKKKIESQISELtEKNEASLRQIEDLS----RQLRKAQLGWKDLQLDVTEAR-AAMEDALAGQRDAEKRARAS 1693
Cdd:TIGR01612 1188 IYD----EIKKLLNEIAEI-EKDKTSLEEVKGINlsygKNLGKLFLEKIDEEKKKSEHMiKAMEAYIEDLDEIKEKSPEI 1262
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1694 EDEIKrLTADIQA------VSSSK-RKAEAERDELIEEVSSLRASSFSNEEKRRLEAKVIDLEDQLDEEASANELAQEKV 1766
Cdd:TIGR01612 1263 ENEMG-IEMDIKAemetfnISHDDdKDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDI 1341
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71983975 1767 RKSQQQLEQMTADLAME--RSVCERTESDKIALERANRDLKQQLQDAEnTAVARLRTQINVAEAKvSSLEQQL 1837
Cdd:TIGR01612 1342 NLYLNEIANIYNILKLNkiKKIIDEVKEYTKEIEENNKNIKDELDKSE-KLIKKIKDDINLEECK-SKIESTL 1412
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1632-1881 |
2.91e-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: 55.16 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1632 SQISELTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAvsssk 1711
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1712 rkAEAERDELIEEVSSLRASSFSNEEKRRLeaKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTE 1791
Cdd:COG4942 95 --LRAELEAQKEELAELLRALYRLGRQPPL--ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1792 SDKIALERANRDLKQQLQdaentavaRLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQ 1871
Cdd:COG4942 171 AERAELEALLAELEEERA--------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|
gi 71983975 1872 GESNRQAVDR 1881
Cdd:COG4942 243 TPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1468-1914 |
2.94e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1468 ERNNTLLAQQERDMAHQMLRDAETKALVlsNELSEKKDIVDQLEKDKRTLKLEIDNLaSTKDDAGKNVYELEKTKRRLD- 1546
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQ--EELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAe 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1547 -----EELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQLASREEDEDDRKKGLTSKIRNLTEELESEQRARQ 1621
Cdd:COG4717 144 lperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1622 AAIANKKKIESQiseltekneaslRQIEDLSRQLRKAQLGWKdlqldvteARAAMEDALAGQRDAEKRARASEDEIKRLT 1701
Cdd:COG4717 224 ELEEELEQLENE------------LEAAALEERLKEARLLLL--------IAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1702 ADIQAVSSSKRKAEAERDELIEEVSSLRA-SSFSNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADL 1780
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPAlEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1781 AMERSVCERTESDKIALERANRDLKQQLQDAEntavarlrtQINVAEAKVSSLEQQLS--LEEQDKMRQGRTLRRMETKM 1858
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEQAE---------EYQELKEELEELEEQLEelLGELEELLEALDEEELEEEL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1859 AEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQ--LEDTEAERDRLTNKLKDERRRA 1914
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEW 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
990-1397 |
3.31e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 990 LKELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRA 1069
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1070 AET--QLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIR----EIRAQLDDAIEETNKEKAA 1143
Cdd:COG4717 128 LPLyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1144 RQKAEKARRDMAEELESYKQELEESNDKTVLHSQLKAKRDEEY-----------AHLQKQLEETVKSSEEVV-------- 1204
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallalLGLGGSLLSLILTIAGVLflvlglla 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1205 ------EEMKAQNQKKIEELN--ETIDQLKRQKISADKAKSSAESDNENFRAElsniASARLEAEKKRKAAETSLMEKDH 1276
Cdd:COG4717 288 llflllAREKASLGKEAEELQalPALEELEEEELEELLAALGLPPDLSPEELL----ELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1277 KMREMQSNLDDLMAKlSKMNNELESIQKAKSADEtlNSNLLKKNASLDMQLSELTEASEE--DRRTRATLNNKIRQLEED 1354
Cdd:COG4717 364 QLEELEQEIAALLAE-AGVEDEEELRAALEQAEE--YQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEE 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 71983975 1355 LAVAVEARDDALDAQEKIEKEVKEVKS--LLAEARKKLDEENREV 1397
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAEL 485
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
852-1294 |
4.13e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 852 KPLLEVTNKDELIAEReQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDA--ESSERAEIFEERSRMAARRDE 929
Cdd:COG4717 65 KPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 930 LEGILEEVSKRL----EIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGN 1005
Cdd:COG4717 144 LPERLEELEERLeelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1006 KLSKEKKALEERCEDLS-SRLIDEVERSKQLVKAKARLEATVAEINDELEK----------------EKQQRHNAETARR 1068
Cdd:COG4717 224 ELEEELEQLENELEAAAlEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallfLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1069 AAETQLREEQEScLEKTRKAEELTNQLMRKESELSQISIrNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAE 1148
Cdd:COG4717 304 AEELQALPALEE-LEEEELEELLAALGLPPDLSPEELLE-LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1149 KARRDMAEELESYKQELEESNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQ 1228
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1229 --KISADKAKSSAESDNENFRAELSNIAsarlEAEKKRKAAETSLmeKDHKMREMQSNLDDLMAKLSK 1294
Cdd:COG4717 462 leQLEEDGELAELLQELEELKAELRELA----EEWAALKLALELL--EEAREEYREERLPPVLERASE 523
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
887-1726 |
4.99e-07 |
|
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: 55.44 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 887 DYKQQMEKMDEERLVLKTRLDaesseraEIFEERSRMAARRDElegILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLE 966
Cdd:TIGR01612 808 DAKQNYDKSKEYIKTISIKED-------EIFKIINEMKFMKDD---FLNKVDKFINFENNCKEKIDSEHEQFAELTNKIK 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 967 ENLEDEERS--------RQKLLLE-KNSIESR-------------LKELEAQGLELEDSGNKLSKEKKALEERcedlssr 1024
Cdd:TIGR01612 878 AEISDDKLNdyekkfndSKSLINEiNKSIEEEyqnintlkkvdeyIKICENTKESIEKFHNKQNILKEILNKN------- 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1025 lIDEVERSKQLVKA-KARLEATVAEINDELEKE-KQQRHNAETARRAAETQLREEQESCLEKTrKAEELTNQLMRKESEL 1102
Cdd:TIGR01612 951 -IDTIKESNLIEKSyKDKFDNTLIDKINELDKAfKDASLNDYEAKNNELIKYFNDLKANLGKN-KENMLYHQFDEKEKAT 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1103 SQISIRNDE--------ELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKAR-RDMAEELESY-------KQELE 1166
Cdd:TIGR01612 1029 NDIEQKIEDanknipniEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINITNfNEIKEKLKHYnfddfgkEENIK 1108
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1167 ESNDKTVLHSQLKaKRDEEYAHLQKQLEETVKSSEEVVEEMKAQ-------------------NQKKIEELNETIDQLKR 1227
Cdd:TIGR01612 1109 YADEINKIKDDIK-NLDQKIDHHIKALEEIKKKSENYIDEIKAQindledvadkaisnddpeeIEKKIENIVTKIDKKKN 1187
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1228 ------------QKISADKAK-SSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHK----MREMQSNLDDLMA 1290
Cdd:TIGR01612 1188 iydeikkllneiAEIEKDKTSlEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEdldeIKEKSPEIENEMG 1267
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1291 KLSKMNNELESIQKAKSADETLNSNLLKKNASldmqLSELTEAS---EEDRRTRATLNNKIRQLEEDLAVAVEARDDALD 1367
Cdd:TIGR01612 1268 IEMDIKAEMETFNISHDDDKDHHIISKKHDEN----ISDIREKSlkiIEDFSEESDINDIKKELQKNLLDAQKHNSDINL 1343
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1368 AQEKIE--------KEVKEVKSLLAEARKKLDEENREVmeelrkkKEKELSAEKERADMAEQARDKAERAKKKAIQEAED 1439
Cdd:TIGR01612 1344 YLNEIAniynilklNKIKKIIDEVKEYTKEIEENNKNI-------KDELDKSEKLIKKIKDDINLEECKSKIESTLDDKD 1416
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1440 VQ---KELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAhqmlrDAETKAlVLSNelsEKKDIVDQLEKDKRT 1516
Cdd:TIGR01612 1417 IDeciKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMA-----DNKSQH-ILKI---KKDNATNDHDFNINE 1487
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1517 LKLEIDNLASTKDDAGKNVYELEKTKrrldEELSRAEQQIIELED---ALQLA---DDARSRVEVNMQAMRSEFERQLAS 1590
Cdd:TIGR01612 1488 LKEHIDKSKGCKDEADKNAKAIEKNK----ELFEQYKKDVTELLNkysALAIKnkfAKTKKDSEIIIKEIKDAHKKFILE 1563
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1591 REEDEDDRKKGLTSKIRnLTEELESEQRARQAAIANKKKIES------QISELTEKNEASLRQIEDLSRQLRKAQLGWKD 1664
Cdd:TIGR01612 1564 AEKSEQKIKEIKKEKFR-IEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKKINDCLKETESIEKKISSFSIDSQD 1642
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983975 1665 LQL-DVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQA----VSSSKRKAEAERDELIEEVS 1726
Cdd:TIGR01612 1643 TELkENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKieidVDQHKKNYEIGIIEKIKEIA 1709
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
976-1660 |
5.16e-07 |
|
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: 55.44 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 976 RQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKA---LEERCEDLSSRLI---DEVERSKQLVKAKARLEATVA-- 1047
Cdd:TIGR01612 1557 HKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAaidIQLSLENFENKFLkisDIKKKINDCLKETESIEKKISsf 1636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1048 EINDELEKEKQQRHNAETARRAAETqLREEQESCLEKTRKAEELTNQLMRKESELSQ---------ISIRNDEELAARQQ 1118
Cdd:TIGR01612 1637 SIDSQDTELKENGDNLNSLQEFLES-LKDQKKNIEDKKKELDELDSEIEKIEIDVDQhkknyeigiIEKIKEIAIANKEE 1715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1119 LEREIREIRAQLDDAIEETNKEKA----ARQKAEKARRDMA----EELESYK---QELEESNDKTVLHSQLKAKRDEEYA 1187
Cdd:TIGR01612 1716 IESIKELIEPTIENLISSFNTNDLegidPNEKLEEYNTEIGdiyeEFIELYNiiaGCLETVSKEPITYDEIKNTRINAQN 1795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1188 HLQKQLEETVKSSEEVveemkaqNQKKIEELNETIDQLKrqkisadkakSSAESDNENFRAELSNIASARLEAEK----- 1262
Cdd:TIGR01612 1796 EFLKIIEIEKKSKSYL-------DDIEAKEFDRIINHFK----------KKLDHVNDKFTKEYSKINEGFDDISKsienv 1858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1263 KRKAAETSLMEKDHKMREMQSNL------------DDLMAKLSKMNNELE-SIQKAKSADETLNSNL------------- 1316
Cdd:TIGR01612 1859 KNSTDENLLFDILNKTKDAYAGIigkkyysykdeaEKIFINISKLANSINiQIQNNSGIDLFDNINIailssldsekedt 1938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1317 --------------LKKNASLDMQLSELTEASEEDRRTRATLN--NKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVK 1380
Cdd:TIGR01612 1939 lkfipspekepeiyTKIRDSYDTLLDIFKKSQDLHKKEQDTLNiiFENQQLYEKIQASNELKDTLSDLKYKKEKILNDVK 2018
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1381 SLLaearKKLDEENRevmeELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQ--EAEDVQKELTDVVAATREME--- 1455
Cdd:TIGR01612 2019 LLL----HKFDELNK----LSCDSQNYDTILELSKQDKIKEKIDNYEKEKEKFGIdfDVKAMEEKFDNDIKDIEKFEnny 2090
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1456 RKMRKFDQQLAEERNNTLlaqQERDMAHQMLRDAETKALVLSNELSEKKDIVDQL-EKDKRTLKLEIDNLASTKDDAGKN 1534
Cdd:TIGR01612 2091 KHSEKDNHDFSEEKDNII---QSKKKLKELTEAFNTEIKIIEDKIIEKNDLIDKLiEMRKECLLFSYATLVETLKSKVIN 2167
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1535 VYELEKTKRRLDEELSraeQQIIELEDALQLADDARsRVEVNMQAMRSEFERQLASREEDED---DRKKGLTSKIRNLTE 1611
Cdd:TIGR01612 2168 HSEFITSAAKFSKDFF---EFIEDISDSLNDDIDAL-QIKYNLNQTKKHMISILADATKDHNnliEKEKEATKIINNLTE 2243
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 71983975 1612 ELESEQRARQAAIANKKKIesQISELTEKNEASLRQIEDLSRQLRKAQL 1660
Cdd:TIGR01612 2244 LFTIDFNNADADILHNNKI--QIIYFNSELHKSIESIKKLYKKINAFKL 2290
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1726-1937 |
6.31e-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: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1726 SSLRASSFSNEEKRRLEAKVIDLEDQLDEEASANEL--AQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRD 1803
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1804 LKQQLQDA-ENTAVARLRTQINVAEAKVSSLEQQLSleeqdkmRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQA-VDR 1881
Cdd:COG3206 252 GPDALPELlQSPVIQQLRAQLAELEAELAELSARYT-------PNHPDVIALRAQIAALRAQLQQEAQRILASLEAeLEA 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1882 QNARIRQLRTQLEDTEAERDRLtNKLKDERRRAEEMTDLNETLSRdvSLLKQRETT 1937
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAEL-PELEAELRRLEREVEVARELYE--SLLQRLEEA 377
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1482-1717 |
6.97e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1482 AHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELED 1561
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1562 ALQLADDARSRVEVNMQAMRSEFERQLASREEDEDDRKKGLTSkirnlteeLESEQRARQAAIAnkkKIESQISELTEKN 1641
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY--------LKYLAPARREQAE---ELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1642 EASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAE 1717
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1243-1939 |
8.29e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1243 NENFRAELSNIAsarLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESiqkaksADETLNsnlLKKNAs 1322
Cdd:COG3096 276 HANERRELSERA---LELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQA------ASDHLN---LVQTA- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1323 ldMQLSELTEASEEDRrtrATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENRevmeelr 1402
Cdd:COG3096 343 --LRQQEKIERYQEDL---EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQT------- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1403 kkkekelsaekeRADMAEQARDKAERAKK---KAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNntllAQQER 1479
Cdd:COG3096 411 ------------RAIQYQQAVQALEKARAlcgLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADA----ARRQF 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1480 DMAHQMLR---------DAETKALVLSNELSEKKDIVDQLEKDKRTLKlEIDNLASTKDDAGKNVYELEKTKRR------ 1544
Cdd:COG3096 475 EKAYELVCkiageversQAWQTARELLRRYRSQQALAQRLQQLRAQLA-ELEQRLRQQQNAERLLEEFCQRIGQqldaae 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1545 -LDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFeRQLASREEDEDDRKKGLTSKIRNLTEELESEQ---RAR 1620
Cdd:COG3096 554 eLEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI-KELAARAPAWLAAQDALERLREQSGEALADSQevtAAM 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1621 QAAIANKKKIESQISELTEKNEASLRQIEDLS--------RQLRKA-QLGWKDLQL---DVTEARAAMEDALAGQ----- 1683
Cdd:COG3096 633 QQLLEREREATVERDELAARKQALESQIERLSqpggaedpRLLALAeRLGGVLLSEiydDVTLEDAPYFSALYGParhai 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1684 --RDAEKRARASE------DEIKRLTADIQAVSSSKRKAEAERDELIEEVS--SLRASSFSNEE---KRRLEAKVIDLED 1750
Cdd:COG3096 713 vvPDLSAVKEQLAgledcpEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSdrQWRYSRFPEVPlfgRAAREKRLEELRA 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1751 QLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVC--------------ERTESDKiALERANRDLKQQLQDAEN--- 1813
Cdd:COG3096 793 ERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAfapdpeaelaalrqRRSELER-ELAQHRAQEQQLRQQLDQlke 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1814 --TAVARLRTQINV-----AEAKVSSLEQQLSLEEQDKM---RQGRTLRRMETKMAEMQQmleeEKRQGESNRQAVDRQN 1883
Cdd:COG3096 872 qlQLLNKLLPQANLladetLADRLEELREELDAAQEAQAfiqQHGKALAQLEPLVAVLQS----DPEQFEQLQADYLQAK 947
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 71983975 1884 ARIRQLRTQLEDTEAERDRLTN-KLKDERRRAEEMTDLNETLSRDVSLLKQRETTAR 1939
Cdd:COG3096 948 EQQRRLKQQIFALSEVVQRRPHfSYEDAVGLLGENSDLNEKLRARLEQAEEARREAR 1004
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1693-1906 |
8.74e-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: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1693 SEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLrassfsNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQ 1772
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEEL------NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1773 LEQMTADLAMERSVCERTE----SDKIA--LERAnrDLKQQLQDAENTAVARLRTQINVAEAKVSSLEQQLSLEEQDKMR 1846
Cdd:COG3883 88 LGERARALYRSGGSVSYLDvllgSESFSdfLDRL--SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1847 QGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNK 1906
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
911-1079 |
9.26e-07 |
|
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: 52.23 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 911 SERAEIFEERSRMAARRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEdeeRSRQKLLLEKNSiesrl 990
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLGNVRNN----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 991 KELEAqgleledsgnkLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAA 1070
Cdd:COG1579 89 KEYEA-----------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
....*....
gi 71983975 1071 ETQLREEQE 1079
Cdd:COG1579 158 LEELEAERE 166
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
888-1525 |
1.02e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 888 YKQQMEKMDEERLVLKTRLDAESSERAEiFEERSRMaarrdeLEGILEEVSKrlEIEEQKAKKADSESRKLtemvRHL-- 965
Cdd:COG3096 446 FRAKEQQATEEVLELEQKLSVADAARRQ-FEKAYEL------VCKIAGEVER--SQAWQTARELLRRYRSQ----QALaq 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 966 -EENLEDEERSRQKLLLEKNSIESRLKEL-EAQGLELEDSGNkLSKEKKALEERCEDLSSRLIDEVERSKQLvkaKARLE 1043
Cdd:COG3096 513 rLQQLRAQLAELEQRLRQQQNAERLLEEFcQRIGQQLDAAEE-LEELLAELEAQLEELEEQAAEAVEQRSEL---RQQLE 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1044 ATVAEIndeleKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISirnDEELAARQQLEREI 1123
Cdd:COG3096 589 QLRARI-----KELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVER---DELAARKQALESQI 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1124 REIRA----------------------------QLDDAIEETNKEKAARQ----KAEKARRDMAEELESYKQEL------ 1165
Cdd:COG3096 661 ERLSQpggaedprllalaerlggvllseiyddvTLEDAPYFSALYGPARHaivvPDLSAVKEQLAGLEDCPEDLyliegd 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1166 EESNDKTVLHSQLKAKRDeeyahlqkqleeTVKSSE---------EVVEEMKAQNQKKIEELNETIDQLKRQ--KISADK 1234
Cdd:COG3096 741 PDSFDDSVFDAEELEDAV------------VVKLSDrqwrysrfpEVPLFGRAAREKRLEELRAERDELAEQyaKASFDV 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1235 AK-SSAESDNENFRAELSNIA------SARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIqkAKS 1307
Cdd:COG3096 809 QKlQRLHQAFSQFVGGHLAVAfapdpeAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQA--NLL 886
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1308 ADETLNSNLlkknasldMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAveaRDDALDaQEKIEKEVKEVKSLLAEAR 1387
Cdd:COG3096 887 ADETLADRL--------EELREELDAAQEAQAFIQQHGKALAQLEPLVAVL---QSDPEQ-FEQLQADYLQAKEQQRRLK 954
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1388 KKLDE-----ENREVMEELRKKKEKELSAE-----KERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAAtREMERk 1457
Cdd:COG3096 955 QQIFAlsevvQRRPHFSYEDAVGLLGENSDlneklRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSS-RDAKQ- 1032
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1458 mrkfdQQLAEernntlLAQQERDMAHQMLRDAETKALV----LSNELSEKKDIVDQLEKDKRTLKLEIDNLA 1525
Cdd:COG3096 1033 -----QTLQE------LEQELEELGVQADAEAEERARIrrdeLHEELSQNRSRRSQLEKQLTRCEAEMDSLQ 1093
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1188-1392 |
1.03e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.86 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1188 HLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASA--RLEAEKKRK 1265
Cdd:PHA02562 188 MKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAlnKLNTAAAKI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1266 AAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASeedrRTRATLN 1345
Cdd:PHA02562 268 KSKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQS----KKLLELK 343
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 71983975 1346 NKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDE 1392
Cdd:PHA02562 344 NKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1424-1934 |
1.15e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1424 DKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAE-ERNNTLLAQQERDMAHQ--MLRDAETKALVLSNEL 1500
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvLREINEISSELPELREEleKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1501 SEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLdEELSRAEQQIIELEDALQLADDARSRVEV---NM 1577
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKrlsRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1578 QAMRSEFERQLASREEDEDDRK--KGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNeaslrqIEDLSRQL 1655
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEelKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLT------PEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1656 RKAQLGWKDLQLDVTEARAamedalagqrdaekRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRASSFSN 1735
Cdd:PRK03918 394 EELEKAKEEIEEEISKITA--------------RIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1736 EEKRrLEAKVIDLEDQLdEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTES-DKIALERANRDLKqqlqdaent 1814
Cdd:PRK03918 460 ELKR-IEKELKEIEEKE-RKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYE--------- 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1815 avaRLRTQINVAEAKVSSLEQQLSLEEQDKMRqgrtLRRMETKMAEMQQMLEE-EKRQGESNRQAVDRQNARIRQLR--- 1890
Cdd:PRK03918 529 ---KLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAElLKELEELGFESVEELEERLKELEpfy 601
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 71983975 1891 ----------TQLEDTEAERDRLTNKLKDERRRAEEMTDLNETLSRDVSLLKQR 1934
Cdd:PRK03918 602 neylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1631-1935 |
1.24e-06 |
|
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: 53.59 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1631 ESQISELTEKNEAS-LRQ-IEDLSRQLRKAqlgwKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRltadiqaVS 1708
Cdd:pfam17380 286 ERQQQEKFEKMEQErLRQeKEEKAREVERR----RKLEEAEKARQAEMDRQAAIYAEQERMAMERERELER-------IR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1709 SSKRKAEAER---DELIEEVSSLRASSFSNEEKRRLEAKVidlEDQLDEEASANELAQEKVRKSQQQLEQMTaDLAMERS 1785
Cdd:pfam17380 355 QEERKRELERirqEEIAMEISRMRELERLQMERQQKNERV---RQELEAARKVKILEEERQRKIQQQKVEME-QIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1786 VCERTESDKIALERANRDLKQQLQDAE-NTAVARLRTQinVAEAKVSSLEQQlslEEQDKMRQGRTLRRM--ETKMAEMQ 1862
Cdd:pfam17380 431 EARQREVRRLEEERAREMERVRLEEQErQQQVERLRQQ--EEERKRKKLELE---KEKRDRKRAEEQRRKilEKELEERK 505
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1863 Q-MLEEEKRQGESNRQAVDRQNArirqLRTQLEDTEAERDRLTNKLKDERRR-AEEMTDLNETLSRDVSLLKQRE 1935
Cdd:pfam17380 506 QaMIEEERKRKLLEKEMEERQKA----IYEEERRREAEEERRKQQEMEERRRiQEQMRKATEERSRLEAMERERE 576
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1262-1685 |
1.80e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1262 KKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADEtlnsnLLKKNASLDMQLSELTEASEEDRRTR 1341
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-----LYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1342 ATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQ 1421
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1422 ARDKAERAKkkaIQEAEDVQKELTDVVAATREMERKMRKFDQ-----QLAEERNNTLLAQQERDMAHQMLRDAETKALVL 1496
Cdd:COG4717 236 LEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTiagvlFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1497 SNELSEK--KDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVE 1574
Cdd:COG4717 313 LEELEEEelEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1575 -----VNMQAMRSEFERQLASREEDEDDR-----KKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEAS 1644
Cdd:COG4717 393 qaeeyQELKEELEELEEQLEELLGELEELlealdEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA 472
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 71983975 1645 --LRQIEDLSRQLRKAQLGWKDLQLdvteARAAMEDALAGQRD 1685
Cdd:COG4717 473 elLQELEELKAELRELAEEWAALKL----ALELLEEAREEYRE 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
861-1312 |
2.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 861 DELIAEREQELKVTAeklRRSEVFISDYKQQMEKMDEERLVLKtRLDAESSERAEIFEERSRMAARRDELEGILEEVSKR 940
Cdd:COG4717 49 ERLEKEADELFKPQG---RKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 941 LEIEEQKAKKADSEsRKLTEMVRHLEEnLEDEERSRQKLLLEKNSIESRLKELEAQ-GLELEDSGNKLSKEKKALEERCE 1019
Cdd:COG4717 125 LQLLPLYQELEALE-AELAELPERLEE-LEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1020 DLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRA-AETQLREEQESCLEKTRKAEELTNQLMRK 1098
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLlIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1099 ESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKtVLHSQL 1178
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE-AEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1179 KAKRDEEYAHLQKQLEETVKSSEEVVEEmKAQNQKKIEELNETIDQLKRQ--KISADKAKSSAESDNENFRAELSNIASA 1256
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELRA-ALEQAEEYQELKEELEELEEQleELLGELEELLEALDEEELEEELEELEEE 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1257 RLEAEKKRKAAETSLMEKDHKMREMQSN--LDDLMAKLSKMNNELESIQKAKSADETL 1312
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLA 498
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1042-1574 |
2.51e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1042 LEATVAEINDELEKEKQQRH--NAETARRAAET--QLREEQESCLEKTRKAEELTNQLMRKESELSQI--SIRNDEELAA 1115
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPelNLKELKELEEElkEAEEKEEEYAELQEELEELEEELEELEAELEELreELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1116 RQQLEREIREIRAQLDDAIEEtnkekaarqkaekarrdmAEELESYKQELEEsndktvlhsqlkakRDEEYAHLQKQLEE 1195
Cdd:COG4717 127 LLPLYQELEALEAELAELPER------------------LEELEERLEELRE--------------LEEELEELEAELAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1196 TVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKD 1275
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1276 HKMREMQSNLDDLMAKLSKMNNELESIQKAKSAdeTLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDL 1355
Cdd:COG4717 255 AAALLALLGLGGSLLSLILTIAGVLFLVLGLLA--LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1356 AVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKkkekelsaekerADMAEQARDKAERAKKKaiq 1435
Cdd:COG4717 333 DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAG------------VEDEEELRAALEQAEEY--- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1436 eaedvqkeltdvvaatREMERKMRKFDQQLAEERNN--TLLAQQERDMAHQMLRDAETKALVLSNELsekkdivDQLEKD 1513
Cdd:COG4717 398 ----------------QELKEELEELEEQLEELLGEleELLEALDEEELEEELEELEEELEELEEEL-------EELREE 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71983975 1514 KRTLKLEIDNLASTKDDAgknvyELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVE 1574
Cdd:COG4717 455 LAELEAELEQLEEDGELA-----ELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
932-1338 |
2.55e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 52.65 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 932 GILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLE----ENLEDEERSRQKLLLEKNSIESRL------KELEAQGLELE 1001
Cdd:COG5185 135 DELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTqelnQNLKKLEIFGLTLGLLKGISELKKaepsgtVNSIKESETGN 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1002 DSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVaEINDELEKEKqQRHNAETARRAAETqlREEQESC 1081
Cdd:COG5185 215 LGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLV-EQNTDLRLEK-LGENAESSKRLNEN--ANNLIKQ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1082 LEKTRK--AEELTNQLMRKESELSQISIRndeELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELE 1159
Cdd:COG5185 291 FENTKEkiAEYTKSIDIKKATESLEEQLA---AAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1160 SYKQELEESNDKTVLHSQLKAKRdEEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSA 1239
Cdd:COG5185 368 GEVELSKSSEELDSFKDTIESTK-ESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNEL 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1240 ESDNENFRAELSNIASARLEAEKKRKAAE--TSLMEKDHKMREMQSNLDDLMAKLSKMNNELEsIQKAKSADETLNSNLL 1317
Cdd:COG5185 447 ISELNKVMREADEESQSRLEEAYDEINRSvrSKKEDLNEELTQIESRVSTLKATLEKLRAKLE-RQLEGVRSKLDQVAES 525
|
410 420
....*....|....*....|.
gi 71983975 1318 KKNASLDMQLSELTEASEEDR 1338
Cdd:COG5185 526 LKDFMRARGYAHILALENLIP 546
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1070-1275 |
2.65e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1070 AETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQlddaIEETNKEKAARQKAEK 1149
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1150 AR-RDMAEE--LESYKQELEESNDKTVLHSQLKAKRDeeYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLK 1226
Cdd:COG3883 90 ERaRALYRSggSVSYLDVLLGSESFSDFLDRLSALSK--IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 71983975 1227 RQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKD 1275
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
913-1346 |
2.65e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 913 RAEIFEERSRMAAR-RDELEGILEEVSKRLEIEEQKAKKADSE-SRKLTEMVRHLEENLEDEERSRQKLlleknsiesrl 990
Cdd:pfam07888 28 RAELLQNRLEECLQeRAELLQAQEAANRQREKEKERYKRDREQwERQRRELESRVAELKEELRQSREKH----------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 991 KELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAA 1070
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1071 ETQLREEQESCLEKTRKAEELTNQLMRKESELSQIS---IRNDEELAARQQLEREIREIRAQLDDAIEETNkekAARQKA 1147
Cdd:pfam07888 177 QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtiTTLTQKLTTAHRKEAENEALLEELRSLQERLN---ASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1148 EKARRDMAE----------ELESYKQELEESNDKTvlhSQLKAKRDEEYAHLQKQ---LEETVKSSEEVVEEMKAQNQKK 1214
Cdd:pfam07888 254 EGLGEELSSmaaqrdrtqaELHQARLQAAQLTLQL---ADASLALREGRARWAQEretLQQSAEADKDRIEKLSAELQRL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1215 IEELNEtiDQLKRQKISADKAKssaESDnenfrAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQsnldDLMAKLSK 1294
Cdd:pfam07888 331 EERLQE--ERMEREKLEVELGR---EKD-----CNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQ----ELLEYIRQ 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1295 MNNELESIQKAKSADETLNSnllkkNASLDMQLSELTEASEEDRRTRATLNN 1346
Cdd:pfam07888 397 LEQRLETVADAKWSEAALTS-----TERPDSPLSDSEDENPEALQPPRPLGH 443
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1419-1662 |
2.82e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1419 AEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSN 1498
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1499 ELSEKKD----IVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRve 1574
Cdd:COG4942 98 ELEAQKEelaeLLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1575 vnMQAMRSEFERQLASREEDEDDRKKgltsKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQ 1654
Cdd:COG4942 176 --LEALLAELEEERAALEALKAERQK----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*...
gi 71983975 1655 LRKAQLGW 1662
Cdd:COG4942 250 ALKGKLPW 257
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
869-1528 |
3.06e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.74 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 869 QELKVTAEKLRRSEVFISDYKQQMEKMDEERLV--LKTRLDAESSERAEIFEERSRMAARRDELEgilEEVSKRLEIEEQ 946
Cdd:TIGR00606 464 QQLEGSSDRILELDQELRKAERELSKAEKNSLTetLKKEVKSLQNEKADLDRKLRKLDQEMEQLN---HHTTTRTQMEML 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 947 KAKKADSESRKLTEMVRHLEE---------NLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEER 1017
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDEltsllgyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1018 -------------CEDLSSRLIDEVERSKQLVKAKARLEATVA---EINDELEKEKQQRHNAETARRAAETQLREEQESC 1081
Cdd:TIGR00606 621 lssyedklfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAvysQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1082 LEKTR----KAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEE 1157
Cdd:TIGR00606 701 QSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1158 LESYKQELeesNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKR-QKISADKAK 1236
Cdd:TIGR00606 781 EESAKVCL---TDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELnRKLIQDQQE 857
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1237 SSaesdnENFRAELSNIASARL---EAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKsadETLN 1313
Cdd:TIGR00606 858 QI-----QHLKSKTNELKSEKLqigTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK---EELI 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1314 SNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQ-EKIEKEVKEVKSLLAEARKKLD- 1391
Cdd:TIGR00606 930 SSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQlEECEKHQEKINEDMRLMRQDIDt 1009
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1392 --------EENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQ 1463
Cdd:TIGR00606 1010 qkiqerwlQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKK 1089
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1464 QLAEERnntllaqqerdmahqmLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTK 1528
Cdd:TIGR00606 1090 ELREPQ----------------FRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMK 1138
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1428-1809 |
3.28e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.61 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1428 RAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIV 1507
Cdd:pfam19220 41 RELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1508 DQLEkdkRTLKLEIDNLAStkddagknvyeLEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQ 1587
Cdd:pfam19220 121 EALE---RQLAAETEQNRA-----------LEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1588 LASreededdrkkglTSKIRNLTEELESEQRARQAAIAnkkKIESQISELTEKNEASLRQIEDlSRQLRKAQLGWKDLQL 1667
Cdd:pfam19220 187 AAE------------LAELTRRLAELETQLDATRARLR---ALEGQLAAEQAERERAEAQLEE-AVEAHRAERASLRMKL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1668 DVTEARAAMEDALAGQRDAEKRARASEdeikrltadIQAVSSSKRKAEAERDELIEEVSSLRASSFSNEEKRR------- 1740
Cdd:pfam19220 251 EALTARAAATEQLLAEARNQLRDRDEA---------IRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQemqrara 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1741 -LEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLamersvcertESDKIALERANRDLKQQLQ 1809
Cdd:pfam19220 322 eLEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRF----------EVERAALEQANRRLKEELQ 381
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1428-1916 |
3.79e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1428 RAKKKAIQEAEDVQKELTDVVAATREMERKMRKfdqqlaeernNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIV 1507
Cdd:pfam05483 78 RLYSKLYKEAEKIKKWKVSIEAELKQKENKLQE----------NRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1508 DQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQ 1587
Cdd:pfam05483 148 KENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1588 LASREEDEDDRKKGLT----------SKIRNLTEELEsEQRARQAAIANKKKIESQ-ISELTEKNEASLRQIEDLSRQLR 1656
Cdd:pfam05483 228 EEEYKKEINDKEKQVSllliqitekeNKMKDLTFLLE-ESRDKANQLEEKTKLQDEnLKELIEKKDHLTKELEDIKMSLQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1657 KAQLGWKDLQLDVT-----------EARAAMEDALAGQ---------------------RDAEKRARASEDEIKRLTADI 1704
Cdd:pfam05483 307 RSMSTQKALEEDLQiatkticqlteEKEAQMEELNKAKaahsfvvtefeattcsleellRTEQQRLEKNEDQLKIITMEL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1705 QAVSSSkrkaeaerdelIEEVSSLRassfSNEEKRRLEAKVIDLEDQ--LDEEASANELAQEKVRKSQ------QQLEQM 1776
Cdd:pfam05483 387 QKKSSE-----------LEEMTKFK----NNKEVELEELKKILAEDEklLDEKKQFEKIAEELKGKEQelifllQAREKE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1777 TADLAMERSVCERTESDKIaleRANRDLKQQLQDAEntavarlrtqinVAEAKVSSLEQQLSLEEQDKMRQGRTlrrMET 1856
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYL---KEVEDLKTELEKEK------------LKNIELTAHCDKLLLENKELTQEASD---MTL 513
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1857 KMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKLKDERRRAEE 1916
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEE 573
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
859-1394 |
3.81e-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: 52.36 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 859 NKDELIAE-REQELKVTAEKLRRSEvfISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEersrmAARRDELEGILEEV 937
Cdd:TIGR01612 1295 KHDENISDiREKSLKIIEDFSEESD--INDIKKELQKNLLDAQKHNSDINLYLNEIANIYN-----ILKLNKIKKIIDEV 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 938 SKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEE-RSRQKLLLEKNSIE---SRLKELEAQGLELEDSGNKLSKEKKA 1013
Cdd:TIGR01612 1368 KEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEEcKSKIESTLDDKDIDeciKKIKELKNHILSEESNIDTYFKNADE 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1014 LEERCEDLSSRLIDEVERSKQLVK-----AKARLEATVAEINDELEKEKQQRHNAETARRAAET------QLREEQESCL 1082
Cdd:TIGR01612 1448 NNENVLLLFKNIEMADNKSQHILKikkdnATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkelfeQYKKDVTELL 1527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1083 EKTrKAEELTNQLMRKESELSQIsIRNDEELAARQQLEREIREIRaqlddaIEETNKEK-------AARQKAEKARRDMA 1155
Cdd:TIGR01612 1528 NKY-SALAIKNKFAKTKKDSEII-IKEIKDAHKKFILEAEKSEQK------IKEIKKEKfrieddaAKNDKSNKAAIDIQ 1599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1156 EELESYKQE-LEESNDKTVLHSQLKakrdeEYAHLQKQLEETVKSSEEVveEMKaQNQKKIEELNETIDQLKRQKISADK 1234
Cdd:TIGR01612 1600 LSLENFENKfLKISDIKKKINDCLK-----ETESIEKKISSFSIDSQDT--ELK-ENGDNLNSLQEFLESLKDQKKNIED 1671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1235 AKSsaESDNENfraelSNIASARLEAEKKRKAAETSLMEKDHKMremqsnlddlmAKLSKmnNELESIQKA-----KSAD 1309
Cdd:TIGR01612 1672 KKK--ELDELD-----SEIEKIEIDVDQHKKNYEIGIIEKIKEI-----------AIANK--EEIESIKELieptiENLI 1731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1310 ETLNSNLLK---KNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEK------------ 1374
Cdd:TIGR01612 1732 SSFNTNDLEgidPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTRINAQNEFLKiieiekksksyl 1811
|
570 580
....*....|....*....|...
gi 71983975 1375 ---EVKEVKSLLAEARKKLDEEN 1394
Cdd:TIGR01612 1812 ddiEAKEFDRIINHFKKKLDHVN 1834
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
889-1269 |
4.11e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 51.95 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 889 KQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEevskRLEIEEQKAKKaDSESRKLteMVRHLEEN 968
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLE----RAQTEEAQAKQ-DSELAKL--RVEEMEQG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 969 LEDEERSRQKLLLE--KNSIESRLKELEAQGLELEdsgnklskekkALEERCEDLSSRLIDEVERSKQLVKAKARLEATV 1046
Cdd:pfam05701 114 IADEASVAAKAQLEvaKARHAAAVAELKSVKEELE-----------SLRKEYASLVSERDIAIKRAEEAVSASKEIEKTV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1047 AEINDELEKEKQQRHNAETARRAAetqlrEEQESCLEKTRKAEELT--NQLMRKESELSQIsirnDEELAARQQLEREIR 1124
Cdd:pfam05701 183 EELTIELIATKESLESAHAAHLEA-----EEHRIGAALAREQDKLNweKELKQAEEELQRL----NQQLLSAKDLKSKLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1125 E-------IRAQLDDAIEET-NKEKAARQKAEKARRDMAEELESYKQELE-----------ESNDKTVLHSQLKAKRDEE 1185
Cdd:pfam05701 254 TasallldLKAELAAYMESKlKEEADGEGNEKKTSTSIQAALASAKKELEevkaniekakdEVNCLRVAAASLRSELEKE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1186 YAHLQ--KQLE--------------ETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQkisADKAKSSAESDNENFRAe 1249
Cdd:pfam05701 334 KAELAslRQREgmasiavssleaelNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQE---AEEAKSLAQAAREELRK- 409
|
410 420
....*....|....*....|
gi 71983975 1250 lsniasARLEAEKKRKAAET 1269
Cdd:pfam05701 410 ------AKEEAEQAKAAAST 423
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
905-1239 |
4.14e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 905 RLDAESSERAEIFEERSRMAARRDELEGILEEVSKRLEIEEQKAKKADSE------SRKLTEMVRHLEENLEDEERSRQK 978
Cdd:PRK04863 787 RIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEaelrqlNRRRVELERALADHESQEQQQRSQ 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 979 LLLEKNSIeSRLKELEAQGLELEDsgNKLSKEKKALEERcedlssrlIDEVERSKQLV----KAKARLEATVAEIN---D 1051
Cdd:PRK04863 867 LEQAKEGL-SALNRLLPRLNLLAD--ETLADRVEEIREQ--------LDEAEEAKRFVqqhgNALAQLEPIVSVLQsdpE 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1052 ELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSqisirndEELAARQ-QLEREIREIRAQL 1130
Cdd:PRK04863 936 QFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLN-------EKLRQRLeQAEQERTRAREQL 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1131 DDAIEETNKEKAARQKAEKARRDMAEELESYKQELEE-------------SNDKTVLHSQLKAKRdEEYAHLQKQLeetv 1197
Cdd:PRK04863 1009 RQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpadsgaeeraRARRDELHARLSANR-SRRNQLEKQL---- 1083
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 71983975 1198 kSSEEvvEEMKAQNqKKIEELNETIDQLKRQKISADKAKSSA 1239
Cdd:PRK04863 1084 -TFCE--AEMDNLT-KKLRKLERDYHEMREQVVNAKAGWCAV 1121
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1114-1309 |
4.84e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1114 AARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKTVLHSQLKAKRDEEYAHLQKQL 1193
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1194 EETVKSSEEVV-------------------------------EEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESD 1242
Cdd:COG4942 100 EAQKEELAELLralyrlgrqpplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983975 1243 NENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSAD 1309
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1792-1933 |
4.95e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 50.73 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1792 SDKIALERANrdlKQQLQDAentaVARLRTQINVAEAKVSSLEQQLsleeqDKMRQGRTlrRMETKMAEMQQMLEEEKRQ 1871
Cdd:PRK09039 66 ADLLSLERQG---NQDLQDS----VANLRASLSAAEAERSRLQALL-----AELAGAGA--AAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71983975 1872 GESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKLKDERRRAEEM-TDLNETLSRDVSLLKQ 1933
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRLNVALAQRVQELNR 194
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
974-1158 |
5.36e-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: 49.92 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 974 RSRQKLLLEKNSIESRLKELEAQGLELEdsgnklsKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDEL 1053
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELP-------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1054 EKEKQQRHNAETARRAaeTQLREEQESCLEKTRKAEELTNQLMRKESELSQisiRNDEELAARQQLEREIREIRAQLDDA 1133
Cdd:COG1579 76 KKYEEQLGNVRNNKEY--EALQKEIESLKRRISDLEDEILELMERIEELEE---ELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|....*.
gi 71983975 1134 IEETNKE-KAARQKAEKARRDMAEEL 1158
Cdd:COG1579 151 LAELEAElEELEAEREELAAKIPPEL 176
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1166-1908 |
6.53e-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: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1166 EESNDKTVLHSQLKAKRdEEYAHLQKQLEEtvksseeVVEEMKAQnqkkiEELNETIDQlkrqkisaDKAKSSAESDNEN 1245
Cdd:pfam10174 50 EEAARISVLKEQYRVTQ-EENQHLQLTIQA-------LQDELRAQ-----RDLNQLLQQ--------DFTTSPVDGEDKF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1246 FRAELSNIASARLEAEKKRKAAETSLMEKdhKMREMQSNLDdlmAKLSKMNNELESIQKAKsadETLNSNLLKKNASLD- 1324
Cdd:pfam10174 109 STPELTEENFRRLQSEHERQAKELFLLRK--TLEEMELRIE---TQKQTLGARDESIKKLL---EMLQSKGLPKKSGEEd 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1325 ----MQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDAldAQEKIEKEVKEVK-SLLAEARKKLDEENREVME 1399
Cdd:pfam10174 181 wertRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDP--AKTKALQTVIEMKdTKISSLERNIRDLEDEVQM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1400 ELRKKKEKELSAEKERADMaEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFD--QQLAEERNNTLLAQQ 1477
Cdd:pfam10174 259 LKTNGLLHTEDREEEIKQM-EVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSdcKQHIEVLKESLTAKE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1478 ERDMAHQmlrdAETKALVLSNE-----LSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRA 1552
Cdd:pfam10174 338 QRAAILQ----TEVDALRLRLEekesfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1553 EQQIIELEDALQladdarsrvevNMQAMRSEFERQLASREEDEDDRKKgltsKIRNLTEELESEQRARQAAIAN------ 1626
Cdd:pfam10174 414 DKQLAGLKERVK-----------SLQTDSSNTDTALTTLEEALSEKER----IIERLKEQREREDRERLEELESlkkenk 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1627 --KKKIESQISELTEKnEASLRQIEDLSRQLR----KAQLGWKDLQLDV---TEARAAMEDALAGQRDAEKRARASE--- 1694
Cdd:pfam10174 479 dlKEKVSALQPELTEK-ESSLIDLKEHASSLAssglKKDSKLKSLEIAVeqkKEECSKLENQLKKAHNAEEAVRTNPein 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1695 DEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRassfsnEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLE 1774
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVE------NEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMK 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1775 QMTADLAMERSVCERTESDKIAleranrdlKQQLQDAENtAVARLRTQINVAEAKVSSLEQqlSLEEQD----KMRQGRT 1850
Cdd:pfam10174 632 KKGAQLLEEARRREDNLADNSQ--------QLQLEELMG-ALEKTRQELDATKARLSSTQQ--SLAEKDghltNLRAERR 700
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1851 lRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKLK 1908
Cdd:pfam10174 701 -KQLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREKDRLVHQLK 757
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1267-1453 |
7.14e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1267 AETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKsadETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNN 1346
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEY---NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1347 KIRQLEE------------------DLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKE 1408
Cdd:COG3883 91 RARALYRsggsvsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71983975 1409 LSAEKERADM-AEQARDKAERAKKKAIQEAEDVQKELTDVVAATRE 1453
Cdd:COG3883 171 AELEAQQAEQeALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1629-1936 |
7.46e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1629 KIESQISELTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDeIKRLTADIQAVS 1708
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQAD-LEELEERLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1709 SSKRKAEAERDELIEEVSSlrassfSNEEKRRLEAKVIDLEDQLDEE---ASANELAQEKVRKSQQ--QLEQMTADLAME 1783
Cdd:PRK04863 369 EVVEEADEQQEENEARAEA------AEEEVDELKSQLADYQQALDVQqtrAIQYQQAVQALERAKQlcGLPDLTADNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1784 RSVCERTESDKIALERanRDLKQQLQDAENTavarlRTQINVAEAKVSSLEQQLSLEE-----QDKMRQGRTLR------ 1852
Cdd:PRK04863 443 WLEEFQAKEQEATEEL--LSLEQKLSVAQAA-----HSQFEQAYQLVRKIAGEVSRSEawdvaRELLRRLREQRhlaeql 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1853 -RMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIR---QLRTQLEDTEAERDRLTNKLKDERRRAEEMTDLNETLSRDV 1928
Cdd:PRK04863 516 qQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDdedELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARI 595
|
....*...
gi 71983975 1929 SLLKQRET 1936
Cdd:PRK04863 596 QRLAARAP 603
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
859-1208 |
7.84e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 51.08 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 859 NKDELIAEREQeLKVTAEKLRRSEVF-ISDYKQQmekmdeerlvlktrldaESSERA-EIFEERSRMAARRDELEGILEE 936
Cdd:PRK05771 7 KKVLIVTLKSY-KDEVLEALHELGVVhIEDLKEE-----------------LSNERLrKLRSLLTKLSEALDKLRSYLPK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 937 VSKRLEiEEQKAKKADSEsrkltEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEaqgleledsgnklsKEKKALeE 1016
Cdd:PRK05771 69 LNPLRE-EKKKVSVKSLE-----ELIKDVEEELEKIEKEIKELEEEISELENEIKELE--------------QEIERL-E 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1017 RCEDLSSRLIDevERSKQLVKAKArleATVAEINDELEKEKQQRHNAETARRAAET------QLREeqesclektrKAEE 1090
Cdd:PRK05771 128 PWGNFDLDLSL--LLGFKYVSVFV---GTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvVLKE----------LSDE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1091 LTNQLmrKESELSQISIRNDEELAAR-QQLEREIREIRAQLDDAIEEtnkekaARQKAEKARRDMAEELESYKQELEESN 1169
Cdd:PRK05771 193 VEEEL--KKLGFERLELEEEGTPSELiREIKEELEEIEKERESLLEE------LKELAKKYLEELLALYEYLEIELERAE 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 71983975 1170 DKtvlhsqLKAKRDEEYAHLQ--------KQLEETVKSSEE---VVEEMK 1208
Cdd:PRK05771 265 AL------SKFLKTDKTFAIEgwvpedrvKKLKELIDKATGgsaYVEFVE 308
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1665-1892 |
8.43e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1665 LQLDVTEARAAMEdALAGQ-RDAEKRARASEDEIKRLTADIQAVSsskrkAEAERDELIEEVSSLRASSFSNEEKRR-LE 1742
Cdd:COG3206 166 LELRREEARKALE-FLEEQlPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAeAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1743 AKVIDLEDQL--DEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQQLQDAENTAVARLR 1820
Cdd:COG3206 240 ARLAALRAQLgsGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1821 TQINVAEAKVSSLEQQLSLEEQDkmrqgrtLRRMETKMAEMQQMleeeKRQGESNRQAVDRQNARIRQLRTQ 1892
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEAR-------LAELPELEAELRRL----EREVEVARELYESLLQRLEEARLA 380
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1292-1775 |
8.55e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1292 LSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQE- 1370
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1371 -KIEKEVKEVKSLLAEARKKLDEENREvMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVA 1449
Cdd:COG4717 128 lPLYQELEALEAELAELPERLEELEER-LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1450 ATREMERKMRKFDQQL--AEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLAST 1527
Cdd:COG4717 207 RLAELEEELEEAQEELeeLEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1528 KDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQlasreededDRKKGLTSKIR 1607
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI---------EELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1608 NLTEELE-SEQRARQAAIANKKKIESqiselteknEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDA 1686
Cdd:COG4717 358 ELEEELQlEELEQEIAALLAEAGVED---------EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1687 EkraraSEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRASSFSNEEKRRLEAKVIDLEdQLDEEASANELAQEKV 1766
Cdd:COG4717 429 E-----LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELR-ELAEEWAALKLALELL 502
|
....*....
gi 71983975 1767 RKSQQQLEQ 1775
Cdd:COG4717 503 EEAREEYRE 511
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1607-1915 |
9.28e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1607 RNLTEELESEQRARQAAIANKKKIESQISELteknEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMedaLAGQRDA 1686
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAEL----KEELRQSREKHEELEEKYKELSASSEELSEEKDAL---LAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1687 EKRARASEDEIKRLT-------ADIQAVSSSKRKAEAERDELIEEVSSLRAS-SFSNEEKRRLEAKVIDLEDQLDEEASA 1758
Cdd:pfam07888 128 EARIRELEEDIKTLTqrvlereTELERMKERAKKAGAQRKEEEAERKQLQAKlQQTEEELRSLSKEFQELRNSLAQRDTQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1759 NELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQQLQDAENTAVARLRTQINVAEAKVSSLEQQLS 1838
Cdd:pfam07888 208 VLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1839 LEEQD-KMRQGRTlrRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQLEDTEAE--RDRLTNKLKDERRRAE 1915
Cdd:pfam07888 288 LADASlALREGRA--RWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVElgREKDCNRVQLSESRRE 365
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
856-1068 |
1.15e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 856 EVTNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIfeeRSRMAARRDELEGILE 935
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---RAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 936 EVSKRLEIEE-------QKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLS 1008
Cdd:COG4942 112 ALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1009 KEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARR 1068
Cdd:COG4942 192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
936-1128 |
1.23e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 50.09 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 936 EVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALE 1015
Cdd:PRK12705 36 ERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1016 ERCEDLS---SRLIDEVERSKQLVKAKARlEATVAEINDELEKEKQQRHNAetarraaetqlrEEQESCLEKTRKAEELT 1092
Cdd:PRK12705 116 ARELELEeleKQLDNELYRVAGLTPEQAR-KLLLKLLDAELEEEKAQRVKK------------IEEEADLEAERKAQNIL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71983975 1093 NQLM-RKESEL-SQISIRN----DEELAARqQLEREIREIRA 1128
Cdd:PRK12705 183 AQAMqRIASETaSDLSVSVvpipSDAMKGR-IIGREGRNIRA 223
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1205-1439 |
1.25e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1205 EEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSniasarlEAEKKRKAAETSLMEKDHKMREMQSN 1284
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-------ALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1285 LDDLMAKLSK---MNNELESIQKAKSADETLNsnllkknasldmQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEA 1361
Cdd:COG3883 88 LGERARALYRsggSVSYLDVLLGSESFSDFLD------------RLSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1362 RDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAED 1439
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
862-1108 |
1.37e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 862 ELIAEREQELKvtaeklrrsevfisdykqqmekmdeerlVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRL 941
Cdd:COG4942 20 DAAAEAEAELE----------------------------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 942 EIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLL--LEKNSIESRLKELEAQG--LELEDSGNKLSKEKKALEER 1017
Cdd:COG4942 72 RALEQELAALEAELAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1018 CEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMR 1097
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|.
gi 71983975 1098 KESELSQISIR 1108
Cdd:COG4942 232 LEAEAAAAAER 242
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1514-1824 |
1.38e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.60 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1514 KRTLKLEIDNLAS--TKDDAGKNVyelektkrRLDEELSRAEQQIIELEDALQLADDARSRVEV---NMQAMRSEFERQL 1588
Cdd:NF012221 1537 TSESSQQADAVSKhaKQDDAAQNA--------LADKERAEADRQRLEQEKQQQLAAISGSQSQLestDQNALETNGQAQR 1608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1589 ASREEDEDDRKKGLTSKIRNL-------TEELESEQRAR-QAAIANKKKIESQiseLTEKNEASLRQIEDLSRQLrkaql 1660
Cdd:NF012221 1609 DAILEESRAVTKELTTLAQGLdaldsqaTYAGESGDQWRnPFAGGLLDRVQEQ---LDDAKKISGKQLADAKQRH----- 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1661 gwKDLQLDVTEARAAMEdalAGQRDAEKRARASEDEIKRLTADiqavsSSKRKAEAERDELIEEVSSLRASSFSNEEKRR 1740
Cdd:NF012221 1681 --VDNQQKVKDAVAKSE---AGVAQGEQNQANAEQDIDDAKAD-----AEKRKDDALAKQNEAQQAESDANAAANDAQSR 1750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1741 LEAKVIDLEDQLDE-EASANELAQEKVRKSQQQL--------EQMTADLAMERSVCERTESDKIALERANRDLKQQLQDA 1811
Cdd:NF012221 1751 GEQDASAAENKANQaQADAKGAKQDESDKPNRQGaagsglsgKAYSVEGVAEPGSHINPDSPAAADGRFSEGLTEQEQEA 1830
|
330
....*....|....
gi 71983975 1812 ENTAVARL-RTQIN 1824
Cdd:NF012221 1831 LEGATNAVnRLQIN 1844
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
924-1184 |
1.59e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 924 AARRDELEGILE--EVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEdeerSRQKLLLEKNSIES-RLKELEAQGLEL 1000
Cdd:PHA02562 150 PARRKLVEDLLDisVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIK----TYNKNIEEQRKKNGeNIARKQNKYDEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1001 EDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDElekEKQQRHNAETArrAAETQLREEQES 1080
Cdd:PHA02562 226 VEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV---IKMYEKGGVCP--TCTQQISEGPDR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1081 CLEKTRKAEELT---NQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEE 1157
Cdd:PHA02562 301 ITKIKDKLKELQhslEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEE 380
|
250 260
....*....|....*....|....*..
gi 71983975 1158 LESYKQELEESNDKtvlHSQLKAKRDE 1184
Cdd:PHA02562 381 LAKLQDELDKIVKT---KSELVKEKYH 404
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
882-1708 |
1.70e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 882 EVFISDYKQQMEKMDEERLVLKTRLDAeSSERAEIFEERSRMAARrdelegILEEVSKRLEIEEQKAKKADSES-RKLTE 960
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQKLSV-AQAAHSQFEQAYQLVRK------IAGEVSRSEAWDVARELLRRLREqRHLAE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 961 MVRHLEENLEDEERSRQklllEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLvkaKA 1040
Cdd:PRK04863 514 QLQQLRMRLSELEQRLR----QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL---RQ 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1041 RLEATVAEINdELEKEKQQRHNAetarRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQisiRNDEELAARQQLE 1120
Cdd:PRK04863 587 QLEQLQARIQ-RLAARAPAWLAA----QDALARLREQSGEEFEDSQDVTEYMQQLLERERELTV---ERDELAARKQALD 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1121 REIREIRA----------------------------QLDDA-------------IEETNKEKAARQKAekARRDMAEEL- 1158
Cdd:PRK04863 659 EEIERLSQpggsedprlnalaerfggvllseiyddvSLEDApyfsalygparhaIVVPDLSDAAEQLA--GLEDCPEDLy 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1159 -----------------ESYKQELEESNDKTVLHSQL-------KAKRDEEYAHLQKQLEETVKSSEEVveemkAQNQKK 1214
Cdd:PRK04863 737 liegdpdsfddsvfsveELEKAVVVKIADRQWRYSRFpevplfgRAAREKRIEQLRAEREELAERYATL-----SFDVQK 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1215 IEELNETIDQLKRQKISAdkaksSAESDNEnfrAELSNIASARLEAEKKRKAAEtslmEKDHKMREMQSNLDDLMAKLSK 1294
Cdd:PRK04863 812 LQRLHQAFSRFIGSHLAV-----AFEADPE---AELRQLNRRRVELERALADHE----SQEQQQRSQLEQAKEGLSALNR 879
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1295 MNNELESIqkaksADETLNSNLlkknasldMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVaveARDDALDaQEKIEK 1374
Cdd:PRK04863 880 LLPRLNLL-----ADETLADRV--------EEIREQLDEAEEAKRFVQQHGNALAQLEPIVSV---LQSDPEQ-FEQLKQ 942
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1375 EVKEVKSLLAEARKKLDE-----ENREVMEELRKKKEKELSAE-----KERADMAEQARDKAERAKKKAIQEAEDVQKEL 1444
Cdd:PRK04863 943 DYQQAQQTQRDAKQQAFAltevvQRRAHFSYEDAAEMLAKNSDlneklRQRLEQAEQERTRAREQLRQAQAQLAQYNQVL 1022
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1445 TDVVAATREMErkmrkfdQQLAEernntlLAQQERDMAHQMLRDAETKALV----LSNELSEKKDIVDQLEKDKRTLKLE 1520
Cdd:PRK04863 1023 ASLKSSYDAKR-------QMLQE------LKQELQDLGVPADSGAEERARArrdeLHARLSANRSRRNQLEKQLTFCEAE 1089
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1521 IDNLAstkddagKNVYELEKTKRRLDEELSRA----------------EQQIIELEDALQLADDARSRVEVNMQAMR--- 1581
Cdd:PRK04863 1090 MDNLT-------KKLRKLERDYHEMREQVVNAkagwcavlrlvkdngvERRLHRRELAYLSADELRSMSDKALGALRlav 1162
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1582 --SEFERQLASREEDED--DRKKGLTSKIRNLTEEleseqRARQaaiankkkiesQISELTEKNEAslrqIEDLSRQLRK 1657
Cdd:PRK04863 1163 adNEHLRDVLRLSEDPKrpERKVQFYIAVYQHLRE-----RIRQ-----------DIIRTDDPVEA----IEQMEIELSR 1222
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1658 AqlgwkdlqldvTEARAAMEDALAGQRDA-----EKRARASEDEIKRLTADIQAVS 1708
Cdd:PRK04863 1223 L-----------TEELTSREQKLAISSESvaniiRKTIQREQNRIRMLNQGLQNIS 1267
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
919-1503 |
1.76e-05 |
|
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: 49.82 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 919 ERSRMAARRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEMV--RHLEENLEDEERSRQKLLLEknsIESRLKELEAQ 996
Cdd:pfam10174 124 EHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLqsKGLPKKSGEEDWERTRRIAE---AEMQLGHLEVL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 997 gLELEDSGNKLSKEKKALEERCEDLSSrlidEVERSKQLVKAKARLEATVAEINDELEKEKQQ-RHNAETArraaeTQLR 1075
Cdd:pfam10174 201 -LDQKEKENIHLREELHRRNQLQPDPA----KTKALQTVIEMKDTKISSLERNIRDLEDEVQMlKTNGLLH-----TEDR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1076 EEQESCLEKTR--------KAEELTNQLMRKESELSQISIRND-----------------EELAARQQ----LEREIREI 1126
Cdd:pfam10174 271 EEEIKQMEVYKshskfmknKIDQLKQELSKKESELLALQTKLEtltnqnsdckqhievlkESLTAKEQraaiLQTEVDAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1127 RAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDK-TVLH-------SQLKAKrDEEYAHLQKQ------ 1192
Cdd:pfam10174 351 RLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKiNVLQkkienlqEQLRDK-DKQLAGLKERvkslqt 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1193 -----------LEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQ-KISADKAKSSaesdnenfRAELSNIASARLEA 1260
Cdd:pfam10174 430 dssntdtalttLEEALSEKERIIERLKEQREREDRERLEELESLKKEnKDLKEKVSAL--------QPELTEKESSLIDL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1261 EKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAksadetlnsnllkknasldmqlselteasEEDRRT 1340
Cdd:pfam10174 502 KEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNA-----------------------------EEAVRT 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1341 RATLNNKIRQLEEDLAvavEARDDALDAQEKIE------KEVKEVKSL----LAEARKKLDEENREVMEELRKKKEKELS 1410
Cdd:pfam10174 553 NPEINDRIRLLEQEVA---RYKEESGKAQAEVErllgilREVENEKNDkdkkIAELESLTLRQMKEQNKKVANIKHGQQE 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1411 AEKERADMAEQA-RDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAE-ERNNTLLAQQERDMAHQMLrd 1488
Cdd:pfam10174 630 MKKKGAQLLEEArRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEkDGHLTNLRAERRKQLEEIL-- 707
|
650
....*....|....*
gi 71983975 1489 aETKALVLSNELSEK 1503
Cdd:pfam10174 708 -EMKQEALLAAISEK 721
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1700-1945 |
1.83e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1700 LTADIQAVSSSKRKAEAERDELIEEVSSLrassfsNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTAD 1779
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAEL------EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1780 LAmersvcertesdkiALERANRDLKQQLQDAEntavARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMA 1859
Cdd:COG4942 85 LA--------------ELEKEIAELRAELEAQK----EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1860 EMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQLEDTEAERDRLTnklKDERRRAEEMTDLNETLSRDVSLLKQRETTAR 1939
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
....*.
gi 71983975 1940 RTPGLI 1945
Cdd:COG4942 224 ELEALI 229
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1410-1620 |
1.91e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1410 SAEKERADMAEQARDKAERAKKKAIQEAEDvqkeltdvvaatrEMERKMRKFDQQLaEERNNTLLAQQERdmahqmLRDA 1489
Cdd:PRK12704 35 EAEEEAKRILEEAKKEAEAIKKEALLEAKE-------------EIHKLRNEFEKEL-RERRNELQKLEKR------LLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1490 EtkalvlsNELSEKKdivDQLEKDKRTLKLEIDNLASTKDdagknvyELEKTKRRLDEelsRAEQQIIELEDALQL-ADD 1568
Cdd:PRK12704 95 E-------ENLDRKL---ELLEKREEELEKKEKELEQKQQ-------ELEKKEEELEE---LIEEQLQELERISGLtAEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71983975 1569 ARSRVevnMQAMRSEFERQLASReededdrkkgltskIRNLTEE--LESEQRAR 1620
Cdd:PRK12704 155 AKEIL---LEKVEEEARHEAAVL--------------IKEIEEEakEEADKKAK 191
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1037-1185 |
2.23e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.44 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1037 KAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREeqesclektrkAEELTNQLMRKESELsqisirNDEELAAR 1116
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKE-----------AEKLKEELEEKKEKL------QEEEDKLL 568
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 1117 QQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDmAEELESYKQELEESNDKTVLHSQLKAKRDEE 1185
Cdd:PRK00409 569 EEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVK-AHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1280-1706 |
2.31e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 49.61 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1280 EMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAV 1359
Cdd:COG5281 14 AAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALAAALAEDAAAAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1360 EARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAED 1439
Cdd:COG5281 94 AAEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALAAAAAAAAAAAAAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1440 VQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKL 1519
Cdd:COG5281 174 AAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAASAAAQALAALAAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1520 EIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQLASREEDEDDRK 1599
Cdd:COG5281 254 AAAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALRAAAQALAA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1600 KGLTSKIRNLTEELESEQRARQAAIANKKKIESQI----SELTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAA 1675
Cdd:COG5281 334 LAQRALAAAALAAAAQEAALAAAAAALQAALEAAAaaaaAELAAAGDWAAGAKAALAEYADSATNVAAQVAQAATSAFSG 413
|
410 420 430
....*....|....*....|....*....|.
gi 71983975 1676 MEDALAGQRDAEKRARASEDEIKRLTADIQA 1706
Cdd:COG5281 414 LTDALAGAVTTGKLLFDALASSIASIADALA 444
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
885-1280 |
2.52e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 49.47 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 885 ISDYKQQMEKMDEERLV----LKTRLDAESSERAEIFEERSRMAARRD-------ELEGILEEVSKrlEIEEQKAKKADS 953
Cdd:PLN03229 378 INENMDELGKMDTEELLkhrmLKFRKIGGFQEGVPVDPERKVNMKKREavktpvrELEGEVEKLKE--QILKAKESSSKP 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 954 ESRKLTEMVRHLEENLEDE-ERSRQKLLLEKNSIESRLKELEAQGLE------LEDSGNKLSKE-KKALEE--RCEDLSS 1023
Cdd:PLN03229 456 SELALNEMIEKLKKEIDLEyTEAVIAMGLQERLENLREEFSKANSQDqlmhpvLMEKIEKLKDEfNKRLSRapNYLSLKY 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1024 RL--IDEVERSKQLVKAKARLEATVAEINDELeKEKQQRhnaetarraaeTQLREEQESClektrkAEELTNQLMRKESE 1101
Cdd:PLN03229 536 KLdmLNEFSRAKALSEKKSKAEKLKAEINKKF-KEVMDR-----------PEIKEKMEAL------KAEVASSGASSGDE 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1102 LsqisirnDEELaaRQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARR------DMAEELESYKQELEESNDKTVLH 1175
Cdd:PLN03229 598 L-------DDDL--KEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAeqtpppNLQEKIESLNEEINKKIERVIRS 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1176 SQLKAKRDEeyahlqKQLEETVKSSEEVVEEmkaqnQKKIEELNETIdqlkRQKISADKAKSSAESDNENFRAELSniAS 1255
Cdd:PLN03229 669 SDLKSKIEL------LKLEVAKASKTPDVTE-----KEKIEALEQQI----KQKIAEALNSSELKEKFEELEAELA--AA 731
|
410 420
....*....|....*....|....*
gi 71983975 1256 ARLEAEKKRKAAETSLMEKDHKMRE 1280
Cdd:PLN03229 732 RETAAESNGSLKNDDDKEEDSKEDG 756
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
926-1337 |
2.53e-05 |
|
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: 49.19 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 926 RRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHlEENLEDEERSRQKlllEKNSIESRLKELEAQGLELEDSGN 1005
Cdd:COG5185 175 NLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETG-NLGSESTLLEKAK---EIINIEEALKGFQDPESELEDLAQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1006 KLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDEL-EKEKQQRHNAETARRAAETQLREEQESCLEK 1084
Cdd:COG5185 251 TSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIaEYTKSIDIKKATESLEEQLAAAEAEQELEES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1085 TRKAEeltnqlmrkeselsqisirndeelAARQQLEREIREIRAQLDDAIEETNKEKaARQKAEKARRDMAEELESYKQE 1164
Cdd:COG5185 331 KRETE------------------------TGIQNLTAEIEQGQESLTENLEAIKEEI-ENIVGEVELSKSSEELDSFKDT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1165 LEESndKTVLHSQLKAKRdEEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNE 1244
Cdd:COG5185 386 IEST--KESLDEIPQNQR-GYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQ 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1245 NFRAELSNIASARLEAEKKRKAAETSLME--KDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNAS 1322
Cdd:COG5185 463 SRLEEAYDEINRSVRSKKEDLNEELTQIEsrVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALE 542
|
410
....*....|....*
gi 71983975 1323 LDMQLSELTEASEED 1337
Cdd:COG5185 543 NLIPASELIQASNAK 557
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
850-1130 |
2.85e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 850 KVKPLLEVTNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERlvlktRLDAESSERAEIFEERSRMAARRDE 929
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED-----KKKAEEAKKAEEDEKKAAEALKKEA 1698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 930 LEG-ILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLL---EKNSIESRLKELEAQGLELEDSGN 1005
Cdd:PTZ00121 1699 EEAkKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1006 KLSKE--KKALEERCEDLSSRLIDE-----------------VERSKQL----VKAKARLEATVAEINDELEKEKQQRHN 1062
Cdd:PTZ00121 1779 AVIEEelDEEDEKRRMEVDKKIKDIfdnfaniieggkegnlvINDSKEMedsaIKEVADSKNMQLEEADAFEKHKFNKNN 1858
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1063 AET------ARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRN----DEELAARQQLEREIREIRAQL 1130
Cdd:PTZ00121 1859 ENGedgnkeADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNndiiDDKLDKDEYIKRDAEETREEI 1936
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1037-1270 |
3.09e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1037 KAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELsqisirndeelaar 1116
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1117 QQLEREIREIRAQLDDAIEETNKEKAARQKAekARRDMAEELESyKQELEESNDKTVLHSQLKAKRDEEYAHLQKQLEEt 1196
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRL--GRQPPLALLLS-PEDFLDAVRRLQYLKYLAPARREQAEELRADLAE- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1197 VKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIAS---------ARLEAEKKRKAA 1267
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQeaeelealiARLEAEAAAAAE 241
|
...
gi 71983975 1268 ETS 1270
Cdd:COG4942 242 RTP 244
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
885-1253 |
3.20e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.06 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 885 ISDYKQQMEKMDEERLVLKTrLDAESSERAE----IFEE-RSRMAARRDELEGILEEVSKRLEIEEQKAKKADsesrKLT 959
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLE-SEEKNREEVEqlkdLYRElRKSLLANRFSFGPALDELEKQLENLEEEFSQFV----ELT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 960 EMVRHLE-----ENLEDEERSRQKLLLEknsIESRLKELE----AQGLELEDSGNKLSKEKKALEErcEDLSSRLIDEVE 1030
Cdd:PRK04778 189 ESGDYVEareilDQLEEELAALEQIMEE---IPELLKELQtelpDQLQELKAGYRELVEEGYHLDH--LDIEKEIQDLKE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1031 RSKQLVKAKARLE-ATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRN 1109
Cdd:PRK04778 264 QIDENLALLEELDlDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLN 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1110 DEELAARQQLEREIREIRAQLDDAIEETNKEKAARQkaekARRDMAEELESYKQELEESNDKtvLHSQLKAKRDEEyAHL 1189
Cdd:PRK04778 344 ESELESVRQLEKQLESLEKQYDEITERIAEQEIAYS----ELQEELEEILKQLEEIEKEQEK--LSEMLQGLRKDE-LEA 416
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 1190 QKQLEETVKSSEEVVEEMKAQNQKKI------------EELNETIDQLKRQKISADKAKSS---AESDNENFRAELSNI 1253
Cdd:PRK04778 417 REKLERYRNKLHEIKRYLEKSNLPGLpedylemffevsDEIEALAEELEEKPINMEAVNRLleeATEDVETLEEETEEL 495
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1233-1393 |
3.28e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1233 DKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETL 1312
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1313 N--SNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALdaqEKIEKEVKEVKSLLAEARKKL 1390
Cdd:COG1579 96 KeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAEREELAAKI 172
|
...
gi 71983975 1391 DEE 1393
Cdd:COG1579 173 PPE 175
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1612-1828 |
3.56e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1612 ELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDAlagQRDAEKRAR 1691
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER---REELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1692 AS-------------------EDEIKRLTAdIQAVSSSKRkaeaerdELIEEVSSLRASsfSNEEKRRLEAKVIDLEDQL 1752
Cdd:COG3883 94 ALyrsggsvsyldvllgsesfSDFLDRLSA-LSKIADADA-------DLLEELKADKAE--LEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1753 DEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQQLQDAENTAVARLRTQINVAEA 1828
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
967-1167 |
3.58e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 967 ENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATV 1046
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1047 AEINDELekeKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREI 1126
Cdd:COG4942 100 EAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71983975 1127 RAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEE 1167
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1572-1922 |
3.71e-05 |
|
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: 48.81 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1572 RVEVNMQAMRSEFERQLASREEDeddRKKGLTSKIRNLTEELE-SEQRARQAAIANKKKIESQISELTEKNEA--SLRQI 1648
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFA---KKKSLHGKAELLTLRSQlLTLCTPCMPDTYHERKQVLEKELKHLREAlqQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1649 EDLSRQLRKAQLGWKDLQLDVTEARA------AMEDALAGQRDAEKRARASE---DEIKRLTA---DIQAVSSSKRKAEA 1716
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQLLKQLRArieelrAQEAVLEETQERINRARKAAplaAHIKAVTQieqQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1717 ERDELIEEVSSLRASSFSNEEKRRLE----AKVIDLEDQLDEEASANELAQEKVRKSQ---QQLEQMTADLAMERSVCER 1789
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLqtlhSQEIHIRDAHEVATSIREISCQQHTLTQhihTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1790 TesDKIALERANRDLKQQLQDAENTAVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRrmetkmaEMQQMLEEEK 1869
Cdd:TIGR00618 402 L--DILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-------ESAQSLKERE 472
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 71983975 1870 RQgESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNklKDERRRAEEMTDLNE 1922
Cdd:TIGR00618 473 QQ-LQTKEQIHLQETRKKAVVLARLLELQEEPCPLC--GSCIHPNPARQDIDN 522
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
856-1219 |
4.10e-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: 48.80 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 856 EVTNKDELIAEREQELKVTAEKLRRsevfISDYKQQMEKMD---EERLVLKTRLDAESSERAEIFEERSRMAARR----- 927
Cdd:COG3096 314 ELEELSARESDLEQDYQAASDHLNL----VQTALRQQEKIEryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLeaaee 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 928 --DELEGILEEVSKRLE------IEEQKAKKADSESRKLTEMVRHLEENLED-EERSRQKLllekNSIESRLKELEAQgl 998
Cdd:COG3096 390 evDSLKSQLADYQQALDvqqtraIQYQQAVQALEKARALCGLPDLTPENAEDyLAAFRAKE----QQATEEVLELEQK-- 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 999 eLEDSGNKLSKEKKALEercedLSSRLIDEVERSKQLVKAK-------------ARLEATVAEINdELEKEKQQRHNAEt 1065
Cdd:COG3096 464 -LSVADAARRQFEKAYE-----LVCKIAGEVERSQAWQTARellrryrsqqalaQRLQQLRAQLA-ELEQRLRQQQNAE- 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1066 aRRAAETQLREEQEsclekTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLddaieetnKEKAARQ 1145
Cdd:COG3096 536 -RLLEEFCQRIGQQ-----LDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI--------KELAARA 601
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983975 1146 KAEKARRDMAEEL-ESYKQELEESNDKTvlhsqlkakrdeeyAHLQKQL--EETVKSSEEVVEEMKAQNQKKIEELN 1219
Cdd:COG3096 602 PAWLAAQDALERLrEQSGEALADSQEVT--------------AAMQQLLerEREATVERDELAARKQALESQIERLS 664
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
855-1382 |
4.59e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 855 LEVTNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAA---RRDELE 931
Cdd:PRK01156 197 LELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMeleKNNYYK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 932 GILEE---------VSKRLEIEE------------QKAKKADSESRKLTEMVRHLEENLED----EERSRQKLLLEKNSI 986
Cdd:PRK01156 277 ELEERhmkiindpvYKNRNYINDyfkykndienkkQILSNIDAEINKYHAIIKKLSVLQKDyndyIKKKSRYDDLNNQIL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 987 ESRLKELEAQGL--ELEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQ----R 1060
Cdd:PRK01156 357 ELEGYEMDYNSYlkSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRiralR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1061 HNAETARRAAEtqLREEQESC--------LEKTRK-AEELTNQLMRKESELSQISIR-NDEELAARQQLEREIREIRAQL 1130
Cdd:PRK01156 437 ENLDELSRNME--MLNGQSVCpvcgttlgEEKSNHiINHYNEKKSRLEEKIREIEIEvKDIDEKIVDLKKRKEYLESEEI 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1131 DDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKTVLHSQLKAKRDEEYAHLQKQLeetvksSEEVVEEMKAQ 1210
Cdd:PRK01156 515 NKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVI------SLIDIETNRSR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1211 NQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAaetslmekdhkMREMQSNLDDLMA 1290
Cdd:PRK01156 589 SNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKIL-----------IEKLRGKIDNYKK 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1291 KLSKMnnelESIQKAKSadeTLNSNLLKKNASLDmQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQE 1370
Cdd:PRK01156 658 QIAEI----DSIIPDLK---EITSRINDIEDNLK-KSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK 729
|
570
....*....|..
gi 71983975 1371 KIEKEVKEVKSL 1382
Cdd:PRK01156 730 KIKKAIGDLKRL 741
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1410-1802 |
4.85e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 48.49 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1410 SAEKERADMAEQARDKAERAKKkAIQEAEDVQK---ELTDVVAATREMERKMRKFDQQLAEERNNTLLA-QQERDMAHQM 1485
Cdd:pfam05701 149 SLRKEYASLVSERDIAIKRAEE-AVSASKEIEKtveELTIELIATKESLESAHAAHLEAEEHRIGAALArEQDKLNWEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1486 LRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLA----STKDDAGKNVYELEKTKRRLDEELSRAEQQIIELED 1561
Cdd:pfam05701 228 LKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLKAELAaymeSKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1562 ALQLADDARSRVEVNMQAMRSEFERQLAsrEEDEDDRKKGLTS-KIRNLTEELESEQRARQAAIANKKKIESQISELTEK 1640
Cdd:pfam05701 308 NIEKAKDEVNCLRVAAASLRSELEKEKA--ELASLRQREGMASiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1641 NEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDA----LAGQRDAEKrARASEdeiKRLTADIQAVSSSKRKAEA 1716
Cdd:pfam05701 386 LQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVesrlEAVLKEIEA-AKASE---KLALAAIKALQESESSAES 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1717 ERDElieevSSLRASSFSNEEKRRLEAKVIDLEDQLDEEASAN----ELAQEKVRKSQQQLEQMTADLAmersvcERTES 1792
Cdd:pfam05701 462 TNQE-----DSPRGVTLSLEEYYELSKRAHEAEELANKRVAEAvsqiEEAKESELRSLEKLEEVNREME------ERKEA 530
|
410
....*....|
gi 71983975 1793 DKIALERANR 1802
Cdd:pfam05701 531 LKIALEKAEK 540
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1101-1268 |
4.99e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1101 ELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKtvlhsQLKA 1180
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-----LGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1181 KRDEEYAHLQKQLEEtvksseevVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIAsARLEA 1260
Cdd:COG1579 86 RNNKEYEALQKEIES--------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL-AELEA 156
|
....*...
gi 71983975 1261 EKKRKAAE 1268
Cdd:COG1579 157 ELEELEAE 164
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1100-1654 |
5.14e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.59 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1100 SELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEesndktVLHSQLK 1179
Cdd:pfam07111 62 SQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAE------MVRKNLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1180 AKRDEEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNiASARLE 1259
Cdd:pfam07111 136 EGSQRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSK-TQEELE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1260 A-----EKKRKAAETSLMEKDHKmREMQSNLDDLMAKLSKMNNELESIQkakSADETLNSNLLKKNASLDMQLSELTEAS 1334
Cdd:pfam07111 215 AqvtlvESLRKYVGEQVPPEVHS-QTWELERQELLDTMQHLQEDRADLQ---ATVELLQVRVQSLTHMLALQEEELTRKI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1335 EEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKE-VKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEK 1413
Cdd:pfam07111 291 QPSDSLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDsVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEV 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1414 ER--ADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATRE----MERKMRKFDQQLAE------------ERNNTLLA 1475
Cdd:pfam07111 371 ERmsAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSStqiwLETTMTRVEQAVARipslsnrlsyavRKVHTIKG 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1476 QQERDMAHQMLR-----------DAETKALVLSNELSEKKDIVD-QLEKDKRTLKLEIdnlASTKDDAGKNVYELEKTKR 1543
Cdd:pfam07111 451 LMARKVALAQLRqescpppppapPVDADLSLELEQLREERNRLDaELQLSAHLIQQEV---GRAREQGEAERQQLSEVAQ 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1544 RLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQL----ASREEDEDDRKKGLTSKIRNLTEELESEQRA 1619
Cdd:pfam07111 528 QLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQeiygQALQEKVAEVETRLREQLSDTKRRLNEARRE 607
|
570 580 590
....*....|....*....|....*....|....*
gi 71983975 1620 RQAAIANKKKIESQISELTEKNEaSLRQIEDLSRQ 1654
Cdd:pfam07111 608 QAKAVVSLRQIQHRATQEKERNQ-ELRRLQDEARK 641
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
663-690 |
5.76e-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: 45.80 E-value: 5.76e-05
10 20
....*....|....*....|....*...
gi 71983975 663 SQLYKEQLARLMSTLNNTNPHFVRCIIP 690
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1365-1623 |
6.02e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1365 ALDAQEKIEKEVKEVKSLLAEARKKLDEenrevmeelrkkkekelsAEKERADMAEQaRDKAERAKKKAIQEAEDVQKEL 1444
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAA------------------LKKEEKALLKQ-LAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1445 TDVVAATREMERKMRKFDQQLAEERNntLLAQQERdMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNL 1524
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKE--ELAELLR-ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1525 ASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQladdARSRVEVNMQAMRSEFERQLASREEDEDDrkkgLTS 1604
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEE----LEA 227
|
250
....*....|....*....
gi 71983975 1605 KIRNLTEELESEQRARQAA 1623
Cdd:COG4942 228 LIARLEAEAAAAAERTPAA 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
914-1118 |
6.99e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 914 AEIFEERSRmAARRDELEGILEEVSKRLEIEEQKAKKADSESRK---------LTEMVRHLEENLEDEERSRQKLLLEKN 984
Cdd:COG3206 158 AEAYLEQNL-ELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 985 SIESRLKELEAQGLELEDSGNKL--SKEKKALEERCEDLSSRLIDEVERSK----QLVKAKARLEATVAEINDELEKEKQ 1058
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1059 QRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELsQISIRNDEELAARQQ 1118
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV-EVARELYESLLQRLE 375
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
886-1301 |
7.25e-05 |
|
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: 47.89 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 886 SDYKQQMEkmdeerlVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRL-EIEEQKAKKAdSESRKLTEMVRH 964
Cdd:pfam10174 320 SDCKQHIE-------VLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLqDLTEEKSTLA-GEIRDLKDMLDV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 965 LE----------ENLEDEERSRQKLLlekNSIESRLKELEaqglelEDSGNK---LSKEKKALEERcEDLSSRLIDEVER 1031
Cdd:pfam10174 392 KErkinvlqkkiENLQEQLRDKDKQL---AGLKERVKSLQ------TDSSNTdtaLTTLEEALSEK-ERIIERLKEQRER 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1032 SKQlvkakarleatvaEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIrnde 1111
Cdd:pfam10174 462 EDR-------------ERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEI---- 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1112 elaarqqlereirEIRAQLDDAIEETNKEKAARQKAEKARRDmaeelesykqelEESNDKTVLHSQLKAKRDEEYAHLQK 1191
Cdd:pfam10174 525 -------------AVEQKKEECSKLENQLKKAHNAEEAVRTN------------PEINDRIRLLEQEVARYKEESGKAQA 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1192 QLEETVKSSEEvVEEMKAQNQKKIEELNE-TIDQLKRQKISADKAKSSAESDNENFRAELSNiaSARLEAEKKRKAAETS 1270
Cdd:pfam10174 580 EVERLLGILRE-VENEKNDKDKKIAELESlTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEE--ARRREDNLADNSQQLQ 656
|
410 420 430
....*....|....*....|....*....|.
gi 71983975 1271 LMEKDHKMREMQSNLDDLMAKLSKMNNELES 1301
Cdd:pfam10174 657 LEELMGALEKTRQELDATKARLSSTQQSLAE 687
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1415-1916 |
8.17e-05 |
|
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: 47.89 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1415 RADMAEQARDKAERAKKKAIQEAEDVQKeltdvvAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKAL 1494
Cdd:pfam10174 212 REELHRRNQLQPDPAKTKALQTVIEMKD------TKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1495 VLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVyelektkRRLDEELSRAEQQIIELEDALqlaDDARSRVE 1574
Cdd:pfam10174 286 FMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHI-------EVLKESLTAKEQRAAILQTEV---DALRLRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1575 vNMQAMRSEFERQLasreEDEDDRKKGLTSKIRNLTEELESEQRARQAAianKKKIESQISELTEKNeaslRQIEDLSRQ 1654
Cdd:pfam10174 356 -EKESFLNKKTKQL----QDLTEEKSTLAGEIRDLKDMLDVKERKINVL---QKKIENLQEQLRDKD----KQLAGLKER 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1655 LrkaqlgwKDLQLDVTE---ARAAMEDALAG----------QRDAEKRARASE-----DEIKRLTADIQAVSSSKRKAEA 1716
Cdd:pfam10174 424 V-------KSLQTDSSNtdtALTTLEEALSEkeriierlkeQREREDRERLEEleslkKENKDLKEKVSALQPELTEKES 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1717 ERDELIEEVSSLRASSFSNEEK-RRLEAKV-------IDLEDQLD--EEASANELAQEKVRKSQQQLEQMTADLAMERSV 1786
Cdd:pfam10174 497 SLIDLKEHASSLASSGLKKDSKlKSLEIAVeqkkeecSKLENQLKkaHNAEEAVRTNPEINDRIRLLEQEVARYKEESGK 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1787 CErTESDKI-----ALERANRDLKQQLQDAENTAVARLRTQiNVAEAKVSSLEQQLSLEEQDKMRQGRTlRRMETKMAEM 1861
Cdd:pfam10174 577 AQ-AEVERLlgilrEVENEKNDKDKKIAELESLTLRQMKEQ-NKKVANIKHGQQEMKKKGAQLLEEARR-REDNLADNSQ 653
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1862 QQMLEEEKRQGESNRQAVDRQNARIrqlrTQLEDTEAERDRLTNKLKDERRRAEE 1916
Cdd:pfam10174 654 QLQLEELMGALEKTRQELDATKARL----SSTQQSLAEKDGHLTNLRAERRKQLE 704
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1121-1570 |
9.29e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.98 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1121 REIREIRAQLDDAIEETNKEKAARQKA----EKARRDMAEELESYKQELEESNDKTVLHSQLKAKRDEEYAHLQKqLEET 1196
Cdd:pfam19220 20 EDLRSLKADFSQLIEPIEAILRELPQAksrlLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAK-LEAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1197 VKSSEEVVEEMKAQnqkkIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDH 1276
Cdd:pfam19220 99 LREAEAAKEELRIE----LRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1277 KMREMQSNLDDLMAKLSKMNNELESIQKAKSAD----ETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRqle 1352
Cdd:pfam19220 175 ENRRLQALSEEQAAELAELTRRLAELETQLDATrarlRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLE--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1353 edlavAVEARDDALDaqekiekevkevkSLLAEARKKLDEENREVMEelrkkkekelsaekeradmAEQARDKAERAKKK 1432
Cdd:pfam19220 252 -----ALTARAAATE-------------QLLAEARNQLRDRDEAIRA-------------------AERRLKEASIERDT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1433 AIQEAEDVQKELTDVVAATREMERKmrkfdQQLAEERNNTLL-AQQERDMAhqmLRDAETKALVLSnelsekkDIVDQLE 1511
Cdd:pfam19220 295 LERRLAGLEADLERRTQQFQEMQRA-----RAELEERAEMLTkALAAKDAA---LERAEERIASLS-------DRIAELT 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 1512 KDkrtlkLEIDNLAstkddagknvyeLEKTKRRLDEELSRAEQQIIELEDALQLADDAR 1570
Cdd:pfam19220 360 KR-----FEVERAA------------LEQANRRLKEELQRERAERALAQGALEIARESR 401
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1321-1571 |
9.34e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1321 ASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVmee 1400
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1401 lrkkkekelsaeKERAdmAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLL---AQQ 1477
Cdd:COG3883 89 ------------GERA--RALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKkaeLEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1478 ERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQII 1557
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
250
....*....|....
gi 71983975 1558 ELEDALQLADDARS 1571
Cdd:COG3883 235 AAAAAAAAAASAAG 248
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1410-1626 |
1.04e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1410 SAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAE-----ERNNTLLAQQERDMAHQ 1484
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaeaeiEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1485 MLRDAETKALVLSNELSE--------------KKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELS 1550
Cdd:COG3883 99 GGSVSYLDVLLGSESFSDfldrlsalskiadaDADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1551 RAEQQIIELEDALQLADDARSRvevnMQAMRSEFERQLASREEDEDDRKKGLTSKIRNLTEELESEQRARQAAIAN 1626
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAE----LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
934-1183 |
1.04e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 934 LEEVSKRLEIEEQKAKK--ADSES-RKLTEMVRHLEENLEDEERSR--QKLLlekNSIESRLKELEAQGLELEDSGNKLS 1008
Cdd:PRK10929 23 PDEKQITQELEQAKAAKtpAQAEIvEALQSALNWLEERKGSLERAKqyQQVI---DNFPKLSAELRQQLNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1009 KEK--KALEERCEDLSSRLIdEVERSKQLVKAKARleatvaEINDELEKEKQQRHNAETARRAAETQLREEQ--ESCLEK 1084
Cdd:PRK10929 100 PNMstDALEQEILQVSSQLL-EKSRQAQQEQDRAR------EISDSLSQLPQQQTEARRQLNEIERRLQTLGtpNTPLAQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1085 T----RKAEELTNQLMRKESELSQISIRNDEELA---------ARQQLEREIREIRAQLDDaieetnkekAARQKAEKAr 1151
Cdd:PRK10929 173 AqltaLQAESAALKALVDELELAQLSANNRQELArlrselakkRSQQLDAYLQALRNQLNS---------QRQREAERA- 242
|
250 260 270
....*....|....*....|....*....|...
gi 71983975 1152 rdmaeeLESYKQELEESND-KTVLHSQLKAKRD 1183
Cdd:PRK10929 243 ------LESTELLAEQSGDlPKSIVAQFKINRE 269
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1761-1915 |
1.07e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 46.65 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1761 LAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALER--ANRDLKQQLQDAENTAVARLRTQINVAEAKVSSLEQQLS 1838
Cdd:pfam00529 48 LFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQAleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1839 LEEQ---DKMRQGRTLRRMETKMAEMQQMLEEEKRQ-GESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKLKDERRRA 1914
Cdd:pfam00529 128 RRRVlapIGGISRESLVTAGALVAQAQANLLATVAQlDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDL 207
|
.
gi 71983975 1915 E 1915
Cdd:pfam00529 208 E 208
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1113-1269 |
1.26e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1113 LAARQQLEREIREIRAQLDDAIEETNKEkaARQKAEKARRDMAEELESYKQELEEsndktvlhsQLKAKRDEeyahLQKQ 1192
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKE--AEAIKKEALLEAKEEIHKLRNEFEK---------ELRERRNE----LQKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1193 lEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIAS-----------ARLEAE 1261
Cdd:PRK12704 88 -EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGltaeeakeillEKVEEE 166
|
....*...
gi 71983975 1262 KKRKAAET 1269
Cdd:PRK12704 167 ARHEAAVL 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1586-1817 |
1.65e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1586 RQLASREEDEDDRKKGLTSKIRNLTEELES----EQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLRKAQLG 1661
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEElneeYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1662 WKDL-QLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELieevsslrassfsNEEKRR 1740
Cdd:COG3883 99 GGSVsYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL-------------EALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983975 1741 LEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQQLQDAENTAVA 1817
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1037-1267 |
1.66e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1037 KAKARLEATVAEINDElEKEKQQRHNAETARRAAETQlREEQESCLEKTRKAEELTNQLMRKESELSQISirndeELAAR 1116
Cdd:PRK05035 450 EAKARFEARQARLERE-KAAREARHKKAAEARAAKDK-DAVAAALARVKAKKAAATQPIVIKAGARPDNS-----AVIAA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1117 QQLEREIREIRAQLDDAIEETNKEKA------ARQKAEKArrdmAEELESYKQELEESNDKTVLHSQL---KAKRDEeya 1187
Cdd:PRK05035 523 REARKAQARARQAEKQAAAAADPKKAavaaaiARAKAKKA----AQQAANAEAEEEVDPKKAAVAAAIaraKAKKAA--- 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1188 hlQKQLEETVKSSEEVVEEMKA-------------QNQKKIEELNETIDQLKRqKISADKAKSSAEsdnenfRAELSNIA 1254
Cdd:PRK05035 596 --QQAASAEPEEQVAEVDPKKAavaaaiarakakkAEQQANAEPEEPVDPRKA-AVAAAIARAKAR------KAAQQQAN 666
|
250
....*....|...
gi 71983975 1255 SARLEAEKKRKAA 1267
Cdd:PRK05035 667 AEPEEAEDPKKAA 679
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1028-1166 |
1.74e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.40 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1028 EVERSKQLVKAKARLEATVAEINDELEKEkqqrhNAETARRAAETQLREEQEscLEKTRKAEELTNQLMRKESELSQISI 1107
Cdd:COG2268 207 EAERETEIAIAQANREAEEAELEQEREIE-----TARIAEAEAELAKKKAEE--RREAETARAEAEAAYEIAEANAEREV 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 1108 RNDEELAARQQlEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELE 1166
Cdd:COG2268 280 QRQLEIAERER-EIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGL 337
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
915-1228 |
1.74e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 915 EIFEERSRMAA----RRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDE----ERSRQKllleknsi 986
Cdd:pfam02029 6 EAARERRRRAReerrRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRtakrEERRQK-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 987 esRLKElEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETA 1066
Cdd:pfam02029 78 --RLQE-ALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1067 RRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISI---------------RNDEELAARQQLEREIREIRAQLD 1131
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKvfldqkrghpevksqNGEEEVTKLKVTTKRRQGGLSQSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1132 DAIEETNKEKAARQKAEKARRDmaeelesyKQELEESNDKTVLHSQLKAkrDEEYAHLQKQLEETVKSSEEVVEEMKAQN 1211
Cdd:pfam02029 235 EREEEAEVFLEAEQKLEELRRR--------RQEKESEEFEKLRQKQQEA--ELELEELKKKREERRKLLEEEEQRRKQEE 304
|
330
....*....|....*..
gi 71983975 1212 QKKIEELNETIDQLKRQ 1228
Cdd:pfam02029 305 AERKLREEEEKRRMKEE 321
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1508-1658 |
1.85e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1508 DQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQladdarsRVEVNMQAMRSEFERQ 1587
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-------KYEEQLGNVRNNKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1588 LASRE-EDEDDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLRKA 1658
Cdd:COG1579 93 ALQKEiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1187-1492 |
2.13e-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: 46.29 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1187 AHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKa 1266
Cdd:pfam09731 128 KALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSE- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1267 aETSLMEKDHKMREmqsNLDDLMAKLSKMNNELESIQKAksadetlnsnllkknASLDMQLSELTEASEED--RRTRATL 1344
Cdd:pfam09731 207 -EEAAPPLLDAAPE---TPPKLPEHLDNVEEKVEKAQSL---------------AKLVDQYKELVASERIVfqQELVSIF 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1345 NNKIRQLEEDLAvAVEARDDAL--DAQEKIEKEVKEVKSLLAEARKKLDEenrevmeelrkkkekelSAEKERADMAEQA 1422
Cdd:pfam09731 268 PDIIPVLKEDNL-LSNDDLNSLiaHAHREIDQLSKKLAELKKREEKHIER-----------------ALEKQKEELDKLA 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983975 1423 RDKAERAKKKAIQEAEDVQKELTDVVAATRE-MERKMR---KFDQQLAEERNNTLLAQQERDMAHQMLRDAETK 1492
Cdd:pfam09731 330 EELSARLEEVRAADEAQLRLEFEREREEIREsYEEKLRtelERQAEAHEEHLKDVLVEQEIELQREFLQDIKEK 403
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1682-1915 |
2.58e-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: 45.83 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1682 GQRDAEKRARASE-----DEIKRLTAD----IQAVSSSKRKAEAERDELIEEVSSLRASSFSNEEKRR----LEAKVIDL 1748
Cdd:pfam19220 2 GQRNELLRVRLGEmadrlEDLRSLKADfsqlIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRelagLTRRLSAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1749 EDQLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQQLQdaentavaRLRTQINVAEA 1828
Cdd:pfam19220 82 EGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENK--------ALREEAQAAEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1829 KVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKLK 1908
Cdd:pfam19220 154 ALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLE 233
|
....*..
gi 71983975 1909 DERRRAE 1915
Cdd:pfam19220 234 EAVEAHR 240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1086-1393 |
2.78e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1086 RKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQEL 1165
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1166 EESNDKTVLHSQLKAKRDEEYAHLQKQLEET------VKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSA 1239
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELqkerqdLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1240 ESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKK 1319
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983975 1320 NASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEE 1393
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1463-1717 |
3.01e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1463 QQLAEERNNTLLAQQERDMAHQMLR-DAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKT 1541
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKeRYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1542 KRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQLASREEDEDDRkKGLTSKIRNLTEELESEQRARQ 1621
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEEELRSLSKEFQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1622 AAIANKKKIESQISELTEKneaslrqIEDLSRQLRKAQlgwkdlqldvtEARAAMEDALAGQRDAEKRARASEDEIKRLT 1701
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDT-------ITTLTQKLTTAH-----------RKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250
....*....|....*.
gi 71983975 1702 ADIQAVSSSKRKAEAE 1717
Cdd:pfam07888 258 EELSSMAAQRDRTQAE 273
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
885-1168 |
3.16e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 885 ISDYKQQMEKMdEERLVLKTRLDAESSERAEIFEERSRMA-ARRDELEGILEEVSKRLEIEE------QKAKKADSESRK 957
Cdd:PRK04863 350 IERYQADLEEL-EERLEEQNEVVEEADEQQEENEARAEAAeEEVDELKSQLADYQQALDVQQtraiqyQQAVQALERAKQ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 958 LTEMVRHLEENLEDeersrqkllleknSIESRLKELEAQGLELEDSGNKLSKEKKALE--ERCEDLSSRLIDEVERS--- 1032
Cdd:PRK04863 429 LCGLPDLTADNAED-------------WLEEFQAKEQEATEELLSLEQKLSVAQAAHSqfEQAYQLVRKIAGEVSRSeaw 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1033 -------KQLVKAKA---RLEATVAEINdELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESEL 1102
Cdd:PRK04863 496 dvarellRRLREQRHlaeQLQQLRMRLS-ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1103 SQISIRNDEELAARQQLEREIREIRAQ------LDDAI----EETNKEKAARQKAEKARRDMAEELESYKQELEES 1168
Cdd:PRK04863 575 SEARERRMALRQQLEQLQARIQRLAARapawlaAQDALarlrEQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1087-1304 |
3.60e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1087 KAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELE 1166
Cdd:COG1340 23 EIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1167 ESNDKTVLHSQLKakrdEEYAHLQKQLEETVKSSEE---VVEEMK-----AQNQKKIEELNETIDQLKRQKISADKAKSS 1238
Cdd:COG1340 103 ELNKAGGSIDKLR----KEIERLEWRQQTEVLSPEEekeLVEKIKelekeLEKAKKALEKNEKLKELRAELKELRKEAEE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1239 AESDNENFRAELSN----IASARLEAEKKRKAAEtslmEKDHKMREMQSNLDDLMAKLSKMNNELESIQK 1304
Cdd:COG1340 179 IHKKIKELAEEAQElheeMIELYKEADELRKEAD----ELHKEIVEAQEKADELHEEIIELQKELRELRK 244
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
963-1914 |
4.35e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.59 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 963 RHLEENLEDEERSRQKLLLEKNSIESRL-KELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDE--VERSKQLVKAK 1039
Cdd:NF041483 105 RILQEHAEHQARLQAELHTEAVQRRQQLdQELAERRQTVESHVNENVAWAEQLRARTESQARRLLDEsrAEAEQALAAAR 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1040 ARLEATVAEINDELEKEKQQ-RHNAET----ARRAAETQLREEQESCLEKTRKAEEL-------TNQLMRKESELSqisi 1107
Cdd:NF041483 185 AEAERLAEEARQRLGSEAESaRAEAEAilrrARKDAERLLNAASTQAQEATDHAEQLrsstaaeSDQARRQAAELS---- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1108 RNDEELAarQQLEREIREIRAQLDDAIEETnKEKAARQKAEKarrdmaeelesykqelEESNDktvlhsQLKAKRDEEYA 1187
Cdd:NF041483 261 RAAEQRM--QEAEEALREARAEAEKVVAEA-KEAAAKQLASA----------------ESANE------QRTRTAKEEIA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1188 HL----QKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDnenfraELSNIASARLEAeKK 1263
Cdd:NF041483 316 RLvgeaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAE------EVLTKASEDAKA-TT 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1264 RKAAEtslmEKDHKMREMQSNLDDLMAKLSKMNNELesiqKAKSADETLNSNllkknasldmqlSELTEASEEDRRTRAT 1343
Cdd:NF041483 389 RAAAE----EAERIRREAEAEADRLRGEAADQAEQL----KGAAKDDTKEYR------------AKTVELQEEARRLRGE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1344 LNN-KIRQLEEDLAVAVEARDDALdaqEKIEKEVKEVKSLLAEARKKLDE----ENREVMEELRKKKEKELSAEKERADM 1418
Cdd:NF041483 449 AEQlRAEAVAEGERIRGEARREAV---QQIEEAARTAEELLTKAKADADElrstATAESERVRTEAIERATTLRRQAEET 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1419 AEQARDKAERAKKKAIQEAEDVQKELTDVVAATR-EMERKMRKFDQQLAEE--RNNTLlAQQERDMAHQMLRDAETKALV 1495
Cdd:NF041483 526 LERTRAEAERLRAEAEEQAEEVRAAAERAARELReETERAIAARQAEAAEEltRLHTE-AEERLTAAEEALADARAEAER 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1496 LSNELSEKKD------------IVDQLEKDKRTLKLEIDNLASTKDDAGKNVyelekTKRRLDEELSRAEQQIIELEDAl 1563
Cdd:NF041483 605 IRREAAEETErlrteaaerirtLQAQAEQEAERLRTEAAADASAARAEGENV-----AVRLRSEAAAEAERLKSEAQES- 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1564 qlADDARSRVEVNMQAMRSEFERQLASREEDEDDRKKGLTSKIRNLTEELESE-QRARQA-----AIANKKKIESQISEL 1637
Cdd:NF041483 679 --ADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQErERAREQseellASARKRVEEAQAEAQ 756
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1638 TEKNEASLRQIEDLS------RQLRKAQLGWKD-LQLDVTEARAAMEDAL-----AGQRDAEK--------RARASEDEI 1697
Cdd:NF041483 757 RLVEEADRRATELVSaaeqtaQQVRDSVAGLQEqAEEEIAGLRSAAEHAAertrtEAQEEADRvrsdayaeRERASEDAN 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1698 KRLTADIQAVSSSKRKAEAERDELIEEVSSLRASSFSNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMT 1777
Cdd:NF041483 837 RLRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAAAQAD 916
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1778 ADLAMERSVCER-TESDKIALERANRDLKQQLQDAENTAVARLRTQINVAEAKVSSLEQQ----LSLEEQDKMRQGRTLR 1852
Cdd:NF041483 917 RLIGEATSEAERlTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEaaetVGSAQQHAERIRTEAE 996
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1853 RMETKMAEMQQMLEEEKRQ------GESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKLKDERRRA 1914
Cdd:NF041483 997 RVKAEAAAEAERLRTEAREeadrtlDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRT 1064
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1634-1935 |
4.38e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1634 ISELTEKNEASLRQIEDLSRqLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSKRK 1713
Cdd:PRK03918 140 ILESDESREKVVRQILGLDD-YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1714 AEAERDELIEEVSSLRASSFSNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTesd 1793
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1794 kIALERANRDLKQQLQDAENTAvARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETkmaemqqmLEEEKRQGE 1873
Cdd:PRK03918 296 -IKLSEFYEEYLDELREIEKRL-SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE--------LEERHELYE 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1874 SNRQAVDrqnaRIRQLRTQLEDTEAErdRLTNKLKDERRRAEEMTDLNETLSRDVSLLKQRE 1935
Cdd:PRK03918 366 EAKAKKE----ELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1103-1217 |
4.96e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1103 SQISIRNDEELAARQQLEREIREIRAQLDDAIEETN---KEKAARQKAEKArrDMAEELESYKQELEESNDKTVLHSQLK 1179
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDeasFERLAELRDELA--ELEEELEALKARWEAEKELIEEIQELK 477
|
90 100 110
....*....|....*....|....*....|....*...
gi 71983975 1180 AKRDEEYAHLQkQLEETVKSSEEVVEEMKAQNQKKIEE 1217
Cdd:COG0542 478 EELEQRYGKIP-ELEKELAELEEELAELAPLLREEVTE 514
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1272-1375 |
5.39e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1272 MEKDHKmREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQL 1351
Cdd:PRK09039 71 LERQGN-QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAAL 149
|
90 100
....*....|....*....|....
gi 71983975 1352 EEDLAvAVEArddALDAQEKIEKE 1375
Cdd:PRK09039 150 RRQLA-ALEA---ALDASEKRDRE 169
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1803-1940 |
7.93e-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: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1803 DLKQQLQDAENtAVARLRTQINV--AEAKVSSLEQQLS-LEEQdkmrqgrtLRRMETKMAEMQQMLEEEKRQGESNRQAV 1879
Cdd:COG3206 186 ELRKELEEAEA-ALEEFRQKNGLvdLSEEAKLLLQQLSeLESQ--------LAEARAELAEAEARLAALRAQLGSGPDAL 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1880 DR--QNARIRQLRTQLEDTEAERDRLTNKLKD---------------ERRRAEEMTDLNETLSRDVSLLKQRETTARR 1940
Cdd:COG3206 257 PEllQSPVIQQLRAQLAELEAELAELSARYTPnhpdvialraqiaalRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1116-1925 |
7.98e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.82 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1116 RQQLEREIREIRAQLDDAIEEtNKEKAARQKAE------KARRDMAEELESYKQELEES-NDKTVLHSQLKAKRDEEYAH 1188
Cdd:NF041483 89 RADAERELRDARAQTQRILQE-HAEHQARLQAElhteavQRRQQLDQELAERRQTVESHvNENVAWAEQLRARTESQARR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1189 LqkqLEETVKSSEEVVEEMKAQNQKKIEElnetidqlKRQKISADKAKSSAESDnenfraelSNIASARLEAEKKRKAAE 1268
Cdd:NF041483 168 L---LDESRAEAEQALAAARAEAERLAEE--------ARQRLGSEAESARAEAE--------AILRRARKDAERLLNAAS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1269 TSLMEKDHKMREMQSNlddlmaklskmnNELESIQKAKSADEtlnsnlLKKNASLDMQlseltEASEEDRRTRATLNNKI 1348
Cdd:NF041483 229 TQAQEATDHAEQLRSS------------TAAESDQARRQAAE------LSRAAEQRMQ-----EAEEALREARAEAEKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1349 RQLEEDLAVAVEARDDALDAQEKIEKEvkEVKSLLAEARKKLDEENREVmeeLRKKKEKELSAEKERADMAEQARD---- 1424
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQRTRTAKE--EIARLVGEATKEAEALKAEA---EQALADARAEAEKLVAEAAEKARTvaae 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1425 -------KAERAKKKAIQEAEDVQKELTDvvAATREMERKMRKFDQQLAEERNNTL-LAQQERDMAHQMLRDAETKALVL 1496
Cdd:NF041483 361 dtaaqlaKAARTAEEVLTKASEDAKATTR--AAAEEAERIRREAEAEADRLRGEAAdQAEQLKGAAKDDTKEYRAKTVEL 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1497 SNELSEKKDIVDQLEKDKRTLKLEIDNLASTKddagkNVYELEKTKRRLDEELSRAEQQIIELE------------DALQ 1564
Cdd:NF041483 439 QEEARRLRGEAEQLRAEAVAEGERIRGEARRE-----AVQQIEEAARTAEELLTKAKADADELRstataeservrtEAIE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1565 LADDARSRVEVNMQAMRSEFERQLASREEDEDDRKKGLTSKIRNLTEELESEQRARQAAIAnkkkiesqiseltekneas 1644
Cdd:NF041483 514 RATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAA------------------- 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1645 lrqiEDLSRqlrkaqlgwkdLQLDVTEARAAMEDALAGQR-DAEKRARASEDEIKRLTADI-QAVSSSKRKAEAE----R 1718
Cdd:NF041483 575 ----EELTR-----------LHTEAEERLTAAEEALADARaEAERIRREAAEETERLRTEAaERIRTLQAQAEQEaerlR 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1719 DELIEEVSSLRAS---------SFSNEEKRRLEAKVIDLEDQLDEEASAnelAQEKVrkSQQQLEQMTAdlAMERSVCER 1789
Cdd:NF041483 640 TEAAADASAARAEgenvavrlrSEAAAEAERLKSEAQESADRVRAEAAA---AAERV--GTEAAEALAA--AQEEAARRR 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1790 TESDKI---ALERANRDLKQ-QLQDAENTAVARLRtqinVAEAKVsslEQQLSLEEQDKmRQG-------RTLRRMETKM 1858
Cdd:NF041483 713 REAEETlgsARAEADQERERaREQSEELLASARKR----VEEAQA---EAQRLVEEADR-RATelvsaaeQTAQQVRDSV 784
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1859 AEMQQMLEEE--------KRQGESNRQAVDRQNARIRQlrtqleDTEAERDRLTNKLKDERRRAEEMTDLNETLS 1925
Cdd:NF041483 785 AGLQEQAEEEiaglrsaaEHAAERTRTEAQEEADRVRS------DAYAERERASEDANRLRREAQEETEAAKALA 853
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
943-1077 |
9.22e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 943 IEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLlleknsiESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLS 1022
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRL-------EEQVERLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1023 SRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREE 1077
Cdd:COG2433 455 SEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGE 509
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1135-1439 |
9.35e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1135 EETNKEKAARQKAEKARrdmaEELESYKQELEESNDKTvlhSQLKAKRDEeyahLQKQLEETVKSSEEVVEEMKaQNQKK 1214
Cdd:COG1340 5 ELSSSLEELEEKIEELR----EEIEELKEKRDELNEEL---KELAEKRDE----LNAQVKELREEAQELREKRD-ELNEK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1215 IEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMRemqsnlddLMAKLSK 1294
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKE--------LVEKIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1295 MNNELESIQKAKSADEtlnsnllkknasldmQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEK 1374
Cdd:COG1340 145 LEKELEKAKKALEKNE---------------KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRK 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1375 EVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAED 1439
Cdd:COG1340 210 EADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
934-1055 |
9.42e-04 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 43.07 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 934 LEEVSKRLEIEEQKAKKADSESrKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQgleledsGNKLSKEKKA 1013
Cdd:pfam14932 49 LDEALKTISAESPGLLNQQDVE-ALEESLEEIREATEDLEAELQELQKTKQLKINRLNKLQAQ-------ASSLSQGLRA 120
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 71983975 1014 LEERCEdlssrlidevERSKQLVKAKARLEATVAEINDELEK 1055
Cdd:pfam14932 121 LVAEEE----------EAAKQLEELQEELAALNAKTNNVLQS 152
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
902-1070 |
1.08e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.52 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 902 LKTRLDAESSER----AEIFEERSRMAARRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDeersrq 977
Cdd:pfam19220 214 LEGQLAAEQAEReraeAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKE------ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 978 kLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDE---VERSKQLVKA---------------K 1039
Cdd:pfam19220 288 -ASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKdaaLERAEERIASlsdriaeltkrfeveR 366
|
170 180 190
....*....|....*....|....*....|.
gi 71983975 1040 ARLEATVAEINDELEKEKQQRHNAETARRAA 1070
Cdd:pfam19220 367 AALEQANRRLKEELQRERAERALAQGALEIA 397
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1665-1873 |
1.28e-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: 43.18 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1665 LQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLtadiQAVSSSKRKAEAERDELIEEVSSLRAssfsneekrrleak 1744
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRL----QALESELAISRQDYDGATAQLRAAQA-------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1745 vidledqldeeasanelaqeKVRKSQQQLEQMTADLAmersvceRTESdkialeRANRDL--KQQLQDAENtAVARLRTQ 1822
Cdd:pfam00529 111 --------------------AVKAAQAQLAQAQIDLA-------RRRV------LAPIGGisRESLVTAGA-LVAQAQAN 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1823 INVAEAKVSSLEQQLSLEEQDKMRQ-GRTLRRMETKMAEMQQMLEEEKRQGE 1873
Cdd:pfam00529 157 LLATVAQLDQIYVQITQSAAENQAEvRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
787-1001 |
1.35e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 787 EFEEMRDQKLSALIESFQAQCRGWLGRRVMVRRREQEVAIKILQRNGLAWMRLREWQWWRLLTKVKPLLEVTNKDE---L 863
Cdd:pfam17380 361 ELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvrrL 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 864 IAEREQELkvtaEKLRRSEVfisDYKQQMEKM---DEERLVLKTRLDAESSERAEIFEERSRMAAR--RDELEGILEEVS 938
Cdd:pfam17380 441 EEERAREM----ERVRLEEQ---ERQQQVERLrqqEEERKRKKLELEKEKRDRKRAEEQRRKILEKelEERKQAMIEEER 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 939 KR----LEIEEQKAKKADSESRKLTEMVRHLEENLED------------EERSRQKLLLEKNSIESRLKELEAQGLELE 1001
Cdd:pfam17380 514 KRklleKEMEERQKAIYEEERRREAEEERRKQQEMEErrriqeqmrkatEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
913-1228 |
1.51e-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: 43.30 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 913 RAEIFEERSRMAARRDELEGILEEVSKRLEIEEQKAKKADSesrkltemvrhleenLEDEERSRQKLLLEKN-------- 984
Cdd:pfam06160 85 KKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEE---------------LKDKYRELRKTLLANRfsygpaid 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 985 SIESRLKELE---AQGLELEDSGN---------KLSKEKKALEERCEDLSSRL----------IDEVER----------- 1031
Cdd:pfam06160 150 ELEKQLAEIEeefSQFEELTESGDylearevleKLEEETDALEELMEDIPPLYeelktelpdqLEELKEgyremeeegya 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1032 -------------SKQLVKAKARLE----ATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQ 1094
Cdd:pfam06160 230 lehlnvdkeiqqlEEQLEENLALLEnlelDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1095 LMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQkaekarrDMAEELESYKQELEESNDKtvl 1174
Cdd:pfam06160 310 LKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYS-------ELQEELEEILEQLEEIEEE--- 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 71983975 1175 hsqlkakrdeeyahlQKQLEETVKSSEEvvEEMKAqnQKKIEELNETIDQLKRQ 1228
Cdd:pfam06160 380 ---------------QEEFKESLQSLRK--DELEA--REKLDEFKLELREIKRL 414
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1190-1618 |
1.52e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1190 QKQLEETVKSSEEVVEEMKAQNQKkIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEkkrkaaet 1269
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDK-IDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTL-------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1270 slmekdhkmremqsNLDDLMAKLSKMNNELESIQKAKSadeTLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKI- 1348
Cdd:PRK11281 122 --------------SLRQLESRLAQTLDQLQNAQNDLA---EYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKv 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1349 --RQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAE-ARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDK 1425
Cdd:PRK11281 185 ggKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDlLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTVQE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1426 AERAKKKA-IQEAEDVQKELtdvvAATREMERKMRKfdqqlAEERNNTL-------------LAQQERDMAHQMlrDAET 1491
Cdd:PRK11281 265 AQSQDEAArIQANPLVAQEL----EINLQLSQRLLK-----ATEKLNTLtqqnlrvknwldrLTQSERNIKEQI--SVLK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1492 KALVLSNELSEKKDIVDQLEKDKRtLKLEIDNLastkddagkNVYELEKTKRRldEELSRAEQQIIELEdalqladdARS 1571
Cdd:PRK11281 334 GSLLLSRILYQQQQALPSADLIEG-LADRIADL---------RLEQFEINQQR--DALFQPDAYIDKLE--------AGH 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 71983975 1572 RVEVNmQAMRSEFERQLASREEDEDDRKKGLTSKIrNLTEELESEQR 1618
Cdd:PRK11281 394 KSEVT-DEVRDALLQLLDERRELLDQLNKQLNNQL-NLAINLQLNQQ 438
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1537-1779 |
1.52e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1537 ELEKTKRRLDEELSRAEQQIIELEDALQladdarsrvevnmqamrsEFERQlaSREEDEDDRKKGLTSKIRNLTEELESE 1616
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALE------------------EFRQK--NGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1617 QRARQAAIANKKKIESQISELTEKNEASLR--QIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARAse 1694
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ-- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1695 dEIKRLTADIQAvssSKRKAEAERDELIEEVSSLRASSFSNEEKrrlEAKVIDLEDQLDEEASANELAQEKVRKSQQQLE 1774
Cdd:COG3206 310 -EAQRILASLEA---ELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
....*
gi 71983975 1775 QMTAD 1779
Cdd:COG3206 383 LTVGN 387
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
818-1348 |
1.61e-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: 43.50 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 818 RRREQEVAIKILQRNGLAWMRLREWQWWRLLTKVKPLLEVTNKDELIAEREQELKVTAEKlrrsevfisDYKQQMEKMDE 897
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE---------QETLLGTIMPE 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 898 ERLVLKTRLDAESSER--AEIFEERSRMAARRDELEGIleEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERS 975
Cdd:TIGR00606 781 EESAKVCLTDVTIMERfqMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 976 RQKLlleknsiESRLKELEAQGLELEDSgnklSKEKKALEERCEDLSSrlidEVERSKQLVKAKARLEATVAEINDELEK 1055
Cdd:TIGR00606 859 IQHL-------KSKTNELKSEKLQIGTN----LQRRQQFEEQLVELST----EVQSLIREIKDAKEQDSPLETFLEKDQQ 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1056 EKQQR-HNAETARRAAETQLREEQESCLEKTRKAEELTN--------QLMRKESELSQISIRNDEELAARQQLEREIREI 1126
Cdd:TIGR00606 924 EKEELiSSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkiqdgkddYLKQKETELNTVNAQLEECEKHQEKINEDMRLM 1003
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1127 RAQLDDA--IEETNKEKAARQKAEKARRDMAEELesyKQELEESNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEVV 1204
Cdd:TIGR00606 1004 RQDIDTQkiQERWLQDNLTLRKRENELKEVEEEL---KQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGY 1080
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1205 EEMKAQNQKKIEElnetidqlkrqkisadKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLME-KDHKMREMQS 1283
Cdd:TIGR00606 1081 EKEIKHFKKELRE----------------PQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKfHSMKMEEINK 1144
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983975 1284 NLDDLMAKLSKmNNELESIQKAKSADETLNSNllKKNASLDMQLSELTEASEEDRRTRATLNNKI 1348
Cdd:TIGR00606 1145 IIRDLWRSTYR-GQDIEYIEIRSDADENVSAS--DKRRNYNYRVVMLKGDTALDMRGRCSAGQKV 1206
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
1126-1395 |
1.61e-03 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 43.18 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1126 IRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEEsnDKTVLHSQLKAKRDEEYAHLQKQleetvksSEEVVE 1205
Cdd:PRK13428 37 VRQQLAESATAADRLAEADQAHTKAVEDAKAEAARVVEEARE--DAERIAEQLRAQADAEAERIKVQ-------GARQVQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1206 EMKAQ--NQKKIEELNETIDQ---LKRQKIsADKAKSSAESDneNFRAELSNIASARLEAE-----KKRKAAETSLMEKD 1275
Cdd:PRK13428 108 LLRAQltRQLRLELGHESVRQageLVRNHV-ADPAQQSATVD--RFLDELDAMAPSTADVDypllaKMRSASRRALASLV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1276 HKMREMQSNLDDlmAKLSKMNNELESIqkaksadetlnSNLLKKNASLDMQLSELTEASEEDRRTRATL-NNKIRQLEED 1354
Cdd:PRK13428 185 DRFDSVAADLDN--QALTTLADELVSV-----------AKLLDREPVLTKHLTEPAEDAAPKIRLVERLfSGKVGAPTLE 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 71983975 1355 -LAVAVEAR----DDALDAQEKI-----------EKEVKEVKSLLAEARKKLDEENR 1395
Cdd:PRK13428 252 vLRTAVSQRwsanSDLIDALEHVarlalleraerAGQVDEVEDQLFRFSRILDAQPR 308
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
928-1183 |
1.66e-03 |
|
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: 43.21 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 928 DELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLlekNSIESRLKELEAQgleledSGNKL 1007
Cdd:pfam09731 215 DAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIF---PDIIPVLKEDNLL------SNDDL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1008 SKEKKALEERCEDLSSRLIDeverskQLVKAKARLEATVAEINDELEK-EKQQRHNAETARRAAETQLREEQESCLEKTR 1086
Cdd:pfam09731 286 NSLIAHAHREIDQLSKKLAE------LKKREEKHIERALEKQKEELDKlAEELSARLEEVRAADEAQLRLEFEREREEIR 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1087 KA--EELTNQLMRKESELSQisIRNDEELAARQQLEREIREIraqLDDAIEEtnkEKAARQ----KAEKARRDMAEELES 1160
Cdd:pfam09731 360 ESyeEKLRTELERQAEAHEE--HLKDVLVEQEIELQREFLQD---IKEKVEE---ERAGRLlklnELLANLKGLEKATSS 431
|
250 260
....*....|....*....|...
gi 71983975 1161 YKQELEESNDKTVLHSQLKAKRD 1183
Cdd:pfam09731 432 HSEVEDENRKAQQLWLAVEALRS 454
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
951-1164 |
1.74e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 951 ADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDEVE 1030
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1031 RSKQ----------LVKAK---------ARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEEL 1091
Cdd:COG3883 94 ALYRsggsvsyldvLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71983975 1092 TNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQE 1164
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1814-1920 |
1.76e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1814 TAVARLRTQINVAEAKVSSLEQQL-SLE--------EQDKMRQGRtLRRMETKMAEMQQMLEEEKRQGESNRQAVDRqna 1884
Cdd:COG0542 397 EAAARVRMEIDSKPEELDELERRLeQLEiekealkkEQDEASFER-LAELRDELAELEEELEALKARWEAEKELIEE--- 472
|
90 100 110
....*....|....*....|....*....|....*.
gi 71983975 1885 rIRQLRTQLEDTEAERDRLTNKLKDERRRAEEMTDL 1920
Cdd:COG0542 473 -IQELKEELEQRYGKIPELEKELAELEEELAELAPL 507
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1369-1705 |
1.79e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1369 QEKIEKEvKEVKSLLAEARKKLDEENRevmeelrkkkEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVV 1448
Cdd:pfam17380 298 QERLRQE-KEEKAREVERRRKLEEAEK----------ARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1449 AATREME-RKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKrtlkleidnlast 1527
Cdd:pfam17380 367 QEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR------------- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1528 kddagknvyelEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQLASREEDEDDRKKGLTSKI- 1606
Cdd:pfam17380 434 -----------QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELe 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1607 ---RNLTEE------LESEQRARQAAIANKKkiESQISELTEKNEASLRQIEDLSRQLRKAqlgwkdlqldvTEARAAME 1677
Cdd:pfam17380 503 erkQAMIEEerkrklLEKEMEERQKAIYEEE--RRREAEEERRKQQEMEERRRIQEQMRKA-----------TEERSRLE 569
|
330 340
....*....|....*....|....*...
gi 71983975 1678 dALAGQRDAEKRARASEDEIKRLTADIQ 1705
Cdd:pfam17380 570 -AMEREREMMRQIVESEKARAEYEATTP 596
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1044-1293 |
1.88e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1044 ATVAEINDELEKEKQQRHNAETARRAAETQLREEQEsclektrkaeeltnqlmrkeselsqisiRNDEELAARQQLEREI 1123
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQ----------------------------KQAAEQERLKQLEKER 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1124 REIRAQLDDAIEETNKEKAARQKAEKARrdmAEELESYKQELEESNDKtvlhSQLKAKRDEEYAHLQKQLEETVKSSEEV 1203
Cdd:PRK09510 111 LAAQEQKKQAEEAAKQAALKQKQAEEAA---AKAAAAAKAKAEAEAKR----AAAAAKKAAAEAKKKAEAEAAKKAAAEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1204 VEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDhkmremQS 1283
Cdd:PRK09510 184 KKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA------AA 257
|
250
....*....|
gi 71983975 1284 NLDDLMAKLS 1293
Cdd:PRK09510 258 EVDDLFGGLD 267
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1063-1245 |
1.92e-03 |
|
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: 43.22 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1063 AETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQisirNDEELAARQQLEREIREIRAQLDDAIEETNKEKA 1142
Cdd:pfam18971 601 AEAKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSG----NKNKMEAKAQANSQKDEIFALINKEANRDARAIA 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1143 ARQKAEKARRDMAEELESYKQELEesnDKTVLHSQLKAKRDEEYAhlqkQLEETVKSSEEVVEEMKAQNQ--KKIEELNE 1220
Cdd:pfam18971 677 YTQNLKGIKRELSDKLEKISKDLK---DFSKSFDEFKNGKNKDFS----KAEETLKALKGSVKDLGINPEwiSKVENLNA 749
|
170 180
....*....|....*....|....*
gi 71983975 1221 TIDQLKRQKISADKAKSSAESDNEN 1245
Cdd:pfam18971 750 ALNEFKNGKNKDFSKVTQAKSDLEN 774
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1034-1222 |
1.99e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1034 QLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMrkeselsqiSIRNDEEL 1113
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG---------NVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1114 AArqqLEREIreiraqlddaieetNKEKAARQKAEKARRDMAEELESYKQELEESNDKtvlhsqlKAKRDEEYAHLQKQL 1193
Cdd:COG1579 92 EA---LQKEI--------------ESLKRRISDLEDEILELMERIEELEEELAELEAE-------LAELEAELEEKKAEL 147
|
170 180
....*....|....*....|....*....
gi 71983975 1194 EETVKSSEEVVEEMKAQNQKKIEELNETI 1222
Cdd:COG1579 148 DEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1158-1446 |
2.26e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.11 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1158 LESYKQELEESNDKTVLHSQLKAKRDEE-YAHLQKQLEETVKSSEEVVEEMKAQNQKKIEelNETIDQLK-RQKISADKA 1235
Cdd:PTZ00108 1101 KEKVEKLNAELEKKEKELEKLKNTTPKDmWLEDLDKFEEALEEQEEVEEKEIAKEQRLKS--KTKGKASKlRKPKLKKKE 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1236 KSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDhkMREMQSNLDDLMAKLSKMNNELESIQKAKSADEtLNSN 1315
Cdd:PTZ00108 1179 KKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKS--NSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSS-KSSE 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1316 LLKKNASLDMQLSELTEASEEDRRTRATLNNKI-RQLEEDLAVAVEARDDALDaqekieKEVKEVKSLLAEARKKLDEEN 1394
Cdd:PTZ00108 1256 DNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPsKRPDGESNGGSKPSSPTKK------KVKKRLEGSLAALKKKKKSEK 1329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1395 REVmeelrkkKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTD 1446
Cdd:PTZ00108 1330 KTA-------RKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVD 1374
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1585-1940 |
2.47e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1585 ERQLASREEDEDDRKKGLTSKIR--NLTEELEsEQRARQAAIAnkkkIESQI-SELTEKNEASLRQIEDLSRqlRKAQLG 1661
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRlvEMARELE-ELSARESDLE----QDYQAaSDHLNLVQTALRQQEKIER--YQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1662 wkDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRL---------------TADIQAVSSSKRKAEAER----DELI 1722
Cdd:COG3096 358 --ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLksqladyqqaldvqqTRAIQYQQAVQALEKARAlcglPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1723 EEVSSLRASSFSNEEKRrLEAKVIDLEDQLdeeaSANELAQEKVRKSQQQLEQMTADLamersvcERTESDKIALE--RA 1800
Cdd:COG3096 436 PENAEDYLAAFRAKEQQ-ATEEVLELEQKL----SVADAARRQFEKAYELVCKIAGEV-------ERSQAWQTAREllRR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1801 NRDLKQQLQDAENtavarLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMEtkmaEMQQMLEEEKRQGESNRQAVD 1880
Cdd:COG3096 504 YRSQQALAQRLQQ-----LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE----ELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1881 RQNARIRQLRTQLEDTEAERDRLTNK------LKDERRRAEEMTDLNETLSRDVS------LLKQRETTARR 1940
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTaamqqlLEREREATVER 646
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
868-1060 |
2.66e-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: 41.55 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 868 EQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRlDAESSERAEIFEERSRMAARRDE-LEGILEEVSKRLEIEEQ 946
Cdd:pfam00261 49 EEELERTEERLAEALEKLEEAEKAADESERGRKVLENR-ALKDEEKMEILEAQLKEAKEIAEeADRKYEEVARKLVVVEG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 947 KAKKADSESRKLTEMVRHLEENLedeersrqkllleKNSIESrLKELEAqgleledSGNKLSKEKKALEERCEDLSSRLI 1026
Cdd:pfam00261 128 DLERAEERAELAESKIVELEEEL-------------KVVGNN-LKSLEA-------SEEKASEREDKYEEQIRFLTEKLK 186
|
170 180 190
....*....|....*....|....*....|....
gi 71983975 1027 DEVERSKQLVKAKARLEATVAEINDELEKEKQQR 1060
Cdd:pfam00261 187 EAETRAEFAERSVQKLEKEVDRLEDELEAEKEKY 220
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1039-1228 |
2.81e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1039 KARLEATVAEINDELEKEKQQRHNAETARRaaetQLREEQEScLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQ 1118
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALE----EFRQKNGL-VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1119 LEREIREIRAQLDDAIEETNKEKAARQKAEkARRDMAEELESYKQEleesndktvlHSQLKAKRdEEYAHLQKQLEETVK 1198
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAE-LEAELAELSARYTPN----------HPDVIALR-AQIAALRAQLQQEAQ 312
|
170 180 190
....*....|....*....|....*....|
gi 71983975 1199 SSEEVVEEMKAQNQKKIEELNETIDQLKRQ 1228
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEAR 342
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1159-1644 |
2.94e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.73 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1159 ESYKQELEESNDKTvlHSQLKAKRD---EEYAHLqkqleeTVKSSEEVVEEMKAQNQKKIEELNETIdqlkrqkisadKA 1235
Cdd:PTZ00108 900 EDYKEFLESETLKE--KDVIVDYRDystANTVHF------TVKLNDGVLEQWEEEGIEKVFKLKSTI-----------ST 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1236 KSSAESDNENFRAELSNIAS-------ARLEAEKKRKAAETSLMEKDhkmREMQSNlddlMAKLSKM--NNELEsIQKAK 1306
Cdd:PTZ00108 961 TNMVLFDENGKIKKYSDALDilkefylVRLDLYKKRKEYLLGKLERE---LARLSN----KVRFIKHviNGELV-ITNAK 1032
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1307 SAD--ETL-------NSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEED-------LAVAVEARDDALDAQE 1370
Cdd:PTZ00108 1033 KKDlvKELkklgyvrFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSYDyllsmpiWSLTKEKVEKLNAELE 1112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1371 KIEKEVKEVKSL---------LAEARKKLDEEnREVMEELRKKKEKELSAEKERADMAEQARDKAErAKKKAIQEAEDVQ 1441
Cdd:PTZ00108 1113 KKEKELEKLKNTtpkdmwledLDKFEEALEEQ-EEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKK-EKKKKKSSADKSK 1190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1442 KELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKAL-VLSNELSEKKDIVDQLEKDKRTLKle 1520
Cdd:PTZ00108 1191 KASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLkSKKNNSSKSSEDNDEFSSDDLSKE-- 1268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1521 iDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQiieledalqlADDARSRVEVNMQAMRSEFErqLASREEDEDDRKK 1600
Cdd:PTZ00108 1269 -GKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKP----------SSPTKKKVKKRLEGSLAALK--KKKKSEKKTARKK 1335
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 71983975 1601 GLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEAS 1644
Cdd:PTZ00108 1336 KSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDE 1379
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1338-1677 |
3.20e-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: 42.53 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1338 RRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERAD 1417
Cdd:pfam06160 85 KKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1418 MAE--------QARDKAERAKKKAIQEAEDVQK--------------ELTDVVAATREMERKMRKFD--------QQLAE 1467
Cdd:pfam06160 165 FEEltesgdylEAREVLEKLEEETDALEELMEDipplyeelktelpdQLEELKEGYREMEEEGYALEhlnvdkeiQQLEE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1468 ERNNTL--LAQQERDMAHQMLRDAET---------------KALVLSNeLSEKKDIVDQLEKDKRTLKLEIDNLASTkdd 1530
Cdd:pfam06160 245 QLEENLalLENLELDEAEEALEEIEEridqlydllekevdaKKYVEKN-LPEIEDYLEHAEEQNKELKEELERVQQS--- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1531 agknvYELEktkrrlDEELSRA---EQQIIELEDALQLADDARSRVEVNMQAMRSEFERQLASREEDEDDRKKgLTSKIR 1607
Cdd:pfam06160 321 -----YTLN------ENELERVrglEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEE-FKESLQ 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1608 NLTEElesEQRARQAAIANKKKIESQISELTEKN------------EASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAA 1675
Cdd:pfam06160 389 SLRKD---ELEAREKLDEFKLELREIKRLVEKSNlpglpesyldyfFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDD 465
|
..
gi 71983975 1676 ME 1677
Cdd:pfam06160 466 VD 467
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
953-1776 |
3.26e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 953 SESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEaqgLELEDSGNKLSKEKKALEERCEDLSSRLIDEVERS 1032
Cdd:PTZ00440 721 NSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFI---LHLYENDKDLPDGKNTYEEFLQYKDTILNKENKIS 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1033 KQLVKakarLEATVAEINDELEK--EKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISirnd 1110
Cdd:PTZ00440 798 NDINI----LKENKKNNQDLLNSynILIQKLEAHTEKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNII---- 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1111 eelaarQQLEREIREIRA--QLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELE-----ESNDKTVLHSQLKakrd 1183
Cdd:PTZ00440 870 ------KDIENMNKNINIikTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINtdniiQKNEKLNLLNNLN---- 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1184 EEYAHLQKQLeetvksSEEVVEEMKAQNQKKIEELNET-----------IDQLKRQKISADKAKSSAESDNENFRAELSN 1252
Cdd:PTZ00440 940 KEKEKIEKQL------SDTKINNLKMQIEKTLEYYDKSkeningndgthLEKLDKEKDEWEHFKSEIDKLNVNYNILNKK 1013
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1253 IASARLEAEKKRKAAETSLM-EKDHKMRE----MQSNLDDLMAKLSKMNNEL-----------ESIQKAKSADETLNSNL 1316
Cdd:PTZ00440 1014 IDDLIKKQHDDIIELIDKLIkEKGKEIEEkvdqYISLLEKMKTKLSSFHFNIdikkyknpkikEEIKLLEEKVEALLKKI 1093
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1317 LKKNASLD---MQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEE 1393
Cdd:PTZ00440 1094 DENKNKLIeikNKSHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVNEIEIEYERILIDH 1173
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1394 NREVMeelrkkkekelsaeKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVvaaTREMERKmRKFDQQLAEERN--- 1470
Cdd:PTZ00440 1174 IVEQI--------------NNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDH---LTTFEYN-AYYDKATASYENiee 1235
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1471 -----NTLLAQQERDmahQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDA-----GKNVYELEK 1540
Cdd:PTZ00440 1236 ltteaKGLKGEANRS---TNVDELKEIKLQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEKilkeiLNSTKKAEE 1312
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1541 TKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMqamrseferqlasreedEDDRKKGLTSKIRNLTEELeseqrar 1620
Cdd:PTZ00440 1313 FSNDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSL-----------------EDKQIDDEIKKIEQIKEEI------- 1368
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1621 qaaIANKKKIESQISELTEKNEASLRQIEDLSRQLRKaqlgwkdlqLDVTEARAAMEDALAGQRDAEKraraSEDEIKRL 1700
Cdd:PTZ00440 1369 ---SNKRKEINKYLSNIKSNKEKCDLHVRNASRGKDK---------IDFLNKHEAIEPSNSKEVNIIK----ITDNINKC 1432
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 1701 TADIQAVSSSKRKAEAERDELIE---EVSSLRASSFSNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQM 1776
Cdd:PTZ00440 1433 KQYSNEAMETENKADENNDSIIKyekEITNILNNSSILGKKTKLEKKKKEATNIMDDINGEHSIIKTKLTKSSEKLNQL 1511
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
865-1157 |
3.39e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 865 AEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRLEIE 944
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLRE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 945 EQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSSR 1024
Cdd:pfam13868 131 EIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1025 LIDEVERskqlvKAKARleatvaeindELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQ 1104
Cdd:pfam13868 211 YQEEQER-----KERQK----------EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 71983975 1105 ISIRNDEELAARQQ-----LEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEE 1157
Cdd:pfam13868 276 IEQEEAEKRRMKRLehrreLEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEE 333
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1592-1940 |
3.61e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1592 EEDEDDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLRKAQlgwkdlqldvTE 1671
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKRE----------ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1672 ARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRASSFSNEEKRRL-EAKVIDLED 1750
Cdd:pfam02029 75 RQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKwSTEVRQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1751 QLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVcerTESDKIALERANRDLKQQLQDAEntavarlrtqinvaeakv 1830
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKV---KYESKVFLDQKRGHPEVKSQNGE------------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1831 sslEQQLSLEEQDKMRQGRTLRRMETKmAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQLEDTEAERDRLtNKLKDE 1910
Cdd:pfam02029 214 ---EEVTKLKVTTKRRQGGLSQSQERE-EEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEEL-KKKREE 288
|
330 340 350
....*....|....*....|....*....|
gi 71983975 1911 RRRAEEMTDLNETLSRDVSLLKQRETTARR 1940
Cdd:pfam02029 289 RRKLLEEEEQRRKQEEAERKLREEEEKRRM 318
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1415-1921 |
3.61e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1415 RADMAEQARDKAERAKKKAiQEAEDVQK---------ELT-DVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQ 1484
Cdd:PRK10246 369 RAQFSQQTSDREQLRQWQQ-QLTHAEQKlnalpaitlTLTaDEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQV 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1485 MLRDAETKALVLSNELSEKKdivdQLEKDKRTLKLEIdnlastkddagKNVYELEKTKRRLDEELSR------------A 1552
Cdd:PRK10246 448 AIQNVTQEQTQRNAALNEMR----QRYKEKTQQLADV-----------KTICEQEARIKDLEAQRAQlqagqpcplcgsT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1553 EQQIIELEDALQLADDarsrvevnmQAMRSEFERQLASREEDeddrKKGLTSKIRNLTEELESEQRARQAAIANKKKIES 1632
Cdd:PRK10246 513 SHPAVEAYQALEPGVN---------QSRLDALEKEVKKLGEE----GAALRGQLDALTKQLQRDESEAQSLRQEEQALTQ 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1633 QISELTEKNEASLRQIEDLSRQLRKAQLgwKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKR-LTADIQAVSSS- 1710
Cdd:PRK10246 580 QWQAVCASLNITLQPQDDIQPWLDAQEE--HERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQqLLTALAGYALTl 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1711 -----------KRKAEAER--------DELIEEVSSLR---------------ASSFSNEEKRRLEAKVIDLEDQLDEEA 1756
Cdd:PRK10246 658 pqedeeaswlaTRQQEAQSwqqrqnelTALQNRIQQLTplletlpqsddlphsEETVALDNWRQVHEQCLSLHSQLQTLQ 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1757 SANELAQEKVRKSQQQLeqmtaDLAMERSVCERTESDKIAL--ERANRDLKQQLQDAENtavaRLRTQINVAEAKVSSLE 1834
Cdd:PRK10246 738 QQDVLEAQRLQKAQAQF-----DTALQASVFDDQQAFLAALldEETLTQLEQLKQNLEN----QRQQAQTLVTQTAQALA 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1835 QQLSLEEQDkMRQGRTLRRMETKMAEM-QQMLEEEKRQGEsnrqavdrqnarIRQLRTQLEDTEAERDRLTNKLKDERRR 1913
Cdd:PRK10246 809 QHQQHRPDG-LDLTVTVEQIQQELAQLaQQLRENTTRQGE------------IRQQLKQDADNRQQQQALMQQIAQATQQ 875
|
....*...
gi 71983975 1914 AEEMTDLN 1921
Cdd:PRK10246 876 VEDWGYLN 883
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
938-1111 |
3.77e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 938 SKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKnSIESRLKELEAQGLELEDSGNKLSKEKKALEER 1017
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEK-ELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1018 CEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEK--------EKQQ---RHNAETARRAAETQLREEQESCLEKTR 1086
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaeeAKEIlleKVEEEARHEAAVLIKEIEEEAKEEADK 188
|
170 180 190
....*....|....*....|....*....|..
gi 71983975 1087 KAEELTNQLMRK-------ESELSQISIRNDE 1111
Cdd:PRK12704 189 KAKEILAQAIQRcaadhvaETTVSVVNLPNDE 220
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1321-1479 |
3.80e-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: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1321 ASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDE--ENREV- 1397
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1398 --------MEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEER 1469
Cdd:COG1579 93 alqkeiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
170
....*....|
gi 71983975 1470 NNTLLAQQER 1479
Cdd:COG1579 173 PPELLALYER 182
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1711-1893 |
4.07e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.76 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1711 KRKAEAERDElIEEVSSLRASSFSNEEKRRLEAKVIDL-------------EDQLDEEASANELAQEKVRKSQQQLEQM- 1776
Cdd:COG3524 126 RRRVKVEYDS-TSGIITLEVRAFDPEDAQAIAEALLAEseelvnqlserarEDAVRFAEEEVERAEERLRDAREALLAFr 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1777 --------TADLAMERSVCERTESDKIALeRANRDLKQQLQDAENTAVARLRTQINvaeakvsSLEQQLSlEEQDKMRQG 1848
Cdd:COG3524 205 nrngildpEATAEALLQLIATLEGQLAEL-EAELAALRSYLSPNSPQVRQLRRRIA-------ALEKQIA-AERARLTGA 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 71983975 1849 RTLRRMETKMAEMqQMLEEEK----RQGESNRQAVDrqNARIRQLRTQL 1893
Cdd:COG3524 276 SGGDSLASLLAEY-ERLELERefaeKAYTSALAALE--QARIEAARQQR 321
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1537-1919 |
4.29e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 42.28 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1537 ELEKTKRRLDEELSRAEQ-QIIEL--EDALQLADDARSRVEVNMQAMRSEFERQL---ASREEdeddrkkgltskIRNLT 1610
Cdd:pfam13779 448 GLRSALARLELARSDEALdEVADLlwELALRIEDGDLSDAERRLRAAQERLSEALergASDEE------------IAKLM 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1611 EELES---------EQRARQAAIANKKKIESQISELTEKN-EASLRQIEDLSRQLRKAQLGwkdlQLdVTEARAAMEDAL 1680
Cdd:pfam13779 516 QELREalddymqalAEQAQQNPQDLQQPDDPNAQEMTQQDlQRMLDRIEELARSGRRAEAQ----QM-LSQLQQMLENLQ 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1681 AGQRDAEKRARASEdeikrltadiqavsssKRKAEAERDELIEEVSSLRASSFSNEEKRRLEAKVIDLED--QLDEEASA 1758
Cdd:pfam13779 591 AGQPQQQQQQGQSE----------------MQQAMDELGDLLREQQQLLDETFRQLQQQGGQQQGQPGQQgqQGQGQQPG 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1759 NELAQEKVRKSQQQLEQMTADLAmersvcERTESDKIALERANRDLKQQLQDAENTAVARLRTQINVAEAkvsSLEQQLS 1838
Cdd:pfam13779 655 QGGQQPGAQMPPQGGAEALGDLA------ERQQALRRRLEELQDELKELGGKEPGQALGDAGRAMRDAEE---ALGQGDL 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1839 LEEQDkmRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARI-----RQLRTQLEDTEAERDRLTNklKDERRR 1913
Cdd:pfam13779 726 AGAVD--AQGRALEALRKGAQQLAEAMQQQQGQGQQPGQGGQGGRQAGqdplgRPLGGGGDFGDDEAVKVPD--EIDAQR 801
|
....*.
gi 71983975 1914 AEEMTD 1919
Cdd:pfam13779 802 AREILE 807
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1342-1450 |
4.51e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.77 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1342 ATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKS----LLAEARKKLDEENREVMEElrkkkekelsAEKERAD 1417
Cdd:COG0711 27 KALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAeaaeIIAEARKEAEAIAEEAKAE----------AEAEAER 96
|
90 100 110
....*....|....*....|....*....|...
gi 71983975 1418 MAEQARDKAERAKKKAIQEaedVQKELTDVVAA 1450
Cdd:COG0711 97 IIAQAEAEIEQERAKALAE---LRAEVADLAVA 126
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
874-1164 |
4.56e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 874 TAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEV-----SKRLEIEEQKA 948
Cdd:pfam19220 39 ILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAeaakeELRIELRDKTA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 949 KKADSE---------SRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCE 1019
Cdd:pfam19220 119 QAEALErqlaaeteqNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1020 DLSSRLIDEVERSK----QLVKAKARLEATVAEINDELEKEKQQRH------NAETARRAA--------ETQLREEQESC 1081
Cdd:pfam19220 199 ELETQLDATRARLRalegQLAAEQAERERAEAQLEEAVEAHRAERAslrmklEALTARAAAteqllaeaRNQLRDRDEAI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1082 LEKTRKAEELTNQLMRKESELSQIsirnDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKA-------------- 1147
Cdd:pfam19220 279 RAAERRLKEASIERDTLERRLAGL----EADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAAleraeeriaslsdr 354
|
330 340 350
....*....|....*....|....*....|..
gi 71983975 1148 ---------------EKARRDMAEELESYKQE 1164
Cdd:pfam19220 355 iaeltkrfeveraalEQANRRLKEELQRERAE 386
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1596-1766 |
5.16e-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: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1596 DDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELteknEASLRQIEDLSRQLRKAQLGWKDLQLDVTEAR-- 1673
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL----EKEIKRLELEIEEVEARIKKYEEQLGNVRNNKey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1674 AAMEDALAGQrdaEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVsslrassfsNEEKRRLEAKVIDLEDQLD 1753
Cdd:COG1579 92 EALQKEIESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAEL---------EEKKAELDEELAELEAELE 159
|
170
....*....|...
gi 71983975 1754 EEASANELAQEKV 1766
Cdd:COG1579 160 ELEAEREELAAKI 172
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
861-970 |
5.18e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 861 DELIA-------EREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDaesseraEIFEERSRMAarRDELEGI 933
Cdd:PRK00409 519 NELIAsleelerELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE-------KEAQQAIKEA--KKEADEI 589
|
90 100 110
....*....|....*....|....*....|....*..
gi 71983975 934 LEEVSkrleiEEQKAKKADSESRKLTEMVRHLEENLE 970
Cdd:PRK00409 590 IKELR-----QLQKGGYASVKAHELIEARKRLNKANE 621
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
905-1232 |
5.55e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 905 RLDAESSERAEIFEERSRMAARRDELEGILEEVSKRLEIEEQKAKKADSE------SRKLTEMVRHLEENLEDEERSRQK 978
Cdd:COG3096 786 RLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEaelaalRQRRSELERELAQHRAQEQQLRQQ 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 979 LLLEKNSIESrLKELEAQGLELEDSGnklskekkaLEERCEDLSSRLiDEVERSKQLV----KAKARLEATVA------E 1048
Cdd:COG3096 866 LDQLKEQLQL-LNKLLPQANLLADET---------LADRLEELREEL-DAAQEAQAFIqqhgKALAQLEPLVAvlqsdpE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1049 INDELEKEKQQrhnAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQiSIRndEELAARQQLEREIREIRA 1128
Cdd:COG3096 935 QFEQLQADYLQ---AKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLNE-KLR--ARLEQAEEARREAREQLR 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1129 QLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKTVLhSQLKAKRDEEYAHL------QKQLEETVKSSEE 1202
Cdd:COG3096 1009 QAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAE-ERARIRRDELHEELsqnrsrRSQLEKQLTRCEA 1087
|
330 340 350
....*....|....*....|....*....|
gi 71983975 1203 VVEEMkaqnQKKIEELNETIDQLKRQKISA 1232
Cdd:COG3096 1088 EMDSL----QKRLRKAERDYKQEREQVVQA 1113
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1457-1721 |
5.75e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1457 KMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKAlvlSNELSEKKDIVDQLEKDKRTLKLEIDnlastkddagknvy 1536
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKN---GENIARKQNKYDELVEEAKTIKAEIE-------------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1537 elektkrRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSE---FER-----QLASREEDEDDRKKGLTSKIRN 1608
Cdd:PHA02562 238 -------ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmYEKggvcpTCTQQISEGPDRITKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1609 LTEELESEQRARQaaiaNKKKIESQISELTEKNEASLRQIEDLSRQLRKAQLGWKDLQldvtearAAMEDALAGQRDaek 1688
Cdd:PHA02562 311 LQHSLEKLDTAID----ELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVK-------AAIEELQAEFVD--- 376
|
250 260 270
....*....|....*....|....*....|...
gi 71983975 1689 raraSEDEIKRLTADIQAVSSSKRKAEAERDEL 1721
Cdd:PHA02562 377 ----NAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
868-1167 |
5.82e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 868 EQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKR------- 940
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvlerete 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 941 LEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLS-------KEKKA 1013
Cdd:pfam07888 152 LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttahRKEAE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1014 LEERCEDLSSrLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQR--HNAETARRAAET--QLREEQES-CLEKT--- 1085
Cdd:pfam07888 232 NEALLEELRS-LQERLNASERKVEGLGEELSSMAAQRDRTQAELHQArlQAAQLTLQLADAslALREGRARwAQEREtlq 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1086 RKAEELTNQLMRKESELSQISIRNDEELAARQQLEREI-REI---RAQLDDAIEETNKEKAARQKAEKARrdmaEELESY 1161
Cdd:pfam07888 311 QSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELgREKdcnRVQLSESRRELQELKASLRVAQKEK----EQLQAE 386
|
....*.
gi 71983975 1162 KQELEE 1167
Cdd:pfam07888 387 KQELLE 392
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
977-1311 |
5.93e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.54 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 977 QKLLLEKNSIESRLKELEAQGL--ELEDSGNKLSKEKKALEERCE-DLSSRLIDEVERS-KQLVKAKARLEATVAEINDE 1052
Cdd:NF033838 68 EKILSEIQKSLDKRKHTQNVALnkKLSDIKTEYLYELNVLKEKSEaELTSKTKKELDAAfEQFKKDTLEPGKKVAEATKK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1053 LEKekqqrhnaetARRAAETQLREEQESCLEKTRKAEELtnQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDD 1132
Cdd:NF033838 148 VEE----------AEKKAKDQKEEDRRNYPTNTYKTLEL--EIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVES 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1133 AIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKTVLHSQLK---------------AKRDEEYAHLQKQLEETV 1197
Cdd:NF033838 216 KKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKrrakrgvlgepatpdKKENDAKSSDSSVGEETL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1198 KSSEEVVEEMKAQNQKKIEELNEtidqlkrqkisadKAKSSAESDNENFraelsniasarleAEKKRKAAETSLMEKDHK 1277
Cdd:NF033838 296 PSPSLKPEKKVAEAEKKVEEAKK-------------KAKDQKEEDRRNY-------------PTNTYKTLELEIAESDVK 349
|
330 340 350
....*....|....*....|....*....|....
gi 71983975 1278 MREMQSNLDDLMAKLSKmnNElESIQKAKSADET 1311
Cdd:NF033838 350 VKEAELELVKEEAKEPR--NE-EKIKQAKAKVES 380
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
820-1165 |
5.94e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 820 REQEVAIKILQRNGLAWMRLREWQwwRLLTKVKPLLEVTNkDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEER 899
Cdd:COG3096 850 RELAQHRAQEQQLRQQLDQLKEQL--QLLNKLLPQANLLA-DETLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLV 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 900 LVLKT-------------RLDAESSE-RAEIFeERSRMAARR-----DELEGILEEVSKRLEIEEQKAKKADSESRKLTE 960
Cdd:COG3096 927 AVLQSdpeqfeqlqadylQAKEQQRRlKQQIF-ALSEVVQRRphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREARE 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 961 MVRHLEENLEDEERSRQKLlleKNSIESRLKELEAQGLELEDSGNKLSK--EKKALEERcEDLSSRLIDEVERSKQLVKA 1038
Cdd:COG3096 1006 QLRQAQAQYSQYNQVLASL---KSSRDAKQQTLQELEQELEELGVQADAeaEERARIRR-DELHEELSQNRSRRSQLEKQ 1081
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1039 KARLEATVAEINDELEKE----KQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIR------ 1108
Cdd:COG3096 1082 LTRCEAEMDSLQKRLRKAerdyKQEREQVVQAKAGWCAVLRLARDNDVERRLHRRELAYLSADELRSMSDKALGalrlav 1161
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1109 -NDEEL---------------------AARQQLEREIREIRAQLDD---AIEEtnkekaarQKAEKARrdMAEELESYKQ 1163
Cdd:COG3096 1162 aDNEHLrdalrlsedprrperkvqfyiAVYQHLRERIRQDIIRTDDpveAIEQ--------MEIELAR--LTEELTSREQ 1231
|
..
gi 71983975 1164 EL 1165
Cdd:COG3096 1232 KL 1233
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1107-1314 |
6.02e-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: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1107 IRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESND--KTVLHSQLKAKRDE 1184
Cdd:cd22656 100 IDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKalKDLLTDEGGAIARK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1185 EYAHLQKQLEETVKsseEVVEEMKaqnqKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKR 1264
Cdd:cd22656 180 EIKDLQKELEKLNE---EYAAKLK----AKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQ 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 71983975 1265 KAaetslmekdhkMREMQSNLDDLmakLSKMNNELESIQKAKSADETLNS 1314
Cdd:cd22656 253 GA-----------WQAIATDLDSL---KDLLEDDISKIPAAILAKLELEK 288
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1032-1160 |
6.18e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1032 SKQLVKAKARLEATVAEINDELEKEKQQrhnAETARRAAETQLREEQES-CLEKTRKAEELTNQLMRKESELSQ----IS 1106
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKE---ALLEAKEEIHKLRNEFEKeLRERRNELQKLEKRLLQKEENLDRklelLE 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 71983975 1107 IRNDEELAARQQLEREIREI---RAQLDDAIEETNK--EKAARQKAEKARRDMAEELES 1160
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELekkEEELEELIEEQLQelERISGLTAEEAKEILLEKVEE 165
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
863-1183 |
6.29e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 863 LIAEREQELKVTAEKLR--RSEVFISDYKQQMEKMDEeRLVLKTRLDAESSERA-EIFEERSRMAARRDELEGILEEVSK 939
Cdd:PRK10929 80 LSAELRQQLNNERDEPRsvPPNMSTDALEQEILQVSS-QLLEKSRQAQQEQDRArEISDSLSQLPQQQTEARRQLNEIER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 940 RLEI-------EEQ---KAKKADSESRKLTemvrhLEEnLEDEERS---RQKL------LLEKnsiesRLKELEAQGLEL 1000
Cdd:PRK10929 159 RLQTlgtpntpLAQaqlTALQAESAALKAL-----VDE-LELAQLSannRQELarlrseLAKK-----RSQQLDAYLQAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1001 EDSGNKLSKEK--KALE------ERCEDLSSRLIDEVERSKQLVKAkarLEATVAEINDELEKEKQQRHNAETARRAAET 1072
Cdd:PRK10929 228 RNQLNSQRQREaeRALEstellaEQSGDLPKSIVAQFKINRELSQA---LNQQAQRMDLIASQQRQAASQTLQVRQALNT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1073 qLREEQESCLEKTRKAEELTNQLMRKEselsqisirndeELAARQQLEREIREIRAQ---LDDAIEETNKEKAARQkaek 1149
Cdd:PRK10929 305 -LREQSQWLGVSNALGEALRAQVARLP------------EMPKPQQLDTEMAQLRVQrlrYEDLLNKQPQLRQIRQ---- 367
|
330 340 350
....*....|....*....|....*....|....
gi 71983975 1150 arrDMAEELesykqeleESNDKTVLHSQLKAKRD 1183
Cdd:PRK10929 368 ---ADGQPL--------TAEQNRILDAQLRTQRE 390
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1091-1376 |
6.76e-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: 41.55 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1091 LTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAAR--------------------QKAEKA 1150
Cdd:pfam05667 194 VTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKllkriaeqlrsaalagteatSGASRS 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1151 RRDMAEELESYKQELEESNDKT----VLHSQ------------------------LKAKRDEEYAHLQKQLEETVKSSEE 1202
Cdd:pfam05667 274 AQDLAELLSSFSGSSTTDTGLTkgsrFTHTEklqftneapaatsspptkveteeeLQQQREEELEELQEQLEDLESSIQE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1203 VVEEMKaQNQKKIEELNETIDQLKRQkisadkakssaesdnenfRAELSNiasarlEAEKKRKAAETsLMEKDHKMREMQ 1282
Cdd:pfam05667 354 LEKEIK-KLESSIKQVEEELEELKEQ------------------NEELEK------QYKVKKKTLDL-LPDAEENIAKLQ 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1283 SNLDDLMAKLSKMNNELESIQKAksadetlnsnLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEAR 1362
Cdd:pfam05667 408 ALVDASAQRLVELAGQWEKHRVP----------LIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELY 477
|
330
....*....|....
gi 71983975 1363 DDALDAQEKIEKEV 1376
Cdd:pfam05667 478 KQLVAEYERLPKDV 491
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1019-1270 |
6.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1019 EDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRK 1098
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1099 ESELSQISI----RNDEELAARQQLereIREIRAQLDDAIEETNKEKaarqkaekarrdmaEELESYKQELEESNDktvl 1174
Cdd:COG3883 99 GGSVSYLDVllgsESFSDFLDRLSA---LSKIADADADLLEELKADK--------------AELEAKKAELEAKLA---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1175 hsQLKAKRDeEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIA 1254
Cdd:COG3883 158 --ELEALKA-ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
250
....*....|....*.
gi 71983975 1255 SARLEAEKKRKAAETS 1270
Cdd:COG3883 235 AAAAAAAAAASAAGAG 250
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1426-1706 |
7.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1426 AERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKD 1505
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1506 IVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDalQLADDARSRVEVNMQAMRSEFE 1585
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE--ELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1586 RQLASREEDEDDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLRKAQLGWKDL 1665
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 71983975 1666 QLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQA 1706
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
885-1195 |
7.26e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 885 ISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELegileevSKRLEIEEQKAKKADSESRKLTEMVRH 964
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDEL-------NAQVKELREEAQELREKRDELNEKVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 965 LEEnledeerSRQKLLLEKNSIESRLKELEAQGLELedsgNKLSKEKKALEERCEDLSSRLIDEV---ERSKQLVKAKAR 1041
Cdd:COG1340 76 LKE-------ERDELNEKLNELREELDELRKELAEL----NKAGGSIDKLRKEIERLEWRQQTEVlspEEEKELVEKIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1042 LEATVAEINDELEKEKqqrhnaetarraaetQLREEQESCLEKTRKAEELTNQLmrkeSELSQISirnDEELAARQQLER 1121
Cdd:COG1340 145 LEKELEKAKKALEKNE---------------KLKELRAELKELRKEAEEIHKKI----KELAEEA---QELHEEMIELYK 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983975 1122 EIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKtvlhsQLKAKRDEEYAHLQKQLEE 1195
Cdd:COG1340 203 EADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKK-----QRALKREKEKEELEEKAEE 271
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
856-1529 |
7.31e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.74 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 856 EVTNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEErsrMAARRDELEGILE 935
Cdd:PTZ00440 718 DISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEE---FLQYKDTILNKEN 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 936 EVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLL--LEKNSIESRLKELEAQGLELEDSGNKLSKEKKA 1013
Cdd:PTZ00440 795 KISNDINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLqkFPTEDENLNLKELEKEFNENNQIVDNIIKDIEN 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1014 LEERCEDL------------SSRLIDEVERSKQLVKAKarLEATVAEIN--------------DELEKEKqqrhnAETAR 1067
Cdd:PTZ00440 875 MNKNINIIktlniainrsnsNKQLVEHLLNNKIDLKNK--LEQHMKIINtdniiqkneklnllNNLNKEK-----EKIEK 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1068 RAAET---QLREEQESCLEKTRKAEELTNQlmRKESELSQISIRNDEELAARQQLER---EIREIRAQLDDAIEETNKEK 1141
Cdd:PTZ00440 948 QLSDTkinNLKMQIEKTLEYYDKSKENING--NDGTHLEKLDKEKDEWEHFKSEIDKlnvNYNILNKKIDDLIKKQHDDI 1025
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1142 AARqkaekarrdMAEELESYKQELEESNDKTVLH-SQLKAKRDEEYAHLQKQLEETVKSSEEV--VEEMKAQNQKKIEEL 1218
Cdd:PTZ00440 1026 IEL---------IDKLIKEKGKEIEEKVDQYISLlEKMKTKLSSFHFNIDIKKYKNPKIKEEIklLEEKVEALLKKIDEN 1096
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1219 NETIDQLKRqKISADKAKSSAESDNENfraelsniasarLEAEKKRKAaetslMEKDHK-MREMQSNLDDLMAKLSKMN- 1296
Cdd:PTZ00440 1097 KNKLIEIKN-KSHEHVVNADKEKNKQT------------EHYNKKKKS-----LEKIYKqMEKTLKELENMNLEDITLNe 1158
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1297 -NELESIQKAKSADETLNS-NLLKKNASLDMQLSELTEASEE--DRRTRATLNNKIRQLEEDlavavEARDDALDAQEKI 1372
Cdd:PTZ00440 1159 vNEIEIEYERILIDHIVEQiNNEAKKSKTIMEEIESYKKDIDqvKKNMSKERNDHLTTFEYN-----AYYDKATASYENI 1233
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1373 EKEVKEVKSLLAEAR-----KKLDEENREVMEELRKKKEKELSAEKERADMAE-----QARDKAERAK------KKAIQE 1436
Cdd:PTZ00440 1234 EELTTEAKGLKGEANrstnvDELKEIKLQVFSYLQQVIKENNKMENALHEIKNmyeflISIDSEKILKeilnstKKAEEF 1313
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1437 AEDVQKELTDVVAATREMERKMRKfdqqlAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRT 1516
Cdd:PTZ00440 1314 SNDAKKELEKTDNLIKQVEAKIEQ-----AKEHKNKIYGSLEDKQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEK 1388
|
730
....*....|...
gi 71983975 1517 LKLEIDNLASTKD 1529
Cdd:PTZ00440 1389 CDLHVRNASRGKD 1401
|
|
| COG4251 |
COG4251 |
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ... |
893-1170 |
7.47e-03 |
|
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];
Pssm-ID: 443393 [Multi-domain] Cd Length: 503 Bit Score: 41.31 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 893 EKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDE 972
Cdd:COG4251 1 LLLLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 973 ERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDE 1052
Cdd:COG4251 81 LLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1053 LEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQ--ISIRNDEELAARQQLEREIREIRAQL 1130
Cdd:COG4251 161 LLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLleAELLLSLGGGLGLLLLLLLLLVLLLL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 71983975 1131 DDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESND 1170
Cdd:COG4251 241 LILLLLLLILVLELLELRLELEELEEELEERTAELERSNE 280
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1195-1478 |
7.77e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1195 ETVKSS---EEVVEEMKAQNQKKIEEL--NETIDQLKRQ-KISADKAKS----SAESDNENFRAELSN-IASARLEAEKK 1263
Cdd:COG3206 88 EILKSRpvlERVVDKLNLDEDPLGEEAsrEAAIERLRKNlTVEPVKGSNvieiSYTSPDPELAAAVANaLAEAYLEQNLE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1264 RKAAETSLMEK--DHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNsnllkknasldmQLSELTEASEEDRRTR 1341
Cdd:COG3206 168 LRREEARKALEflEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQ------------QLSELESQLAEARAEL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1342 ATLNNKIRQLEEDLAVAVEARDDALDAQE--KIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMA 1419
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1420 EQARDKAERAKKKA---IQEAEDVQKELTDVVAATREMERKMRkfDQQLAEERNNTLLAQQE 1478
Cdd:COG3206 316 ASLEAELEALQAREaslQAQLAQLEARLAELPELEAELRRLER--EVEVARELYESLLQRLE 375
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1629-1780 |
8.62e-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: 39.91 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1629 KIESQISELTEKNEASLRQIEDLSRQLRKaqlgwkdLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVS 1708
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1709 SSKrkaeaERDELIEEVSSLRassfsnEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADL 1780
Cdd:COG1579 87 NNK-----EYEALQKEIESLK------RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1033-1185 |
9.09e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1033 KQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEEL---TNQLMRKESELSQISIRN 1109
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLvqkEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1110 DEELAARQQLEREIREIRAQLDDAIEEtnkekAARQKAEKARRDMAEELESykqELEEsnDKTVLHSQLKAKRDEE 1185
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYR-----VAGLTPEQARKLLLKLLDA---ELEE--EKAQRVKKIEEEADLE 173
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
839-1365 |
9.26e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 839 LREWQWWRLLTKVKPLLEVTNKDeliAEREQELKVTAEKLRRsevfisDYKQQMEKMDEERLVLKTRLDAESSERAEIFE 918
Cdd:PRK04863 502 LRRLREQRHLAEQLQQLRMRLSE---LEQRLRQQQRAERLLA------EFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 919 ERSRMAARRDELEGILEEVS---KRLEIEEQKAKKADSESRKLTE----------MVRHLEENLEDEERSrqkLLLEKNS 985
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQariQRLAARAPAWLAAQDALARLREqsgeefedsqDVTEYMQQLLERERE---LTVERDE 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 986 IESRLKELEAQGLELEDSGNKLSKEKKALEERCED-LSSRLIDEVE--------------RSKQLVKAKARLEATVAEIN 1050
Cdd:PRK04863 650 LAARKQALDEEIERLSQPGGSEDPRLNALAERFGGvLLSEIYDDVSledapyfsalygpaRHAIVVPDLSDAAEQLAGLE 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1051 D-----------------------ELEKEKQQRHNAETAR-----------RAAE----TQLREEQESCLEKTRKAEELT 1092
Cdd:PRK04863 730 DcpedlyliegdpdsfddsvfsveELEKAVVVKIADRQWRysrfpevplfgRAARekriEQLRAEREELAERYATLSFDV 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1093 NQLMRKESELSQ-------ISIRNDEElAARQQLEREIREIRAQLDDaIEETNKEKAARQKAEKARRDMAEEL------- 1158
Cdd:PRK04863 810 QKLQRLHQAFSRfigshlaVAFEADPE-AELRQLNRRRVELERALAD-HESQEQQQRSQLEQAKEGLSALNRLlprlnll 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1159 --ESYKQELEESNDKtvLHSQLKAKRD-EEYAHLQKQLEE---TVKSSEEVVEEMKA---QNQKKIEELNETIDQLK--- 1226
Cdd:PRK04863 888 adETLADRVEEIREQ--LDEAEEAKRFvQQHGNALAQLEPivsVLQSDPEQFEQLKQdyqQAQQTQRDAKQQAFALTevv 965
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1227 --RQKIS-ADKAKSSAESD--NENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELES 1301
Cdd:PRK04863 966 qrRAHFSyEDAAEMLAKNSdlNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQD 1045
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983975 1302 I---------QKAKSADETLNSNLLK---KNASLDMQLSELTEASEEdrrtratLNNKIRQLEEDLAVAVEARDDA 1365
Cdd:PRK04863 1046 LgvpadsgaeERARARRDELHARLSAnrsRRNQLEKQLTFCEAEMDN-------LTKKLRKLERDYHEMREQVVNA 1114
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
868-1080 |
9.29e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 868 EQELKVTAEKLRRSEVFISDYKQQ--MEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRL---- 941
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALpell 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 942 ---EIEEQKAKKADSESRKLTEMVRHLEENLEdeersRQKLLLEKNSIESRLKELEAQGLEledsgnKLSKEKKALEERC 1018
Cdd:COG3206 261 qspVIQQLRAQLAELEAELAELSARYTPNHPD-----VIALRAQIAALRAQLQQEAQRILA------SLEAELEALQARE 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983975 1019 EDLSSRLIDEVERSKQLvkakARLEATVAEINDELEKeKQQRHNaETARRAAETQLREEQES 1080
Cdd:COG3206 330 ASLQAQLAQLEARLAEL----PELEAELRRLEREVEV-ARELYE-SLLQRLEEARLAEALTV 385
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1627-1888 |
9.72e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1627 KKKIESQISELTEKNEASL--------RQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIK 1698
Cdd:pfam00038 27 NKLLETKISELRQKKGAEPsrlyslyeKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1699 RLTADIQAVSSSKRKAEAERDELIEEVSSLRasSFSNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTa 1778
Cdd:pfam00038 107 GLRKDLDEATLARVDLEAKIESLKEELAFLK--KNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIA- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983975 1779 dlamERSVCERTESDKIALERANRDLKQQLQDAENTavarlRTQINVAEAKVSSLEQQLslEEQDKMRQGrtlrrMETKM 1858
Cdd:pfam00038 184 ----AKNREEAEEWYQSKLEELQQAAARNGDALRSA-----KEEITELRRTIQSLEIEL--QSLKKQKAS-----LERQL 247
|
250 260 270
....*....|....*....|....*....|
gi 71983975 1859 AEMQQMLEEEKRQGESNRQAVDRQNARIRQ 1888
Cdd:pfam00038 248 AETEERYELQLADYQELISELEAELQETRQ 277
|
|
| |
