|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
431-1181 |
0e+00 |
|
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: 1133.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGtKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 590
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVG-GVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 591 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEE 670
Cdd:cd01386 160 LLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 671 QKTCWLILASIYHLGAAGATKEAaEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFRQGPEESGL 750
Cdd:cd01386 240 QRAIWSILAAIYHLGAAGATKAA-SAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQESPARSS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 751 GEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGSARGASFEELCHNYAQDRLQ 830
Cdd:cd01386 319 SGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERLQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 831 RLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASH--LVRSLAHADEARGLLWLLEEEALVPGATEDALLDR 908
Cdd:cd01386 399 LLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqaLVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFLER 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 909 LFSYYGPQEGDkKGQSPLLRSSKPRHFLLGHSHGTNWVEYNVAGWLNYTKQNPATQNAPRLLQDSQKKiisnlflgrags 988
Cdd:cd01386 479 LFSHYGDKEGG-KGHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE------------ 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 989 atvlsgsiagleggsqlalrratsmrktfttgMAAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGEPRs 1068
Cdd:cd01386 546 --------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDERS- 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1069 assrrvsssseldlppGDPCEAGLLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNY 1148
Cdd:cd01386 593 ----------------TSSPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNS 656
|
730 740 750
....*....|....*....|....*....|...
gi 600971660 1149 IVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd01386 657 EVADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
432-1181 |
3.95e-142 |
|
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: 457.05 E-value: 3.95e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGTKVFS-----VEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 585
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSSsassiEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 586 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAEN---NVFGIVPLSKPEEKQKAAQQFSKLQAAMK 662
Cdd:cd00124 162 SIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYyylNDYLNSSGCDRIDGVDDAEEFQELLDALD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 663 VLAISPEEQKTCWLILASIYHLGAAGATKEAAEAGRK-QFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTlqrstsf 741
Cdd:cd00124 242 VLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSaEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGG------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 742 rqgpeESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSS--QHSLCSMMIVDTPGFQNPEWggsargASFEE 819
Cdd:cd00124 315 -----ETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTdaAESTSFIGILDIFGFENFEV------NSFEQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 820 LCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDLEPVAD------DSV-AAVDQASHLvrslahadeargllw 889
Cdd:cd00124 384 LCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSfidFPDNQDCLDliegkpLGIlSLLDEECLF--------------- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 890 lleeealvPGATEDALLDRLFSYYGPQEGDKKGqspllRSSKPRHFllGHSHGTNWVEYNVAGWLNYTKQNpatqnaprl 969
Cdd:cd00124 449 --------PKGTDATFLEKLYSAHGSHPRFFSK-----KRKAKLEF--GIKHYAGDVTYDADGFLEKNKDT--------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 970 lqdsqkkiisnlflgragsatvLSGSIAGLeggsqlaLRRATSMRKtfttgmaavkkkslciqiklQVDALIDTIKRSKM 1049
Cdd:cd00124 505 ----------------------LPPDLVDL-------LRSGSQFRS--------------------QLDALMDTLNSTQP 535
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1050 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1129
Cdd:cd00124 536 HFVRCIKPNDEKKPG-----------------------------LFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 600971660 1130 RRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd00124 587 LKRYRILAPGATEKA-----SDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
412-1193 |
2.41e-112 |
|
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: 374.19 E-value: 2.41e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 412 NAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQ 491
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 492 TAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGtSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFS 569
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG-SNTEVGSVED-QILESnpILEAFGNAKTLRNNNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 570 QILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFgivpLSKPEEKQK 649
Cdd:smart00242 159 KFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRY----LNQGGCLTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 650 A----AQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAI 725
Cdd:smart00242 234 DgiddAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKEELSNAAELLGVDPEELEKAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 726 fkhqlkggtLQRSTSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQ- 804
Cdd:smart00242 314 ---------TKRKIKTGGEVITKPL---NVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEi 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 805 ---NpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVRS- 877
Cdd:smart00242 382 fevN----------SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDwtfIDFFDNQDCID-----------LIEKk 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 878 ----LAHADEArgllwlleeeALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEYNV 950
Cdd:smart00242 441 ppgiLSLLDEE----------CRFPKGTDQTFLEKLNQHH--------KKHPHFSKPKKKgrtEFIIKHYAGD--VTYDV 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 951 AGWLnytKQN--PATQNAPRLLQDSQKKIISNLFlgragsatvlsGSIAGleggsqlalrRATSMRKTFTTGMaavkkks 1028
Cdd:smart00242 501 TGFL---EKNkdTLSDDLIELLQSSKNPLIASLF-----------PSGVS----------NAGSKKRFQTVGS------- 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1029 lciQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSR 1108
Cdd:smart00242 550 ---QFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPG-----------------------------DFDSSLVLHQLRYLG 597
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1109 LLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFRAGTLARL 1188
Cdd:smart00242 598 VLENIRIRRAGFPYRLPFDEFLQRYRVLLPD-TWPPWGG----DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAEL 672
|
....*
gi 600971660 1189 EEQRD 1193
Cdd:smart00242 673 EELRE 677
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
420-1181 |
3.95e-107 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 358.90 E-value: 3.95e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 420 EDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLM 499
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 500 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGT-SGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDF 576
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSgSAGNVGRLEE-QILQSnpILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 577 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL---------NHLAENNVFGIvplskpeek 647
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyhylSQSGCYTIDGI--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 648 qKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAGRKqFARHEWAQKAAYLLGCSLEELSSAIFK 727
Cdd:pfam00063 232 -DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAV-PDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 728 HQLKGGTLQRSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNP 806
Cdd:pfam00063 310 RRIKTGRETVSKPQ------------NVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIgVLDIYGFEIF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 807 EWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVRS-----L 878
Cdd:pfam00063 378 EKN------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEwtfIDFGDNQPCID-----------LIEKkplgiL 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 879 AHADEArgllwlleeeALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLN 955
Cdd:pfam00063 441 SLLDEE----------CLFPKATDQTFLDKLYSTF--------SKHPHFQKPRLQgetHFIIKHYAGD--VEYNVEGFLE 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 956 YTKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvLSGSIAGLEGGSQLALRRATSMRKtfTTGMaavkkkslciQIKL 1035
Cdd:pfam00063 501 KNK-DPLNDDLVSLLKSSSDPLLAELFPDYE-----TAESAAANESGKSTPKRTKKKRFI--TVGS----------QFKE 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1036 QVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRM 1115
Cdd:pfam00063 563 SLGELMKTLNSTNPHYIRCIKPNEKKRAG-----------------------------VFDNSLVLHQLRCNGVLEGIRI 613
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1116 YRQGYPDHMVFSEFRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:pfam00063 614 RRAGFPNRITFQEFVQRYRILAPKTWPK-----WKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
393-1907 |
1.80e-106 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 375.96 E-value: 1.80e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 393 KLDHDGAILDVDEDDIEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMH 472
Cdd:COG5022 42 KEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 473 MFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKwQALST--L 550
Cdd:COG5022 122 SYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEK-QILATnpI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 551 LEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL--- 627
Cdd:COG5022 201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLqnp 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 628 ---NHLAENNVFGIVPLSKPEEkqkaaqqFSKLQAAMKVLAISPEEQKTCWLILASIYHLG--AAGATKEaaeaGRKQFA 702
Cdd:COG5022 281 kdyIYLSQGGCDKIDGIDDAKE-------FKITLDALKTIGIDEEEQDQIFKILAAILHIGniEFKEDRN----GAAIFS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 703 RHEWAQKAAYLLGCSLEELSSAIFKHQLKGG--TLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISL 780
Cdd:COG5022 350 DNSVLDKACYLLGIDPSLFVKWLVKRQIKTGgeWIVVPLNLEQ--------------ALAIRDSLAKALYSNLFDWIVDR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 781 VNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDL 857
Cdd:COG5022 416 INKSLDHSAAASNFIGVLDIYGFEIFEKN------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEwsfIDYFDN 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 858 EPVADDSvaavdQASHLVRSLAHADEArgllwlleeeALVPGATEDALLDRLFSYYgPQEGDKKGQSPLLRSSKprhFLL 937
Cdd:COG5022 490 QPCIDLI-----EKKNPLGILSLLDEE----------CVMPHATDESFTSKLAQRL-NKNSNPKFKKSRFRDNK---FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 938 GHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvlsgsiaglEGGSQLALRRATSMrktf 1017
Cdd:COG5022 551 KHYAGD--VEYDVEGFLDKNK-DPLNDDLLELLKASTNEFVSTLFDDEE-------------NIESKGRFPTLGSR---- 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1018 ttgmaavkkkslciqIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDV 1097
Cdd:COG5022 611 ---------------FKESLNSLMSTLNSTQPHYIRCIKPNEEKSPW-----------------------------TFDN 646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1098 SLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNYIVVDEKRAVEELLESLDLEKSSCCLGLSR 1177
Cdd:COG5022 647 QMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPS-KSWTGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTK 725
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1178 VFFRAGTLARLEEQRDEQTSRHLTLFQAACRGYLARQHF-KKRKIQDlAIRCVQKNIKKNKGVKDWPWWKLFTTVRPLIQ 1256
Cdd:COG5022 726 VFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYlQALKRIK-KIQVIQHGFRLRRLVDYELKWRLFIKLQPLLS 804
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1257 VQLSEEQIRNKDEEIQQLRSKLEKV----EKERNELRLSSDRLETRISEltSELTDERNTGESASQLLDAETAERLRTEK 1332
Cdd:COG5022 805 LLGSRKEYRSYLACIIKLQKTIKREkklrETEEVEFSLKAEVLIQKFGR--SLKAKKRFSLLKKETIYLQSAQRVELAER 882
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1333 EMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDF----TKKRLQQELEDKMEVE 1408
Cdd:COG5022 883 QLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLeegpSIEYVKLPELNKLHEV 962
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1409 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRrfdsELSQAHEETQREKLQ 1488
Cdd:COG5022 963 ESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPV----EVAELQSASKIISSE 1038
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1489 REKLQREKDMLLAEAFSLKQQME-EKDLdiagftqKVVSLEAELQDIssqESKDEASLAKVKKQLRDLEAK---VKDQEE 1564
Cdd:COG5022 1039 STELSILKPLQKLKGLLLLENNQlQARY-------KALKLRRENSLL---DDKQLYQLESTENLLKTINVKdleVTNRNL 1108
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1565 ELDEQAGSIQMLEQAKLRLEMEMERM--RQTHSKEMESRDEEVEEARQSCQKKLKQMEvqlEEEYEDKQKALREKRELES 1642
Cdd:COG5022 1109 VKPANVLQFIVAQMIKLNLLQEISKFlsQLVNTLEPVFQKLSVLQLELDGLFWEANLE---ALPSPPPFAALSEKRLYQS 1185
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1643 KL----STLSDQVNQ---RDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLknqleESEFTCAAAVKark 1715
Cdd:COG5022 1186 ALydekSKLSSSEVNdlkNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNL-----NKKFDTPASMS--- 1257
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1716 ameveMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLeeDQEDMNEL-MKKHKAAVAQASRDmaqmnDLQAQIEES 1794
Cdd:COG5022 1258 -----NEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYI--NVGLFNALrTKASSLRWKSATEV-----NYNSEELDD 1325
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1795 NKEKQELQEklqaLQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKT-QVKRLENlasrlketmeklteeRDQRAAA 1873
Cdd:COG5022 1326 WCREFEISD----VDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPaEIQNLKS---------------RYDPADK 1386
|
1530 1540 1550
....*....|....*....|....*....|....*
gi 600971660 1874 ENR-EKEQNKRLQRQLRDTKEEMSELARKEAEASR 1907
Cdd:COG5022 1387 ENNlPKEILKKIEALLIKQELQLSLEGKDETEVHL 1421
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
432-1181 |
1.58e-97 |
|
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: 330.58 E-value: 1.58e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPyKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW-----QALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 583
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledQILQAnpILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 584 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFgIVPLSKPEEKQKAAQQFSKLQAAMKV 663
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFF-LSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 664 LAISPEEQKTCWLILASIYHLGAAGATKEaaeaGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRS 738
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQR----RREEQAEldgTEEADKAAHLLGVNSSDLLKALLKPRIKVGRewVTKG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 739 TSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQ----Npewggsarg 814
Cdd:cd01377 316 QNKEQ--------------VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN--------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 815 aSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF----DDLEPVADdsvaavdqashLVRS-----LAHADEar 885
Cdd:cd01377 373 -SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgLDLQPTID-----------LIEKpnmgiLSILDE-- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 886 gllwlleeEALVPGATEDALLDRLFSYygpQEGDKKGQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLnyTK-QNPATQ 964
Cdd:cd01377 439 --------ECVFPKATDKTFVEKLYSN---HLGKSKNFKKPKPKKSEAHFILKHYAGD--VEYNIDGWL--EKnKDPLNE 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 965 NAPRLLQDSQKKIISNLFlgragsatvlsgSIAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTI 1044
Cdd:cd01377 504 NVVALLKKSSDPLVASLF------------KDYEESGGGGGKKKKKGGSFRT----VSQLHKEQL--------NKLMTTL 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1045 KRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHM 1124
Cdd:cd01377 560 RSTHPHFVRCIIPNEEKKPGK-----------------------------IDAPLVLHQLRCNGVLEGIRICRKGFPNRI 610
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1125 VFSEFRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd01377 611 IFAEFKQRYSILAPNAIPK-----GFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
431-1181 |
1.94e-89 |
|
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: 307.32 E-value: 1.94e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIA-----GTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 583
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAsshkgRKDHNIPGELER-QLLQAnpILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 584 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF--GIVPLSkpeeKQKAAQQFSKLQAAM 661
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsnGYIPIP----GQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 662 KVLAISPEEQKTCWLILASIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRST 739
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKE-RNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRdyVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 740 sfrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFE 818
Cdd:cd14920 315 --------------TKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIgILDIAGFEIFELN------SFE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 819 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFD----DLEPVADdsvaAVDQASHLVRSLAHADEargllwlleeE 894
Cdd:cd14920 375 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIdfglDLQPCID----LIERPANPPGVLALLDE----------E 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 895 ALVPGATEDALLDRLfsyygpqEGDKKGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQ 971
Cdd:cd14920 441 CWFPKATDKTFVEKL-------VQEQGSHSKFQKPRQLKdkaDFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVATLLH 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 972 DSQKKIISNLFlgRAGSATVlsgSIAGLEGGSQLALRRATSMRKTFTTGMAAVKKKSLciqiklqvDALIDTIKRSKMHF 1051
Cdd:cd14920 511 QSSDRFVAELW--KDVDRIV---GLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESL--------TKLMATLRNTNPNF 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1052 VHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1131
Cdd:cd14920 578 VRCIIPNHEKRAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 600971660 1132 RFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14920 629 RYEILTPNAIPK-----GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
431-1181 |
1.44e-83 |
|
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: 289.99 E-value: 1.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIA----GTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 584
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAsshkGKKDTSITGELEKQLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 585 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNV--FGIVPLSkpeeKQKAAQQFSKLQAAMK 662
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFlsNGFVPIP----AAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 663 VLAISPEEQKTCWLILASIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTSFR 742
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKE-RNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVG-----RDVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 743 QGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEELC 821
Cdd:cd14921 311 QKAQ-------TKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEIFEVN------SFEQLC 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 822 HNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPGAT 901
Cdd:cd14921 378 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDE----------ECWFPKAT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 902 EDALLDRLFSyygPQEGDKKGQSPLLRSSKPRHFLLghsHGTNWVEYNVAGWLNyTKQNPATQNAPRLLQDSQKKIISNL 981
Cdd:cd14921 448 DKSFVEKLCT---EQGNHPKFQKPKQLKDKTEFSII---HYAGKVDYNASAWLT-KNMDPLNDNVTSLLNASSDKFVADL 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 982 FLGragsatvlSGSIAGLEGGSQLALRRATSMRKTfTTGMAavkkKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEG 1061
Cdd:cd14921 521 WKD--------VDRIVGLDQMAKMTESSLPSASKT-KKGMF----RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEK 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1062 WPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLT 1141
Cdd:cd14921 588 RSG-----------------------------KLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAI 638
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 600971660 1142 KKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14921 639 PKG-----FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
431-1181 |
3.74e-83 |
|
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: 288.80 E-value: 3.74e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIA-----GTSGTKVFSV-------EKWQAL---STLLEAFGNSPTIMNGSATRFSQILSLD 575
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpkGSGAVPHPAVnpavligELEQQLlqaNPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 576 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVF---GIVPLSKPEEkqkaAQ 652
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDD-VKSYAFlsnGSLPVPGVDD----YA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 653 QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAgATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKG 732
Cdd:cd14911 236 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSM-KFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 733 GtlqrstsfRQGPEESGLGEGTKLSalecLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgs 811
Cdd:cd14911 315 G--------RDFVTKAQTKEQVEFA----VEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIgILDMAGFEIFELN-- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 812 argaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFD----DLEPVADdsvaavdqashLVrslahaDEARGL 887
Cdd:cd14911 381 ----SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIdfglDLQPTID-----------LI------DKPGGI 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 888 LWLLEEEALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLnYTKQNPATQ 964
Cdd:cd14911 440 MALLDEECWFPKATDKTFVDKLVSAH--------SMHPKFMKTDFRgvaDFAIVHYAGR--VDYSAAKWL-MKNMDPLNE 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 965 NAPRLLQDSQKKIISNLFlgraGSATVLSGSIAGLeGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQVDALIDTI 1044
Cdd:cd14911 509 NIVSLLQGSQDPFVVNIW----KDAEIVGMAQQAL-TDTQFGARTRKGMFRTVSH------------LYKEQLAKLMDTL 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1045 KRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHM 1124
Cdd:cd14911 572 RNTNPNFVRCIIPNHEKRAG-----------------------------KIDAPLVLDQLRCNGVLEGIRICRQGFPNRI 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1125 VFSEFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14911 623 PFQEFRQRYELLTPNVIPKG-----FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
431-1181 |
2.75e-81 |
|
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: 283.46 E-value: 2.75e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGTK------VFS---VEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQA 579
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKkdqssiALShgeLEK-QLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 580 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQA 659
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDK--ELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 660 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsT 739
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKE-RNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVG-----R 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 740 SFRQGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFE 818
Cdd:cd14932 312 DYVQKAQ-------TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN------SFE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 819 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVP 898
Cdd:cd14932 379 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDE----------ECWFP 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 899 GATEDALLDRLFSYYGpqeGDKKGQSPlLRSSKPRHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKII 978
Cdd:cd14932 449 KATDKSFVEKVVQEQG---NNPKFQKP-KKLKDDADFCIIHYAGK--VDYKANEWL-MKNMDPLNENVATLLNQSTDKFV 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 979 SNLFlgRAGSATVLSGSIAGLEGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQVDALIDTIKRSKMHFVHCFLPV 1058
Cdd:cd14932 522 SELW--KDVDRIVGLDKVAGMGESLHGAFKTRKGMFRTVGQ------------LYKEQLMNLMTTLRNTNPNFVRCIIPN 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1059 AEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1138
Cdd:cd14932 588 HEKKAG-----------------------------KLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 638
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 600971660 1139 HLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14932 639 NAIPKG-----FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
431-1181 |
2.12e-79 |
|
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: 277.74 E-value: 2.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQAL---STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASI 587
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLlqaNPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 588 QTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQAAMKVLAIS 667
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK--DMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 668 PEEQKTCWLILASIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTSFRQGPEe 747
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKE-RNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG-----RDYVQKAQ- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 748 sglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEELCHNYAQ 826
Cdd:cd14919 312 ------TKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIgILDIAGFEIFDLN------SFEQLCINYTN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 827 DRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPGATEDALL 906
Cdd:cd14919 380 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDE----------ECWFPKATDKSFV 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 907 DRLFSYYGPQegdKKGQSPLLRSSKPrHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKIISNLFlgRA 986
Cdd:cd14919 450 EKVVQEQGTH---PKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWL-MKNMDPLNDNIATLLHQSSDKFVSELW--KD 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 987 GSATVLSGSIAGLeggSQLALRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDTIKRSKMHFVHCFLPVAEGWPGep 1066
Cdd:cd14919 521 VDRIIGLDQVAGM---SETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIPNHEKKAG-- 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1067 rsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHgr 1146
Cdd:cd14919 588 ---------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-- 638
|
730 740 750
....*....|....*....|....*....|....*
gi 600971660 1147 nyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14919 639 ---FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
431-1181 |
1.89e-77 |
|
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: 271.85 E-value: 1.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGTKvfsvEKWQAL-------STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 583
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESK----KKLGALedqimqaNPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 584 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDATLRTELHLN------HLAENNVFGIvplskpeEKQKAAQQFSKL 657
Cdd:cd14929 157 SADIDIYLLEKSRVIFQQPGERNYHIFYQILS-GKKELRDLLLVSanpsdfHFCSCGAVAV-------ESLDDAEELLAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 658 QAAMKVLAISPEEQKTCWLILASIYHLG----AAGATKEAAEAGRKqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKGG 733
Cdd:cd14929 229 EQAMDILGFLPDEKYGCYKLTGAIMHFGnmkfKQKPREEQLEADGT-----ENADKAAFLMGINSSELVKGLIHPRIKVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 734 T--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgs 811
Cdd:cd14929 304 NeyVTRSQNIEQVTYAVG--------------ALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYN-- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 812 argaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELafddlepvaddsvAAVDQASHLVRSLAHADEARGLLWLL 891
Cdd:cd14929 368 ----SLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDW-------------VSIDFGLDLQACIDLIEKPMGIFSIL 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 892 EEEALVPGATEDALLDRLFSYYgpqegdkKGQSPLLRSSKPR------HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQN 965
Cdd:cd14929 431 EEECMFPKATDLTFKTKLFDNH-------FGKSVHFQKPKPDkkkfeaHFELVHYAGV--VPYNISGWLEKNK-DLLNET 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 966 APRLLQDSQKKIISNLFlgragSATVLSGSiaGLEGGSQlALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIK 1045
Cdd:cd14929 501 VVAVFQKSSNRLLASLF-----ENYISTDS--AIQFGEK-KRKKGASFQT-----VASLHKENL--------NKLMTNLK 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1046 RSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMV 1125
Cdd:cd14929 560 STAPHFVRCINPNVNKIPG-----------------------------VLDPYLVLQQLRCNGVLEGIRICREGFPNRLL 610
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1126 FSEFRRRFDVLAPHLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14929 611 YADFKQRYCILNPRTFPKSK----FVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
431-1181 |
1.36e-75 |
|
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: 266.55 E-value: 1.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAG 580
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELekqllqanpiLEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 581 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQAA 660
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDK--DLFTETMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 661 MKVLAISPEEQKTCWLILASIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRS 738
Cdd:cd15896 239 FRIMGIPEDEQIGMLKVVASVLQLGNMSFKKE-RHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRdyVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 739 TSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSF 817
Cdd:cd15896 318 QTQEQ--------------AEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN------SF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 818 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALV 897
Cdd:cd15896 378 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDE----------ECWF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 898 PGATEDALLDRLFSYYGPQEGDKKGQspllRSSKPRHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKI 977
Cdd:cd15896 448 PKATDKSFVEKVLQEQGTHPKFFKPK----KLKDEADFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVATLLNQSTDKF 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 978 ISNLFLGragsatvlSGSIAGLEGGSQLA-LRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDTIKRSKMHFVHCFL 1056
Cdd:cd15896 521 VSELWKD--------VDRIVGLDKVSGMSeMPGAFKTRKGMFRTVGQLYKE--------QLSKLMATLRNTNPNFVRCII 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1057 PVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1136
Cdd:cd15896 585 PNHEKKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 600971660 1137 APHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd15896 636 TPNAIPKG-----FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
431-1181 |
8.35e-72 |
|
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: 255.65 E-value: 8.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIA--GTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQ 578
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalGDGPGKKAQFLATKTGGTLedqiieanpaMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 579 AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLN------HLAENNVFGIVPLSKPEEkqkaaq 652
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmnpydyHFCSQGVTTVDNMDDGEE------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 653 qFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATK----EAAEAGRKqfarhEWAQKAAYLLGCSLEELSSAIFKH 728
Cdd:cd14927 235 -LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQkqreEQAEADGT-----ESADKAAYLMGVSSADLLKGLLHP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 729 QLKGGtlQRSTSFRQGPEESGLGEGtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEW 808
Cdd:cd14927 309 RVKVG--NEYVTKGQSVEQVVYAVG----------ALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 809 GgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDqashLVrslahaDEARGLL 888
Cdd:cd14927 377 N------SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDF---GLDLQACID----LI------EKPLGIL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 889 WLLEEEALVPGATEDALLDRLFSYYgpqegdkKGQSPLLRSSKP-------RHFLLGHSHGTnwVEYNVAGWLNYTKqNP 961
Cdd:cd14927 438 SILEEECMFPKASDASFKAKLYDNH-------LGKSPNFQKPRPdkkrkyeAHFEVVHYAGV--VPYNIVGWLDKNK-DP 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 962 ATQNAPRLLQDSQKKIISNLFLGRAGSAtvlsgSIAGLEGGSQLALRRATSmrktFTTgMAAVKKKSLciqiklqvDALI 1041
Cdd:cd14927 508 LNETVVAIFQKSQNKLLATLYENYVGSD-----STEDPKSGVKEKRKKAAS----FQT-VSQLHKENL--------NKLM 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1042 DTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYP 1121
Cdd:cd14927 570 TNLRATQPHFVRCIIPNETKTPG-----------------------------VMDPFLVLHQLRCNGVLEGIRICRKGFP 620
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1122 DHMVFSEFRRRFDVLAPHLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14927 621 NRILYADFKQRYRILNPSAIPDDK----FVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
431-1181 |
5.31e-71 |
|
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: 253.09 E-value: 5.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGT-SGTKVFSV-----EKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 584
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSpKGRKEPGVpgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 585 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQkaaQQFSKLQAAMKVL 664
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER---ELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 665 AISPEEQKTCWLILASIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTSFRQG 744
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRE-RNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG-----RDYVQK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 745 PEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEELCHN 823
Cdd:cd14930 312 AQ-------TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFEIFQLN------SFEQLCIN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 824 YAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPGATED 903
Cdd:cd14930 379 YTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDE----------ECWFPKATDK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 904 ALLDRLfsyygpqeGDKKGQSPllRSSKPRH------FLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKI 977
Cdd:cd14930 449 SFVEKV--------AQEQGGHP--KFQRPRHlrdqadFSVLHYAGK--VDYKANEWL-MKNMDPLNDNVAALLHQSTDRL 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 978 ISNLFLGRAGsatvlsgsIAGLEGGSQL--ALRRATSMRKTFTTgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCF 1055
Cdd:cd14930 516 TAEIWKDVEG--------IVGLEQVSSLgdGPPGGRPRRGMFRT-VGQLYKESL--------SRLMATLSNTNPSFVRCI 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1056 LPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1135
Cdd:cd14930 579 VPNHEKRAG-----------------------------KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 629
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 600971660 1136 LAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14930 630 LTPNAIPKG-----FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
431-1181 |
2.74e-70 |
|
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: 250.91 E-value: 2.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW----QALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 584
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGsledQVVQTnpVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 585 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlaeNNVFGIVPLSKPE---EKQKAAQQFSKLQAAM 661
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLS----DNIYDYYIVSQGKvtvPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 662 KVLAISPEEQKTCWLILASIYHLGaagaTKEAAEAGRKQFARH---EWAQKAAYLLGCSLEELSSAIFKHQLKGGTlQRS 738
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMG----GMKFKQRGREEQAEQdgeEEGGRVSKLFGCDTAELYKNLLKPRIKVGN-EFV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 739 TSFRQgpeesglgegtKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGsargasFE 818
Cdd:cd14909 312 TQGRN-----------VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------FE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 819 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQASHLVRSLAHADEargllwlleeEALVP 898
Cdd:cd14909 375 QLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDF---GMDLLACIDLIEKPMGILSILEE----------ESMFP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 899 GATEDALLDRLFSyygpqegDKKGQSPLLRSSKP-------RHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQ 971
Cdd:cd14909 442 KATDQTFSEKLTN-------THLGKSAPFQKPKPpkpgqqaAHFAIAHYAGC--VSYNITGWLEKNK-DPLNDTVVDQFK 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 972 DSQKKIISNLFLGRAGSatvlSGSIAGLEGGsqlalrratsmRKTFTTGMAAVKKkslciQIKLQVDALIDTIKRSKMHF 1051
Cdd:cd14909 512 KSQNKLLIEIFADHAGQ----SGGGEQAKGG-----------RGKKGGGFATVSS-----AYKEQLNSLMTTLRSTQPHF 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1052 VHCFLPvaegwpgeprsassrrvsssSELDLPpgdpceaGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1131
Cdd:cd14909 572 VRCIIP--------------------NEMKQP-------GV--VDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKM 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 600971660 1132 RFDVLAPHLTKKHgrnyivVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14909 623 RYKILNPAGIQGE------EDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
432-1181 |
9.29e-69 |
|
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: 246.50 E-value: 9.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 511
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLATIAGT------SGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 583
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdlakkKDSKMKGTLEDQIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 584 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA---A 660
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILS----NKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLAtdsA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 661 MKVLAISPEEQKTCWLILASIYHLGaagaTKEAAEAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGTlqr 737
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYG----NMKFKQKQREEQAEpdgTEVADKTAYLMGLNSSDLLKALCFPRVKVGN--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 738 stsfrqgpEESGLGEgTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSF 817
Cdd:cd14913 311 --------EYVTKGQ-TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN------SL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 818 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALV 897
Cdd:cd14913 376 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPMGIFSILEEECMF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 898 PGATEDALLDRLFSYYGPQEGDKkgQSPLLRSSKPR-HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKK 976
Cdd:cd14913 443 PKATDTSFKNKLYDQHLGKSNNF--QKPKVVKGRAEaHFSLIHYAGT--VDYSVSGWLEKNK-DPLNETVVGLYQKSSNR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 977 IISNLFLGRAGS-ATVLSGSIAGLEGGSqlalrratsmrktFTTgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCF 1055
Cdd:cd14913 518 LLAHLYATFATAdADSGKKKVAKKKGSS-------------FQT-VSALFRENL--------NKLMSNLRTTHPHFVRCI 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1056 LPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1135
Cdd:cd14913 576 IPNETKTPGA-----------------------------MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 626
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 600971660 1136 LAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14913 627 LNASAIPE-GQ---FIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
432-1138 |
1.06e-68 |
|
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: 245.69 E-value: 1.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 511
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLATIAGTSGtkvfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 589
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSS----GIEN-EILQTnpILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 590 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKpeekqkaAQQFSKLQAAMKV 663
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLksaseyKYLNQSNCLTIDGVDD-------AKKFHELKEALDT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 664 LAISPEEQKTCWLILASIYHLG---------AAGATKEAAEAgrkqfarhewAQKAAYLLGCSLEELSSAIFKHQLKGGT 734
Cdd:cd01383 228 VGISKEDQEHIFQMLAAVLWLGnisfqvidnENHVEVVADEA----------VSTAASLLGCNANDLMLALSTRKIQAGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 735 LQRSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQH-SLCSMMIVDTPGFQnpewggSAR 813
Cdd:cd01383 298 DKIVKKL------------TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRrTGRSISILDIYGFE------SFQ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 814 GASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEpvadDSVAAVDqashLVRS-----LAHADEargll 888
Cdd:cd01383 360 KNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFE----DNQECLD----LIEKkplglISLLDE----- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 889 wlleeEALVPGATEDALLDRLFSYYGPQEGDKKGQSpllrsskpRHFLLGHSHGTnwVEYNVAGWLNytkqnpatQNAPR 968
Cdd:cd01383 427 -----ESNFPKATDLTFANKLKQHLKSNSCFKGERG--------GAFTIRHYAGE--VTYDTSGFLE--------KNRDL 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 969 LLQDsqkkiISNLFLGRAGSATVLSGSIAGLEGGSQLALRRATSMRKTfttgmaavkKKSLCIQIKLQVDALIDTIKRSK 1048
Cdd:cd01383 484 LHSD-----LIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQ---------KQSVATKFKGQLFKLMQRLENTT 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1049 MHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSE 1128
Cdd:cd01383 550 PHFIRCIKPNNKQLPGV-----------------------------FDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQE 600
|
730
....*....|
gi 600971660 1129 FRRRFDVLAP 1138
Cdd:cd01383 601 FARRYGFLLP 610
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
432-1181 |
1.54e-65 |
|
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: 236.92 E-value: 1.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 511
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLATIAG---------TSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQV 582
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 583 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA--- 659
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILS----NKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMAtdn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 660 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAGRKQFARHEwAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQR 737
Cdd:cd14917 237 AFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEE-ADKSAYLMGLNSADLLKGLCHPRVKVGNeyVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 738 STSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSF 817
Cdd:cd14917 316 GQNVQQVIYATG--------------ALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 818 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQAshlvrslahaDEARGLLWLLEEEALV 897
Cdd:cd14917 376 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---GMDLQACIDLI----------EKPMGIMSILEEECMF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 898 PGATEDALLDRLFSYYGPQEGDKkgQSPLLRSSKPR-HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKK 976
Cdd:cd14917 443 PKATDMTFKAKLFDNHLGKSNNF--QKPRNIKGKPEaHFSLIHYAGT--VDYNIIGWLQKNK-DPLNETVVGLYQKSSLK 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 977 IISNLFLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFL 1056
Cdd:cd14917 518 LLSNLFANYAGADAPIEKGKGKAKKGS------------SFQT-VSALHRENL--------NKLMTNLRSTHPHFVRCII 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1057 PVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1136
Cdd:cd14917 577 PNETKSPG-----------------------------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 627
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 600971660 1137 APHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14917 628 NPAAIPE-GQ---FIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
431-1181 |
2.14e-65 |
|
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: 236.08 E-value: 2.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTS-----GTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 585
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGkqssdGKGSLEDQIIQA-NPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 586 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKPEEKQKAaqqfsklQA 659
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvpnpkeYHWVSQGVTVVDNMDDGEELQIT-------DV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 660 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQR 737
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREE-QAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNefVQK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 738 STSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSF 817
Cdd:cd14934 312 GQNMEQCNNSIG--------------ALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN------SF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 818 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQashlvrslahADEARGLLWLLEEEALV 897
Cdd:cd14934 372 EQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDF---GLDLQACIDL----------LEKPMGIFSILEEQCVF 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 898 PGATE--------DALLDRLFSYYGPQEGDKKGQSPllrsskprHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRL 969
Cdd:cd14934 439 PKATDatfkaalyDNHLGKSSNFLKPKGGKGKGPEA--------HFELVHYAGT--VGYNITGWLEKNK-DPLNETVVGL 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 970 LQDSQkKIISNLFLGRAGSAtvlsgsiagleGGSQLALRRATSMrktfttgmaavkkkSLCIQIKLQVDALIDTIKRSKM 1049
Cdd:cd14934 508 FQKSS-LGLLALLFKEEEAP-----------AGSKKQKRGSSFM--------------TVSNFYREQLNKLMTTLHSTAP 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1050 HFVHCFLpvaegwpgeprsassrrvsssseldlpPGDPCEAGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1129
Cdd:cd14934 562 HFVRCIV---------------------------PNEFKQSGV--VDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEF 612
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 600971660 1130 RRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14934 613 KQRYQVLNPNVIPQG-----FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
431-1181 |
4.35e-65 |
|
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: 235.30 E-value: 4.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGpSLLVlstrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 502
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTG-SILV-------AVnpykelpiYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 503 DQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTkvFSVEKwQAL--STLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 580
Cdd:cd14883 73 NQSVIISGESGAGKTETTKLILQYLC--AVTNNH--SWVEQ-QILeaNTILEAFGNAKTVRNDNSSRFGKFIEVCFDASG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 581 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACG--DATLRTELHL---NHLAENNVFGIVPLSKPEEKQKaaqqFS 655
Cdd:cd14883 148 HIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLgepEDYHYLNQSGCIRIDNINDKKD----FD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 656 KLQAAMKVLAISPEEQKTCWLILASIYHLGaaGATKEAAEAGRKQFAR--HEWAQKAAYLLGCSLEELSSA-IFKHQLKG 732
Cdd:cd14883 224 HLRLAMNVLGIPEEMQEGIFSVLSAILHLG--NLTFEDIDGETGALTVedKEILKIVAKLLGVDPDKLKKAlTIRQINVR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 733 GTLqrsTSFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsa 812
Cdd:cd14883 302 GNV---TEIPLKVQE----------ARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN--- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 813 rgaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDLEPVADdsvaAVDQASHLVRSLAhADEARgllw 889
Cdd:cd14883 366 ---SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWShivFTDNQECLD----LIEKPPLGILKLL-DEECR---- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 890 lleeealVPGATEDALLDRLFSYYGPQEGDKKgqsPLLRSSKPRhFLLGHSHGTnwVEYNVAGWLNytkQNPATQ--NAP 967
Cdd:cd14883 434 -------FPKGTDLTYLEKLHAAHEKHPYYEK---PDRRRWKTE-FGVKHYAGE--VTYTVQGFLD---KNKDTQqdDLF 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 968 RLLQDSQKKIISNLFLGRAgsatvlsgsiagleggsQLALRRATSMRKTFTTGMAAVKKK-SLCIQIKLQVDALIDTIKR 1046
Cdd:cd14883 498 DLMSRSKNKFVKELFTYPD-----------------LLALTGLSISLGGDTTSRGTSKGKpTVGDTFKHQLQSLVDVLSA 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1047 SKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVF 1126
Cdd:cd14883 561 TQPWYVRCIKPNSLKEPN-----------------------------VFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTF 611
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 600971660 1127 SEFRRRFDVLAPHLTKKHGRnyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14883 612 KEFVDRYLCLDPRARSADHK-----ETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
433-1143 |
1.64e-64 |
|
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: 233.34 E-value: 1.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 433 VLHTLRQRYGASLLHTYAGPSLL-VLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 511
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIaVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 589
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQ-QVLESnpLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 590 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKPEEkqkaaqqFSKLQAAMKV 663
Cdd:cd01384 162 YLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 664 LAISPEEQKTCWLILASIYHLG--AAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQlkggtlqrstsf 741
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGniEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRV------------ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 742 RQGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQnpewggSARGASFEELC 821
Cdd:cd01384 303 IVTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE------SFKTNSFEQFC 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 822 HNYAQDRLQRLFHERTFLQELERYKEDNIELAF----------DDLEPVADDSVAAVDQASHLVRSlahadeargllwll 891
Cdd:cd01384 377 INLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYiefvdnqdvlDLIEKKPGGIIALLDEACMFPRS-------------- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 892 eeealvpgaTEDALLDRLFSYYgpqeGDKKgqspllRSSKPR----HFLLGHSHGTnwVEYNVAGWLNYTKQN--PATQN 965
Cdd:cd01384 443 ---------THETFAQKLYQTL----KDHK------RFSKPKlsrtDFTIDHYAGD--VTYQTDLFLDKNKDYvvAEHQA 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 966 aprLLQDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKtFTtgmaavkkkSLCIQIKLQVDALIDTIK 1045
Cdd:cd01384 502 ---LLNASKCPFVAGLF--------------------PPLPREGTSSSSK-FS---------SIGSRFKQQLQELMETLN 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1046 RSKMHFVHCFLPVAEgwpgeprsassrrvsssseldLPPGDPCEAGLLQldvsllraQLRGSRLLDAMRMYRQGYPDHMV 1125
Cdd:cd01384 549 TTEPHYIRCIKPNNL---------------------LKPGIFENANVLQ--------QLRCGGVLEAVRISCAGYPTRKP 599
|
730
....*....|....*...
gi 600971660 1126 FSEFRRRFDVLAPHLTKK 1143
Cdd:cd01384 600 FEEFLDRFGLLAPEVLKG 617
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
432-1181 |
1.23e-63 |
|
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: 231.11 E-value: 1.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 511
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLATIAgTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 581
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIA-VTGDKKKEQQPGKMQGTLedqiiqanplLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 582 VASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 659
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMS----NKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLAtd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 660 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELssaifkhqLKGGTLQRs 738
Cdd:cd14923 237 nAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAGYLMGLNSAEM--------LKGLCCPR- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 739 tsFRQGPEESGLGEGTKlSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFE 818
Cdd:cd14923 307 --VKVGNEYVTKGQNVQ-QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 819 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALVP 898
Cdd:cd14923 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFSILEEECMFP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 899 GATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKII 978
Cdd:cd14923 445 KATDTSFKNKLYDQHLGKSNNFQKPKPA-KGKAEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSSLKLL 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 979 SNLFLGRAGSAtvlsgsiAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLPV 1058
Cdd:cd14923 521 SFLFSNYAGAE-------AGDSGGSKKGGKKKGSSFQT----VSAVFRENL--------NKLMTNLRSTHPHFVRCLIPN 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1059 AEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1138
Cdd:cd14923 582 ETKTPG-----------------------------VMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNA 632
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 600971660 1139 HLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14923 633 SAIPEGQ----FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
432-1181 |
2.40e-63 |
|
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: 230.39 E-value: 2.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 511
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 581
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLedqiisanplLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 582 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 659
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 660 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQ 736
Cdd:cd14910 238 sAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNeyVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 737 RSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaS 816
Cdd:cd14910 317 KGQTVQQ--------------VYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------S 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 817 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEAL 896
Cdd:cd14910 377 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFSILEEECM 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 897 VPGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKK 976
Cdd:cd14910 444 FPKATDTSFKNKLYEQHLGKSNNFQKPKPA-KGKVEAHFSLIHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSSMK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 977 IISNLFLGrAGSATVLSGsiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFL 1056
Cdd:cd14910 520 TLALLFSG-AAAAEAEEG------GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTHPHFVRCII 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1057 PVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1136
Cdd:cd14910 580 PNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 600971660 1137 APHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14910 631 NASAIPE-GQ---FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
432-1181 |
1.25e-62 |
|
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: 228.08 E-value: 1.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 511
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLATIA---------GTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 580
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAvtgekkkeeAASGKMQGTLED-QIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 581 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA- 659
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMAt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 660 --AMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--L 735
Cdd:cd14915 237 dsAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNeyV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 736 QRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsarga 815
Cdd:cd14915 316 TKGQTVQQVYNSVG--------------ALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 816 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEA 895
Cdd:cd14915 376 SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFSILEEEC 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 896 LVPGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQK 975
Cdd:cd14915 443 MFPKATDTSFKNKLYEQHLGKSNNFQKPKPA-KGKAEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSGM 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 976 KIISNLFLGraGSATVLSGSiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCF 1055
Cdd:cd14915 519 KTLAFLFSG--GQTAEAEGG-----GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTHPHFVRCL 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1056 LPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1135
Cdd:cd14915 579 IPNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 600971660 1136 LAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14915 630 LNASAIPE-GQ---FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
433-1181 |
1.88e-62 |
|
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: 227.69 E-value: 1.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 433 VLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSS 512
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 513 GSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQ--------ALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 584
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 585 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA---AM 661
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtdsAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 662 KVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTlqrstsf 741
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGN------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 742 rqgpEESGLGEgTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELC 821
Cdd:cd14918 311 ----EYVTKGQ-TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLC 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 822 HNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALVPGAT 901
Cdd:cd14918 380 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPLGIFSILEEECMFPKAT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 902 EDALLDRLFSYYGPQEGDKKgQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNL 981
Cdd:cd14918 447 DTSFKNKLYDQHLGKSANFQ-KPKVVKGKAEAHFSLIHYAGT--VDYNITGWLDKNK-DPLNDTVVGLYQKSAMKTLASL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 982 FLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTGMAAVKKkslciqiklQVDALIDTIKRSKMHFVHCFLPVAEG 1061
Cdd:cd14918 523 FSTYASAEADSGAKKGAKKKGS------------SFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCIIPNETK 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1062 WPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLT 1141
Cdd:cd14918 582 TPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAI 632
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 600971660 1142 KKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14918 633 PE-GQ---FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
432-1181 |
1.34e-61 |
|
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: 225.38 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 511
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 581
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLedqiisanplLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 582 VASASIQTMLLEKLRVARRPASEATFNVFYYLlacgDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 659
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQI----TSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 660 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQ 736
Cdd:cd14912 238 sAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREE-QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNeyVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 737 RSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaS 816
Cdd:cd14912 317 KGQTVEQVTNAVG--------------ALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------S 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 817 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEAL 896
Cdd:cd14912 377 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPMGIFSILEEECM 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 897 VPGATEDALLDRLFSYYGPQEGDKKgQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKK 976
Cdd:cd14912 444 FPKATDTSFKNKLYEQHLGKSANFQ-KPKVVKGKAEAHFSLIHYAGV--VDYNITGWLDKNK-DPLNETVVGLYQKSAMK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 977 IISNLFLGragsATVLSGSIAGleGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFL 1056
Cdd:cd14912 520 TLAYLFSG----AQTAEGASAG--GGAKKGGKKKGSSFQT----VSALFRENL--------NKLMTNLRSTHPHFVRCII 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1057 PVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1136
Cdd:cd14912 582 PNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 632
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 600971660 1137 APHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14912 633 NASAIPE-GQ---FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
431-1138 |
1.59e-61 |
|
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: 224.65 E-value: 1.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMS----RQDQS 505
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPyKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSgvldPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 506 IVLLGSSGSGKTTSFQHLVQYLATIagTSGTKVFSVEKWQALST------------------LLEAFGNSPTIMNGSATR 567
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARI--TSGFAQGASGEGEAASEaieqtlgsledrvlssnpLLESFGNAKTLRNDNSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 568 FSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLnhlaENNVFGIVPLSK--PE 645
Cdd:cd14890 159 FGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKL----QTPVEYFYLRGEcsSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 646 EKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAI 725
Cdd:cd14890 235 PSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSLKLAAELLGVNEDALEKAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 726 FKHQL--KGGTLQRstsfrqgPEESGLGEgTKLSALeclegmASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGF 803
Cdd:cd14890 315 LTRQLfvGGKTIVQ-------PQNVEQAR-DKRDAL------AKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 804 QNPEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADDSVAAVDQASHLVRSLah 880
Cdd:cd14890 381 EKFEWNT------FEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDwqyITFNDNQACLELIEGKVNGKPGIFITL-- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 881 aDEARGLLWLLEEEALVpgatedALLDRLF--SYYGPQEGDKKGQSPLLRSSK---PRHFLLGHSHGTnwVEYNVAGwln 955
Cdd:cd14890 453 -DDCWRFKGEEANKKFV------SQLHASFgrKSGSGGTRRGSSQHPHFVHPKfdaDKQFGIKHYAGD--VIYDASG--- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 956 YTKQNPATqnaprlLQDSQKKIIsnlflgragsatvlsgsiagleggsqlalrrATSMRktfttgmaAVKKKSLCIQIKL 1035
Cdd:cd14890 521 FNEKNNET------LNAEMKELI-------------------------------KQSRR--------SIREVSVGAQFRT 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1036 QVDALIDTIKRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagLLQLDVSLlraQLRGSRLLDAMRM 1115
Cdd:cd14890 556 QLQELMAKISLTNPRYVRCIKPNETKAPGK--------------------------FDGLDCLR---QLKYSGMMEAIQI 606
|
730 740
....*....|....*....|....*.
gi 600971660 1116 YRQGYP---DHMVFseFrRRFDVLAP 1138
Cdd:cd14890 607 RQQGFAlreEHDSF--F-YDFQVLLP 629
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
432-1138 |
1.23e-60 |
|
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: 222.24 E-value: 1.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 511
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLATIA--GTSGTKVFSVEKWQAL-------STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQV 582
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAaiGDRSKKENPNANKGTLedqiiqaNPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 583 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA--- 659
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILS----NKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLAtds 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 660 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQR 737
Cdd:cd14916 238 AFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREE-QAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNeyVTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 738 STSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSF 817
Cdd:cd14916 317 GQSVQQ--------------VYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 818 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQAshlvrslahaDEARGLLWLLEEEALV 897
Cdd:cd14916 377 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---GMDLQACIDLI----------EKPMGIMSILEEECMF 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 898 PGATEDALLDRLF-SYYGPQEGDKKGQSplLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKK 976
Cdd:cd14916 444 PKASDMTFKAKLYdNHLGKSNNFQKPRN--VKGKQEAHFSLVHYAGT--VDYNILGWLEKNK-DPLNETVVGLYQKSSLK 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 977 IISNLFLGRAGSATvlsgsiaGLEGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFL 1056
Cdd:cd14916 519 LMATLFSTYASADT-------GDSGKGKGGKKKGSSFQT-----VSALHRENL--------NKLMTNLKTTHPHFVRCII 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1057 PVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1136
Cdd:cd14916 579 PNERKAPG-----------------------------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 629
|
..
gi 600971660 1137 AP 1138
Cdd:cd14916 630 NP 631
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
431-1057 |
2.58e-59 |
|
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: 217.80 E-value: 2.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLL-VLSTRGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 509
Cdd:cd01378 1 EAINENLKKRFENDEIYTYIGHVLIsVNPFKDLG-IYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 510 GSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVeKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASI 587
Cdd:cd01378 80 GESGAGKTEASKRIMQYIAAVSGGSESEVERV-KDMLLASnpLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 588 QTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKpeekqkaAQQFSKLQAAM 661
Cdd:cd01378 159 TNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLqrpeqyYYYSKSGCFDVDGIDD-------AADFKEVLNAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 662 KVLAISPEEQKTCWLILASIYHLGAAGATKEaaEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRST-S 740
Cdd:cd01378 232 KVIGFTEEEQDSIFRILAAILHLGNIQFAED--EEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGRSVyE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 741 FRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGF----QNpewggsarga 815
Cdd:cd01378 310 VPLNVEQ----------AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIgVLDIYGFeifeKN---------- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 816 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA----FDDlEPVADdsvaavdqashLVRS-----LAHADEArg 886
Cdd:cd01378 370 SFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTpikyFNN-KIICD-----------LIEEkppgiFAILDDA-- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 887 llwlleeEALVPGATEDALLDRLFSYYGPQEGDKKGQSPllRSSKPRHFLLGHSHGTnwVEYNVAGwlnYTKQNPAT--Q 964
Cdd:cd01378 436 -------CLTAGDATDQTFLQKLNQLFSNHPHFECPSGH--FELRRGEFRIKHYAGD--VTYNVEG---FLDKNKDLlfK 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 965 NAPRLLQDSQKKIISNLFlgragsatvlsgsiagLEGGSQLALRRATsmrktfTTGMaavkkkslciQIKLQVDALIDTI 1044
Cdd:cd01378 502 DLKELMQSSSNPFLRSLF----------------PEGVDLDSKKRPP------TAGT----------KFKNSANALVETL 549
|
650
....*....|...
gi 600971660 1045 KRSKMHFVHCFLP 1057
Cdd:cd01378 550 MKKQPSYIRCIKP 562
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
431-1138 |
3.88e-58 |
|
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: 214.64 E-value: 3.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 509
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPyQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 510 GSSGSGKTTSFQHLVQYLATIAGtsGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 589
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 590 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAennVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 669
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANEC---AYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 670 EQKTCWLILASIYHLGAAGATKEAAEAGRKQFAR-HEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFRqgpees 748
Cdd:cd14903 236 KQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPgDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 749 glgegtKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCHNYAQDR 828
Cdd:cd14903 310 ------KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHN------SFEQFCINYANEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 829 LQRLFHERTFLQELERYKEDNIELAFDDLepvADDS-VAAVDQASHLVRSLAHADEARgllwlleeealvPGATEDALLD 907
Cdd:cd14903 378 LQQKFTQDVFKTVQIEYEEEGIRWAHIDF---ADNQdVLAVIEDRLGIISLLNDEVMR------------PKGNEESFVS 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 908 RLFSYYgpqeGDKKGQSPLLRSSKPRhFLLGHSHGTnwVEYNVAGWLNYTKQNpatqnaprLLQD-------SQKKIISN 980
Cdd:cd14903 443 KLSSIH----KDEQDVIEFPRTSRTQ-FTIKHYAGP--VTYESLGFLEKHKDA--------LLPDlsdlmrgSSKPFLRM 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 981 LFLGRAGSATVLSGSIAGLEGgsqlalRRATSMRKTFTTGMaavkkkslciQIKLQVDALIDTIKRSKMHFVHCFLPVAE 1060
Cdd:cd14903 508 LFKEKVESPAAASTSLARGAR------RRRGGALTTTTVGT----------QFKDSLNELMTTIRSTNVHYVRCIKPNSI 571
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 600971660 1061 GWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1138
Cdd:cd14903 572 KSPTE-----------------------------LDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLP 620
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
431-1138 |
1.50e-57 |
|
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: 212.50 E-value: 1.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGpSLLVlstrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 502
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTG-SILV-------AVnpyqilpiYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 503 DQSIVLLGSSGSGKTTSFQHLVQYLATIAGtsgtKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 580
Cdd:cd01381 73 DQCVVISGESGAGKTESTKLILQYLAAISG----QHSWIEQ-QILEAnpILEAFGNAKTIRNDNSSRFGKYIDIHFNKNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 581 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNH------LAENNVFGIvplskpeEKQKAAQQF 654
Cdd:cd01381 148 VIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDasdyyyLTQGNCLTC-------EGRDDAAEF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 655 SKLQAAMKVLAISPEEQKTCWLILASIYHLGAAG------ATKEAAEagrkqFARHEWAQKAAYLLGCSLEELSSAIFKH 728
Cdd:cd01381 221 ADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKfeatvvDNLDASE-----VRDPPNLERAAKLLEVPKQDLVDALTTR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 729 QL--KGGTLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRAL---KSSQHSLCSMMIVDTPGF 803
Cdd:cd01381 296 TIftRGETVVSPLSAEQ--------------ALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 804 QNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsVAAVDQAShlvrSLAH 880
Cdd:cd01381 362 ENFEVN------SFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINwqhIEFVDNQDVLD--LIALKPMN----IMSL 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 881 ADEargllwlleeEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLLRSSKPRHFLlghshGTnwVEYNVAGWLNytKQN 960
Cdd:cd01381 430 IDE----------ESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFA-----GV--VFYDTRGFLE--KNR 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 961 PA-TQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsQLALRRATSMRKtfttgmaavKKKSLCIQIKLQVDA 1039
Cdd:cd01381 491 DTfSADLLQLVQSSKNKFLKQLF---------------------NEDISMGSETRK---------KSPTLSSQFRKSLDQ 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1040 LIDTIKRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQG 1119
Cdd:cd01381 541 LMKTLSACQPFFVRCIKPNEYKKPML-----------------------------FDRELCVRQLRYSGMMETIRIRKAG 591
|
730
....*....|....*....
gi 600971660 1120 YPDHMVFSEFRRRFDVLAP 1138
Cdd:cd01381 592 YPIRHTFEEFVERYRVLVP 610
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
432-856 |
9.51e-57 |
|
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: 209.70 E-value: 9.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYG-ASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGTKVfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQ 588
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET-QVEE-KVLASnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 589 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISP 668
Cdd:cd01380 160 TYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGS-AEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 669 EEQKTCWLILASIYHLGAAgATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLK--GGTLQRSTSFRQgpe 746
Cdd:cd01380 239 EEQMEIFRILAAILHLGNV-EIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVtrSEVIVKPLTLQQ--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 747 esglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQ-HSLCSMM-IVDTPGFQNPEWGgsargaSFEELCHNY 824
Cdd:cd01380 315 -----------AIVARDALAKHIYAQLFDWIVDRINKALASPVkEKQHSFIgVLDIYGFETFEVN------SFEQFCINY 377
|
410 420 430
....*....|....*....|....*....|..
gi 600971660 825 AQDRLQRLFHERTFLQELERYKEDNIELAFDD 856
Cdd:cd01380 378 ANEKLQQQFNQHVFKLEQEEYVKEEIEWSFID 409
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
432-1141 |
1.10e-56 |
|
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: 210.04 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGpSLL--VLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 509
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIG-SILasVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 510 GSSGSGKTTSFQHLVQYLATIAGTS-----GTKVFSVEKWQALST-LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 583
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelslKEKTSCVEQAILESSpIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 584 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhLAEN----NVFGIVPLSKPEEKqkaaQQFSKLQA 659
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENyhylNQSGCVEDKTISDQ----ESFREVIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 660 AMKVLAISPEEQKTCWLILASIYHLGAAgatkEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIfkhqlkggtLQRST 739
Cdd:cd14873 236 AMEVMQFSKEEVREVSRLLAGILHLGNI----EFITAGGAQVSFKTALGRSAELLGLDPTQLTDAL---------TQRSM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 740 SFRqGPEESglgegTKLS---ALECLEGMASGLYSELFTLLISLVNRALKSSQHsLCSMMIVDTPGFQNPEWGgsargaS 816
Cdd:cd14873 303 FLR-GEEIL-----TPLNvqqAVDSRDSLAMALYARCFEWVIKKINSRIKGKED-FKSIGILDIFGFENFEVN------H 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 817 FEELCHNYAQDRLQRLFHERTF-LQELERYKEDnieLAFDDLEPVadDSVAAVDQASHLVRSLAHADEargllwlleeEA 895
Cdd:cd14873 370 FEQFNINYANEKLQEYFNKHIFsLEQLEYSREG---LVWEDIDWI--DNGECLDLIEKKLGLLALINE----------ES 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 896 LVPGATEDALLDRLFSyygpqeGDKKGQSPLlrssKPR--HFLLGHSHGTNWVEYNVAGWLnytKQNPAT--QNAPRLLQ 971
Cdd:cd14873 435 HFPQATDSTLLEKLHS------QHANNHFYV----KPRvaVNNFGVKHYAGEVQYDVRGIL---EKNRDTfrDDLLNLLR 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 972 DSQKKIISNLFlgragsatvlsgsiagleggsqlalRRATSMRKTFTTGMAAVKKK-SLCIQIKLQVDALIDTIKRSKMH 1050
Cdd:cd14873 502 ESRFDFIYDLF-------------------------EHVSSRNNQDTLKCGSKHRRpTVSSQFKDSLHSLMATLSSSNPF 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1051 FVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1130
Cdd:cd14873 557 FVRCIKPNMQKMPD-----------------------------QFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFY 607
|
730
....*....|.
gi 600971660 1131 RRFDVLAPHLT 1141
Cdd:cd14873 608 KRYKVLMRNLA 618
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
432-862 |
7.56e-56 |
|
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: 207.13 E-value: 7.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 511
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLaTIAGTSGTKVFSvEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTML 591
Cdd:cd01379 82 SGAGKTESANLLVQQL-TVLGKANNRTLE-EKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 592 LEKLRVARRPASEATFNVFYYLLA-------CGDATLRTELHLNHLAEnnvFGIVPLSKpEEKQKAAQQFSKLQAAMKVL 664
Cdd:cd01379 160 LEKSRVVHQAIGERNFHIFYYIYAglaedkkLAKYKLPENKPPRYLQN---DGLTVQDI-VNNSGNREKFEEIEQCFKVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 665 AISPEEQKTCWLILASIYHLGA---AGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQL--KGGTLQRST 739
Cdd:cd01379 236 GFTKEEVDSVYSILAAILHIGDiefTEVESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVvtRGETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 740 SFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHS---LCSMMIVDTPGFQNpewggsARGAS 816
Cdd:cd01379 316 TVEE--------------ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAsdePLSIGILDIFGFEN------FQKNS 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 600971660 817 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL---AFDDLEPVAD 862
Cdd:cd01379 376 FEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVdliEYEDNRPLLD 424
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
432-983 |
9.98e-56 |
|
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: 206.85 E-value: 9.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGTkvFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 590
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPSDDS--DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 591 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNH------LAENNVFGIVpLSKPEEKQKAAQQFSKLQAAMKVL 664
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDpdchriLRDDNRNRPV-FNDSEELEYYRQMFHDLTNIMKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 665 AISPEEQKTCWLILASIYHLgAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIF--KHQLKGGTLQRSTSFR 742
Cdd:cd14897 239 GFSEEDISVIFTILAAILHL-TNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALIsnVNTIRGERIQSWKSLR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 743 QgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQ-----HSLCSMMIVDTPGFQNpewggsARGASF 817
Cdd:cd14897 318 Q--------------ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKdfqimTRGPSIGILDMSGFEN------FKINSF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 818 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAfdDLEPVADDSV------------AAVDQASHLvrslahadear 885
Cdd:cd14897 378 DQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR--DIEYHDNDDVlelffkkplgilPLLDEESTF----------- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 886 gllwlleeealvPGATEDALLDRLFSYYGPqegdkkgqSPLLRSSKPRHFLLGHSHGTNWVEYNVAGWLNYTKQNpATQN 965
Cdd:cd14897 445 ------------PQSTDSSLVQKLNKYCGE--------SPRYVASPGNRVAFGIRHYAEQVTYDADGFLEKNRDN-LSSD 503
|
570
....*....|....*...
gi 600971660 966 APRLLQDSQKKIISNLFL 983
Cdd:cd14897 504 IVGCLLNSNNEFISDLFT 521
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
431-1181 |
3.97e-54 |
|
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: 202.68 E-value: 3.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGTKVfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQaGQVASASIQTM 590
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLV--TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 591 LLEKLRVARRPASEATFNVFYYLLACGDATLRTE---------LHLNHLAENNVFGivplskpeekQKAAQQFSKLQAAM 661
Cdd:cd01387 158 LLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKyglqeaekyFYLNQGGNCEIAG----------KSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 662 KVLAISPEEQKTCWLILASIYHLG-------AAGATKEAAEAGRKqfARHEWaqkAAYLLGCSLEELSSAIfkhqlkggt 734
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGnvyfhkrQLRHGQEGVSVGSD--AEIQW---VAHLLQISPEGLQKAL--------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 735 LQRSTSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsarg 814
Cdd:cd01387 294 TFKVTETRRERIFTPL---TIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN----- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 815 aSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVAddsvaavdqasHLVrslahADEARGLLWLL 891
Cdd:cd01387 366 -SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDwteIAFADNQPVI-----------NLI-----SKKPVGILHIL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 892 EEEALVPGATEDALLDRLFSYYGPQEgdkkgqspllRSSKPR----HFLLGHSHGTNWveYNVAGWLNYTKqNPATQNAP 967
Cdd:cd01387 429 DDECNFPQATDHSFLEKCHYHHALNE----------LYSKPRmplpEFTIKHYAGQVW--YQVHGFLDKNR-DQLRQDVL 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 968 RLLQDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAAVKKKSLCIQIKLQ--VDALIDTIK 1045
Cdd:cd01387 496 ELLVSSRTRVVAHLF--------------------SSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQdsLLQLLEKME 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1046 RSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRGSRLLDAMRMYRQGYPDHMV 1125
Cdd:cd01387 556 RCNPWFVRC---------------------------LKPNHKKEPMLFDMDVVM--AQLRYSGMLETIRIRKEGYPVRLP 606
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1126 FSEFRRRFDvlapHLTKKHGRNYIVVDEKRAVeELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd01387 607 FQVFIDRYR----CLVALKLPRPAPGDMCVSL-LSRLCTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
428-860 |
7.66e-54 |
|
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: 201.24 E-value: 7.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 428 LNESSVLHTLRQRYGASLLHTYAGPS-LLVLSTRGAPAVYSEKVMHMFK-------GCRREDMAPHIYAVAQTAYRAMLM 499
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 500 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTS--GTKVfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFD 577
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSkkGTKL--SSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 578 QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF---GIVPL-SKPEEKQkaAQQ 653
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLpLGPGSDD--AEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 654 FSKLQAAMKVLAISPEEQKTCWLILASIYHLgaagatkeaaeaGRKQFA-----RHEWA--------QKAAYLLGCSLEE 720
Cdd:cd14879 237 FQELKTALKTLGFKRKHVAQICQLLAAILHL------------GNLEFTydhegGEESAvvkntdvlDIVAAFLGVSPED 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 721 LSSAI-FKHQLKGGtlQRSTSFrqgpeesgLG-EGTKLSALEclegMASGLYSELFTLLISLVNRALKSSQHSLCSMM-I 797
Cdd:cd14879 305 LETSLtYKTKLVRK--ELCTVF--------LDpEGAAAQRDE----LARTLYSLLFAWVVETINQKLCAPEDDFATFIsL 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 798 VDTPGFQNPewgGSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA----FDDLEPV 860
Cdd:cd14879 371 LDFPGFQNR---SSTGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPatsyFDNSDCV 434
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
433-1136 |
2.34e-53 |
|
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: 200.13 E-value: 2.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 433 VLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAML----MSRQDQSIVL 508
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 509 LGSSGSGKTTSFQHLVQYLATIAgtSGTKVFSVEKWQaLSTLLEAFGNSPTIMNGSATRFSQILSLDFdQAGQVASASIQ 588
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC--RGNSQLEQQILQ-VNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 589 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL----NHLAENNVFGivplsKPEEKQKAAQQFSKLQAAMKVL 664
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLldpgKYRYLNNGAG-----CKREVQYWKKKYDEVCNAMDMV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 665 AISPEEQKTCWLILASIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSsaifkhqlkgGTLQRSTSFRQG 744
Cdd:cd14889 234 GFTEQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGWLKAAAGQFGVSEEDLL----------KTLTCTVTFTRG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 745 peESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHS---LCSMMIVDTPGFQNPEWGgsargaSFEELC 821
Cdd:cd14889 304 --EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSsveLREIGILDIFGFENFAVN------RFEQAC 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 822 HNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDLEPVADDSVAA-------VDQASHLvrslahadeargllwll 891
Cdd:cd14889 376 INLANEQLQYFFNHHIFLMEQKEYKKEGIdwkEITYKDNKPILDLFLNKpigilslLDEQSHF----------------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 892 eeealvPGATEDALLDRLFSYYGPQEGDKKGQspllrsSKPRHFLLGHSHGTnwVEYNVAGWLNYTKQN-PATQNAprLL 970
Cdd:cd14889 439 ------PQATDESFVDKLNIHFKGNSYYGKSR------SKSPKFTVNHYAGK--VTYNASGFLEKNRDTiPASIRT--LF 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 971 QDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSQlalrratsmrktfttGMAAVKKKSLCIQIKLQVDALIDTIKRSKMH 1050
Cdd:cd14889 503 INSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD---------------NFNSTRKQSVGAQFKHSLGVLMEKMFAASPH 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1051 FVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1130
Cdd:cd14889 568 FVRCIKPNHVKVPG-----------------------------QLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFA 618
|
....*.
gi 600971660 1131 RRFDVL 1136
Cdd:cd14889 619 ERYKIL 624
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
431-1137 |
3.58e-53 |
|
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: 199.24 E-value: 3.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIagtsGTKVFSVEKWQALSTL--LEAFGNSPTIMNGSATRFSQILSLDFdQAGQVASASIQ 588
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVLpiLESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 589 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAEN----NVFGIVPLSKPEEkqkaAQQFSKLQAAMKVL 664
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETyyylNQGGACRLQGKED----AQDFEGLLKALQGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 665 AISPEEQKTCWLILASIYHLGA---AGATKEAAEAGrkqfARHEWA--QKAAYLLGCSLEELSSAIFKHQLKGGTLQRST 739
Cdd:cd14896 231 GLCAEELTAIWAVLAAILQLGNicfSSSERESQEVA----AVSSWAeiHTAARLLQVPPERLEGAVTHRVTETPYGRVSR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 740 SFrqgPEEsglgegtklSALECLEGMASGLYSELFTLLISLVNRAL--KSSQHSLCSMMIVDTPGFQnpewggSARGASF 817
Cdd:cd14896 307 PL---PVE---------GAIDARDALAKTLYSRLFTWLLKRINAWLapPGEAESDATIGVVDAYGFE------ALRVNGL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 818 EELCHNYAQDRLQRLFHERTFLQELERYKEDniELAFDDLEPVADDSVA--AVDQASHLVRSLahadeargllwllEEEA 895
Cdd:cd14896 369 EQLCINLASERLQLFSSQTLLAQEEEECQRE--LLPWVPIPQPPRESCLdlLVDQPHSLLSIL-------------DDQT 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 896 LVPGATEDALLDRLFSYYGPQEGDKKGQSPLlrsskPRhFLLGHSHGTnwVEYNVAGWLNYTKQ--NPATQNaprLLQDS 973
Cdd:cd14896 434 WLSQATDHTFLQKCHYHHGDHPSYAKPQLPL-----PV-FTVRHYAGT--VTYQVHKFLNRNRDqlDPAVVE---MLAQS 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 974 QKKIISNLFlgragsatvlsgsiagLEGGSQLALRRatsmrktfttgmaavKKKSLCIQIKLQVDALIDTIKRSKMHFVH 1053
Cdd:cd14896 503 QLQLVGSLF----------------QEAEPQYGLGQ---------------GKPTLASRFQQSLGDLTARLGRSHVYFIH 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1054 CFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRF 1133
Cdd:cd14896 552 CLNPNPGKLPG-----------------------------LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARF 602
|
....
gi 600971660 1134 DVLA 1137
Cdd:cd14896 603 GALG 606
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
432-1138 |
1.82e-52 |
|
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: 197.47 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPyKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGtsGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 590
Cdd:cd14904 82 ESGAGKTETTKIVMNHLASVAG--GRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 591 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEE 670
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 671 QKTCWLILASIYHLGAAGATKEAAEAGRKQfaRHEWAQKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRQgpeESGL 750
Cdd:cd14904 240 QRTLFKILSGVLHLGEVMFDKSDENGSRIS--NGSQLSQVAKMLGLPTTRIEEAL---------CNRSVVTRN---ESVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 751 GEGTKLSALECLEGMASGLYSELFTLLISLVNRALkSSQHSLCSMMI--VDTPGFQNPEWGGsargasFEELCHNYAQDR 828
Cdd:cd14904 306 VPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAI-STDDDRIKGQIgvLDIFGFEDFAHNG------FEQFCINYANEK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 829 LQRLFHERTFLQELERYKEDNieLAFDDLEPVADDSVAAVDQASHLVRSLAHaDEARGllwlleeealvPGATEDALLDR 908
Cdd:cd14904 379 LQQKFTTDVFKTVEEEYIREG--LQWDHIEYQDNQGIVEVIDGKMGIIALMN-DHLRQ-----------PRGTEEALVNK 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 909 LFSYYGPQEGDKKGQSPllrSSKPRHFLLGHSHGTnwVEYNVAGWLNytKQNPATQN-APRLLQDSQKKIISNLFlgraG 987
Cdd:cd14904 445 IRTNHQTKKDNESIDFP---KVKRTQFIINHYAGP--VTYETVGFME--KHRDTLQNdLLDLVLLSSLDLLTELF----G 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 988 SATVLSGSIAGLEGGSQLAlrratsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGEpr 1067
Cdd:cd14904 514 SSEAPSETKEGKSGKGTKA-------------------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTE-- 572
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1068 sassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1138
Cdd:cd14904 573 ---------------------------FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP 616
|
|
| PDZ_MYO18-like |
cd06747 |
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein ... |
220-308 |
8.70e-52 |
|
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MYO18 protein and related domains. MYO18 (also known as myosin XVIIIA, KIAA0216, MysPDZ), a member of the myosin superfamily, is involved in regulating cell protrusion and migration, and Golgi trafficking and morphology, and is required for myoblast adhesion and muscle integrity. The MYO18A/MRCK/LRAP35a complex regulates actomyosin retrograde flow in cell protrusion and migration; the PtdIns(4)P/GOLPH3/MYO18A/F-actin complex is a hub for signals that regulate Golgi trafficking function. The MYO18A PDZ domain binds p190Rho-guanine nucleotide exchange factor (p190RhoGEF), Golgin45, and leucine repeat adaptor protein 1 (Lurap1, also known as Lrap35a). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MYO18-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.
Pssm-ID: 467229 [Multi-domain] Cd Length: 90 Bit Score: 177.12 E-value: 8.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPTGDFGFSLRRTTMLDRAPE-GQAYRRVVHFAEPGAGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQ 298
Cdd:cd06747 1 EITLKRQPTGDFGFSLRRGTIVERGPDdGQELKRTVHFAEPGAGTKNLATGLLPGDRLIEVNGVNVENASRDEIIEMIRK 80
|
90
....*....|
gi 600971660 299 SGDSVRLKVQ 308
Cdd:cd06747 81 SGDTVTLKVQ 90
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
432-1181 |
9.39e-52 |
|
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: 194.99 E-value: 9.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVM--HMFKGCRRedMAPHIYAVAQTAYRAMLMSRQDQSIVLL 509
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMdqYMHKGPKE--MPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 510 GSSGSGKTTSFQHLVQYLATIAGTSGtkvfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASI 587
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTN----GVEQ-RVLLAnpILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 588 QTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlaenNVFGIVPLSKPEEKQKA--AQQFSKLQAAMKVLA 665
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSS-----AAYGYLSLSGCIEVEGVddVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 666 ISPEEQKTCWLILASIYHLG----AAGATKEAAEAgrKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QLKGgtlQRST 739
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGniefASGGGKSLVSG--STVANRDVLKEVATLLGVDAATLEEALTSRlmEIKG---CDPT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 740 SFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSL-CSMMIVDTPGFQNPEWGgsargaSFE 818
Cdd:cd14872 305 RIPLTPAQ----------ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKtTFIGVLDIFGFEIFEKN------SFE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 819 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVrslahadEAR--GLLWLLEE 893
Cdd:cd14872 369 QLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKfehIDFIDNQPVLD-----------LI-------EKKqpGLMLALDD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 894 EALVPGATEDALLDRLfsyyGPQEGDKKGQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDS 973
Cdd:cd14872 431 QVKIPKGSDATFMIAA----NQTHAAKSTFVYAEVRTSRTEFIVKHYAGD--VTYDITGFLEKNK-DTLQKDLYVLLSSS 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 974 QKKIISNLFlgragsatvlsgsiagleggSQLALRRATSmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVH 1053
Cdd:cd14872 504 KNKLIAVLF--------------------PPSEGDQKTS-------------KVTLGGQFRKQLSALMTALNATEPHYIR 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1054 CflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRF 1133
Cdd:cd14872 551 C---------------------------VKPNQEKRARLFDGFMSL--EQLRYAGVFEAVKIRKTGYPFRYSHERFLKRY 601
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 600971660 1134 DVLAPHLTKKHGRnyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1181
Cdd:cd14872 602 RFLVKTIAKRVGP-----DDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
432-1138 |
2.63e-51 |
|
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: 194.14 E-value: 2.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLL-VLSTRGAPAVYSEKVM--HMFKGcrrEDMAPHIYAVAQTAYRAMLMSRQDQSIVL 508
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIaVNPFKTIPGLYSDEMLlkFIQPS---ISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 509 LGSSGSGKTTSFQHLVQYLATiAGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQ-------- 578
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLAC-AGSEDIKKRSLVEAQVLESnpLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 579 -AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIV--PLSKPEEKQKAAQQFS 655
Cdd:cd14888 158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADakPISIDMSSFEPHLKFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 656 KLQ--------------------AAMKVLAISPEEQKTCWLILASIYHLGAAG-ATKEAAEAGRKQFA-RHEWAQKAAYL 713
Cdd:cd14888 238 YLTksschelpdvddleefestlYAMQTVGISPEEQNQIFSIVAAILYLGNILfENNEACSEGAVVSAsCTDDLEKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 714 LGCSLEELSSAifkhqLKGGTLQRSTSFRQGPEESGLGEGTKlsaleclEGMASGLYSELFTLLISLVNRAL-KSSQHSL 792
Cdd:cd14888 318 LGVDAEDLLNA-----LCYRTIKTAHEFYTKPLRVDEAEDVR-------DALARALYSCLFDKVVERTNESIgYSKDNSL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 793 CSMMIVDTPGFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLE-PVADDSVAAVDQA 871
Cdd:cd14888 386 LFCGVLDIFGFE------CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIS--WNPLDfPDNQDCVDLLQEK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 872 SHLVrsLAHADEargllwlleeEALVPGATEDALLDRLFSYYGpqeGDKKGQSPllrSSKPRHFLLGHSHGTnwVEYNVA 951
Cdd:cd14888 458 PLGI--FCMLDE----------ECFVPGGKDQGLCNKLCQKHK---GHKRFDVV---KTDPNSFVIVHFAGP--VKYCSD 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 952 GWLNYTKqNPATQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsqlalrrATSMRKTFTTGMAAVKKKSLCI 1031
Cdd:cd14888 518 GFLEKNK-DQLSVDAQEVIKNSKNPFISNLF---------------------------SAYLRRGTDGNTKKKKFVTVSS 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1032 QIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPgeprsassrrvsssSELDlppgdpceagllQLDVSllrAQLRGSRLLD 1111
Cdd:cd14888 570 EFRNQLDVLMETIDKTEPHFIRCIKPNSQNVP--------------DLFD------------RISVN---EQLKYGGVLQ 620
|
730 740
....*....|....*....|....*..
gi 600971660 1112 AMRMYRQGYPDHMVFSEFRRRFDVLAP 1138
Cdd:cd14888 621 AVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
434-1137 |
2.69e-51 |
|
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: 193.82 E-value: 2.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 434 LHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSekVMHMFKGCRREDMA----PHIYAVAQTAYRAMLMSR----QDQ 504
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPyKSIPLLYD--VPGFDSQRKEEATAssppPHVFSIAERAYRAMKGVGkgqgTPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 505 SIVLLGSSGSGKTTSFQHLVQYLATI----AGTSGTKVF-----SVEKWQALS-TLLEAFGNSPTIMNGSATRFSQILSL 574
Cdd:cd14892 82 SIVVSGESGAGKTEASKYIMKYLATAsklaKGASTSKGAanaheSIEECVLLSnLILEAFGNAKTIRNDNSSRFGKYIQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 575 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAEnnvFGIVPLSKPEEKQKA--AQ 652
Cdd:cd14892 162 HYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAES---FLFLNQGNCVEVDGVddAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 653 QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAGRK-QFARHEWAQKAAYLLGCSLEELSSAIFKHQLK 731
Cdd:cd14892 239 EFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFaQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 732 GGtlqRSTSFRQ--GPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRAlkSSQHSLCSMMIVDTP-------- 801
Cdd:cd14892 319 TA---RGSVLEIklTARE----------AKNALDALCKYLYGELFDWLISRINAC--HKQQTSGVTGGAASPtfspfigi 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 802 ----GFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaaVDQASHL 874
Cdd:cd14892 384 ldifGFE------IMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDvsaIEFQDNQDCLD-----LIQKKPL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 875 vrslahadeargllwlleeeALVPGATEDALLDR-------LFSYYgpQEGDKKGQSpllrSSKPR----HFLLGHSHGT 943
Cdd:cd14892 453 --------------------GLLPLLEEQMLLKRkttdkqlLTIYH--QTHLDKHPH----YAKPRfecdEFVLRHYAGD 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 944 nwVEYNVAGWLnyTKQNPATQNAPRLLQDSQKKiisnlflgragsatvlsgsiagleggsqlalrratsmrktFTTgmaa 1023
Cdd:cd14892 507 --VTYDVHGFL--AKNNDNLHDDLRDLLRSSSK----------------------------------------FRT---- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1024 vkkkslciqiklQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvsssSELDLPPGDPCEagllqldvsLLRAQ 1103
Cdd:cd14892 539 ------------QLAELMEVLWSTTPSYIKCIKP--------------------NNLKFPGGFSCE---------LVRDQ 577
|
730 740 750
....*....|....*....|....*....|....
gi 600971660 1104 LRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1137
Cdd:cd14892 578 LIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLA 611
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
432-1143 |
3.39e-51 |
|
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: 194.73 E-value: 3.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFK--------GCRREDMAPHIYAVAQTAYRAMLMS-R 501
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPlKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 502 QDQSIVLLGSSGSGKTTSFQHLVQYLATI-----AGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSL 574
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLTSVgrdqsSTEQEGSDAVEIGKRILQTnpILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 575 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAE---NNVFGIVPLSKPEEKQKAA 651
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKyelLNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 652 QQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG--AAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQ 729
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGnvNFTAENGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSRE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 730 LKGGtlQRSTSFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVN---------RALKSSQHSLCSMMIVDT 800
Cdd:cd14902 322 IKAG--VEVMVLKLTPEQ----------AKEICGSLAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGILDI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 801 PGFQNPEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVaddsVAAVDqashlvrs 877
Cdd:cd14902 390 FGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDwknISYPSNAAC----LALFD-------- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 878 lahaDEARGLLWLLEEEALVPGATEDALLDRLFSYYGPQEgdkkgqspllrsskprHFLLGHSHGTnwVEYNVAGWLNyT 957
Cdd:cd14902 452 ----DKSNGLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAGR--VCYNVEQFVE-K 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 958 KQNPATQNAPRLLQDSQKKIISNLFL-GRAGSATVLSGSiagleggsqlALRRATSMrktfttgmaaVKKKSLCIQIKLQ 1036
Cdd:cd14902 509 NTDALPADASDILSSSSNEVVVAIGAdENRDSPGADNGA----------AGRRRYSM----------LRAPSVSAQFKSQ 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1037 VDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMY 1116
Cdd:cd14902 569 LDRLIVQIGRTEAHYVRCLKPNEVKKPG-----------------------------IFDRERMVEQMRSVGVLEAVRIA 619
|
730 740
....*....|....*....|....*..
gi 600971660 1117 RQGYPDHMVFSEFRRRFDVLAPHLTKK 1143
Cdd:cd14902 620 RHGYSVRLAHASFIELFSGFKCFLSTR 646
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
432-1179 |
3.64e-51 |
|
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: 193.47 E-value: 3.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSE--KVMHMFKGCRRED----MAPHIYAVAQTAYRAMLMSR---- 501
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDetKEAYYEHGERRAAgerkLPPHVYAVADKAFRAMLFASrgqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 502 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW----QALST--LLEAFGNSPTIMNGSATRFSQILSLD 575
Cdd:cd14901 82 CDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATEREnvrdRVLESnpILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 576 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFS 655
Cdd:cd14901 162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 656 KLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTL 735
Cdd:cd14901 242 KTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 736 QRSTSFRqgPEESGLGEgtklsaleclEGMASGLYSELFTLLISLVNRALK--SSQHSLCSMMIVDTPGF----QNpewg 809
Cdd:cd14901 322 YITMPLS--VEQALLTR----------DVVAKTLYAQLFDWLVDRINESIAysESTGASRFIGIVDIFGFeifaTN---- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 810 gsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLePVADDSVAAVDQASHLVRSLahADEargllw 889
Cdd:cd14901 386 ------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-PNNDACVAMFEARPTGLFSL--LDE------ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 890 lleeEALVPGATEDALLDrlfSYYgpqegDKKGQSPLLRSSK----PRHFLLGHSHGTnwVEYNVAGWLNYTKQNPATqN 965
Cdd:cd14901 451 ----QCLLPRGNDEKLAN---KYY-----DLLAKHASFSVSKlqqgKRQFVIHHYAGA--VCYATDGFCDKNKDHVHS-E 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 966 APRLLQDSqkkiiSNLFLgragSATVLSgsiagleggsqlalrratsmrktfttgmaavkkkslciQIKLQVDALIDTIK 1045
Cdd:cd14901 516 ALALLRTS-----SNAFL----SSTVVA--------------------------------------KFKVQLSSLLEVLN 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1046 RSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDpcEAGLLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMV 1125
Cdd:cd14901 549 ATEPHFIRC---------------------------IKPND--VLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1126 FSEFRRRFDVLAPHLTKKHGRNYIVVDEKRAVEELLESLDLEKSSCCLGLSRVF 1179
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
432-1138 |
5.51e-51 |
|
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: 193.75 E-value: 5.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 511
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLaTIAGTSGTKVfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 589
Cdd:cd01385 82 SGSGKTESTNFLLHHL-TALSQKGYGS-GVEQ-TILGAgpVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 590 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 669
Cdd:cd01385 159 YLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 670 EQKTCWLILASIYHLGaagatkeAAEAGRKQFARHEWAQKA--------AYLLGCSLEELSSAIF--KHQLKGGTLQRST 739
Cdd:cd01385 238 TQRQIFSVLSAVLHLG-------NIEYKKKAYHRDESVTVGnpevldiiSELLRVKEETLLEALTtkKTVTVGETLILPY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 740 SFrqgPEesglgegtklsALECLEGMASGLYSELFTLLISLVNRAL---KSSQHSLC-SMMIVDTPGFQNPEWGgsarga 815
Cdd:cd01385 311 KL---PE-----------AIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEAKGlSIGVLDIFGFEDFGNN------ 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 816 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLEPVadDSVAAVdqasHLVRSLAHadearGLLWLLEEEA 895
Cdd:cd01385 371 SFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGIS--WHNIEYT--DNTGCL----QLISKKPT-----GLLCLLDEES 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 896 LVPGATEDALLDRLFS-------YYGPQEgdkkgqspllrssKPRHFLLGHSHGTnwVEYNVAGW----LNYTKQNPATq 964
Cdd:cd01385 438 NFPGATNQTLLAKFKQqhkdnkyYEKPQV-------------MEPAFIIAHYAGK--VKYQIKDFreknLDLMRPDIVA- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 965 naprLLQDSQKKIISNL-----------------FLGRAGSATVLSGSIAGLEGGSQLALRRATSMRktfttGMAAVKKK 1027
Cdd:cd01385 502 ----VLRSSSSAFVRELigidpvavfrwavlrafFRAMAAFREAGRRRAQRTAGHSLTLHDRTTKSL-----LHLHKKKK 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1028 SLCIQIKLQV--DALIDTIKRSKMHFVHCFLPVAEGWPgeprsassrrvsssseldlppgdpceaglLQLDVSLLRAQLR 1105
Cdd:cd01385 573 PPSVSAQFQTslSKLMETLGQAEPFFIRCIKSNAEKKP-----------------------------LRFDDELVLRQLR 623
|
730 740 750
....*....|....*....|....*....|...
gi 600971660 1106 GSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1138
Cdd:cd01385 624 YTGMLETVRIRRSGYSVRYTFQEFITQFQVLLP 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
431-1136 |
5.11e-47 |
|
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: 181.38 E-value: 5.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRRE--------DMAPHIYAVAQTAYRAMLMSR 501
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPyKQIDNLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 502 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAG----------------TSGTKVFSVEKwQALST--LLEAFGNSPTIMNG 563
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssirATSKSTKSIEQ-KILSCnpILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 564 SATRFSQILSLDFD-QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL-NHLAENNVFgivPL 641
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLkNQLSGDRYD---YL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 642 SKPE----EKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAGRKQFARH-EWAQKAAYLLGC 716
Cdd:cd14907 237 KKSNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPCCVKNkETLQIIAKLLGI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 717 SLEELSSAIFKHQLKGGTlQRSTSfrqgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRAL-------- 785
Cdd:cd14907 317 DEEELKEALTTKIRKVGN-QVITS--------------PLSKKECinnRDSLSKELYDRLFNWLVERLNDTImpkdekdq 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 786 KSSQHSLCSMMIVDTPGFQNPEwggsarGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE-----LAFDDLEPV 860
Cdd:cd14907 382 QLFQNKYLSIGLLDIFGFEVFQ------NNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdylnqLSYTDNQDV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 861 ADdsvaAVDQashlvrslahadEARGLLWLLEEEALVPGATEDALLDRLFSYYGpqeGDKKGQSPllRSSKPRHFLLGHS 940
Cdd:cd14907 456 ID----LLDK------------PPIGIFNLLDDSCKLATGTDEKLLNKIKKQHK---NNSKLIFP--NKINKDTFTIRHT 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 941 HGTnwVEYNVAGWL--NYTKQNPATQNaprLLQDSQKKIISNLFLGRAGSATVLSGSIAGleggsqlalrratsmrktft 1018
Cdd:cd14907 515 AKE--VEYNIEGFRekNKDEISQSIIN---CIQNSKNRIISSIFSGEDGSQQQNQSKQKK-------------------- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1019 tgmAAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGwpgeprsassrrvsssseldlppgdpcEAGLLQLDVS 1098
Cdd:cd14907 570 ---SQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEK---------------------------KADLFIQGYV 619
|
730 740 750
....*....|....*....|....*....|....*...
gi 600971660 1099 LLraQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1136
Cdd:cd14907 620 LN--QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
432-1137 |
2.75e-45 |
|
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: 176.68 E-value: 2.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSekvMHMFkgcrREDM------APHIYAVAQTAYRAMLM----- 499
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPfKHIPGLYD---LHKY----REEMpgwtalPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 500 --SRQDQSIVLLGSSGSGKTTSFQHLVQYLA-----TIAGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQ 570
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskhTTATSSSKRRRAISGSELLSAnpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 571 ILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNvFGIVPLSKPE 645
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQE-FQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 646 EKQKAAQ---QFSKLQAAMKVLAISPEEQKTCWLILASIYHLG-----------------AAGATKEAAEAGRKQFARHE 705
Cdd:cd14895 234 QRNDGVRddkQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvassedegeedngAASAPCRLASASPSSLTVQQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 706 WAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrstsfrqgpEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRAL 785
Cdd:cd14895 314 HLDIVSKLFAVDQDELVSALTTRKISVG------------GETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 786 KSSQHSLCS-----------MMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 854
Cdd:cd14895 382 PQRQFALNPnkaankdttpcIAVLDIFGFEEFEVN------QFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 855 DDLEpvaDDSVA--AVDQASHLVRSLAhaDEargllwlleeEALVPGATEDALLDRLFSYYGpqegDKKGQSPLLRSSKP 932
Cdd:cd14895 456 VDYE---DNSVCleMLEQRPSGIFSLL--DE----------ECVVPKGSDAGFARKLYQRLQ----EHSNFSASRTDQAD 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 933 RHFLLGHSHGTnwVEYNVAGWLNYTKQNPaTQNAPRLLQDSQKKIISNLFlgragsaTVLSGSIAGLEGGSQLALRRATS 1012
Cdd:cd14895 517 VAFQIHHYAGA--VRYQAEGFCEKNKDQP-NAELFSVLGKTSDAHLRELF-------EFFKASESAELSLGQPKLRRRSS 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1013 MRKTFTTGMaavkkkslciQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGl 1092
Cdd:cd14895 587 VLSSVGIGS----------QFKQQLASLLDVVQQTQTHYIRC---------------------------IKPNDESASD- 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 600971660 1093 lQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1137
Cdd:cd14895 629 -QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
432-1145 |
4.74e-44 |
|
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: 171.64 E-value: 4.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF-------------KGcrREDMAPHIYAVAQTAYRAM 497
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfQKLPGLYSSDTMAKYllsfearssstrnKG--SDPMPPHIYQVAGEAYKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 498 LMSR----QDQSIVLLGSSGSGKTTSFQHLVQYLA---------TIAGTSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGS 564
Cdd:cd14900 80 MLGLngvmSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQT-NILLESFGNARTLRNDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 565 ATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDAtlrtelhlnhlaennvfgivplskp 644
Cdd:cd14900 159 SSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAI-GAS------------------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 645 eEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGaaGATKEAAEAGrkqfarHEWAQKAAYLLGCSLEELSSA 724
Cdd:cd14900 213 -EAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIG--NLTFEHDENS------DRLGQLKSDLAPSSIWSRDAA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 725 IFKHQLKGGTLQRSTS---FRQGPEESGLgegtKLSALEC---LEGMASGLYSELFTLLISLVNRALK-----SSQHSLC 793
Cdd:cd14900 284 ATLLSVDATKLEKALSvrrIRAGTDFVSM----KLSAAQAnnaRDALAKALYGRLFDWLVGKMNAFLKmddssKSHGGLH 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 794 SMMIVDTPGF----QNpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEpvadDSVA 866
Cdd:cd14900 360 FIGILDIFGFevfpKN----------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDwkyVEFCDNQ----DCVN 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 867 AVDQASHLVRSLahADEargllwlleeEALVPGATEDALLDRLFSyygpqegdKKGQSPLLRSSKPRH----FLLGHSHG 942
Cdd:cd14900 426 LISQRPTGILSL--IDE----------ECVMPKGSDTTLASKLYR--------ACGSHPRFSASRIQRarglFTIVHYAG 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 943 TnwVEYNVAGWLNytkqnpatQNAPRLLQDsqkkiISNLFLGragsatvlsgsiagleggsqlalrratsmrktfttgma 1022
Cdd:cd14900 486 H--VEYSTDGFLE--------KNKDVLHQE-----AVDLFVY-------------------------------------- 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1023 avkkkslCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrA 1102
Cdd:cd14900 513 -------GLQFKEQLTTLLETLQQTNPHYVRC---------------------------LKPNDLCKAGIYERERVL--N 556
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 600971660 1103 QLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL----APHLTKKHG 1145
Cdd:cd14900 557 QLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLarakNRLLAKKQG 603
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
483-851 |
6.22e-44 |
|
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: 171.38 E-value: 6.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 483 APHIYAVAQTAYRAMLMSR---QDQSIVLLGSSGSGKTTSFQHLVQYLAT-----IAGTSGTKVFSVEKWQALST----- 549
Cdd:cd14891 52 PPHPYAIAEMAYQQMCLGSgrmQNQSIVISGESGAGKTETSKIILRFLTTravggKKASGQDIEQSSKKRKLSVTslder 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 550 ------LLEAFGNSPTIMNGSATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLR 622
Cdd:cd14891 132 lmdtnpILESFGNAKTLRNHNSSRFGKFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 623 TELHlnhlaennvfgivpLSKPEEKQKAAQ-------------QFSKLQAAMKVLAISPEEQKTCWLILASIYHLG---- 685
Cdd:cd14891 212 KELL--------------LLSPEDFIYLNQsgcvsddniddaaNFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGnief 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 686 -----AAGATKEAAEAGRKQFArhewaqKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRqgpeesGLGEGTKLSALE 760
Cdd:cd14891 278 deedtSEGEAEIASESDKEALA------TAAELLGVDEEALEKVI---------TQREIVTR------GETFTIKRNARE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 761 CL---EGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEwggsaRGASFEELCHNYAQDRLQRLFHERT 837
Cdd:cd14891 337 AVysrDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFE-----TKNDFEQLLINYANEALQATFNQQV 411
|
410
....*....|....
gi 600971660 838 FLQELERYKEDNIE 851
Cdd:cd14891 412 FIAEQELYKSEGID 425
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
432-846 |
2.10e-43 |
|
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: 170.12 E-value: 2.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIAGTSGTKVFS--VEKwqalSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQ 588
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIEQriLEA----NPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 589 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENnvfgivplskpeekqkaAQQFSKLQAAMKVLAISP 668
Cdd:cd01382 158 HYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLDD-----------------VGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 669 EEQKTCWLILASIYHLG--AAGATKEAAEAGRKQFARHEWA-QKAAYLLGCSLEELSSAI---FKHQLKGGTlqRSTSFR 742
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGniEFEENGSDSGGGCNVKPKSEQSlEYAAELLGLDQDELRVSLttrVMQTTRGGA--KGTVIK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 743 QG--PEESGlgegtklSALECLegmASGLYSELFTLLISLVNRAL--KSSQHSLCsmmIVDTPGFQ----Npewggsarg 814
Cdd:cd01382 299 VPlkVEEAN-------NARDAL---AKAIYSKLFDHIVNRINQCIpfETSSYFIG---VLDIAGFEyfevN--------- 356
|
410 420 430
....*....|....*....|....*....|..
gi 600971660 815 aSFEELCHNYAQDRLQRLFHERTFLQELERYK 846
Cdd:cd01382 357 -SFEQFCINYCNEKLQQFFNERILKEEQELYE 387
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1232-1926 |
9.16e-42 |
|
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: 168.43 E-value: 9.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1232 NIKKNKGVKDWPWWKLFTTVRPLIQVQLSEEQIRNKDE-EIQQLRSKLEKVEKERNELrlssdrlETRISELTSELtder 1310
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESERQRAEL-------AEKLSKLQSEL---- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1311 ntgESASQLLDAETAERLRTEKEMKELQTQ-YDALKKQMEVMEMEVMEARLIRA--AEINGEVDDDDAGGEWRLKYERAV 1387
Cdd:pfam01576 443 ---ESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQleDERNSLQEQLEEEEEAKRNVERQL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1388 REVDF----TKKRLQQELEdKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE 1463
Cdd:pfam01576 520 STLQAqlsdMKKKLEEDAG-TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1464 LEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSqeSKDEA 1543
Cdd:pfam01576 599 LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVS--SKDDV 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1544 --SLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEV 1621
Cdd:pfam01576 677 gkNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1622 QLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLrKDLKRTKALLADAQIMLDHLKNN-----APSKREIAQL 1696
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV-KQLKKLQAQMKDLQRELEEARASrdeilAQSKESEKKL 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1697 KN------QLEESeftCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1770
Cdd:pfam01576 836 KNleaellQLQED---LAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL 912
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1771 KAAVAQ---------ASRDMAQMND-LQAQIEESNKekqELQEKLQALQSQVEFLEqsmvdKSLVSRQEAKIRELETRLE 1840
Cdd:pfam01576 913 RKSTLQveqlttelaAERSTSQKSEsARQQLERQNK---ELKAKLQEMEGTVKSKF-----KSSIAALEAKIAQLEEQLE 984
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1841 FEKTQ----VKRLENLASRLKETMEKLTEER---DQRAAAENREKEQNKRLQRQLRDTKEEMSelarkEAEASRKKheLE 1913
Cdd:pfam01576 985 QESRErqaaNKLVRRTEKKLKEVLLQVEDERrhaDQYKDQAEKGNSRMKQLKRQLEEAEEEAS-----RANAARRK--LQ 1057
|
730
....*....|...
gi 600971660 1914 MDLESLEAANQSL 1926
Cdd:pfam01576 1058 RELDDATESNESM 1070
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
432-1149 |
2.22e-39 |
|
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: 158.60 E-value: 2.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 509
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 510 GSSGSGKTTSFQHLVQYLATiagTSGTKVF----------SVEKWQALST-LLEAFGNSPTIMNGSATRFSQILSLDFDQ 578
Cdd:cd14906 82 GESGSGKTEASKTILQYLIN---TSSSNQQqnnnnnnnnnSIEKDILTSNpILEAFGNSRTTKNHNSSRFGKFLKIEFRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 579 A-GQVASASIQTMLLEKLRVARRP-ASEATFNVFYYLLACGDATLRTELHLNH--------LAENNVFGIV------PLS 642
Cdd:cd14906 159 SdGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNdpskyrylDARDDVISSFksqssnKNS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 643 KPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEA--AEAGRKQFARHEWAQKAAYLLGCSLEE 720
Cdd:cd14906 239 NHNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfSKYAYQKDKVTASLESVSKLLGYIESV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 721 LSSAIFKHQLKGGTlqRSTSFRQgPEESGLGEGTKlsaleclEGMASGLYSELFTLLISLVNR-----------ALKSSQ 789
Cdd:cd14906 319 FKQALLNRNLKAGG--RGSVYCR-PMEVAQSEQTR-------DALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 790 HSLCSMMIVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDlepvADDSVA 866
Cdd:cd14906 389 KNNLFIGVLDIFGFEN------LSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSnsnFID----NKECIE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 867 AVDQASHLVRSLAHaDEArgllwlleeeaLVPGATEDALLDRLFSYYgpqegdKKGQSPLLRSSKPRHFLLGHSHGTnwV 946
Cdd:cd14906 459 LIEKKSDGILSLLD-DEC-----------IMPKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGD--V 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 947 EYNVAGWLNYTKQNPATqNAPRLLQDSQKKIISNLFLGRAGSATvlsgsiagleggsqlalrrATSMRKTFTTGMAAvkk 1026
Cdd:cd14906 519 TYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT-------------------NTTKKQTQSNTVSG--- 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1027 kslciQIKLQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvssssELDLPPGDpceagllqLDVSLLRAQLRG 1106
Cdd:cd14906 576 -----QFLEQLNQLIQTINSTSVHYIRCIKP---------------------NQTMDCNN--------FNNVHVLSQLRN 621
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 600971660 1107 SRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYI 1149
Cdd:cd14906 622 VGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPK 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
431-1137 |
1.25e-38 |
|
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: 155.36 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMF---KGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIV 507
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 508 LLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSveKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDF-DQAGQVASAS 586
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDS--RFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 587 IQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVfgiVPLSKPEEKQKAA-----QQFSKLQAAM 661
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRY---LNQTMREDVSTAErslnrEKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 662 KVLAISPEEQKTCWLILASIYHLGAAGATKeAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFK--HQLKGGTLQRST 739
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTA-LTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTdiQYFKGDMIIRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 740 SFRQGPEESGLgegtklsaleclegMASGLYSELFTLLISLVNRALKsSQHSLCSMM-----IVDTPGFQNpewggsARG 814
Cdd:cd14878 315 TIQIAEFYRDL--------------LAKSLYSRLFSFLVNTVNCCLQ-SQDEQKSMQtldigILDIFGFEE------FQK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 815 ASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE-------------LAFDDLEPVADDSVaaVDQASHLVRSLAHA 881
Cdd:cd14878 374 NEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTmetayspgnqtgvLDFFFQKPSGFLSL--LDEESQMIWSVEPN 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 882 DEARgllwlleeealVPGATEDALLDRLFSYYGPQEGD--KKGQSPLlrsskprhFLLGHSHGTnwVEYNVAGWLNYTKq 959
Cdd:cd14878 452 LPKK-----------LQSLLESSNTNAVYSPMKDGNGNvaLKDQGTA--------FTVMHYAGR--VMYEIVGAIEKNK- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 960 NPATQNAPRLLQDSQKKIISNLFlgRAGSATVlsgsiaglegGSQLalrratsmrktfttgmaavkKKSLC-IQIKLQvd 1038
Cdd:cd14878 510 DSLSQNLLFVMKTSENVVINHLF--QSKLVTI----------ASQL--------------------RKSLAdIIGKLQ-- 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1039 alidtikRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQ 1118
Cdd:cd14878 556 -------KCTPHFIHCIKPNNSKLPD-----------------------------TFDNFYVSAQLQYIGVLEMVKIFRY 599
|
730
....*....|....*....
gi 600971660 1119 GYPDHMVFSEFRRRFDVLA 1137
Cdd:cd14878 600 GYPVRLSFSDFLSRYKPLA 618
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
434-1181 |
2.27e-37 |
|
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: 152.50 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 434 LHTLRQRYGA--------SLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQS 505
Cdd:cd14887 4 LENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 506 IVLLGSSGSGKTTSFQHLVQYLATI------AGTSGTKvfsvEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQA 579
Cdd:cd14887 84 ILISGESGAGKTETSKHVLTYLAAVsdrrhgADSQGLE----ARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 580 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLlaCGDATLRTELHlnhlaennvfgivplSKPEEKQKAAQQFSKLQA 659
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYAL--CNAAVAAATQK---------------SSAGEGDPESTDLRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 660 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAGRKQFARH-------EWAQKAAYLLgcSLEELSSAIFKHQLKG 732
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceETAADRSHSS--EVKCLSSGLKVTEASR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 733 GTLQRSTSFRQGPEESGLGEGTKLS-----------------ALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSM 795
Cdd:cd14887 301 KHLKTVARLLGLPPGVEGEEMLRLAlvsrsvretrsffdldgAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSESD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 796 MIVDTP--------------GFQNPEWGGSARgasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL-----AFDD 856
Cdd:cd14887 381 SDEDTPsttgtqtigildlfGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQnqdcsAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 857 LEPVADDSVAAVDQASHLvrSLAHADEARGLLWLLEEEALVPGATEDALLdrlfsyygpqegdkkgQSPLLRSSKPRHFL 936
Cdd:cd14887 458 SFPLASTLTSSPSSTSPF--SPTPSFRSSSAFATSPSLPSSLSSLSSSLS----------------SSPPVWEGRDNSDL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 937 LGHShgtnwVEYNVAGWLNYTKQNPAtqnaprlLQDSQKKIISNLFLGRA---------GSATVLSGSIAGLEGGSQLAL 1007
Cdd:cd14887 520 FYEK-----LNKNIINSAKYKNITPA-------LSRENLEFTVSHFACDVtydardfcrANREATSDELERLFLACSTYT 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1008 RRATSMRKTFTTGMAAvKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGwpgeprsassrrvsssseldlppgdp 1087
Cdd:cd14887 588 RLVGSKKNSGVRAISS-RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQ-------------------------- 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1088 cEAGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHgrnyivVDEKRAVEELLESLDLE 1167
Cdd:cd14887 641 -EAGI--FEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREA------LTPKMFCKIVLMFLEIN 711
|
810
....*....|....
gi 600971660 1168 KSSCCLGLSRVFFR 1181
Cdd:cd14887 712 SNSYTFGKTKIFFR 725
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
431-854 |
1.28e-36 |
|
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: 149.23 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQ--DQSI 506
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPfKPVPQLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 507 VLLGSSGSGKTTSFQHLVQYLATIAG--TSGTKVFSVEKWQAL----STLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 580
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAspTSWESHKIAERIEQRilnsNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 581 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnHLAENNVFGIVPLSkpeEKQKAAQQFSKLQAA 660
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQW---HLPEGAAFSWLPNP---ERNLEEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 661 MKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAGRKQFA--RHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRs 738
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMddTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQ- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 739 tSFRQgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQN-PEwggsar 813
Cdd:cd14880 314 -VFKK-----------PCSRAECdtrRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIgLLDVYGFESfPE------ 375
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 600971660 814 gASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 854
Cdd:cd14880 376 -NSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSF 415
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
432-854 |
1.90e-36 |
|
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: 148.90 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFK--GCRRE-------DMAPHIYAVAQTAYRAMLM-SR 501
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiespqALGPHVFAIADRSYRQMMSeIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 502 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL---------LEAFGNSPTIMNGSATRFSQIL 572
Cdd:cd14908 82 ASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSIMdrvlqsnpiLEAFGNARTLRNDNSSRFGKFI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 573 SLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGivplskPEEKQKAAQ 652
Cdd:cd14908 162 ELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQL------PNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 653 -------------QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAG--ATKEAAEAGRKQFARHEWAQKAAYLLGCS 717
Cdd:cd14908 236 ggapdlreftdedGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEfeSKEEDGAAEIAEEGNEKCLARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 718 LEELSSAIFKHQLKGGTLQRSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALK--SSQHSLCSM 795
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKL------------TPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRSSV 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 796 MIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 854
Cdd:cd14908 384 GVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAF 436
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
432-1140 |
6.22e-36 |
|
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: 146.20 E-value: 6.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGpsLLVLSTRGAPAVYSEKVMHMFKGCRREdMAPHIYAVAQTAYRAMLMSrQDQSIVLLGS 511
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSG--LVFLALNPYETIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 512 SGSGKTTSFQHLVQYLatIAGTSGTKvfSVEK-WQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDqaGQVASASIQTM 590
Cdd:cd14898 78 SGSGKTENAKLVIKYL--VERTASTT--SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 591 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSkpeekqkaaQQFSKLQAAMKVLAI-SPE 669
Cdd:cd14898 152 LLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFIDTSSTAGNKESIVQLS---------EKYKMTCSAMKSLGIaNFK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 670 EQKTCwliLASIYHLGAAGATKEaaeaGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QLKGGTLQRSTSFRQgpee 747
Cdd:cd14898 223 SIEDC---LLGILYLGSIQFVND----GILKLQRNESFTEFCKLHNIQEEDFEESLVKFsiQVKGETIEVFNTLKQ---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 748 sglgegtklsALECLEGMASGLYSELFTLLISLVNRALK-SSQHSLCsmmIVDTPGFQNPEWGGsargasFEELCHNYAQ 826
Cdd:cd14898 292 ----------ARTIRNSMARLLYSNVFNYITASINNCLEgSGERSIS---VLDIFGFEIFESNG------LDQLCINWTN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 827 DRLQRLFHERTFLQELERYKEDNIElaFDDLEPVADDSVaavdqashlvrsLAHADEARGLLWLLEEEALVPGATEDALL 906
Cdd:cd14898 353 EKIQNDFIKKMFRAKQGMYKEEGIE--WPDVEFFDNNQC------------IRDFEKPCGLMDLISEESFNAWGNVKNLL 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 907 DRLFSYYGPQEGDKKGQSPLLrsskprhfllghSHGTNWVEYNVAGWLNYTKQNpatqnaprllqdSQKKIISNLFLGRA 986
Cdd:cd14898 419 VKIKKYLNGFINTKARDKIKV------------SHYAGDVEYDLRDFLDKNREK------------GQLLIFKNLLINDE 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 987 GSatvlsgsiagleggsqlalrratsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPgep 1066
Cdd:cd14898 475 GS-------------------------------------KEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRP--- 514
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1067 rsassrrvsssseldlppgdpceaglLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHL 1140
Cdd:cd14898 515 --------------------------WCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
431-1133 |
2.21e-35 |
|
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: 146.01 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF----------KGCRREDMAPHIYAVAQTAYRAMLM 499
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPfQDLPQLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 500 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW-------------QALST--LLEAFGNSPTIMNGS 564
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESIsppaspsrttieeQVLQSnpILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 565 ATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLA----CGDATLRTELHLNHLAEN-NVFGI 638
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSadnnCVSKEQKQVLALSGGPQSfRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 639 VPLSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAA-----------GATKEAAEAGRKQFARHEWA 707
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVdfeqiphkgddTVFADEARVMSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 708 QKAAYLLGCSLEELSSAIFKHQLKGGtlqrSTSFRQGPEESGLGEGTKLSALEClegmasglYSELFTLLISLVNRALK- 786
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHAS----NETLVVGVDVAHARNTRNALTMEC--------YRLLFEWLVARVNNKLQr 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 787 --------------SSQHSLCSMMIVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL 852
Cdd:cd14899 389 qasapwgadesdvdDEEDATDFIGLLDIFGFED------MAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 853 AFDDLEpvadDSVAAVDQASHlvrslahadEARGLLWLLEEEALVPGATEDALLDRlfsYYgpQEGDKKGQSPLLRSS-- 930
Cdd:cd14899 463 SFVDFP----NNRACLELFEH---------RPIGIFSLTDQECVFPQGTDRALVAK---YY--LEFEKKNSHPHFRSApl 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 931 --KPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLflgRAGSATVLSGSIAGLEGGSQLALR 1008
Cdd:cd14899 525 iqRTTQFVVAHYAGC--VTYTIDGFLAKNK-DSFCESAAQLLAGSSNPLIQAL---AAGSNDEDANGDSELDGFGGRTRR 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1009 RATSmrktfttgmaAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPC 1088
Cdd:cd14899 599 RAKS----------AIAAVSVGTQFKIQLNELLSTVRATTPRYVRC---------------------------IKPNDSH 641
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 600971660 1089 EAGLLQldVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRF 1133
Cdd:cd14899 642 VGSLFQ--STRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
397-1237 |
1.02e-34 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 144.79 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 397 DGAILDVDEDDIEKANAP-SCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFK 475
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 476 GCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTKVFSVEK--WQAlSTLLE 552
Cdd:PTZ00014 155 DAKDsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA--SSKSGNMDLKIQNaiMAA-NPVLE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 553 AFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAE 632
Cdd:PTZ00014 232 AFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 633 NNVfgIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG-------AAGATKEAAEAGRKQFarhE 705
Cdd:PTZ00014 312 YKY--INPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGnveiegkEEGGLTDAAAISDESL---E 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 706 WAQKAAYLLGCSLEELS-SAIFKHQLKGGTLQRStsfRQGPEESglgEGTKLSaleclegMASGLYSELFTLLISLVNRA 784
Cdd:PTZ00014 387 VFNEACELLFLDYESLKkELTVKVTYAGNQKIEG---PWSKDES---EMLKDS-------LSKAVYEKLFLWIIRNLNAT 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 785 LKSSQHSLCSMMIVDTPGFQ----NpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDL 857
Cdd:PTZ00014 454 IEPPGGFKVFIGMLDIFGFEvfknN----------SLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteELEYTSN 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 858 EPVAD------DSVAAV--DQashlvrSLAhadeargllwlleeealvPGATEDALLDRLFSYYGPQEGDKKGqspllRS 929
Cdd:PTZ00014 524 ESVIDllcgkgKSVLSIleDQ------CLA------------------PGGTDEKFVSSCNTNLKNNPKYKPA-----KV 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 930 SKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGragsATVLSGSIAgleggsqlalrr 1009
Cdd:PTZ00014 575 DSNKNFVIKHTIGD--IQYCASGFLFKNK-DVLRPELVEVVKASPNPLVRDLFEG----VEVEKGKLA------------ 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1010 atsmrktfttgmaavKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvssssELDLPPGDPCE 1089
Cdd:PTZ00014 636 ---------------KGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKP---------------------NENKKPLDWNS 679
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1090 AGLLqldvsllrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGrnyivVDEKRAVEELLESLDLEKS 1169
Cdd:PTZ00014 680 SKVL--------IQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSS-----LDPKEKAEKLLERSGLPKD 746
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1170 SCCLGLSRVFFR---AGTLARLEEQRDEQTSRHLTLFQAACRGYLARQHFKKRkIQDLAIrcVQKNIKKNK 1237
Cdd:PTZ00014 747 SYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKN-IKSLVR--IQAHLRRHL 814
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
431-1139 |
1.13e-31 |
|
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: 134.71 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRRE----------DMAPHIYAVAQTAYRAMLMS 500
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 501 RQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALS----------TLLEAFGNSPTIMNGSATRFSQ 570
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHpigqqilhafTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 571 ILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAC--GDATLRTELHLNHLAENnvFGIVPLSKPEEKQ 648
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKCVNE--FVMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 649 KA--AQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAG-----ATKEAAEAGRKQFARHEWA----QKAAYLLGCS 717
Cdd:cd14893 239 FAldARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDfvpdpEGGKSVGGANSTTVSDAQScalkDPAQILLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 718 LEELSSAIFKHQLKggtLQRSTSFRQGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVN--------RALKS-- 787
Cdd:cd14893 319 LLEVEPVVLDNYFR---TRQFFSKDGNKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNgilggifdRYEKSni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 788 ---SQhslcSMMIVDTPGFQNPEwggsARGASFEELCHNYAQDRLQRLFHERTfLQELERYKEDNIELAFDDLepvADDS 864
Cdd:cd14893 396 vinSQ----GVHVLDMVGFENLT----PSQNSFDQLCFNYWSEKVHHFYVQNT-LAINFSFLEDESQQVENRL---TVNS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 865 VAAVDQASHLVRSLAHaDEARGLLWLLEEEALVPGATEDALLDRLFS-------YYGPQEGDKKGQSPLLRSSKPR-HFL 936
Cdd:cd14893 464 NVDITSEQEKCLQLFE-DKPFGIFDLLTENCKVRLPNDEDFVNKLFSgneavggLSRPNMGADTTNEYLAPSKDWRlLFI 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 937 LGHSHGTnwVEYNVAGwlnYTKQNPATQNA--PRLLQDSQkkiisNLFLGRAGSATVLSGSIAglEGGSQLALRRATS-- 1012
Cdd:cd14893 543 VQHHCGK--VTYNGKG---LSSKNMLSISStcAAIMQSSK-----NAVLHAVGAAQMAAASSE--KAAKQTEERGSTSsk 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1013 MRKTFTTGMAAVK-KKSLCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAG 1091
Cdd:cd14893 611 FRKSASSARESKNiTDSAATDVYNQADALLHALNHTGKNFLVC---------------------------IKPNETLEEG 663
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 600971660 1092 LlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1139
Cdd:cd14893 664 V--FDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH 709
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
432-850 |
2.47e-31 |
|
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: 132.56 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKvMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQE-FHAKYRCKsRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLATIA-GTSGTkvfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 589
Cdd:cd14882 81 ESYSGKTTNARLLIKHLCYLGdGNRGA----TGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 590 MLLEKLRVARRPASEATFNVFYYLLACGDATLRteLHLNHLAENNVFGIVPLSKPEEKQKA----------AQQFSKLQA 659
Cdd:cd14882 157 YQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNR--LKEYNLKAGRNYRYLRIPPEVPPSKLkyrrddpegnVERYKEFEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 660 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEAAEAgrkQFARHEWAQKAAYLLGCSLEELSSAIFKHQL-KGGTLQRS 738
Cdd:cd14882 235 ILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGYA---ELENTEIASRVAELLRLDEKKFMWALTNYCLiKGGSAERR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 739 tsfRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVN------RALKSSQHSLcsmMIVDTPGFQNPEWGGsa 812
Cdd:cd14882 312 ---KHTTEE----------ARDARDVLASTLYSRLVDWIINRINmkmsfpRAVFGDKYSI---SIHDMFGFECFHRNR-- 373
|
410 420 430
....*....|....*....|....*....|....*...
gi 600971660 813 rgasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI 850
Cdd:cd14882 374 ----LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDI 407
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1271-1945 |
3.70e-30 |
|
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: 130.96 E-value: 3.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1271 IQQLRSKLEKVEKERNELRLSSDRLETRISELTSE---LTDERNTGESASQLL----DAETAERLR----TEKEMKELQT 1339
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerLRREREKAERYQALLkekrEYEGYELLKekeaLERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1340 QYDALKKQMEVMEMEVME------ARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTK-KRLQQELEDKMEVEQQSR 1412
Cdd:TIGR02169 245 QLASLEEELEKLTEEISElekrleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1413 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKL 1492
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1493 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEEL----DE 1568
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrveKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1569 QAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDE------------EVEEARQSCQK-----KLKQMEVQLEE------ 1625
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgtvaqlgSVGERYATAIEvaagnRLNNVVVEDDAvakeai 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1626 EYEDKQKA----------LREKRELESKLST------------------------LSDQVNQRDFESEKRL--------- 1662
Cdd:TIGR02169 565 ELLKRRKAgratflplnkMRDERRDLSILSEdgvigfavdlvefdpkyepafkyvFGDTLVVEDIEAARRLmgkyrmvtl 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1663 ------------------RKDLKRTKALLADAQIMLDHLKNnapSKREIAQLKNQLEESEftcaaavKARKAMEVEMEDL 1724
Cdd:TIGR02169 645 egelfeksgamtggsrapRGGILFSRSEPAELQRLRERLEG---LKRELSSLQSELRRIE-------NRLDELSQELSDA 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1725 HLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESnkEKQELQEK 1804
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1805 LQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRL 1884
Cdd:TIGR02169 793 IPEIQAELSKLEEE------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1885 QRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1945
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1395-1974 |
1.13e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 129.29 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1395 KRLQQELED-KMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1473
Cdd:COG1196 216 RELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1474 ELSQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR 1553
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLE-------ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1554 DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMEsRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKA 1633
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1634 LREKRELESKLSTLSDQVnqrdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESeftcAAAVKA 1713
Cdd:COG1196 448 AEEEAELEEEEEALLELL--------AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG----VKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1714 RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQReknEIQNRLEEDQEDMNELMKKHKAAVA-------QASRDMAQMND 1786
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ---NIVVEDDEVAAAAIEYLKAAKAGRAtflpldkIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1787 LQAQIEESNKEKQELQEKLQALQSQveFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEE 1866
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYV--LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1867 RDQRAAAENREKEQNKRLQRQLRDTKEEmsELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAfkrigDLQAAIED 1946
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEA--LLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE-----ELLEELLE 743
|
570 580
....*....|....*....|....*...
gi 600971660 1947 EMESDENEDLINSEGDSDVDsELEDRVD 1974
Cdd:COG1196 744 EEELLEEEALEELPEPPDLE-ELERELE 770
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
433-851 |
1.20e-29 |
|
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: 127.70 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 433 VLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRRE-----DMAPHIYAVAQTAYRAMLMSRQDQSI 506
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfKQIRNLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 507 VLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVekwqALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 584
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSL----ILGSnpLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 585 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF-GIVPLSKPE-EKQKaaqQFSKLQAAMK 662
Cdd:cd14886 159 GKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLnASKCYDAPGiDDQK---EFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 663 VLaISPEEQKTCWLILASIYHLG--------AAGATKEAAEAGRKQFarhewaQKAAYLLGCSLEELSSAIfkhqlkggt 734
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGniefseegDMGVINAAKISNDEDF------GKMCELLGIESSKAAQAI--------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 735 LQRSTSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsarg 814
Cdd:cd14886 300 ITKVVVINNETIISPV---TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN----- 371
|
410 420 430
....*....|....*....|....*....|....*..
gi 600971660 815 aSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE 851
Cdd:cd14886 372 -TYEQLLINYANERLQQYFINQVFKSEIQEYEIEGID 407
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1269-1946 |
3.82e-29 |
|
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: 127.60 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1269 EEI-QQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDErntgESASQLLDAEtaeRLRTEKEMKELQTQYDALKKQ 1347
Cdd:pfam01576 74 EEIlHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE----EAARQKLQLE---KVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1348 MEVMEMEVMEARLiRAAEINGEVDDDDAG----GEWRLKYERAVREVDftkKRLQQELEDKMEVEQqSRRQLERRLGDLQ 1423
Cdd:pfam01576 147 NSKLSKERKLLEE-RISEFTSNLAEEEEKakslSKLKNKHEAMISDLE---ERLKKEEKGRQELEK-AKRKLEGESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1424 ADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEA 1503
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1504 FSLKQQMEEkdldiagfTQKVVSLEAELQdissqeSKDEASLAKVKK-----------QLRDLEAKVKDQEEELDEQags 1572
Cdd:pfam01576 302 EALKTELED--------TLDTTAAQQELR------SKREQEVTELKKaleeetrsheaQLQEMRQKHTQALEELTEQ--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1573 iqmLEQAKlRLEMEMERMRQTHSKEMESRDEEV---EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLS- 1648
Cdd:pfam01576 365 ---LEQAK-RNKANLEKAKQALESENAELQAELrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQs 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1649 --DQVNQRDFESEK---RLRKDLKRTKALLADAQIML-------------------------DHLKNNAPSKREI----- 1693
Cdd:pfam01576 441 elESVSSLLNEAEGkniKLSKDVSSLESQLQDTQELLqeetrqklnlstrlrqledernslqEQLEEEEEAKRNVerqls 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1694 ------AQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQRE----------KNEIQNRLE 1757
Cdd:pfam01576 521 tlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElddllvdldhQRQLVSNLE 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1758 EDQEDMNELMKKHKAAVAQAS--RDMAQMN---------DLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM--VDKSL 1824
Cdd:pfam01576 601 KKQKKFDQMLAEEKAISARYAeeRDRAEAEareketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKddVGKNV 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1825 VSRQEAKiRELETRLEFEKTQVKRL-------ENLASRLKETME--KLTEERDQRAAAENREkEQNKRLQRQLRDTKEEM 1895
Cdd:pfam01576 681 HELERSK-RALEQQVEEMKTQLEELedelqatEDAKLRLEVNMQalKAQFERDLQARDEQGE-EKRRQLVKQVRELEAEL 758
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1896 SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED 1946
Cdd:pfam01576 759 EDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD 809
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
484-1143 |
1.03e-28 |
|
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: 124.54 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 484 PHIYAVAQTAYRAMLM-SRQDQSIVLLGSSGSGKTTSFQHLVQYLA---------TIAGTSGTKVFSVEKWQalSTLLEA 553
Cdd:cd14875 56 PHIWQVAHKAFNAIFVqGLGNQSVVISGESGSGKTENAKMLIAYLGqlsymhssnTSQRSIADKIDENLKWS--NPVMES 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 554 FGNSPTIMNGSATRFSQILSLDFDQA-GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDAT-------LRTEL 625
Cdd:cd14875 134 FGNARTVRNDNSSRFGKYIKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEekkelggLKTAQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 626 HLNHLAENNVF---GI--VPLSKPEEkqkaaqqFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEaaeagrkQ 700
Cdd:cd14875 214 DYKCLNGGNTFvrrGVdgKTLDDAHE-------FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESD-------Q 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 701 FARHEWAQKAAYLLGCSLEELSSAifkhQLKGGTLQRS-----TSFRQGPEESGLgegtklsalecLEGMASGLYSELFT 775
Cdd:cd14875 280 NDKAQIADETPFLTACRLLQLDPA----KLRECFLVKSktslvTILANKTEAEGF-----------RNAFCKAIYVGLFD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 776 LLISLVNRALKSSQH-SLCSMM-IVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE-- 851
Cdd:cd14875 345 RLVEFVNASITPQGDcSGCKYIgLLDIFGFEN------FTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQip 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 852 -LAFDDlepvADDSVAAVDQASHLVRSLahADEargllwlleeEALVPGATEDALLDRLFSYYGpqegdkkGQSPLL--- 927
Cdd:cd14875 419 kIEFPD----NSECVNMFDQKRTGIFSM--LDE----------ECNFKGGTTERFTTNLWDQWA-------NKSPYFvlp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 928 RSSKPRHFllGHSHGTNWVEYNVAGWLNytKQNPA-TQNAPRLLQDSQKKIISNLFLGRAGSAtvlsgsiagleggsqla 1006
Cdd:cd14875 476 KSTIPNQF--GVNHYAAFVNYNTDEWLE--KNTDAlKEDMYECVSNSTDEFIRTLLSTEKGLA----------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1007 lRRatsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgd 1086
Cdd:cd14875 535 -RR----------------KQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPS---------------------- 575
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1087 pceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKK 1143
Cdd:cd14875 576 -------FLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTAS 625
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1280-1959 |
7.69e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.12 E-value: 7.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1280 KVEKERNELRLSS--DRLEtRISELTSELtdERNTGESASQlldAETAERLRtekemkELQTQYDALKKQMEVMEMEVME 1357
Cdd:COG1196 171 KERKEEAERKLEAteENLE-RLEDILGEL--ERQLEPLERQ---AEKAERYR------ELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1358 ARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQ-QELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQL 1436
Cdd:COG1196 239 AELEELEAELEELEAELE----ELEAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1437 KKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLD 1516
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1517 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSK 1596
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1597 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLrkdlkrtkALLADA 1676
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL--------EAALAA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1677 QIMLDHLKNNAPSKREIAQLK-NQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR 1755
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1756 LEEDQEDM-NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvSRQEAKIRE 1834
Cdd:COG1196 627 LVAARLEAaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA------------ERLAEEELE 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1835 LETRLEFEKTQVKRLEnlasrlketmekltEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEM 1914
Cdd:COG1196 695 LEEALLAEEEEERELA--------------EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1915 DLESLEAANQSLQADLklafKRIGDL-QAAIE--DEME------SDENEDLINS 1959
Cdd:COG1196 761 DLEELERELERLEREI----EALGPVnLLAIEeyEELEerydflSEQREDLEEA 810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1255-1961 |
3.12e-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: 121.32 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1255 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldaetAERLRTEKEM 1334
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--------------LEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1335 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQ------ELEDKMEVE 1408
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeleSLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1409 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdSELSQAHEETQREKLQ 1488
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI----EELLKKLEEAELKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1489 R--EKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQeskdEASLAKVKKQLRDLEAKVKDQEEEL 1566
Cdd:TIGR02168 440 AelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR----LDSLERLQENLEGFSEGVKALLKNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1567 DEQAGSIQMLEQ-----AKLRLEMEM---ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR 1638
Cdd:TIGR02168 516 SGLSGILGVLSElisvdEGYEAAIEAalgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1639 ELESKLSTLSDQVnqrdfESEKRLRKDLkrtKALLA------DAQIMLDHLKNNAPS----------------------- 1689
Cdd:TIGR02168 596 NIEGFLGVAKDLV-----KFDPKLRKAL---SYLLGgvlvvdDLDNALELAKKLRPGyrivtldgdlvrpggvitggsak 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1690 --------KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE 1761
Cdd:TIGR02168 668 tnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1762 DMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKS-LVSRQEAKIRELETRLE 1840
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRaELTLLNEEAANLRERLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1841 FEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLE 1920
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 600971660 1921 AANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINSEG 1961
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEY 949
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
432-870 |
3.39e-27 |
|
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: 120.01 E-value: 3.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF-------KGCRREDMAPHIYAVAQTAYRAMLMSRQD 503
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPyKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 504 QSIVLLGSSGSGKTTSFQHLVQYLATIAGTSgTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQ----- 578
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTDS-QMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 579 ----AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLL-ACGDATLRT-----ELHLNHLAENNVFGIVPLSK----- 643
Cdd:cd14884 161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLrGLSDEDLARrnlvrNCGVYGLLNPDESHQKRSVKgtlrl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 644 --------PEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAgATKEAAEagrkqfarhewaqkaayLLG 715
Cdd:cd14884 241 gsdsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNR-AYKAAAE-----------------CLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 716 CSLEELssaifKHQLKGGTLQ-RSTSFRQgpeesglgEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCS 794
Cdd:cd14884 303 IEEEDL-----ENVIKYKNIRvSHEVIRT--------ERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDES 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 795 M------------MIVDTPGFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIeLAFDDLEPVAD 862
Cdd:cd14884 370 DnediysineaiiSILDIYGFE------ELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCSDVAPSYS 442
|
....*...
gi 600971660 863 DSVAAVDQ 870
Cdd:cd14884 443 DTLIFIAK 450
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
431-1138 |
9.89e-27 |
|
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: 118.05 E-value: 9.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVmhmFKGCrredmapHIYAVAQTAYRAML-MSRQDQSIVLL 509
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLV---IKKC-------HISGVAENALDRIKsMSSNAESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 510 GSSGSGKTTSFQHLVQYLATIAGTSGTKVFSvekwQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 589
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHS----SAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 590 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLaeNNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 669
Cdd:cd14874 147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 670 EQKTCWLILASIYHLG--------AAGATKEAAEAGrkQFARHEWaqkAAYLLGCSLEELSSAIFKHQLKGGTLQRStsf 741
Cdd:cd14874 225 HCISIYKIISTILHIGniyfrtkrNPNVEQDVVEIG--NMSEVKW---VAFLLEVDFDQLVNFLLPKSEDGTTIDLN--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 742 rqgpeesglgegtklSALECLEGMASGLYSELFTLLISLVNRALKSSQHSlCSMMIVDTPGFQNPEWGGsargasFEELC 821
Cdd:cd14874 297 ---------------AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHT-GVISILDHYGFEKYNNNG------VEEFL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 822 HNYAQDRLQRLFHERTFLQELERYKEDNIELafddlepvaDDSVAAVDQASHLVRSLAHADEarGLLWLLEEEALVPGAT 901
Cdd:cd14874 355 INSVNERIENLFVKHSFHDQLVDYAKDGISV---------DYKVPNSIENGKTVELLFKKPY--GLLPLLTDECKFPKGS 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 902 EDALLDRL------FSYYGPQegdkkgqspllRSSKPRHFLLGHSHGTNWveYNVAGWLNYTKQNpATQNAPRLLQDSQK 975
Cdd:cd14874 424 HESYLEHCnlnhtdRSSYGKA-----------RNKERLEFGVRHCIGTTW--YNVTDFFSRNKRI-ISLSAVQLLRSSKN 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 976 KIISNLFLGRAGSATVLSGSIAgleggsQLALRRATSmrktfttgmaavkkkslciqiklqvdaLIDTIKRSKMHFVHCF 1055
Cdd:cd14874 490 PIIGLLFESYSSNTSDMIVSQA------QFILRGAQE---------------------------IADKINGSHAHFVRCI 536
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1056 LPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1135
Cdd:cd14874 537 KSNNERQPK-----------------------------KFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
...
gi 600971660 1136 LAP 1138
Cdd:cd14874 588 LLP 590
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1255-1947 |
1.07e-26 |
|
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: 119.51 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1255 IQVQLSE--EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLD--AETAERLRT 1330
Cdd:pfam01576 227 LQAQIAElrAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRdlGEELEALKT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1331 EKEmkelQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgEWRLKYERAVRE--------------VDFTKKR 1396
Cdd:pfam01576 307 ELE----DTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQ-EMRQKHTQALEElteqleqakrnkanLEKAKQA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1397 LQQELED-----------KMEVEQQsRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELE 1465
Cdd:pfam01576 382 LESENAElqaelrtlqqaKQDSEHK-RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1466 KKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1545
Cdd:pfam01576 461 KDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1546 AKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME--RMRQTHSKEMESRDEEVeearqscQKKLKQMevqL 1623
Cdd:pfam01576 541 EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDdlLVDLDHQRQLVSNLEKK-------QKKFDQM---L 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1624 EEE-------YEDKQKALREKRELESKLSTLSdqvnqRDFESEKRLRKDLKRT-KALLADAQIML---DHLKNNA----P 1688
Cdd:pfam01576 611 AEEkaisaryAEERDRAEAEAREKETRALSLA-----RALEEALEAKEELERTnKQLRAEMEDLVsskDDVGKNVheleR 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1689 SKR----EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID-DIAKAKTALEEQLSRLQREKNEIQNRLEEDQedm 1763
Cdd:pfam01576 686 SKRaleqQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFErDLQARDEQGEEKRRQLVKQVRELEAELEDER--- 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1764 nelmKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLeQSMVDKSLVSRQEAKIRELETRlefek 1843
Cdd:pfam01576 763 ----KQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-QRELEEARASRDEILAQSKESE----- 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1844 tqvKRLENLASRLKETMEKLteerdqrAAAEnrekeqnkrlqRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAan 1923
Cdd:pfam01576 833 ---KKLKNLEAELLQLQEDL-------AASE-----------RARRQAQQERDELADEIASGASGKSALQDEKRRLEA-- 889
|
730 740
....*....|....*....|....
gi 600971660 1924 qslqadlklafkRIGDLQAAIEDE 1947
Cdd:pfam01576 890 ------------RIAQLEEELEEE 901
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
433-1057 |
1.23e-26 |
|
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: 118.17 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 433 VLHTLRQRYGASLLHTYAGPSLLVLST---------------RGAPAVysekvmhmfkgcrrEDMAPHIYAVAQTAYRAM 497
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirkyRDAPDL--------------TKLPPHVFYTARRALENL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 498 LMSRQDQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTKVFSVEKW-QALSTLLEAFGNSPTIMNGSATRFSQILSLDF 576
Cdd:cd14876 69 HGVNKSQTIIVSGESGAGKTEATKQIMRYFA--SAKSGNMDLRIQTAiMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 577 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENN--------VFGIVPLskpeekq 648
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKflnpkcldVPGIDDV------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 649 kaaQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH 728
Cdd:cd14876 220 ---ADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK-TEQGVDDAAAISNESLEVFKEACSLLFLDPEALKR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 729 QL------KGGtlQRSTSFRQGPEesglGEGTKLSaleclegMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPG 802
Cdd:cd14876 296 ELtvkvtkAGG--QEIEGRWTKDD----AEMLKLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 803 F---QNpewggsargASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDLEPVAD------DSVAAV-- 868
Cdd:cd14876 363 FevfKN---------NSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIptaELEYTSNAEVIDvlcgkgKSVLSIle 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 869 DQAshlvrsLAhadeargllwlleeealvPGATEDALLDRLFSyygpQEGDKKGQSPLLRSSKpRHFLLGHSHGTnwVEY 948
Cdd:cd14876 434 DQC------LA------------------PGGSDEKFVSACVS----KLKSNGKFKPAKVDSN-INFIVVHTIGD--IQY 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 949 NVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGragsATVLSGSIA-GLEGGSQLalrratsMRktfttgmaavkkk 1027
Cdd:cd14876 483 NAEGFLFKNK-DVLRAELVEVVQASTNPVVKALFEG----VVVEKGKIAkGSLIGSQF-------LK------------- 537
|
650 660 670
....*....|....*....|....*....|
gi 600971660 1028 slciqiklQVDALIDTIKRSKMHFVHCFLP 1057
Cdd:cd14876 538 --------QLESLMGLINSTEPHFIRCIKP 559
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1261-1954 |
2.38e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 118.62 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1261 EEQIRNKDEEIQQLRSKLEKVEKERNELR-----LSSD--RLETRISELTSELTDERNTGESASQLLDAETAERLRTEKE 1333
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQkelyaLANEisRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1334 MKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAggewrlkYERAVREVDftkkrlqqELEDKMEVEQQSRR 1413
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVA--------QLELQIASLNNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1414 QLERRLGDLQADSDESQRALQQLKKKCQRltAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQ 1493
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1494 REKDMLLAEAFSLKQQMEEKDldiaGFTQKVVSLEAE----------LQDISSQESKDEASLAKVkkqlrdLEAKVKDQE 1563
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLE----GFSEGVKALLKNqsglsgilgvLSELISVDEGYEAAIEAA------LGGRLQAVV 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1564 EELDEQAGS-IQMLEQAKLRLEMEMErMRQTHSKEMESRDEEVEEARQSCQKKLKQMeVQLEEEY--------------E 1628
Cdd:TIGR02168 552 VENLNAAKKaIAFLKQNELGRVTFLP-LDSIKGTEIQGNDREILKNIEGFLGVAKDL-VKFDPKLrkalsyllggvlvvD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1629 DKQKALREKRELESKLS--TL--------------SDQVNQRDFESE---KRLRKDLKRTKALLADAQIMLDHLKNNAPS 1689
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRivTLdgdlvrpggvitggSAKTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEE 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1690 KR-EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMk 1768
Cdd:TIGR02168 710 LEeELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE- 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1769 khkaavAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKS-LVSRQEAKIRELETRLEFEKTQVK 1847
Cdd:TIGR02168 789 ------AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErRLEDLEEQIEELSEDIESLAAEIE 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1848 RLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQ 1927
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
730 740
....*....|....*....|....*..
gi 600971660 1928 ADLKLAFKRIGDLQAAIEDEMESDENE 1954
Cdd:TIGR02168 943 ERLSEEYSLTLEEAEALENKIEDDEEE 969
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1259-1977 |
7.09e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 117.55 E-value: 7.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1259 LSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRL--ETRISELTSELTDERNTgESASQLLDAETAERLRTEKEMKE 1336
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaeDARKAEEARKAEDAKRV-EIARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1337 LQTQYDALKKQMEVMEMEVMEARLIRAAEingevddddaggewRLKYERAVREVdftkkrlqQELEDKMEVEQqSRRQLE 1416
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAAR--------------KAEEERKAEEA--------RKAEDAKKAEA-VKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1417 RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK--QRRFDSELSQAHEETQREKLQREKLQR 1494
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1495 EKdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-AKVKDQEEELDEQAGSI 1573
Cdd:PTZ00121 1315 KK----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1574 QMLEQAKLRLEMEMERMRQTHSKEMESRdeEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQ 1653
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1654 RDFESEKRLRKDLKR----TKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCA-AAVKARKAMEVEMEDLHLQI 1728
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKkadeAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkKAEEAKKADEAKKAEEKKKA 1548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1729 DDIAKA---KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL 1805
Cdd:PTZ00121 1549 DELKKAeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1806 QALQSQVEFLEQSMVDKSlvsRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQ 1885
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEK---KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1886 R-------------QLRDTKEE----MSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEM 1948
Cdd:PTZ00121 1706 ElkkkeaeekkkaeELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
730 740 750
....*....|....*....|....*....|
gi 600971660 1949 -ESDENEDLINSEGDSDVDSELEDRVDGVK 1977
Cdd:PTZ00121 1786 dEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1399-1970 |
2.12e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 115.54 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1399 QELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQA 1478
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1479 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEA--------------S 1544
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqletlrskvaqlelQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1545 LAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMEsrdEEVEEARQSCQKKLKQMEVQLE 1624
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL---EELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1625 EEYEDKQKALREKRELESKLSTLSDQVNQRDFESE--------------------KRLRKDLKRTKALLADAQIMLDHL- 1683
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkallknqsglsgilgvlsELISVDEGYEAAIEAALGGRLQAVv 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1684 -KNNAPSKREIAQLK-------------------------NQLEESEFTCAAAV-------KARKAM------------- 1717
Cdd:TIGR02168 552 vENLNAAKKAIAFLKqnelgrvtflpldsikgteiqgndrEILKNIEGFLGVAKdlvkfdpKLRKALsyllggvlvvddl 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1718 --------------------------------------------EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ 1753
Cdd:TIGR02168 632 dnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1754 NRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV-DKSLVSRQEAKI 1832
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAeAEAEIEELEAQI 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1833 RELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHEL 1912
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 1913 EMDLESLEAANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINSEGDSDVDSELE 1970
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRElESKRSELRRELEELREKLAQLELR 930
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1265-1959 |
7.36e-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: 113.62 E-value: 7.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1265 RNKDEEIQQLRSKLEKVE------------KERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAE-RLRTE 1331
Cdd:TIGR02169 207 REKAERYQALLKEKREYEgyellkekealeRQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1332 KEMKELQTQYDALKKQMEVMEMEVMEA--RLIRAAE--INGEVDDDDAGGEWRlKYERAVREVDFTKKRLQQELEDKmev 1407
Cdd:TIGR02169 287 EEQLRVKEKIGELEAEIASLERSIAEKerELEDAEErlAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAEL--- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1408 eQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhLEGQQVRnheLEKKQRRFDSELSQAHEETQREKL 1487
Cdd:TIGR02169 363 -KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE----LKRELDR---LQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1488 QREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKV---KDQEE 1564
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVrggRAVEE 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1565 ELD------------------------EQAGS-----------------IQMLEQAKL-RLE-MEMERMRQTHS-KEMES 1600
Cdd:TIGR02169 515 VLKasiqgvhgtvaqlgsvgeryataiEVAAGnrlnnvvveddavakeaIELLKRRKAgRATfLPLNKMRDERRdLSILS 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1601 RD------------------------------EEVEEAR----------------------------------------- 1609
Cdd:TIGR02169 595 EDgvigfavdlvefdpkyepafkyvfgdtlvvEDIEAARrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepa 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1610 --QSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEkRLRKDLKRTKALLADAQIMLDHLKNN- 1686
Cdd:TIGR02169 675 elQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEi 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1687 APSKREIAQLKNQLEESEftcAAAVKARKAME-VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNE 1765
Cdd:TIGR02169 754 ENVKSELKELEARIEELE---EDLHKLEEALNdLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1766 LMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKT 1844
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlKKERDELEAQLRELERKIEELEA 910
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1845 QVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRDTKEEMSELARKEAEASRKKhELEMDLESLEAANQ 1924
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEAL--------------EEELSEIEDPKGEDEEIPEEELSLEDVQAELQ-RVEEEIRALEPVNM 975
|
810 820 830
....*....|....*....|....*....|....*.
gi 600971660 1925 SLQADLKLAFKRIGDLQAAIED-EMESDENEDLINS 1959
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAKlEEERKAILERIEE 1011
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1256-1901 |
2.60e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.61 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1256 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLD----AETAERL-RT 1330
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelKELQAELeEL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1331 EKEMKELQTQYDALKKQMEVMEMEVMEARLIR------AAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRL---QQEL 1401
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALdaaereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgiLGVL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1402 EDKMEVEQQSRRQLERRLG-DLQA----DSDESQRALQQLKK--------------KCQRLTAELQDTKLHLEGQQVRNH 1462
Cdd:TIGR02168 526 SELISVDEGYEAAIEAALGgRLQAvvveNLNAAKKAIAFLKQnelgrvtflpldsiKGTEIQGNDREILKNIEGFLGVAK 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1463 ELEKKQRRFDSELS------------QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAE 1530
Cdd:TIGR02168 606 DLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEK 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1531 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERmrqtHSKEMESRDEEVEEArq 1610
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTEL-- 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1611 scQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSK 1690
Cdd:TIGR02168 760 --EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1691 -REIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1769
Cdd:TIGR02168 837 eRRLEDLEEQIEELS-------EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1770 HKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQsQVEFleqsMVDKSLVSRQEAKIRELETRLEFEKTQVKRL 1849
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY-SLTL----EEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1850 E--NLASrlketMEKLTEERdQRAAAENREKEQNKRLQRQLRDTKEEMSELARK 1901
Cdd:TIGR02168 985 GpvNLAA-----IEEYEELK-ERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
431-850 |
5.33e-23 |
|
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: 106.25 E-value: 5.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 431 SSVLHTLRQRYGASLLHTYAGPSLLVLStrgaPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISIN----PYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLatIAGTSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 590
Cdd:cd14937 77 ESGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDS-NFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 591 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISpEE 670
Cdd:cd14937 154 LLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIR--SENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMH-DM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 671 QKTCWLILASIYHLG-------AAGATKEAAEAGRKQFarhEWAQKAAYLLGCSLEELSSAIfkhqlkggTLQRSTSFRQ 743
Cdd:cd14937 231 KDDLFLTLSGLLLLGnveyqeiEKGGKTNCSELDKNNL---ELVNEISNLLGINYENLKDCL--------VFTEKTIANQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 744 GPEesglgegTKLSALECL---EGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQnpewggSARGASFEEL 820
Cdd:cd14937 300 KIE-------IPLSVEESVsicKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFE------IFSKNSLEQL 366
|
410 420 430
....*....|....*....|....*....|
gi 600971660 821 CHNYAQDRLQRLFHERTFLQELERYKEDNI 850
Cdd:cd14937 367 LINIANEEIHSIYLYIVYEKETELYKAEDI 396
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1181-1964 |
6.17e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 107.92 E-value: 6.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1181 RAGTLARLEEQRDEQTSRHLTLF---QAACRGYLARQHFKKRKIQDlAIRCVQ----KNIKKNKGVKDWPWWKLFTTVRP 1253
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIArkaEDARKAEEARKAEDAKKAEA-ARKAEEvrkaEELRKAEDARKAEAARKAEEERK 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1254 LIQVQLSEEQIR----NKDEEIQQLRSKLEKVEKERNE---LRLSSDRLETRISELTSELTDERNTGESASQLLDAETAE 1326
Cdd:PTZ00121 1214 AEEARKAEDAKKaeavKKAEEAKKDAEEAKKAEEERNNeeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1327 RLRTEKEMKELqtqyDALKKQMEVMEMEVMEARliRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKME 1406
Cdd:PTZ00121 1294 EAKKAEEKKKA----DEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1407 VEQQSRRQLERRLGDLQADSDESQRAlQQLKKKCQrltaelQDTKlhlEGQQVRNHELEKKQRrfdSELSQAHEETQREK 1486
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAE------EDKK---KADELKKAAAAKKKA---DEAKKKAEEKKKAD 1434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1487 LQREKLQREKdmllaEAFSLKQQMEEKDldiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEEL 1566
Cdd:PTZ00121 1435 EAKKKAEEAK-----KADEAKKKAEEAK-------------KAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEA 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1567 DEQAGSIQMLEQAKLRLEmEMERMRQTHSKEMESRDEE---VEEARQSCQKKlKQMEVQLEEEY---EDKQKALREKREL 1640
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEakkADEAKKAEEKK-KADELKKAEELkkaEEKKKAEEAKKAE 1573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1641 ESKLSTL-----SDQVNQRDFESEKRLRKDLKRTKALLA----DAQIMLDHLKNNAPSKREIAQLKNQLEES-------- 1703
Cdd:PTZ00121 1574 EDKNMALrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaeelk 1653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1704 ----EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTalEEQLSRLQREK---NEIQNRLEEDQEDMNELMKKHKAAVAQ 1776
Cdd:PTZ00121 1654 kaeeENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--AEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1777 ASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLAS-- 1854
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANii 1811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1855 --------RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSL 1926
Cdd:PTZ00121 1812 eggkegnlVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
810 820 830
....*....|....*....|....*....|....*...
gi 600971660 1927 QADLKlafkrigDLQAAIEDEMESDENEDLINSEGDSD 1964
Cdd:PTZ00121 1892 KIDKD-------DIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1398-1983 |
1.40e-22 |
|
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: 105.49 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1398 QQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQR--RFDSEL 1475
Cdd:TIGR04523 35 EKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN---------DKLKKNKDKinKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1476 SQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKdeaslakVKKQLRDL 1555
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELN-------KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1556 EAKVKDQEEELDEQAGSIQMLEQAKLRLEMEM---ERMRQTHsKEMESRDEEVEEARQSCQKKLKQmevqLEEEYEDKQK 1632
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKN-KSLESQISELKKQNNQLKDNIEK----KQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1633 ALREKrelESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESeftCAAAVK 1712
Cdd:TIGR04523 247 EISNT---QTQLNQLKDE-QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS------EISDLNNQKEQD---WNKELK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1713 AR-KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKN-------EIQNRLEEDQEDMnELMKKHKAAVAQASRDM-AQ 1783
Cdd:TIGR04523 314 SElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTnsesensEKQRELEEKQNEI-EKLKKENQSYKQEIKNLeSQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1784 MNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQ--------------EAKIRELETRLEFEKTQVKR 1848
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlKETIIKNnseikdltnqdsvkELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1849 LENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQA 1928
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1929 DLKLAF--KRIGDLQAAIEDEMESDENEDLINSEGDSDVDsELEDRVDGVKSWLSKN 1983
Cdd:TIGR04523 553 ELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELID-QKEKEKKDLIKEIEEK 608
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1185-1870 |
3.66e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1185 LARLEEQRdEQTSRHLTLfQAACRGYLARQHFKKRKIQDLAIRCVQKNIKKNKgvkdwpwwklfttvrplIQVQLSEEQI 1264
Cdd:COG1196 202 LEPLERQA-EKAERYREL-KEELKELEAELLLLKLRELEAELEELEAELEELE-----------------AELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1265 RNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDAL 1344
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1345 KKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREvdftkkrlQQELEDKMEVEQQSRRQLERRLGDLQA 1424
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE--------LLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1425 DSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAF 1504
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1505 SLKQQMEEKDLDIAGftqkvvSLEAELQDISSQESKDEASLAKVKKQLRD-----LEAKVKDQEEELDEQAGS-IQMLEQ 1578
Cdd:COG1196 495 LLLEAEADYEGFLEG------VKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaaLAAALQNIVVEDDEVAAAaIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1579 AKL--RLEMEMERMRQTHSKEMESRDEEVEEARqscqkklkqmevqLEEEYEDKQKALREKRELESKLSTLSDQvnqrdf 1656
Cdd:COG1196 569 AKAgrATFLPLDKIRARAALAAALARGAIGAAV-------------DLVASDLREADARYYVLGDTLLGRTLVA------ 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1657 eseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaaVKARKAMEVEMEDLHLQIDDIAKAKT 1736
Cdd:COG1196 630 ---ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL------LEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1737 ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLE 1816
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1817 QsmVDksLVSRQEAKirELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQR 1870
Cdd:COG1196 781 P--VN--LLAIEEYE--ELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1377-1945 |
3.98e-22 |
|
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: 104.49 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1377 GEWRLKYERAVREVDFTKKRLQQELE-----DKMEVEQQSRRQ-LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDT 1450
Cdd:pfam01576 29 KELEKKHQQLCEEKNALQEQLQAETElcaeaEEMRARLAARKQeLEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1451 KLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMllaeafslkqqmeekdldiagftqkvvsLEAE 1530
Cdd:pfam01576 109 EEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL----------------------------LEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1531 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSkEMESRDEEVEEARQ 1610
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA-ELQAQIAELRAQLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1611 SCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLsdqvnQRDFESEKRLRKDLKRTK-----ALLADAQIMLDHLKN 1685
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISEL-----QEDLESERAARNKAEKQRrdlgeELEALKTELEDTLDT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1686 NAP-----SKR--EIAQLKNQLEESEFTCAAAVKA-RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLE 1757
Cdd:pfam01576 315 TAAqqelrSKReqEVTELKKALEEETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1758 EDQEDMNELMKKHKAAvaqasrdMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLeqsmvdKSLVSRQEAKIRELEt 1837
Cdd:pfam01576 395 TLQQAKQDSEHKRKKL-------EGQLQELQARLSESERQRAELAEKLSKLQSELESV------SSLLNEAEGKNIKLS- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1838 rlefektqvKRLENLASRLKETMEKLTEERDQRAAAENR----EKEQNKrLQRQLRDTKE-------EMSELARKEAEAS 1906
Cdd:pfam01576 461 ---------KDVSSLESQLQDTQELLQEETRQKLNLSTRlrqlEDERNS-LQEQLEEEEEakrnverQLSTLQAQLSDMK 530
|
570 580 590
....*....|....*....|....*....|....*....
gi 600971660 1907 RKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1945
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1256-1885 |
6.45e-22 |
|
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: 103.56 E-value: 6.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1256 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMK 1335
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1336 ELQTQYDALKKQMEVMEMEVMEARLIRAaEINgevddddaggewrlKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQL 1415
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKSLES-QIS--------------ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1416 E----------RRLGDLQADSDESQRALQQLKKKCQRLTAELQDtkLHLEGQQVRNHEL-------EKKQRRFDSELSQA 1478
Cdd:TIGR04523 256 NqlkdeqnkikKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELkselknqEKKLEEIQNQISQN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1479 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAK 1558
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEK--------------QNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1559 VKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHS------KEMESRDEEVEEARQSCQKKLKQMEVQLEE---EYED 1629
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVlsrSINK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1630 KQKALREK-RELESKLSTLsDQVNQRDFESEKRLrKDLKRTKALLADAQIMLDHLKNNapSKREIAQLKNQLEESEFTca 1708
Cdd:TIGR04523 480 IKQNLEQKqKELKSKEKEL-KKLNEEKKELEEKV-KDLTKKISSLKEKIEKLESEKKE--KESKISDLEDELNKDDFE-- 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1709 aavkarkamevemedlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQ 1788
Cdd:TIGR04523 554 -----------------LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1789 AQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA--KIRELETRL-EFEKTQVKRLENLASRLKET 1859
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVkqiketIKEIRNKWPEIikKIKESKTKIdDIIELMKDWLKELSLHYKKY 696
|
650 660
....*....|....*....|....*...
gi 600971660 1860 MEKLTEERDQRAAAENRE--KEQNKRLQ 1885
Cdd:TIGR04523 697 ITRMIRIKDLPKLEEKYKeiEKELKKLD 724
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1382-1904 |
2.04e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 102.06 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1382 KYERAVREVDFTKKRLQqELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN 1461
Cdd:PRK03918 225 KLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1462 HELEKKQR--RFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFtQKVVSLEAELQDISSQES 1539
Cdd:PRK03918 304 EYLDELREieKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1540 kdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSK----EMESRDEEVEEARQSCQKK 1615
Cdd:PRK03918 383 --GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1616 LKQMEVQLEEEYEDKQKALREKRELESKLstlsdqvnqrdfESEKRLRKDLKrtkalladaqiMLDHLKN--NAPSKREI 1693
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVL------------KKESELIKLKE-----------LAEQLKEleEKLKKYNL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1694 AQLKNQLEESEFTCAAAVKARKAMEVEMEDLHlQIDDIAKAKTALEEQLSRLQREKNEIQNRL--------EEDQEDMNE 1765
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1766 LMKKH------KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLvSRQEAKIRELETRL 1839
Cdd:PRK03918 597 LEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY-EELREEYLELSREL 675
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1840 EFEKTQVKRLENLASRLKETMEKLTEERDQRAAAE------NREKEQNKRLQRQLRDTKEEMSELARKEAE 1904
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKkeleklEKALERVEELREKVKKYKALLKERALSKVG 746
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1252-1970 |
3.84e-21 |
|
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: 101.59 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1252 RPLIQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTseLTDERNTGESASQLLDAETAERLRTE 1331
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL--YLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1332 KEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQS 1411
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1412 RRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREK 1491
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1492 LQREKDMLLAEAFSL--KQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1569
Cdd:pfam02463 414 ARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1570 AG--SIQMLEQAKLRLEMEMERMRQTHSKEM----------------------------ESRDEEVEEARQSCQK---KL 1616
Cdd:pfam02463 494 KLeeRSQKESKARSGLKVLLALIKDGVGGRIisahgrlgdlgvavenykvaistaviveVSATADEVEERQKLVRaltEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1617 KQMEVQLEEEYEDKQKALREKRELESKLST-------------------------LSDQVNQRDFESEKRLRKDLKRTKA 1671
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILnlaqldkatleadeddkrakvvegiLKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1672 LLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNE 1751
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1752 IQ-----NRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVS 1826
Cdd:pfam02463 734 INeelklLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEE 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1827 RQEAKIRELETRLEfEKTQVKRLENLASRLKETM--EKLTEERDQRAAAENREKEQNKRLQRQLRDTKEE--MSELARKE 1902
Cdd:pfam02463 814 AELLEEEQLLIEQE-EKIKEEELEELALELKEEQklEKLAEEELERLEEEITKEELLQELLLKEEELEEQklKDELESKE 892
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 1903 AEASRKKHELEMDLESLEAAN-QSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSELE 1970
Cdd:pfam02463 893 EKEKEEKKELEEESQKLNLLEeKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1528-1971 |
1.40e-20 |
|
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: 99.48 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1528 EAELQDISSQESKDEASLAKVKKQLRDLEAKVkdqeEELDEQAGSIQMLEQAKLRLEMEMERMRQTHS----------KE 1597
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKH----QQLCEEKNALQEQLQAETELCAEAEEMRARLAarkqeleeilHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1598 MESRDEEVEEARQSCQ---KKLKQ----MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTK 1670
Cdd:pfam01576 80 LESRLEEEEERSQQLQnekKKMQQhiqdLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLE-DQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1671 ALLADAQI----------MLDHLKNNAPSKreIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE 1740
Cdd:pfam01576 159 ERISEFTSnlaeeeekakSLSKLKNKHEAM--ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1741 QLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVE-FLEQSM 1819
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1820 VDKSLVSRQEAKIRELETRLEFE-KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSEL 1898
Cdd:pfam01576 317 AQQELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTL 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1899 ARKEAEASRKKHELEMDLESLEA-ANQSLQADLKLAfKRIGDLQAAIED---EMESDENEDLINSEGDSDVDSELED 1971
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQArLSESERQRAELA-EKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQD 472
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
432-877 |
4.46e-20 |
|
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: 97.09 E-value: 4.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 510
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPlRYLPFLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 511 SSGSGKTTSFQHLVQYLAT--IAGTSGTKVFSVEKwqalSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQ 588
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTtdLSRSKYLRDYILES----GIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 589 TMLLEKLRVARRPASEATFNVFYYLLAcgdatlrtelhlnhlaennvfGIVplskpeEKQKAAQQFSKLQaamkvlaisp 668
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLK---------------------GIT------DEEKAAYQLGDIN---------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 669 eeqktcwlilaSIYHLGAAGATKEAAEAGRKQFARhewaQKAAYLLGCSLEELSSAIFK-------------HQLKGGTL 735
Cdd:cd14905 199 -----------SYHYLNQGGSISVESIDDNRVFDR----LKMSFVFFDFPSEKIDLIFKtlsfiiilgnvtfFQKNGKTE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 736 QRSTSFRQGPEESGLGEGTKL-------------SALECLEGMASGLYSELFTLLISLVNRALKSSQHSLcSMMIVDTPG 802
Cdd:cd14905 264 VKDRTLIESLSHNITFDSTKLenilisdrsmpvnEAVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 803 FQNPEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI----ELAFDDLE---PVADDSVAAVDQASHLV 875
Cdd:cd14905 343 QESSQLNG------YEQFSINFLEERLQQIYLQTVLKQEQREYQTERIpwmtPISFKDNEesvEMMEKIINLLDQESKNI 416
|
..
gi 600971660 876 RS 877
Cdd:cd14905 417 NS 418
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1361-1946 |
5.89e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 97.44 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1361 IRAAEINGEVDDDDA---------GGEwrlKYERA-------VREVDFTKKRLQQELEDKMEVEQQSRRQlERRLGDLQA 1424
Cdd:PRK03918 132 IRQGEIDAILESDESrekvvrqilGLD---DYENAyknlgevIKEIKRRIERLEKFIKRTENIEELIKEK-EKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1425 DSDESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRRFDSELSQAhEETQREKLQREKLQREKDMLLA 1501
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIREL-EERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1502 EAfslkQQMEEKDLDIAGFTQKVVSleaELQDISSQESKDEASLAKVKKQLRDLE---AKVKDQEEELDEQAGSIQMLEQ 1578
Cdd:PRK03918 287 EL----KEKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1579 AKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQrdFES 1658
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKL----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE--LKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1659 EKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQidDIAKAKTAL 1738
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR---KELRELEKVLKKESELIKLK--ELAEQLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1739 EEQLSRLQREKNEiqnRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS 1818
Cdd:PRK03918 509 EEKLKKYNLEELE---KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1819 MVDKSlvsrqEAKIRELET---RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQ---------- 1885
Cdd:PRK03918 586 SVEEL-----EERLKELEPfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEelekkyseee 660
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1886 -RQLRDTKEEMS-ELARKEAE---ASRKKHELEMDLESLEAAnqslQADLKLAFKRIGDLQAAIED 1946
Cdd:PRK03918 661 yEELREEYLELSrELAGLRAEleeLEKRREEIKKTLEKLKEE----LEEREKAKKELEKLEKALER 722
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1254-1894 |
6.23e-20 |
|
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: 97.35 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1254 LIQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLE-----TRISELTSELTDERNTGESASQLLDAETAERl 1328
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1329 rtekeMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgeWRLKYERAVREVDFTKKrLQQELEDKMEVE 1408
Cdd:TIGR00618 324 -----AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS--IREISCQQHTLTQHIHT-LQQQKTTLTQKL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1409 QQSRRQLE--RRLGDLQADSDESQRALQQlkkkcqrltaelqdTKLHLEGQQVRNHELEKKQRRFDSElsQAHEETQREK 1486
Cdd:TIGR00618 396 QSLCKELDilQREQATIDTRTSAFRDLQG--------------QLAHAKKQQELQQRYAELCAAAITC--TAQCEKLEKI 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1487 LQREKLQ--REKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISS---QESKDEASLAKVKKQLRDLEAKVKD 1561
Cdd:TIGR00618 460 HLQESAQslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnPARQDIDNPGPLTRRMQRGEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1562 QEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRD---EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR 1638
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNrskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1639 ELESKLSTLSDQVNQRDFESEKRLRK-DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAM 1717
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1718 EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKE 1797
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1798 KQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQvKRLENLASRLKETMEKLTEERDQRAAAENRE 1877
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-QEEEQFLSRLEEKSATLGEITHQLLKYEECS 858
|
650
....*....|....*..
gi 600971660 1878 KEQNKRLQRQLRDTKEE 1894
Cdd:TIGR00618 859 KQLAQLTQEQAKIIQLS 875
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
462-580 |
1.10e-19 |
|
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: 88.17 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 462 APAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTK---- 537
Cdd:cd01363 11 LPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgete 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 600971660 538 ---------VFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 580
Cdd:cd01363 91 gwvylteitVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1480-1950 |
1.13e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 96.29 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1480 EETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftQKVVSLEAELQD-ISSQESKDEASLAKVKK---QLRDL 1555
Cdd:PRK03918 148 EKVVRQILGLDDYENAYKNLGEVIKEIKRRIERL--------EKFIKRTENIEElIKEKEKELEEVLREINEissELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1556 EAKVKDQE---EELDEQAGSIQMLEQAKLRLEMEM----ERMRQTHS--KEMESRDEEVEEARqscqKKLKQMEvQLEEE 1626
Cdd:PRK03918 220 REELEKLEkevKELEELKEEIEELEKELESLEGSKrkleEKIRELEEriEELKKEIEELEEKV----KELKELK-EKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1627 YED----KQKALREKRELESKLSTLSDQVN--QRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQL 1700
Cdd:PRK03918 295 YIKlsefYEEYLDELREIEKRLSRLEEEINgiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1701 EEseftcaaaVKARKAMEvEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmKKHKAAVAQASRD 1780
Cdd:PRK03918 375 ER--------LKKRLTGL-TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL-KKAKGKCPVCGRE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1781 MAQ------MNDLQAQIEESNKEKQELQEKLQALqsqvefleqsmvdkslvsrqEAKIRELETRLEFEKTqVKRLENLAS 1854
Cdd:PRK03918 445 LTEehrkelLEEYTAELKRIEKELKEIEEKERKL--------------------RKELRELEKVLKKESE-LIKLKELAE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1855 RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRdtkeemSELARKEAEASRKKhELEMDLESLEAANQSLQADLKLAF 1934
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK------GEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELL 576
|
490
....*....|....*.
gi 600971660 1935 KRIGDLQAAIEDEMES 1950
Cdd:PRK03918 577 KELEELGFESVEELEE 592
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1262-1920 |
2.10e-19 |
|
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: 95.09 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1262 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESasqlLDAET---AERLRTEKEMK-EL 1337
Cdd:TIGR04523 47 NELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK----LNSDLskiNSEIKNDKEQKnKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1338 QTQYDALKKQMEVMEMEVmearliraAEINGEV-DDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ------Q 1410
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNI--------DKFLTEIkKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKnidkikN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1411 SRRQLERRLGDLQAdsdesqralqqLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFdSELSQAHEETQrEKLQRE 1490
Cdd:TIGR04523 195 KLLKLELLLSNLKK-----------KIQKNKSLESQISELK---KQNNQLKDNIEKKQQEI-NEKTTEISNTQ-TQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1491 KLQREKDmllaeafslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKVKDQEEE 1565
Cdd:TIGR04523 259 KDEQNKI---------KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1566 LDEQAGSIQMLEQAKLRLEMEmermRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLS 1645
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1646 TLSDQVNQRD-----FESEKRLRkdLKRTKALLADaqimldhlknNAPSKREIAQLKNQLEESEftcaaavkarkameve 1720
Cdd:TIGR04523 402 NQEKLNQQKDeqikkLQQEKELL--EKEIERLKET----------IIKNNSEIKDLTNQDSVKE---------------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1721 medlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASrdmaqmnDLQAQIEESNKEKQE 1800
Cdd:TIGR04523 454 -----LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK-------ELEEKVKDLTKKISS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1801 LQEKLQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFE--KTQVKRLENLASRLKETMEKLTEERDQ-RAAAENRE 1877
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDL------EDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEkQELIDQKE 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1878 KEQNK-------------RLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLE 1920
Cdd:TIGR04523 596 KEKKDlikeieekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1516-1906 |
7.79e-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: 93.98 E-value: 7.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1516 DIAG---FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEELDEQAGSIQMLEQAKLRLEMEmermrq 1592
Cdd:TIGR02169 161 EIAGvaeFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR-REREKAERYQALLKEKREYEGYELLKEKE------ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1593 thskEMESRDEEVEEARQSCQKKLKQMEVQLEEeyedkqkalREKR--ELESKLSTLSDQVNQRDFESEKRLRKDLKRTK 1670
Cdd:TIGR02169 234 ----ALERQKEAIERQLASLEEELEKLTEEISE---------LEKRleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1671 ALLADAQimldhlknnapskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKN 1750
Cdd:TIGR02169 301 AEIASLE-------------RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1751 EIQNRLEEDQEDMNELMKKHKAAVaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKslvsrqEA 1830
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYR-------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI------EA 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1831 KIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRaaaenreKEQNKRLQRQLRDTKeemSELARKEAEAS 1906
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQ---RELAEAEAQAR 500
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1261-1969 |
3.29e-18 |
|
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: 91.72 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1261 EEQIRNKDEEIQQLRSKL----EKVEKERNELRLSSDRLETRISELTSE---LTDERNTgESASQ----------LLDAE 1323
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLnesnELHEKQKFYLRQSVIDLQTKLQEMQMErdaMADIRRR-ESQSQedlrnqlqntVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1324 TAERLRtEKEMKELQTQYDALKKQMEVMEMEVMEARLIRaaeingeVDDDDAGGEWRLKYERA----VREVDFTKKRLQQ 1399
Cdd:pfam15921 156 AAKCLK-EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL-------VDFEEASGKKIYEHDSMstmhFRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1400 ELEDKMEVEQQSRRQLERRLGDLQADS-DESQRALQQLKKKCQRLTAE--LQDTKLHLEGQQVRNhELEKKQRRFDSELS 1476
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSESqNKIELLLQQHQDRIEQLISEheVEITGLTEKASSARS-QANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1477 QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE 1556
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1557 AKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVeearQSCQKKLKQMEVQLEEEYEDKQKALRE 1636
Cdd:pfam15921 384 ADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLR----RELDDRNMEV----QRLEALLKAMKSECQGQMERQMAAIQG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1637 KRELESKLSTLSDQVnqrdfESEKRLrkdLKRTKALLADAQIMLDHlknnapSKREIAQLKNQLEESE----FTCAAAVK 1712
Cdd:pfam15921 456 KNESLEKVSSLTAQL-----ESTKEM---LRKVVEELTAKKMTLES------SERTVSDLTASLQEKEraieATNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1713 ARKAMEVEMEDL-HLQIDDIAKAKTALEEQLSRLQ-REKNEIQNRLEEDQEDMNELmkkhkaaVAQASRDMAQMNDLQAQ 1790
Cdd:pfam15921 522 LRSRVDLKLQELqHLKNEGDHLRNVQTECEALKLQmAEKDKVIEILRQQIENMTQL-------VGQHGRTAGAMQVEKAQ 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1791 IE-ESNKEKQELQEKlqalqsqvefleqsmvdKSLVSRQEAKIRELETR---LEFEKTqvkRLENLASRLKETMEKLTEE 1866
Cdd:pfam15921 595 LEkEINDRRLELQEF-----------------KILKDKKDAKIRELEARvsdLELEKV---KLVNAGSERLRAVKDIKQE 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1867 RDQ-------RAAAENREKEQNKRLQRQLRDTKEEMSELARK-EAEASRKKHELEM---DLESLEAAN-------QSLQA 1928
Cdd:pfam15921 655 RDQllnevktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQtrnTLKSMEGSDghamkvaMGMQK 734
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 600971660 1929 DLKLAFKRIGDLQAAI---EDEMESDENEDLINSEGDSDVDSEL 1969
Cdd:pfam15921 735 QITAKRGQIDALQSKIqflEEAMTNANKEKHFLKEEKNKLSQEL 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1261-1932 |
4.71e-18 |
|
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: 90.94 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1261 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSE---LTDERNTGESASQLLD---AETAERL-RTEKE 1333
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdLIKENNATRHLCNLLKetcARSAEKTkKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1334 MKELQTQYDALKKQMEvmemevmeaRLIRAAEiNGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKmevEQQSRR 1413
Cdd:pfam05483 178 REETRQVYMDLNNNIE---------KMILAFE-ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK---EKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1414 QL------ERRLGDLQADSDESQRALQQLKKKcqrltAELQDTKLHlegqqvrnhELEKKQRRFDSELSQAHEETQREKL 1487
Cdd:pfam05483 245 LLiqitekENKMKDLTFLLEESRDKANQLEEK-----TKLQDENLK---------ELIEKKDHLTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1488 QREKLQREKDMLLAEAFSLKQ----QMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1563
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEekeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1564 EELDEQAG-----SIQMLEQAKLRLEMEM----ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKAL 1634
Cdd:pfam05483 391 SELEEMTKfknnkEVELEELKKILAEDEKlldeKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1635 REKRELESKLstlsdqvnqrdfESEKrlrkdLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaaVKAR 1714
Cdd:pfam05483 471 KEVEDLKTEL------------EKEK-----LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED--------IINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1715 KAMEvemEDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQ 1790
Cdd:pfam05483 526 KKQE---ERMLKQIENLEEKEMNLRDELESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1791 IEESNKEKQELQEKLQALQsqveflEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKE----TMEKLTEE 1866
Cdd:pfam05483 603 IENKNKNIEELHQENKALK------KKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEdkkiSEEKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1867 RDQRAA----AENREKEQNKRLQRQLRD---------------TKEEMSELA---RKEAEASRKKHELEMDLESLEAANQ 1924
Cdd:pfam05483 677 VEKAKAiadeAVKLQKEIDKRCQHKIAEmvalmekhkhqydkiIEERDSELGlykNKEQEQSSAKAALEIELSNIKAELL 756
|
....*...
gi 600971660 1925 SLQADLKL 1932
Cdd:pfam05483 757 SLKKQLEI 764
|
|
| PDZ_canonical |
cd00136 |
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ... |
220-308 |
1.15e-17 |
|
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467153 [Multi-domain] Cd Length: 81 Bit Score: 79.51 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPTGDFGFSLRRTTMLDRAPegqayrrVVHFAEPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:cd00136 1 TVTLEKDPGGGLGFSIRGGKDGGGGI-------FVSRVEPG-GPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSA 72
|
....*....
gi 600971660 300 GDSVRLKVQ 308
Cdd:cd00136 73 GGEVTLTVR 81
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1386-1958 |
1.65e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 89.33 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1386 AVREVDFTKKRLQQELEDkmEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELE 1465
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKA--QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1466 kkqrrfdsELSQAHEETQREKLQREklqREKDMLLAEAFSLKQQMEEkdldiagftqkvvsLEAELQDISSQESKDEASL 1545
Cdd:PRK02224 255 --------TLEAEIEDLRETIAETE---REREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1546 AKVKKQLRDLEAKVKDQEEELDEQAGSIQML-EQAK------LRLEMEMERMRqTHSKEMESRDEEVEEARQSCQKKLKQ 1618
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHnEEAEslredaDDLEERAEELR-EEAAELESELEEAREAVEDRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1619 MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqRDFESEKRLRKDLKRTKALLADAQIMLDHLKnnAPskrEIAQlkn 1698
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERD-ELREREAELEATLRTARERVEEAEALLEAGK--CP---ECGQ--- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1699 QLEESEFTCAAAVK--ARKAMEVEMEDLHLQIDDIAKAKTALEEqLSRLQREKNeiqnRLEEDQEDMNELMKKHKAAVAQ 1776
Cdd:PRK02224 460 PVEGSPHVETIEEDreRVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIE----RLEERREDLEELIAERRETIEE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1777 ASRdmaqmndlqaQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKslvsRQEAKirELETRLEFEKTQVKRLENLASRL 1856
Cdd:PRK02224 535 KRE----------RAEELRERAAELEAEAEEKREAAAEAEEEAEEA----REEVA--ELNSKLAELKERIESLERIRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1857 ------KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHE-----LEMDLESLEAANQS 1925
Cdd:PRK02224 599 aaiadaEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEeyleqVEEKLDELREERDD 678
|
570 580 590
....*....|....*....|....*....|....*
gi 600971660 1926 LQadlklafKRIGDLQAAIEdEMES--DENEDLIN 1958
Cdd:PRK02224 679 LQ-------AEIGAVENELE-ELEElrERREALEN 705
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1326-1964 |
1.66e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.18 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1326 ERLRTEKEM---KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERA---VREVDFTKKRLQQ 1399
Cdd:pfam02463 154 RRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEkleLEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1400 ELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAH 1479
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1480 EETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLaKVKKQLRDLEAKV 1559
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1560 KDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRE 1639
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEK---KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1640 LESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAM-- 1717
Cdd:pfam02463 470 SEDLLKETQLVKLQEQ-LELLLSRQKLEERSQKESKARSGLK--VLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAis 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1718 ---EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM----NELMKKHKAAVAQASRDMAQMNDLQAQ 1790
Cdd:pfam02463 547 tavIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleiDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1791 IEESNKEKQELQEKLQALQSQVefLEQSMVDKSLVSRQEAKIRELETRLEfekTQVKRLENLASRLKETMEKLTEERDQR 1870
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGL--RKGVSLEEGLAEKSEVKASLSELTKE---LLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1871 AAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMES 1950
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650
....*....|....
gi 600971660 1951 DENEDLINSEGDSD 1964
Cdd:pfam02463 782 KTEKLKVEEEKEEK 795
|
|
| PDZ_NHERF-like |
cd06768 |
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ... |
222-307 |
4.23e-16 |
|
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467249 [Multi-domain] Cd Length: 80 Bit Score: 74.78 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 222 ELQRRPTGdFGFSLRRttmlDRAPEGQaYRRVVhfaEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGD 301
Cdd:cd06768 4 HLVKGPEG-YGFNLHA----EKGRPGH-FIREV---DPG-SPAERA-GLKDGDRLVEVNGENVEGESHEQVVEKIKASGN 72
|
....*.
gi 600971660 302 SVRLKV 307
Cdd:cd06768 73 QVTLLV 78
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1393-1960 |
4.94e-16 |
|
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: 84.64 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1393 TKKRLQQELEDKMEVEQQSRRQLeRRLGDLQADSDESQRALQQLKKKCQRLTA-----ELQDTKLHLEGQQVRNHELEKK 1467
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAqeavlEETQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1468 QRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQ--MEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1545
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1546 AKVKKQLRDLEAKVK---DQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVEEARQSCQKKLkQMEVQ 1622
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQslcKELDILQREQATIDTRTSAFRDLQGQLAHAK----KQQELQQRYAELCAAAITCTA-QCEKL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1623 LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL-------RKDLKRTKALLADAQIMLDHLKNNAPSKR---E 1692
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeqT 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1693 IAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKKHKA 1772
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE---AEDMLACE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1773 AVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ---------EAKIRELETRLEFEK 1843
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkellasrQLALQKMQSEKEQLT 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1844 TQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEA--------SRKKHELEMD 1915
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkarteahFNNNEEVTAA 773
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1916 L------ESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSE 1960
Cdd:TIGR00618 774 LqtgaelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE 824
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
432-614 |
4.94e-16 |
|
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: 84.12 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKgCRR--EDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 509
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYK-CIDciEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 510 GSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQAL---------------------STLLEAFGNSPTIMNGSATRF 568
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDnihneentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 600971660 569 SQILSLDFDQAgQVASASIQTMLLEKLRVARRPASEATFNVFYYLL 614
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYII 205
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1252-1968 |
5.90e-16 |
|
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: 84.71 E-value: 5.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1252 RPLIQVQLSEEQIRNKDEEIQ--QLRSKLEKVEKE-------RNELRLSSDRLETR---ISELTSELTDERNTGESASQL 1319
Cdd:TIGR00606 351 RLQLQADRHQEHIRARDSLIQslATRLELDGFERGpfserqiKNFHTLVIERQEDEaktAAQLCADLQSKERLKQEQADE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1320 LDAETAERLRT--------EKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVR--- 1388
Cdd:TIGR00606 431 IRDEKKGLGRTielkkeilEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQnek 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1389 -EVDFTKKRLQQELE-----------------DKMEVEQQSRRQLERRLGDLQA------DSDESQRALQQLKKKCQRLT 1444
Cdd:TIGR00606 511 aDLDRKLRKLDQEMEqlnhhtttrtqmemltkDKMDKDEQIRKIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTR 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1445 AELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-----------ETQREKLQR--EKLQREKDMLLAEAFSLKQQME 1511
Cdd:TIGR00606 591 DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcgsqdeESDLERLKEeiEKSSKQRAMLAGATAVYSQFIT 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1512 EKDLDIAG---FTQKVVSLEAELQDISsqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME 1588
Cdd:TIGR00606 671 QLTDENQSccpVCQRVFQTEAELQEFI---SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1589 RMRQTHSK------EMESRDEEVEEARQSCQKKLKQMEV---------QLEEEYEDKQKALREK-RELESKLSTLS-DQV 1651
Cdd:TIGR00606 748 ELRNKLQKvnrdiqRLKNDIEEQETLLGTIMPEEESAKVcltdvtimeRFQMELKDVERKIAQQaAKLQGSDLDRTvQQV 827
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1652 NQRDFESEKRLRK---DLKRTKALLADAQIMLDHLKNNApskreiaqlkNQLEESEFTCAAAVKARKAME-------VEM 1721
Cdd:TIGR00606 828 NQEKQEKQHELDTvvsKIELNRKLIQDQQEQIQHLKSKT----------NELKSEKLQIGTNLQRRQQFEeqlvelsTEV 897
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1722 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEED----QEDMNELMKKHKAAVA---------------QASRDMA 1782
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSnkkaQDKVNDIKEKVKNIHGymkdienkiqdgkddYLKQKET 977
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1783 QMNDLQAQIEESNKEKQELQEKLQALQSQVE---FLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLasRLKET 1859
Cdd:TIGR00606 978 ELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVL--QMKQE 1055
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1860 MEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAsrKKHELEMDLESLEAANQSL--------QADLK 1931
Cdd:TIGR00606 1056 HQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE--KYREMMIVMRTTELVNKDLdiyyktldQAIMK 1133
|
810 820 830
....*....|....*....|....*....|....*...
gi 600971660 1932 LAFKRIGDLQAAIEDEMESDEN-EDLINSEGDSDVDSE 1968
Cdd:TIGR00606 1134 FHSMKMEEINKIIRDLWRSTYRgQDIEYIEIRSDADEN 1171
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
432-1154 |
2.47e-15 |
|
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: 81.70 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 432 SVLHTLRQRYGASLLHTYAGPSLLVLST---RGAPAVYSEKvmhmfkgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVL 508
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPyrdVGNPLTLTST--------RSSPLAPQLLKVVQEAVRQQSETGYPQAIIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 509 LGSSGSGKTTSFQHLVQYLATIAGtSGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQaGQVASASIQ 588
Cdd:cd14881 74 SGTSGSGKTYASMLLLRQLFDVAG-GGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 589 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLN--------HLAENNVFgivplskpEEKQKAAQQFSKLQAA 660
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgyspanlrYLSHGDTR--------QNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 661 MKVLAISpeeqktcWL----ILASIYHLG----AAGATKEAAEAGRKQFarhewaQKAAYLLGCSleelSSAIFKhqlkg 732
Cdd:cd14881 224 LGILGIP-------FLdvvrVLAAVLLLGnvqfIDGGGLEVDVKGETEL------KSVAALLGVS----GAALFR----- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 733 GTLQRSTSFRQGPEESGLGEGTKLSALECLegmASGLYSELFTLLISLVNrALKSSQHSLC------SMMIVDTPGFQNP 806
Cdd:cd14881 282 GLTTRTHNARGQLVKSVCDANMSNMTRDAL---AKALYCRTVATIVRRAN-SLKRLGSTLGthatdgFIGILDMFGFEDP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 807 ewggsaRGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELafdDLEPVADDSVAAVDqashLVRSLahadeARG 886
Cdd:cd14881 358 ------KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQC---EVEVDYVDNVPCID----LISSL-----RTG 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 887 LLWLLEEEALVPGATEdalldrlfSYYGPQEGDKKGQSPLLRSSK--PRHFLLGHSHGTnwVEYNVAGWLnytkqnpatq 964
Cdd:cd14881 420 LLSMLDVECSPRGTAE--------SYVAKIKVQHRQNPRLFEAKPqdDRMFGIRHFAGR--VVYDASDFL---------- 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 965 naprllqDSQKKIISNlflgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAavkkkslciQIKLQVDALIDTI 1044
Cdd:cd14881 480 -------DTNRDVVPD----------------------DLVAVFYKQNCNFGFATHTQ---------DFHTRLDNLLRTL 521
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1045 KRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHM 1124
Cdd:cd14881 522 VHARPHFVRCIRSNTTETPN-----------------------------HFDRGTVVRQIRSLQVLETVNLMAGGYPHRM 572
|
730 740 750
....*....|....*....|....*....|
gi 600971660 1125 VFSEFRRRFDVLAPHLTKKHGRNYIVVDEK 1154
Cdd:cd14881 573 RFKAFNARYRLLAPFRLLRRVEEKALEDCA 602
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1261-1742 |
4.34e-15 |
|
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: 81.76 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1261 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISEL---TSELTDERNTGESAsqlldaetaeRLRTEKEMKEL 1337
Cdd:pfam01576 656 ERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMktqLEELEDELQATEDA----------KLRLEVNMQAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1338 QTQYDAlkkqmevmemevmearliraaEINGEvddDDAGGEWRLKYERAVREvdftkkrLQQELEDKMEVEQQ---SRRQ 1414
Cdd:pfam01576 726 KAQFER---------------------DLQAR---DEQGEEKRRQLVKQVRE-------LEAELEDERKQRAQavaAKKK 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1415 LERRLGDLQADSDESQR----ALQQLKK---KCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKL 1487
Cdd:pfam01576 775 LELDLKELEAQIDAANKgreeAVKQLKKlqaQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1488 QREKLQREKDmllaeafslkqqmeekdldiagftqkvvsleaELQDISSQESKDEASLAKVKkqlRDLEAKVKDQEEELD 1567
Cdd:pfam01576 855 ARRQAQQERD--------------------------------ELADEIASGASGKSALQDEK---RRLEARIAQLEEELE 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1568 EQAGSIQMLEQAKLRLEMEMERMRQTHSKEmESRDEEVEEARQSCQKKLKQMEVQL-EEEYEDKQKALREKRELESKLST 1646
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLQVEQLTTELAAE-RSTSQKSESARQQLERQNKELKAKLqEMEGTVKSKFKSSIAALEAKIAQ 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1647 LSDQVNQrdfESEKRLR--KDLKRTKALLADAQIMLDHLKNNAPSKREIA--------QLKNQLEESEFTCAAAVKARKA 1716
Cdd:pfam01576 979 LEEQLEQ---ESRERQAanKLVRRTEKKLKEVLLQVEDERRHADQYKDQAekgnsrmkQLKRQLEEAEEEASRANAARRK 1055
|
490 500
....*....|....*....|....*.
gi 600971660 1717 MEVEMEDLHLQIDDIAKAKTALEEQL 1742
Cdd:pfam01576 1056 LQRELDDATESNESMNREVSTLKSKL 1081
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1278-1749 |
4.61e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.97 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1278 LEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVME 1357
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1358 ARLI-RAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQLerrlgdlqadSDESQRALQQL 1436
Cdd:COG4717 128 LPLYqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL----------SLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1437 KKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEtqreklqrEKLQREKDMLLAEA-----FSLKQQME 1511
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--------ERLKEARLLLLIAAallalLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1512 EKDLDIAGFTQKVVSLeaeLQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKL-RLEMEMERM 1590
Cdd:COG4717 270 SLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1591 RQTHSKEMESRDEE----VEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQR--------DFES 1658
Cdd:COG4717 347 EELQELLREAEELEeelqLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgeleellEALD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1659 EKRLRKDLKRTKALLADAQIMLDHLknnapsKREIAQLKNQLE--ESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKT 1736
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEEL------REELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
490
....*....|...
gi 600971660 1737 ALEEQLSRLQREK 1749
Cdd:COG4717 501 LLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1463-1943 |
4.98e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.97 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1463 ELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQ--DISSQESK 1540
Cdd:COG4717 57 ELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1541 DEASLAKVKKQLRDLEAkvkdQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQME 1620
Cdd:COG4717 137 LEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1621 VQLEEEYEDKQKALREKRELESKLSTLSDQvnqrdfesekrlrKDLKRTKALLADAQIMLdhlknnapskrEIAQLKNQL 1700
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALE-------------ERLKEARLLLLIAAALL-----------ALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1701 EESEFTCAAAVKARKAMevemedLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRD 1780
Cdd:COG4717 269 LSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1781 MAQMNDLQAQIEESNKEKQELQEKlQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFEKTQVKRLENLASRLKETM 1860
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED------EEELRAALEQAEEYQELKEELEELEEQLEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1861 EKLTEERDQRAAAENREKEQnkRLQRQLRDTKEEMSELARKEAEASRKKHELEMD--LESLEAANQSLQADLKLAFKRIG 1938
Cdd:COG4717 416 GELEELLEALDEEELEEELE--ELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWA 493
|
....*
gi 600971660 1939 DLQAA 1943
Cdd:COG4717 494 ALKLA 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1255-1771 |
5.16e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 81.26 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1255 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLET---------RISELTSELTDERNTGE-------SASQ 1318
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEkrlsrleEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1319 LLDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEvddddaggewRLKYERAVREVDFTKKRLQ 1398
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE----------RLKKRLTGLTPEKLEKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1399 QELEDKMEVEQQsRRQLERRLGDLQADSDESQRALQQLKK---KCQRLTAELQDtklhlegqqvrnHELEKKQRRFDSEL 1475
Cdd:PRK03918 395 ELEKAKEEIEEE-ISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTE------------EHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1476 SQAHEETQREKLQREKLQREKDMLlaEAFSLKQQMEEKDLDIAgftQKVVSLEAELQDISSQE-SKDEASLAKVKKQLRD 1554
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELA---EQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1555 LEAKVKDQEEELDEQagsiqmleqaklrlememermrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEE----YEDK 1630
Cdd:PRK03918 537 LKGEIKSLKKELEKL--------------------------EELKKKLAELEKKLDELEEELAELLKELEELgfesVEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1631 QKALREKRELESKLSTLSDQVnqRDFESEKRLRKDLKRTkalLADAQIMLDHLKNNAPSKR-EIAQLKNQLEESEFTCAA 1709
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAE--KELEREEKELKKLEEE---LDKAFEELAETEKRLEELRkELEELEKKYSEEEYEELR 665
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1710 AVKARKAMEV-----EMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNrLEEDQEDMNELMKKHK 1771
Cdd:PRK03918 666 EEYLELSRELaglraELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVK 731
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1635-1976 |
6.23e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.27 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1635 REKRELESKLSTLS--DQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcaAAVK 1712
Cdd:TIGR02169 153 VERRKIIDEIAGVAefDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGY--ELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1713 ARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM-AQMNDLQAQI 1791
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELeAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1792 EESNKEKQELQEKLQ-------ALQSQVEFLEQSMVDKSL--------VSRQEAKIRELETRLEFEKTQVKRLENLASRL 1856
Cdd:TIGR02169 311 AEKERELEDAEERLAkleaeidKLLAEIEELEREIEEERKrrdklteeYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1857 KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1936
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1937 IGDLQA---AIEDEMESDENEdLINSE-----------GDSDVDSELEDRVDGV 1976
Cdd:TIGR02169 471 LYDLKEeydRVEKELSKLQRE-LAEAEaqaraseervrGGRAVEEVLKASIQGV 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1255-1601 |
7.74e-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: 80.87 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1255 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLET-------RISELTSELTDERNTGESASQLLDAETAER 1327
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAeveqleeRIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1328 LRTEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDD-DDAGGEWRLKYERAVREVDFTKKRLqQELEDKME 1406
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALRE--------ALDELRAELTLlNEEAANLRERLESLERRIAATERRL-EDLEEQIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1407 VEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREK 1486
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1487 LQREKLQREKDMLLaEAFSLKQQMeekdldiagftqkvvsleaELQDISSQESKDEASLAKVKKQLRDLEAKVK------ 1560
Cdd:TIGR02168 929 LRLEGLEVRIDNLQ-ERLSEEYSL-------------------TLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvn 988
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 600971660 1561 --------DQEEELDEQAGSIQMLEQAKLRLEMEMERMrqthSKEMESR 1601
Cdd:TIGR02168 989 laaieeyeELKERYDFLTAQKEDLTEAKETLEEAIEEI----DREARER 1033
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1217-1806 |
8.87e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.45 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1217 KKRKIQDLAIRCVQKNIKKNKgvkdwpwwKLFTTVRPLIQVQLS-EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRL 1295
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNK--------SLESQISELKKQNNQlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1296 ETRISELTSELtderntgESASQLLDaetaerlRTEKEMKELQTQYDALKKQmevmemevmearliRAAEINGEVDDDDA 1375
Cdd:TIGR04523 266 KKQLSEKQKEL-------EQNNKKIK-------ELEKQLNQLKSEISDLNNQ--------------KEQDWNKELKSELK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1376 GGEWRLkyERAVREVDFTKKRLQQeLEDKMEveqqsrrQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLE 1455
Cdd:TIGR04523 318 NQEKKL--EEIQNQISQNNKIISQ-LNEQIS-------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1456 GQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDIS 1535
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1536 SQESKDEASLAKVKKQLRDLEAKVKDQEEELDeqagsiqMLEQAKLRLEMEMermrqthsKEMESRdeeveearqscQKK 1615
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELK-------KLNEEKKELEEKV--------KDLTKK-----------ISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1616 LKQMEVQLEeeyedkqkalREKRELESKLSTLSDQVNQRDFESEKRLRKD-----------LKRTKALLADAQIMLDHLK 1684
Cdd:TIGR04523 522 LKEKIEKLE----------SEKKEKESKISDLEDELNKDDFELKKENLEKeideknkeieeLKQTQKSLKKKQEEKQELI 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1685 NNapSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR--------- 1755
Cdd:TIGR04523 592 DQ--KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKwpeiikkik 669
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1756 -LEEDQEDMNELMKKHK----AAVAQASRDMAQMNDLQaQIEESNKEKQELQEKLQ 1806
Cdd:TIGR04523 670 eSKTKIDDIIELMKDWLkelsLHYKKYITRMIRIKDLP-KLEEKYKEIEKELKKLD 724
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1400-1876 |
8.88e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1400 ELEDKMEVEQQSRRQLERRLGDLQ---ADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELS 1476
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1477 QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFT---------------------QKVVSLEAELQDIS 1535
Cdd:PRK02224 297 DLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNeeaeslredaddleeraeelrEEAAELESELEEAR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1536 SQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQThskeMESRDEEVEEARQ----- 1610
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT----LRTARERVEEAEAlleag 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1611 ---SCQKKLKQME-VQLEEEYEDKQKALREKRE-LESKLSTLSDQVNQRD--FESEKRLRKDLKRTKA---LLADAQIML 1680
Cdd:PRK02224 453 kcpECGQPVEGSPhVETIEEDRERVEELEAELEdLEEEVEEVEERLERAEdlVEAEDRIERLEERREDleeLIAERRETI 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1681 DHLKNNAPSKREIAQ-LKNQLEESEftcAAAVKARKAMEVEMEdlhlQIDDIAKAKTALEEQLSRLQREKnEIQNRLEED 1759
Cdd:PRK02224 533 EEKRERAEELRERAAeLEAEAEEKR---EAAAEAEEEAEEARE----EVAELNSKLAELKERIESLERIR-TLLAAIADA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1760 QEDMNELMKKHKaavaqasrDMAQMNDL-QAQIEESNKEKQELQEKLQAlqsqvEFLEQSMVDKslvSRQEAKIRELETR 1838
Cdd:PRK02224 605 EDEIERLREKRE--------ALAELNDErRERLAEKRERKRELEAEFDE-----ARIEEAREDK---ERAEEYLEQVEEK 668
|
490 500 510
....*....|....*....|....*....|....*...
gi 600971660 1839 LEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENR 1876
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELEELEELRERREALENR 706
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1396-1901 |
1.75e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1396 RLQQELEDKMEVEQQSRRQLERR--LGDLQADSDESQRALQQLKkkcqrlTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1473
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIelLEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1474 ELSQAHEETQREKLQREKLQREKDMLLAEAFS--------LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1545
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1546 AKVKKQLR------------------DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKE---------- 1597
Cdd:COG4913 383 AALRAEAAallealeeelealeealaEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlgldeaelpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1598 ----MESRDEE-------------------VEEARQSC------QKKLKQmEVQLEEEYEDKQKALREK-------RELE 1641
Cdd:COG4913 463 vgelIEVRPEEerwrgaiervlggfaltllVPPEHYAAalrwvnRLHLRG-RLVYERVRTGLPDPERPRldpdslaGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1642 SKLSTLSDQVNQ---RDF-----ESEKRLRKDlkrTKALLADAQImldhlKNNApSKREIaQLKNQLEESEFTCAAAVKA 1713
Cdd:COG4913 542 FKPHPFRAWLEAelgRRFdyvcvDSPEELRRH---PRAITRAGQV-----KGNG-TRHEK-DDRRRIRSRYVLGFDNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1714 RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelmkkhkaaVAQASRDMAQMNDLQAQIEE 1793
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID---------VASAEREIAELEAELERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1794 SNKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFEKTQVK----RLENLASRLKETMEKLTEERDQ 1869
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEE------ELDELKGEIGRLEKELEQAEEELDelqdRLEAAEDLARLELRALLEERFA 756
|
570 580 590
....*....|....*....|....*....|..
gi 600971660 1870 RAAAENREKEQNKRLQRQLRDTKEEMSELARK 1901
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1265-1870 |
4.68e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1265 RNKDEEIQQLRSKLEkvEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDaETAERLrteKEMKELQTQYDAL 1344
Cdd:PRK02224 183 SDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRD-EADEVL---EEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1345 KkqmevmemevmearliraAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELED---KMEVEQQSRRQLERRLGD 1421
Cdd:PRK02224 257 E------------------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDllaEAGLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1422 LQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDmlla 1501
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE---- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1502 eafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD-------QEEELDEQAGSIQ 1574
Cdd:PRK02224 395 ---ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1575 MLEQAKLRLEMEMERMRQTHskemESRDEEVEEArqscqKKLKQMEVQLEEeyedkqkaLREKRELESKLSTlsdqvNQR 1654
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEV----EEVEERLERA-----EDLVEAEDRIER--------LEERREDLEELIA-----ERR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1655 DFESEKRLRKDLKRTKAlladaqimlDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE----MEDLHLQIDD 1730
Cdd:PRK02224 530 ETIEEKRERAEELRERA---------AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKEriesLERIRTLLAA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1731 IAKAKTALE---EQLSRLQREKNEIQNRLEEDQEDMNELMKKH-KAAVAQASRDMAQMNDLQAQIEEsnkEKQELQEKLQ 1806
Cdd:PRK02224 601 IADAEDEIErlrEKREALAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEE---KLDELREERD 677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1807 ALQSQVEFLEQSMvdkslvsrqeAKIRELETRLEFEKTQVKRLENL---ASRLKETMEKLTEERDQR 1870
Cdd:PRK02224 678 DLQAEIGAVENEL----------EELEELRERREALENRVEALEALydeAEELESMYGDLRAELRQR 734
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1690-1906 |
5.85e-14 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 75.96 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1690 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1769
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1770 -------HKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdkslvsRQEAKIRELETRLEFE 1842
Cdd:COG4942 113 lyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA---------ELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1843 KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAS 1906
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1258-1909 |
7.68e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 77.70 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1258 QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDaetaERLRTEKEMKEL 1337
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ----GKLTEEKEELEK 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1338 QTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELE--DKMEVEQQSRRQL 1415
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggRIISAHGRLGDLG 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1416 ERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEETQREKLQREKLQRE 1495
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK---LPLKSIAVLEIDPILNLAQLDKAT 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1496 KDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQE------SKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1569
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaekSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1570 AGSIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSD 1649
Cdd:pfam02463 693 EILRRQLEIKKKEQREK-EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1650 QVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID 1729
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1730 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqasrdMAQMNDLQAQIEESNKEKQELQEKLQALQ 1809
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEK------EEKKELEEESQKLNLLEEKENEIEERIKE 925
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1810 SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLEN---LASRLKETMEKLTEERDQRAAAENREKEQN----K 1882
Cdd:pfam02463 926 EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLakeELGKVNLMAIEEFEEKEERYNKDELEKERLeeekK 1005
|
650 660
....*....|....*....|....*..
gi 600971660 1883 RLQRQLRDTKEEMSELARKEAEASRKK 1909
Cdd:pfam02463 1006 KLIRAIIEETCQRLKEFLELFVSINKG 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1653-1960 |
9.51e-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: 77.40 E-value: 9.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1653 QRDFESEKRLRK---DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaavkarkamevemedlhLQID 1729
Cdd:TIGR02168 172 ERRKETERKLERtreNLDRLEDILNELERQLKSLERQAEKAERYKELKAELRE-----------------------LELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1730 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkhkaavaqasrdmaqmndlQAQIEESNKEKQELQEKLQALQ 1809
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQEL---------------------EEKLEELRLEVSELEEEIEELQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1810 SqvEFLEQSmvdkslvsrqeAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLR 1889
Cdd:TIGR02168 288 K--ELYALA-----------NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1890 DTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSE 1960
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1262-1898 |
3.10e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1262 EQIRNKDEEIQQLRSKLEKVEKERNELRLssDRLETRISELTSELTDERntgesasQLLDAETAERLRTEKEMKELQTQY 1341
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAELEELR-------AELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1342 DALKKQMevmemevmearliraaeingevddDDAGGEwRLkyERAVREVdftkKRLQQELEDKmeveQQSRRQLERRLGD 1421
Cdd:COG4913 326 DELEAQI------------------------RGNGGD-RL--EQLEREI----ERLERELEER----ERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1422 LQADSDESQRALQQLKKKCQRLTAELQDtklHLEGQQVRNHELEKKQRRFDSELSQAHEE----TQREKLQREKLQREKD 1497
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEE---ELEALEEALAEAEAALRDLRRELRELEAEiaslERRKSNIPARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1498 MLlAEAFSLKqqmeEKDLDIAGftqkvvsleaELQDISSQESK------------------DEASLAKVKKQL--RDLEA 1557
Cdd:COG4913 448 AL-AEALGLD----EAELPFVG----------ELIEVRPEEERwrgaiervlggfaltllvPPEHYAAALRWVnrLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1558 KVKDQEEELDEQAGSIQMLEQAKL--RLEMEMERMRQTHSKEMESRD-----EEVEEARQ-------SCQKKL------K 1617
Cdd:COG4913 513 RLVYERVRTGLPDPERPRLDPDSLagKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRhpraitrAGQVKGngtrheK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1618 QMEVQLEEEY------EDKQKALREKR-ELESKLSTLSDQVNQRdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSK 1690
Cdd:COG4913 593 DDRRRIRSRYvlgfdnRAKLAALEAELaELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1691 REIAQLKNQ---LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE----DQEDM 1763
Cdd:COG4913 668 REIAELEAElerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlARLEL 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1764 NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQveFLEQSMVDKSLVSRQEAKIRELETRLEfek 1843
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA--FNREWPAETADLDADLESLPEYLALLD--- 822
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1844 tqvkRLENlaSRLKETMEKLteeRDQRAAAENREKEQ-NKRLQRQLRDTKEEMSEL 1898
Cdd:COG4913 823 ----RLEE--DGLPEYEERF---KELLNENSIEFVADlLSKLRRAIREIKERIDPL 869
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1534-1958 |
5.92e-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: 74.29 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1534 ISSQESKD---EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEmemERMRQTHSKEMESRD-------- 1602
Cdd:TIGR04523 28 ANKQDTEEkqlEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILE---QQIKDLNDKLKKNKDkinklnsd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1603 -----EEVEEARQSCQKK---LKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesekrlrkDLKRTKALLA 1674
Cdd:TIGR04523 105 lskinSEIKNDKEQKNKLeveLNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN------------DLKKQKEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1675 DAQIMLDHLKNNApsKREIAQLKNQLEESEFTCAAAVKARKamevEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQN 1754
Cdd:TIGR04523 173 NELNLLEKEKLNI--QKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1755 RLEEDQEDMNELMKKHKaavaqasRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD------KSLVSRQ 1828
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQN-------KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelKSELKNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1829 EAKIRELEtrlefekTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRK 1908
Cdd:TIGR04523 320 EKKLEEIQ-------NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1909 KHELEMDLESLEAANQSLQADLK-------LAFKRIGDLQAAIEDemESDENEDLIN 1958
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKklqqekeLLEKEIERLKETIIK--NNSEIKDLTN 447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1475-1677 |
7.01e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.49 E-value: 7.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1475 LSQAHEETQREKlQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1554
Cdd:COG4942 16 AAQADAAAEAEA-ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1555 LEAKVKDQEEELDEQAGSIQML-EQAKLRLEM------EMERMRQTHSKEMESRDEEVEEARQScQKKLKQMEVQLEEEY 1627
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgRQPPLALLLspedflDAVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 600971660 1628 EDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQ 1677
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1732-1936 |
7.21e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.49 E-value: 7.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1732 AKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1811
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1812 VEFLEQSMVD--------------KSLVSRQEAK-----IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAA 1872
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqpplALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1873 AENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1936
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1584-1924 |
9.09e-13 |
|
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: 73.62 E-value: 9.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1584 EMEMERMRQTH---SKEMESRD--EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTlsDQVNQRDFES 1658
Cdd:pfam17380 295 KMEQERLRQEKeekAREVERRRklEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKREL--ERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1659 EKRLRKDLKRtkalladaqIMLDHLKNNAPSKREI-AQLKNQLEESEFTcaaavKARKAMEVEMEDLHLQIDDiakaktA 1737
Cdd:pfam17380 373 EISRMRELER---------LQMERQQKNERVRQELeAARKVKILEEERQ-----RKIQQQKVEMEQIRAEQEE------A 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1738 LEEQLSRLQREKNEIQNRLEEDqedmnELMKKHkaavaqasrdmaQMNDLQAQIEESNKEKQELqEKLQALQSQVEFLEQ 1817
Cdd:pfam17380 433 RQREVRRLEEERAREMERVRLE-----EQERQQ------------QVERLRQQEEERKRKKLEL-EKEKRDRKRAEEQRR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1818 SMVDKSLVSRQEAKIRELETRLEFEKtqvkrlenlasRLKETMEKLTEERDQRAAAENREKEQN----KRLQRQLRDTKE 1893
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLEK-----------EMEERQKAIYEEERRREAEEERRKQQEmeerRRIQEQMRKATE 563
|
330 340 350
....*....|....*....|....*....|...
gi 600971660 1894 EMSEL--ARKEAEASRKKHELEMDLESLEAANQ 1924
Cdd:pfam17380 564 ERSRLeaMEREREMMRQIVESEKARAEYEATTP 596
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1705-1961 |
1.05e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.10 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1705 FTCAAAVKARKAMEVEMEDLHLQIDdiakaktALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQM 1784
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIA-------ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1785 NDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKirELETRLEFEKTQVKRLENLASRLKETMEKLT 1864
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1865 EERDQRAaaenrekEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAI 1944
Cdd:COG4942 164 ALRAELE-------AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*..
gi 600971660 1945 EDEMESDENEDLINSEG 1961
Cdd:COG4942 237 AAAAERTPAAGFAALKG 253
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1434-1960 |
3.03e-12 |
|
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: 72.31 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1434 QQLKKKCQRLTAELQDTKLHLEGQQVRNHElekKQRRFDSELSQAHEETQREKLQREKLQREkDMLLAEAFSLKQQMEEK 1513
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHE---RKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1514 DLDIAGFT--QKVVSLEAELQDISSQESK---DEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME 1588
Cdd:TIGR00618 266 RARIEELRaqEAVLEETQERINRARKAAPlaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1589 RMRQTHSKEMESRDE-EVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFE--SEKRLRKD 1665
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAhEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRtsAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1666 LKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcaaAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1745
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ---SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1746 QREKNE-----------------IQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQAL 1808
Cdd:TIGR00618 503 PCPLCGscihpnparqdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1809 QSQVEFLEQSMVD------------KSLVSRQEAKIRELETRLE------FEKTQVKRLENLASRLKETMEKLTEERDQR 1870
Cdd:TIGR00618 583 KEDIPNLQNITVRlqdlteklseaeDMLACEQHALLRKLQPEQDlqdvrlHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1871 AAAENREKEQNKRLQRQLRDTKEE-------------------MSELARKEAEASRKKHELEMDLESLEaanQSLQADLK 1931
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQsekeqltywkemlaqcqtlLRELETHIEEYDREFNEIENASSSLG---SDLAARED 739
|
570 580
....*....|....*....|....*....
gi 600971660 1932 LAFKRIGDLQAAIEDEMESDENEDLINSE 1960
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNE 768
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1384-1922 |
3.58e-12 |
|
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: 72.18 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1384 ERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRL----GDLQADSDESQRALQQLKkkcQRLTAELQDTKLHLEGQQV 1459
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHG---AFLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1460 RNHELEKKQRRFDSeLSQAHEETQREKLQREKL--QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQ 1537
Cdd:pfam12128 352 WQSELENLEERLKA-LTGKHQDVTAKYNRRRSKikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1538 eSKDEASLAKVKKQLRDLEAKVK-----DQEEELDEQAGSIQMLEQAKLRLEM---EMERMrQTHSKEMESRDEEVEEAR 1609
Cdd:pfam12128 431 -GKLEFNEEEYRLKSRLGELKLRlnqatATPELLLQLENFDERIERAREEQEAanaEVERL-QSELRQARKRRDQASEAL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1610 QSCQKKLKQMEVQLEE-------------EYEDKQKALREK---RELESKLSTLSDQVNQRDFESEKR------LRKDLK 1667
Cdd:pfam12128 509 RQASRRLEERQSALDElelqlfpqagtllHFLRKEAPDWEQsigKVISPELLHRTDLDPEVWDGSVGGelnlygVKLDLK 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1668 RTKALladaqimlDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDiakAKTALEEQLSRLQR 1747
Cdd:pfam12128 589 RIDVP--------EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETF---ARTALKNARLDLRR 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1748 EKNEIQNrleeDQEDMNELMKKHKAAVAQASRDMAQ-----MNDLQAQIEESNKEKQELQ-EKLQALQSQVEFLEQSM-- 1819
Cdd:pfam12128 658 LFDEKQS----EKDKKNKALAERKDSANERLNSLEAqlkqlDKKHQAWLEEQKEQKREARtEKQAYWQVVEGALDAQLal 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1820 VDKSLVSRQEAKIRELETRLEFEKTQVKRL---ENLASRLKETMEKLTE-----ERDQRAAAENRE------KEQNKRLQ 1885
Cdd:pfam12128 734 LKAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIRTLERkieriAVRRQEVLRYFDwyqetwLQRRPRLA 813
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 600971660 1886 RQLRDTKEEMSE----LARKEAEASRKKHELEMDLESLEAA 1922
Cdd:pfam12128 814 TQLSNIERAISElqqqLARLIADTKLRRAKLEMERKASEKQ 854
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1381-1933 |
3.91e-12 |
|
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: 71.78 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1381 LKYERAVREVDFTKKRLqqeLEDKMEVEQQSRRQLERRLGDLQaDSDESQRALQQL----KKKCQRLTAELQDTKLHLEG 1456
Cdd:pfam10174 41 LKKERALRKEEAARISV---LKEQYRVTQEENQHLQLTIQALQ-DELRAQRDLNQLlqqdFTTSPVDGEDKFSTPELTEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1457 QQVRNHELEKKQRRFDSELSQAHEE------TQREKL--QREKLQREKDMLLAEAFSLKQQMEEKDLD--IAGFTQKVVS 1526
Cdd:pfam10174 117 NFRRLQSEHERQAKELFLLRKTLEEmelrieTQKQTLgaRDESIKKLLEMLQSKGLPKKSGEEDWERTrrIAEAEMQLGH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1527 LEAELQDISSQESKDEASLaKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVE 1606
Cdd:pfam10174 197 LEVLLDQKEKENIHLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1607 --EARQSCQKKLKQMEVQLEEEYEDKQKalrEKRELESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLK 1684
Cdd:pfam10174 276 qmEVYKSHSKFMKNKIDQLKQELSKKES---ELLALQTKLETLTNQ-NSDCKQHIEVLKESLTAKEQRAAILQTEVDALR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1685 NNAPSKREIAQLKNQ----LEESEFTCAAA---------VKARKAMEVE--MEDLHLQIDDIAKAKTALEEQLSRLQREK 1749
Cdd:pfam10174 352 LRLEEKESFLNKKTKqlqdLTEEKSTLAGEirdlkdmldVKERKINVLQkkIENLQEQLRDKDKQLAGLKERVKSLQTDS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1750 NEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDlqaQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-----KSL 1824
Cdd:pfam10174 432 SNTDTALTTLEEALSEKERIIERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDlkehaSSL 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1825 VSR---QEAKIRELETRLEFEKTQVKRLENLASRLKETmeklteERDQRAAAENREKEQNkrLQRqlrdtkeemsELARK 1901
Cdd:pfam10174 509 ASSglkKDSKLKSLEIAVEQKKEECSKLENQLKKAHNA------EEAVRTNPEINDRIRL--LEQ----------EVARY 570
|
570 580 590
....*....|....*....|....*....|...
gi 600971660 1902 EAEASRKKHELEMDLESL-EAANQSLQADLKLA 1933
Cdd:pfam10174 571 KEESGKAQAEVERLLGILrEVENEKNDKDKKIA 603
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1574-1956 |
6.02e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1574 QMLEQaklRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQVNQ 1653
Cdd:COG4717 45 AMLLE---RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1654 -RDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS----KREIAQLKNQLEESEFTCAAAVK-ARKAMEVEMEDLHLQ 1727
Cdd:COG4717 121 lEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1728 IDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK-----------AAVA--------------------- 1775
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaAALLallglggsllsliltiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1776 ---------------QASRDMAQMNDLQAQIEESNKEKQELQEKLQALQ----SQVEFLEQSMVDKSLVSRQEAKIRELE 1836
Cdd:COG4717 281 lvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGlppdLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1837 TRLEFEKTQvKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAsrkkhELEMDL 1916
Cdd:COG4717 361 EELQLEELE-QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEEL 434
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 600971660 1917 ESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDL 1956
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1256-1836 |
9.17e-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: 70.92 E-value: 9.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1256 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGEsasqlLDAETAERLRTEKE-M 1334
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD-----LKLQELQHLKNEGDhL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1335 KELQTQYDALKKQMEVMEMEVMEAR--LIRAAEINGEvDDDDAGGewrLKYERAVREVDFTKKRLQ-QELEDKMEVEQQS 1411
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRqqIENMTQLVGQ-HGRTAGA---MQVEKAQLEKEINDRRLElQEFKILKDKKDAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1412 RRQLERRLGDLQADS-------DESQRALQQLKKKCQRLTAELQDTKLHLEG---------QQVRN--HELEKKQRRFDS 1473
Cdd:pfam15921 620 IRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNksEEMETTTNKLKM 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1474 ELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLE---------------------AELQ 1532
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeamtnankekhflkeeknklsQELS 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1533 DISSQESKDEASLAKVKKQLRDLEAKVKDQEEELD-------EQAGSIQMLEQAKLRLEM-------EMERMRQTHSKEM 1598
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDkaslqfaECQDIIQRQEQESVRLKLqhtldvkELQGPGYTSNSSM 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1599 ESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALRE--KRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLAD 1675
Cdd:pfam15921 860 KPRlLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEdpTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALD 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1676 AQIMLDHLKNNAPSK---REIAQLKNQLEESEFTCAAAVKARKAMevEMEDLHLQIDDIAKAKTALEEQLSR---LQREK 1749
Cdd:pfam15921 940 DRVRDCIIESSLRSDichSSSNSLQTEGSKSSETCSREPVLLHAG--ELEDPSSCFTFPSTASPSVKNSASRsfhSSPKK 1017
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1750 NEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQmnDLQAQ-IEESNKEKQELQEKLQALQSQVEFLE---QSMvdKSLV 1825
Cdd:pfam15921 1018 SPVHSLLTSSAEGSIGSSSQYRSAKTIHSPDSVK--DSQSLpIETTGKTCRKLQNRLESLQTLVEDLQlknQAM--SSMI 1093
|
650
....*....|.
gi 600971660 1826 SRQEAKIRELE 1836
Cdd:pfam15921 1094 RNQEKRIQKVK 1104
|
|
| PDZ_SHANK1_3-like |
cd06746 |
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ... |
223-307 |
1.20e-11 |
|
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.
Pssm-ID: 467228 [Multi-domain] Cd Length: 101 Bit Score: 63.00 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 223 LQRRPTGdFGFSLRRT---------TMLDRAPEGQAYRRVvhfaEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIV 293
Cdd:cd06746 11 LQKGDKG-FGFVLRGAkavgpilefTPTPAFPALQYLESV----DPG-GVADKA-GLKKGDFLLEINGEDVVKASHEQVV 83
|
90
....*....|....
gi 600971660 294 EMIRQSGDSVRLKV 307
Cdd:cd06746 84 NLIRQSGNTLVLKV 97
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1735-1943 |
1.50e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 68.70 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1735 KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL--QALQSQV 1812
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeRARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1813 EFLEQSMVDKSLVSRQeakIRELETRLEFektqvkrLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTK 1892
Cdd:COG3883 98 SGGSVSYLDVLLGSES---FSDFLDRLSA-------LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1893 EEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAA 1943
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1405-1979 |
1.78e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.87 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1405 MEVEQQSRRQLERRLGDLQADsDESQRALQQLKKkcQRLTAELQDTKlHLEGQQVRNHELEKKQRRFDS------ELSQA 1478
Cdd:pfam12128 188 MHSKEGKFRDVKSMIVAILED-DGVVPPKSRLNR--QQVEHWIRDIQ-AIAGIMKIRPEFTKLQQEFNTlesaelRLSHL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1479 HEETQREKLQREKLQREKDMLLAEafslkqqmeekdldiagFTQKVVSLEAELQdissqESKDEASLakvkkQLRDLEAK 1558
Cdd:pfam12128 264 HFGYKSDETLIASRQEERQETSAE-----------------LNQLLRTLDDQWK-----EKRDELNG-----ELSAADAA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1559 VKDQEEEL---DEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEE-------YE 1628
Cdd:pfam12128 317 VAKDRSELealEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnnrdiagIK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1629 DKQKALREKRE------------LESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDhlknnapskreiaqL 1696
Cdd:pfam12128 397 DKLAKIREARDrqlavaeddlqaLESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE--------------L 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1697 KNQLEESEFTCAAAVKARKAMEVEMEDLHlqiDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQ 1776
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQ---SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1777 ASRDMAQMNDLQAQIEESNK-EKQELQEKLQALQSQVEF--------LEQSMVDKSLVSRQEAKIR--ELETRLEFEKTQ 1845
Cdd:pfam12128 540 LRKEAPDWEQSIGKVISPELlHRTDLDPEVWDGSVGGELnlygvkldLKRIDVPEWAASEEELRERldKAEEALQSAREK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1846 VKRLENLASRLKETMEKLT-EERDQRAAAENREKEQnKRL---QRQLRDTKEEMSELARKEAEASRKK--HELEMDLESL 1919
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASrEETFARTALKNARLDL-RRLfdeKQSEKDKKNKALAERKDSANERLNSleAQLKQLDKKH 698
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1920 EAANQSLQADLKLAfkRIGDLQAAIEDEMESDENEDLINSEGDSdVDSELEDRVDGVKSW 1979
Cdd:pfam12128 699 QAWLEEQKEQKREA--RTEKQAYWQVVEGALDAQLALLKAAIAA-RRSGAKAELKALETW 755
|
|
| PDZ |
smart00228 |
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
220-309 |
1.84e-11 |
|
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.
Pssm-ID: 214570 [Multi-domain] Cd Length: 85 Bit Score: 62.01 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPTGdFGFSLRRttmlDRAPEGQAYrrVVHFAEPGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:smart00228 4 LVELEKGGGG-LGFSLVG----GKDEGGGVV--VSSVVPGSPAAKA---GLRVGDVILEVNGTSVEGLTHLEAVDLLKKA 73
|
90
....*....|
gi 600971660 300 GDSVRLKVQP 309
Cdd:smart00228 74 GGKVTLTVLR 83
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1459-1978 |
2.02e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1459 VRNHELEKKQ--RRFDS------ELSQAHEETQREKLQREKLQREKDmlLAEAF-SLKQQMEEKDLDIAGFTQKVVSLEA 1529
Cdd:COG4913 213 VREYMLEEPDtfEAADAlvehfdDLERAHEALEDAREQIELLEPIRE--LAERYaAARERLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1530 ELQdissqeskdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKL--------RLEMEMERMRQTHskemesr 1601
Cdd:COG4913 291 ELL---------EAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLEREL------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1602 dEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQImLD 1681
Cdd:COG4913 355 -EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS-LE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1682 HLKNNAPskREIAQLKNQLEEseftcAAAVKARKA------MEVEMED-------------------------------- 1723
Cdd:COG4913 433 RRKSNIP--ARLLALRDALAE-----ALGLDEAELpfvgelIEVRPEEerwrgaiervlggfaltllvppehyaaalrwv 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1724 ------LHLQIDDI------AKAKTALEEQLSR-LQREKNEIQNRLE------------EDQEDMnelmKKHKAAVAQA- 1777
Cdd:COG4913 506 nrlhlrGRLVYERVrtglpdPERPRLDPDSLAGkLDFKPHPFRAWLEaelgrrfdyvcvDSPEEL----RRHPRAITRAg 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1778 ----SRDMAQMNDL-------------QAQIEESNKEKQELQEKLQALQSQVEFLEQSMvdKSLVSRQEAKIRELETRle 1840
Cdd:COG4913 582 qvkgNGTRHEKDDRrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAEL--DALQERREALQRLAEYS-- 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1841 FEKTQVKRLENLASRLKETMEKLTEERDQRAAaenrekeqnkrLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLE 1920
Cdd:COG4913 658 WDEIDVASAEREIAELEAELERLDASSDDLAA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 600971660 1921 AANQSLQADLKLAFKRIGDLQAAIEDEMesdeNEDLINSEGDSDVDSELEDRVDGVKS 1978
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLEER----FAAALGDAVERELRENLEERIDALRA 780
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1409-1633 |
2.38e-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: 67.87 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1409 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQ 1488
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1489 REKLQREKDMLLAEAFSLKQQMEEKDL-DIAGFTQKVVSLEAeLQDISSQeskDEASLAKVKKQLRDLEAKVKDQEEELD 1567
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLlSPEDFLDAVRRLQY-LKYLAPA---RREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 1568 EQAGSIQMLEQAKLRLEMEMERMRQT---HSKEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKA 1633
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1719-1880 |
2.69e-11 |
|
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: 65.72 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1719 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ---EDMNELMKKHKAAVAQASRDMAQMNDLQAQIeESN 1795
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1796 KEkqelqekLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1875
Cdd:COG1579 89 KE-------YEALQKEIESLKR------RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*
gi 600971660 1876 REKEQ 1880
Cdd:COG1579 156 AELEE 160
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1253-1899 |
3.39e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.10 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1253 PLIQVQLSeeqirNKDEEIQQLRSKLEKVEKERNELRLSSD-RLETRISELTSELTDERntgesasqlldaETAERLRTE 1331
Cdd:pfam12128 350 PSWQSELE-----NLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIR------------EARDRQLAV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1332 KEmKELQTQYDALKKQMEVMEMEVMEARL---IRAAEINGEVDDDDAGGEWRLKYERAVREVDftkkRLQQELEDKMEve 1408
Cdd:pfam12128 413 AE-DDLQALESELREQLEAGKLEFNEEEYrlkSRLGELKLRLNQATATPELLLQLENFDERIE----RAREEQEAANA-- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1409 QQSRRQLERRLgdLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdselSQAHEETQREKLQ 1488
Cdd:pfam12128 486 EVERLQSELRQ--ARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKE-------APDWEQSIGKVIS 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1489 REKLQREKDMLLAEAFSLKQQ-------MEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1561
Cdd:pfam12128 557 PELLHRTDLDPEVWDGSVGGElnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1562 QEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR--- 1638
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARtek 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1639 --ELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHL----KNNAPSKREIAQLKNQLEESEFTCAAAVK 1712
Cdd:pfam12128 717 qaYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIERIAVRRQEVLR 796
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1713 ARKAME----VEMEDLHLQIDDIAKAKTALEEQLSRLQ------REKNEIQNRLEEDQED-MNELMKKHKAAVAQASRDM 1781
Cdd:pfam12128 797 YFDWYQetwlQRRPRLATQLSNIERAISELQQQLARLIadtklrRAKLEMERKASEKQQVrLSENLRGLRCEMSKLATLK 876
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1782 AQMNDLQAQ--IEESNKEKQELQEKLQ----ALQSQVEFLEQSMVDKS---------LVSRQEAKIRELETRLEFEKTQV 1846
Cdd:pfam12128 877 EDANSEQAQgsIGERLAQLEDLKLKRDylseSVKKYVEHFKNVIADHSgsglaetweSLREEDHYQNDKGIRLLDYRKLV 956
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1847 KRLENLASRLKETMEKLTEER------------DQRAAAENREKEQNKRLQRQLRDTK--EEMSELA 1899
Cdd:pfam12128 957 PYLEQWFDVRVPQSIMVLREQvsilgvdltefyDVLADFDRRIASFSRELQREVGEEAffEGVSESA 1023
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1262-1757 |
3.41e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1262 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntGESASQLLDAETAERLRTEKEMKELQTQy 1341
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL--AEAGLDDADAEAVEARREELEDRDEELR- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1342 DALKKQMevmemevmearlIRAAEINGEVddddaggewrlkyERAVREVDftkkrlqqELEDKMEVEQQSRRQLERRLGD 1421
Cdd:PRK02224 328 DRLEECR------------VAAQAHNEEA-------------ESLREDAD--------DLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1422 LQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEkkqrrfdSELSQAHEetqREKLQREKLQREKDMlLA 1501
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR-------EERDELRE---REAELEATLRTARER-VE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1502 EAFSLK---------QQMEEKDL--DIAGFTQKVVSLEAELQDISSQESKDEA------SLAKVKKQLRDLEAKVK---- 1560
Cdd:PRK02224 444 EAEALLeagkcpecgQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEERREdlee 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1561 ---DQEEELDEQAGSIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLE------------E 1625
Cdd:PRK02224 524 liaERRETIEEKRERAEELRERAAELEAEAEEKREA-AAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllaaiA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1626 EYEDKQKALREKRElesKLSTLSDQvnQRDFESEKRLRKDlkrtkalladaqimldhlknnapskreiaQLKNQLEESEF 1705
Cdd:PRK02224 603 DAEDEIERLREKRE---ALAELNDE--RRERLAEKRERKR-----------------------------ELEAEFDEARI 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1706 TCAAAVKARKA-----MEVEMEDLHLQIDDIAKAKTALE---EQLSRLQREKNEIQNRLE 1757
Cdd:PRK02224 649 EEAREDKERAEeyleqVEEKLDELREERDDLQAEIGAVEnelEELEELRERREALENRVE 708
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1638-1901 |
3.41e-11 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 68.12 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1638 RELESKLSTLSDQVN--------QRDFESEKRlrkdlKRTKALLADAQIMLDHLKNNAPS-KREIAQLKNQLEEseftca 1708
Cdd:PHA02562 177 RELNQQIQTLDMKIDhiqqqiktYNKNIEEQR-----KKNGENIARKQNKYDELVEEAKTiKAEIEELTDELLN------ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1709 aavkarkaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQR-----EKNEIQNRLEEDQEDMNELMKKHKAavaqasrdmaQ 1783
Cdd:PHA02562 246 --------LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyEKGGVCPTCTQQISEGPDRITKIKD----------K 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1784 MNDLQAQIEESNKEKQELQEKLqalqsqVEFLEQSMvdkslvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKL 1863
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIM------DEFNEQSK-----------KLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|....*...
gi 600971660 1864 TEERDQRaaaenreKEQNKRLQRQLRDTKEEMSELARK 1901
Cdd:PHA02562 371 QAEFVDN-------AEELAKLQDELDKIVKTKSELVKE 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1269-1486 |
3.42e-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: 67.48 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1269 EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQm 1348
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1349 eVMEMEVMEARLIRAAEINGEVD--------DDDAGGEWRLKYERAVREVDFTK----KRLQQELEDKMEVEQQSRRQLE 1416
Cdd:COG4942 99 -LEAQKEELAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARREQaeelRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1417 RRLGDLQadsdESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAHEETQREK 1486
Cdd:COG4942 178 ALLAELE----EERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1269-1586 |
3.47e-11 |
|
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: 68.94 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1269 EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTD-ERNTGE---SASQLLDAETAERLRTEKEMKELQTQYDAL 1344
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDaSRKIGEiekEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1345 -----KKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRlKYERAVREVDFTKKRLQ----------QELEDKMEVEQ 1409
Cdd:TIGR02169 754 envksELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP-EIQAELSKLEEEVSRIEarlreieqklNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1410 QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQR 1489
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1490 EKLQREKDMLLAEAFSLKQQMEE-------------KDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE 1556
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEiedpkgedeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
330 340 350
....*....|....*....|....*....|
gi 600971660 1557 AKVKDQEEELDEQAGSIQMLEQAKLRLEME 1586
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1258-1699 |
3.92e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 68.61 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1258 QLSEEQiRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETR-------ISELTSELTDERNTGESASQLLDAETAE-RLR 1329
Cdd:pfam15921 367 QFSQES-GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1330 TEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAeingeVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ 1409
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV-----VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEIT 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1410 QSRRQLERRLGDLQADSDESQRaLQQLKKKCQRLTAEL--QDTKLHLEGQQVRNHelekkqrrfdSELSQAHEET----Q 1483
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDH-LRNVQTECEALKLQMaeKDKVIEILRQQIENM----------TQLVGQHGRTagamQ 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1484 REKLQREKLQREKDMLLAEAFSLKqqmEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1563
Cdd:pfam15921 590 VEKAQLEKEINDRRLELQEFKILK---DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1564 EELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS-------------------------------C 1612
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkvamgmqkqitakrgqidaL 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1613 QKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTKALLADAQIMLDHLKNNAPSKRE 1692
Cdd:pfam15921 747 QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
....*..
gi 600971660 1693 IAQLKNQ 1699
Cdd:pfam15921 826 IIQRQEQ 832
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1454-1840 |
5.08e-11 |
|
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: 67.61 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1454 LEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREkdmllaeafsLKQQMEEKDLDIAGFTQKVVSLEAELQD 1533
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE----------LESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1534 ISsqeskdeASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQScQ 1613
Cdd:pfam07888 106 LS-------ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-Q 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1614 KKLKQMEVQLeeeyedkqkalrekRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREI 1693
Cdd:pfam07888 178 AKLQQTEEEL--------------RSLSKEFQELRNSLAQRD-TQVLQLQDTITTLTQKLTTAH---RKEAENEALLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1694 AQLKNQLEESEFTCAA-------AVKARKAMEVEMEDLHLQIDD----IAKAKTALEEQLSRLQREKNEIQNRLEEDQED 1762
Cdd:pfam07888 240 RSLQERLNASERKVEGlgeelssMAAQRDRTQAELHQARLQAAQltlqLADASLALREGRARWAQERETLQQSAEADKDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1763 M----NELMKKHKAAVAQASR------DMAQMNDL-QAQIEESNKEKQELQEKLQALQSQVEFLeqsmvdksLVSRQE-- 1829
Cdd:pfam07888 320 IeklsAELQRLEERLQEERMEreklevELGREKDCnRVQLSESRRELQELKASLRVAQKEKEQL--------QAEKQEll 391
|
410
....*....|.
gi 600971660 1830 AKIRELETRLE 1840
Cdd:pfam07888 392 EYIRQLEQRLE 402
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1373-1978 |
9.79e-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: 67.77 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1373 DDAGGEWRLKYERAVREVDFTKKRLQQeledkmeveqqsrrQLERRLGDLQADSDESQRALQQLKKKCQRLTaELQDTKL 1452
Cdd:TIGR01612 1099 DDFGKEENIKYADEINKIKDDIKNLDQ--------------KIDHHIKALEEIKKKSENYIDEIKAQINDLE-DVADKAI 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1453 HLEGQQvrnhELEKKQRRFDSELSQA---HEETQreKLQREKLQREKDmllaeafslKQQMEE-KDLDIAgFTQKVVSLE 1528
Cdd:TIGR01612 1164 SNDDPE----EIEKKIENIVTKIDKKkniYDEIK--KLLNEIAEIEKD---------KTSLEEvKGINLS-YGKNLGKLF 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1529 aeLQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEELDEQAGsIQMLEQAklrlemEMERMRQTHSKEM------ESRD 1602
Cdd:TIGR01612 1228 --LEKIDEEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMG-IEMDIKA------EMETFNISHDDDKdhhiisKKHD 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1603 EEVEEARQscqKKLKQMEVQLEE-EYEDKQKAL--------REKRELESKLSTLSDQVNQRDFESEKRLRKDLKR-TKAL 1672
Cdd:TIGR01612 1298 ENISDIRE---KSLKIIEDFSEEsDINDIKKELqknlldaqKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKEyTKEI 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1673 LADAQIMLDHLKNnapSKREIAQLKNQLeeSEFTCAAAVKArkamEVEMEDLHLQIDDIAKAKTALEEQLSRLQ------ 1746
Cdd:TIGR01612 1375 EENNKNIKDELDK---SEKLIKKIKDDI--NLEECKSKIES----TLDDKDIDECIKKIKELKNHILSEESNIDtyfkna 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1747 REKNE----IQNRLEEDQEDMNELMKKHKAavaQASRDMA-QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvd 1821
Cdd:TIGR01612 1446 DENNEnvllLFKNIEMADNKSQHILKIKKD---NATNDHDfNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQY--- 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1822 KSLVSRQEAKIRELETRLEFEKTQvKRLENLASRLKETMEKLTEErdqraaAENREKEQNKRLQRQLRDTKEemselARK 1901
Cdd:TIGR01612 1520 KKDVTELLNKYSALAIKNKFAKTK-KDSEIIIKEIKDAHKKFILE------AEKSEQKIKEIKKEKFRIEDD-----AAK 1587
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 600971660 1902 EAEASRKKHELEMDLESLEAanqslqadlklAFKRIGDLQAAIEDEM-ESDENEDLINSEGDSDVDSELEDRVDGVKS 1978
Cdd:TIGR01612 1588 NDKSNKAAIDIQLSLENFEN-----------KFLKISDIKKKINDCLkETESIEKKISSFSIDSQDTELKENGDNLNS 1654
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1523-1929 |
1.23e-10 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 66.69 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1523 KVVSLEAELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAgsiqmleQAKLRLEMEMERMRQTHSKEMESRD 1602
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH---KRARIELEKKASALKRQLDRES-------DRNQELQKRIRLLEKREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1603 EEVEEARQsCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFEsekrlrkdLKRTKALLADAQIMLDH 1682
Cdd:pfam05557 73 EQAELNRL-KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELE--------LQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1683 LKNNApskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhLQIDDIAKAKTALEEQLS--------RLQREKNEIQN 1754
Cdd:pfam05557 144 LKAKA---SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ---SQEQDSEIVKNSKSELARipelekelERLREHNKHLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1755 RLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ----------ALQSQVEFLEQSmvDKSL 1824
Cdd:pfam05557 218 ENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQdtglnlrspeDLSRRIEQLQQR--EIVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1825 VSRQ-----------------EAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERD-QRAAAENREKEQN-KRLQ 1885
Cdd:pfam05557 296 KEENssltssarqlekarrelEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgYRAILESYDKELTmSNYS 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 600971660 1886 RQLRDTKEEMSELARK-EAEASRKKHELEMDLESLEAANQSLQAD 1929
Cdd:pfam05557 376 PQLLERIEEAEDMTQKmQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1261-1775 |
1.55e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 66.67 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1261 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELtderntgESASQLLDAETAERLRTEKEMKELQTQ 1340
Cdd:pfam05483 274 EEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL-------QIATKTICQLTEEKEAQMEELNKAKAA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1341 YDALKKQMEVMEMEVMeaRLIRAAEINGEVDDDdaggewRLKyeraVREVDFTKKRLQQE----LEDKMEVEQQSRRQLE 1416
Cdd:pfam05483 347 HSFVVTEFEATTCSLE--ELLRTEQQRLEKNED------QLK----IITMELQKKSSELEemtkFKNNKEVELEELKKIL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1417 RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREK 1496
Cdd:pfam05483 415 AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1497 DMLLAEAFSLKQQMEEKDLDIAGFTQKVVS-------LEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1569
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKKHQEDIINckkqeerMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1570 AGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQ--KKLKQMEVQLEEEYEDKQKALreKRELESKLSTL 1647
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKalKKKGSAENKQLNAYEIKVNKL--ELELASAKQKF 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1648 SDQVN--QRDFE----SEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKreIAQLKNQLEESEFTCAAAVKARKAmevEM 1721
Cdd:pfam05483 653 EEIIDnyQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHK--IAEMVALMEKHKHQYDKIIEERDS---EL 727
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1722 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1775
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1262-1878 |
2.14e-10 |
|
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: 66.61 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1262 EQIRNKDEE-IQQLRSKLEKVEKERNELRLSSD--RLETRISELTSELTDERNTGESASQLLDaETAErlrTEKEmkelQ 1338
Cdd:TIGR01612 1135 EEIKKKSENyIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLN-EIAE---IEKD----K 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1339 TQYDALKKQMEVMEMEVMEARLiraaeinGEVDDDDAGGEWRLK-YERAVREVDFTKKRlQQELEDKMEVEQQSRRQLEr 1417
Cdd:TIGR01612 1207 TSLEEVKGINLSYGKNLGKLFL-------EKIDEEKKKSEHMIKaMEAYIEDLDEIKEK-SPEIENEMGIEMDIKAEME- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1418 rLGDLQADSDESQRALQQLKKKcqrltaELQDtklhlegqqVRNHELEKKQRRF-DSELSQAHEETQREKLQREKLQREK 1496
Cdd:TIGR01612 1278 -TFNISHDDDKDHHIISKKHDE------NISD---------IREKSLKIIEDFSeESDINDIKKELQKNLLDAQKHNSDI 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1497 DMLLAEAFSLKQQMEEKDL-----DIAGFTQKVvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdQEEELDEQ-- 1569
Cdd:TIGR01612 1342 NLYLNEIANIYNILKLNKIkkiidEVKEYTKEI---EENNKNIKDELDKSEKLIKKIKDDINLEECKSK-IESTLDDKdi 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1570 AGSIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEV-------EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELES 1642
Cdd:TIGR01612 1418 DECIKKIKELKNHILSE-ESNIDTYFKNADENNENVlllfkniEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1643 KLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDhLKNN-APSKREIAQLKNQLEE--SEFTCAAAVKARKAMEV 1719
Cdd:TIGR01612 1497 GCKDEADK-NAKAIEKNKELFEQYKKDVTELLNKYSALA-IKNKfAKTKKDSEIIIKEIKDahKKFILEAEKSEQKIKEI 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1720 EMEDLHLQiDDIAKA----KTALEEQLSrlqrekneIQNrLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESn 1795
Cdd:TIGR01612 1575 KKEKFRIE-DDAAKNdksnKAAIDIQLS--------LEN-FENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDT- 1643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1796 kekqELQEKLQALQSQVEFLEQsmvdkslVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1875
Cdd:TIGR01612 1644 ----ELKENGDNLNSLQEFLES-------LKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIAN 1712
|
...
gi 600971660 1876 REK 1878
Cdd:TIGR01612 1713 KEE 1715
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1243-1674 |
2.56e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1243 PWWKLFTTVRPLiQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgESASQLLDA 1322
Cdd:PRK03918 359 ERHELYEEAKAK-KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK---KAIEELKKA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1323 E----TAERLRTEKEMKELQTQYDA-LKKQMEVMEMEVMEARLIRAAEIngEVDDDDAGGEWRLKYERAVREVDFTKKRL 1397
Cdd:PRK03918 435 KgkcpVCGRELTEEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKELR--ELEKVLKKESELIKLKELAEQLKELEEKL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1398 QQELEDKMEVEQQSRRQLERRLGDLQADS---DESQRALQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSE 1474
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIkslKKELEKLEELKKKLAELEKKLDELEEELA-------ELLKELEELGFE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1475 LSQAHEETQREklqREKLQREkdmlLAEAFSLKQQMEEKDldiagftQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1554
Cdd:PRK03918 586 SVEELEERLKE---LEPFYNE----YLELKDAEKELEREE-------KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1555 LEAKVKDQEEEldeqagsiqMLEQAKLRLEMEMERMRqthskemeSRDEEVEEARQSCQKKLKqmevQLEEEYEDKQKAL 1634
Cdd:PRK03918 652 LEKKYSEEEYE---------ELREEYLELSRELAGLR--------AELEELEKRREEIKKTLE----KLKEELEEREKAK 710
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 600971660 1635 REKRELESKLSTLsdqvnqrdfeseKRLRKDLKRTKALLA 1674
Cdd:PRK03918 711 KELEKLEKALERV------------EELREKVKKYKALLK 738
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1259-1807 |
3.16e-10 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 65.15 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1259 LSEEQIRNKDEEIQQLRSKLEKVEKERNElrlsSDRLETRISELTSELTDErnTGESASQLLDAETAERlRTEKEMKELQ 1338
Cdd:pfam05557 66 EAEEALREQAELNRLKKKYLEALNKKLNE----KESQLADAREVISCLKNE--LSELRRQIQRAELELQ-STNSELEELQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1339 TQYDALKKqmevmemevmearliRAAEINGEVDDDDAGGEWRLKYERAVREVDFtkkRLQQELEDKMEVEQQSRRQLerR 1418
Cdd:pfam05557 139 ERLDLLKA---------------KASEAEQLRQNLEKQQSSLAEAEQRIKELEF---EIQSQEQDSEIVKNSKSELA--R 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1419 LGDLQadsdesqRALQQLKKKCQRLTaELQDTKLHLEGQQvrnHELEKKQRRfdselsqahEETQREKLQreKLQREKDM 1498
Cdd:pfam05557 199 IPELE-------KELERLREHNKHLN-ENIENKLLLKEEV---EDLKRKLER---------EEKYREEAA--TLELEKEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1499 LLAEAFSLKQQMEEKDLDIA---GFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK-------DQEEELDE 1568
Cdd:pfam05557 257 LEQELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAqylkkieDLNKKLKR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1569 QAGSIQMLEQAKLRLEMEMERMRQ------------THSKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqKALRE 1636
Cdd:pfam05557 337 HKALVRRLQRRVLLLTKERDGYRAilesydkeltmsNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLS-------VAEEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1637 KRELESKLSTLSDQVnqrdfesekrlrkDLKRTKALLADAqimldhlknnAPSKREIAQLKNQLEESEFTCAAAVKARKA 1716
Cdd:pfam05557 410 LGGYKQQAQTLEREL-------------QALRQQESLADP----------SYSKEEVDSLRRKLETLELERQRLREQKNE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1717 MEVEMED--------------LHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRdma 1782
Cdd:pfam05557 467 LEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFK--- 543
|
570 580
....*....|....*....|....*
gi 600971660 1783 QMNDLQAQIEESNKEKQELQEKLQA 1807
Cdd:pfam05557 544 EVLDLRKELESAELKNQRLKEVFQA 568
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1600-1952 |
3.83e-10 |
|
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: 65.58 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1600 SRDEEVEEARqscqkklkqmEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQrdfesekrLRKDLKRTKALLADAQIM 1679
Cdd:pfam01576 1 TRQEEEMQAK----------EEELQKVKERQQKAESELKELEKKHQQLCEEKNA--------LQEQLQAETELCAEAEEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1680 LDHLKNNAPSKREIAQ-LKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL-------------------- 1738
Cdd:pfam01576 63 RARLAARKQELEEILHeLESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvtteakikkleedill 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1739 -EEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQE--------------LQE 1803
Cdd:pfam01576 143 lEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQElekakrklegestdLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1804 KLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFEKTQ----VKRLENLASRLKETMEKLTEERDQRAAAEnreke 1879
Cdd:pfam01576 223 QIAELQAQIAELRAQL------AKKEEELQAALARLEEETAQknnaLKKIRELEAQISELQEDLESERAARNKAE----- 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 600971660 1880 qnkrlqRQLRDTKEEMSELarkeaeasrkKHELEMDLESlEAANQSLQADLKlafKRIGDLQAAIEDEMESDE 1952
Cdd:pfam01576 292 ------KQRRDLGEELEAL----------KTELEDTLDT-TAAQQELRSKRE---QEVTELKKALEEETRSHE 344
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1603-1828 |
4.10e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1603 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTKALLADAQIMLDH 1682
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1683 LKNNAPSKREIAQLKNQLEESEF-----TCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ---N 1754
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEallA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1755 RLEEDQEDMNELMKKHKAAVAQASRDMAQmndLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ 1828
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PDZ7_MUPP1-PD6_PATJ-like |
cd06671 |
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ... |
221-310 |
4.88e-10 |
|
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of MUPP1 and PDZ domain 6 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467159 [Multi-domain] Cd Length: 96 Bit Score: 58.10 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 221 LELQRRPTGDFGFSL---RrtTMLDRAPEGQAYRRVV--HFAE-PGAGTKDLalgLVPGDRLVEINGQNVENKSRDEIVE 294
Cdd:cd06671 5 VELWREPGKSLGISIvggR--VMGSRLSNGEEIRGIFikHVLEdSPAGRNGT---LKTGDRILEVNGVDLRNATHEEAVE 79
|
90
....*....|....*.
gi 600971660 295 MIRQSGDSVRLKVQPI 310
Cdd:cd06671 80 AIRNAGNPVVFLVQSL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1256-1534 |
5.22e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1256 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAE-----TAERLRT 1330
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1331 EKEMKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQqELEDKMEVEQQ 1410
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRI---DLKEQIKSIEKEIENLNGKKE-ELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1411 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQrEKLQRE 1490
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLE 954
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1491 KLQREKDMLLAEAFSLK-------QQMEEKDLDIAGFTQKVVSLEAELQDI 1534
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1722-1927 |
8.69e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.88 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1722 EDLHLQIDDIAKAKTALEEQLsrlqrekNEIQNRLEEDQEDMNELMKKHKAAVAQAsrdmaQMNDLQAQIEESNKEKQEL 1801
Cdd:COG3206 164 QNLELRREEARKALEFLEEQL-------PELRKELEEAEAALEEFRQKNGLVDLSE-----EAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1802 QEKLQALQSQVEFLEQSM----------VDKSLVSRQEAKIRELETRLEFEKTQV-----------KRLENLASRLKETM 1860
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpdalpelLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 600971660 1861 EKLTEE-RDQRAAAENREKEqnkrLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQ 1927
Cdd:COG3206 312 QRILASlEAELEALQAREAS----LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| PDZ5_MAGI-1_3-like |
cd06735 |
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
222-309 |
2.60e-09 |
|
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467217 [Multi-domain] Cd Length: 84 Bit Score: 55.66 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 222 ELQRRPTGdFGFSLRrttmldrapEGQAYRR----VVHFAEPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMI 296
Cdd:cd06735 5 ELERGPKG-FGFSIR---------GGREYNNmplyVLRLAEDGPAQRD---GrLRVGDQILEINGESTQGMTHAQAIELI 71
|
90
....*....|...
gi 600971660 297 RQSGDSVRLKVQP 309
Cdd:cd06735 72 RSGGSVVRLLLRR 84
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1473-1861 |
3.27e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 61.78 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1473 SELSQAHEETQREKLQREKLQRE--KDmLLAEAFS-------LKQQMEEKDLDIAGFTQKVVS---LEAE--LQDISSQE 1538
Cdd:PRK04778 129 QELLESEEKNREEVEQLKDLYRElrKS-LLANRFSfgpaldeLEKQLENLEEEFSQFVELTESgdyVEAReiLDQLEEEL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1539 SKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGSIQMLEQ----AKLRLEMEMERMRQTHSK---EMESRD-EEVEEARQ 1610
Cdd:PRK04778 208 AALEQIMEEIPELLKELQTELPDQLQEL--KAGYRELVEEgyhlDHLDIEKEIQDLKEQIDEnlaLLEELDlDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1611 SCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEkRLR-------KDLKRTKALLADAQIM---- 1679
Cdd:PRK04778 286 EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEID-RVKqsytlneSELESVRQLEKQLESLekqy 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1680 LDHLKNNAPSKREIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLE-- 1757
Cdd:PRK04778 365 DEITERIAEQEIAYSELQEELEEIL-------KQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEks 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1758 ------EDQEDMNELMKKH-KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM----------- 1819
Cdd:PRK04778 438 nlpglpEDYLEMFFEVSDEiEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQLIqyanryrsdne 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 600971660 1820 -VDKSLVS--------RQEAKIRELETRLE-FEKTQVKRLENLASRLKETME 1861
Cdd:PRK04778 518 eVAEALNEaerlfreyDYKAALEIIATALEkVEPGVTKRIEDSYEKEKETIR 569
|
|
| PDZ_FRMPD1_3_4-like |
cd06769 |
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ... |
220-307 |
3.32e-09 |
|
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This FRMPD1,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467250 [Multi-domain] Cd Length: 75 Bit Score: 54.94 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPTGDFGFSLRRTTMLdrapegqayrrVVHFAEPGaGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQ 298
Cdd:cd06769 1 TVEIQRDAVLGFGFVAGSERPV-----------VVRSVTPG-GPSE---GkLLPGDQILKINNEPVEDLPRERVIDLIRE 65
|
....*....
gi 600971660 299 SGDSVRLKV 307
Cdd:cd06769 66 CKDSIVLTV 74
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1385-1933 |
3.64e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.28 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1385 RAVREVDFTKKRLQQELEDKMEVEQQSRRQLERR--LGDLQADSDES----QRALQQLKKKCQRLTA------ELQDTKL 1452
Cdd:PRK04863 534 RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLesLSESVSEARERrmalRQQLEQLQARIQRLAArapawlAAQDALA 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1453 HLEGQQvrNHELEKKQRRfdSELSQAHEETQRE-KLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKV--VSLEA 1529
Cdd:PRK04863 614 RLREQS--GEEFEDSQDV--TEYMQQLLERERElTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFggVLLSE 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1530 ELQDISSQESKD-EASLAKVKKQL--RDLEAkVKDQEEELDEQAGSIQMLEQAKLRL--------EMEMERMRQTHSKEM 1598
Cdd:PRK04863 690 IYDDVSLEDAPYfSALYGPARHAIvvPDLSD-AAEQLAGLEDCPEDLYLIEGDPDSFddsvfsveELEKAVVVKIADRQW 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1599 E-SRDEEV----EEARQscqKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQR-------DFESE-KRLRKD 1665
Cdd:PRK04863 769 RySRFPEVplfgRAARE---KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHlavafeaDPEAElRQLNRR 845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1666 LKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESeftcaAAVKARKAMEVEMEDLHLQIDDIAKAK---------- 1735
Cdd:PRK04863 846 RVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPR-----LNLLADETLADRVEEIREQLDEAEEAKrfvqqhgnal 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1736 TALEEQLSRLQREKNEI---QNRLEEDQEDMNELMKKHKA-----------AVAQASRDMAQMNDLQAQIEESNKEKQEL 1801
Cdd:PRK04863 921 AQLEPIVSVLQSDPEQFeqlKQDYQQAQQTQRDAKQQAFAltevvqrrahfSYEDAAEMLAKNSDLNEKLRQRLEQAEQE 1000
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1802 QEKL--QALQSQVEFLEQSMVDKSLVSRQEAKireLETRLEFEKtqvkRLENLASRLKETME-KLTEERDQRAAAENREK 1878
Cdd:PRK04863 1001 RTRAreQLRQAQAQLAQYNQVLASLKSSYDAK---RQMLQELKQ----ELQDLGVPADSGAEeRARARRDELHARLSANR 1073
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 600971660 1879 EQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEmdlESLEAANQSLQADLKLA 1933
Cdd:PRK04863 1074 SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR---EQVVNAKAGWCAVLRLV 1125
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1381-1945 |
3.92e-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: 61.99 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1381 LKYERAVREVDFTKKRLQQ---ELEDKME-VEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQdtklhLEG 1456
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKdnsELELKMEkVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR-----LLN 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1457 QQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISS 1536
Cdd:TIGR00606 340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1537 QESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKL 1616
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1617 KQMEVQLEEeyedkqkalrEKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMldhlKNNAPSKREIAQL 1696
Cdd:TIGR00606 500 KKEVKSLQN----------EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR----KIKSRHSDELTSL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1697 ------KNQLEEsefTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRL------EEDQEDMN 1764
Cdd:TIGR00606 566 lgyfpnKKQLED---WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1765 ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ-ALQSQVEFLEqsmvdksLVSRQEAKIRELETRLEFEK 1843
Cdd:TIGR00606 643 RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQrVFQTEAELQE-------FISDLQSKLRLAPDKLKSTE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1844 TQVKRLENlasRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEA--EASRKKHELEMDLESLEA 1921
Cdd:TIGR00606 716 SELKKKEK---RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllGTIMPEEESAKVCLTDVT 792
|
570 580
....*....|....*....|....
gi 600971660 1922 ANQSLQADLKLAFKRIGDLQAAIE 1945
Cdd:TIGR00606 793 IMERFQMELKDVERKIAQQAAKLQ 816
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1261-1706 |
4.28e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1261 EEQIRNKD-EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDE-----------RNTGESASQLLDAETAERL 1328
Cdd:COG4913 329 EAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefaalraeaAALLEALEEELEALEEALA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1329 RTEKEMKELQTQYDALKKQMEV---------MEMEVMEARLIRAAEING----------EVDDDDAggEWRL-------- 1381
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASlerrksnipARLLALRDALAEALGLDEaelpfvgeliEVRPEEE--RWRGaiervlgg 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1382 ---------KYERAVRE----------VDFTKKRLQQELEDKMEVEQQS----------------RRQLERRLGDLQADS 1426
Cdd:COG4913 487 faltllvppEHYAAALRwvnrlhlrgrLVYERVRTGLPDPERPRLDPDSlagkldfkphpfrawlEAELGRRFDYVCVDS 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1427 desqraLQQLKKKCQRLTAELQ----------DTKLHLEGQQV-------RNHELEKKQRRFDSELSQAHEETQREKLQR 1489
Cdd:COG4913 567 ------PEELRRHPRAITRAGQvkgngtrhekDDRRRIRSRYVlgfdnraKLAALEAELAELEEELAEAEERLEALEAEL 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1490 EKLQRekdmlLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDIssqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1569
Cdd:COG4913 641 DALQE-----RREALQRLAEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDEL 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1570 AGSIQMLEQAKLRLEMEMERMRQTHSkemESRDEEVEEARQSCQKKLKQmeVQLEEEYEDKQKALREKRE-LESKLSTLS 1648
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLELRALLEERFAA--ALGDAVERELRENLEERIDaLRARLNRAE 786
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1649 DQVN------QRDFESEKRlrkDLKRTKALLADAQIMLDHLKNNA-PSKRE-IAQLKNQLEESEFT 1706
Cdd:COG4913 787 EELEramrafNREWPAETA---DLDADLESLPEYLALLDRLEEDGlPEYEErFKELLNENSIEFVA 849
|
|
| PDZ4_MAGI-1_3-like |
cd06734 |
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
270-309 |
4.56e-09 |
|
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467216 [Multi-domain] Cd Length: 84 Bit Score: 54.93 E-value: 4.56e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 600971660 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06734 45 LKVGDRILAVNGISILNLSHGDIVNLIKDSGLSVTLTIVP 84
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1536-1949 |
5.43e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.52 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1536 SQESKDEASLAKVKKQLRDLEAKVKDQ--EEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEmeSRDEEVEEARQSCQ 1613
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLctPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL--TQKREAQEEQLKKQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1614 KKLKQMEVQLEE------EYEDKQKALREKRELEsKLSTLSDQVNQRDFESEkRLRKDLKRTKALLADAQIMLDHLKNNA 1687
Cdd:TIGR00618 260 QLLKQLRARIEElraqeaVLEETQERINRARKAA-PLAAHIKAVTQIEQQAQ-RIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1688 PSKREIAQLKNQL--EESEFTCAAAVKA--RKAMEVEMEDLHlQIDDIAKAKTALEEQ-------LSRLQREKNEIQNRL 1756
Cdd:TIGR00618 338 SSIEEQRRLLQTLhsQEIHIRDAHEVATsiREISCQQHTLTQ-HIHTLQQQKTTLTQKlqslckeLDILQREQATIDTRT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1757 EEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdKSLVSRQEAKIRELE 1836
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK---EQIHLQETRKKAVVL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1837 TRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQnKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDL 1916
Cdd:TIGR00618 494 ARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTY-AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
410 420 430
....*....|....*....|....*....|...
gi 600971660 1917 ESLEAANQSLQADLKLAFKRIGDLQAAIEDEME 1949
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE 605
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1261-1803 |
5.53e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.46 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1261 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRIS-------ELTSELTDERNTGESASQLL---DAETAERLRT 1330
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINdpvyknrNYINDYFKYKNDIENKKQILsniDAEINKYHAI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1331 EKEMKELQTQYDA-LKKQMevmemevmearliRAAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ 1409
Cdd:PRK01156 328 IKKLSVLQKDYNDyIKKKS-------------RYDDLNNQILELE---GYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1410 QSRRQLERRLGD---LQADSDESQRALQQLKKKCQRLTA----------ELQDTKLHLEGQQV----RNHELEKKQRR-- 1470
Cdd:PRK01156 392 FISEILKIQEIDpdaIKKELNEINVKLQDISSKVSSLNQriralrenldELSRNMEMLNGQSVcpvcGTTLGEEKSNHii 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1471 --FDSELSQAHEETQREKLQREKLQREKDMLLaeafSLKQQMEEKDLD-IAGFTQKVVSLEAELQDissqeskDEASLAK 1547
Cdd:PRK01156 472 nhYNEKKSRLEEKIREIEIEVKDIDEKIVDLK----KRKEYLESEEINkSINEYNKIESARADLED-------IKIKINE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1548 VKKQlrdleakvKDQEEELDEQAGSIQmLEQAKLRLEMEMERMRQTHSKEME---SRDEEVEEARQSCQKKLKQMEVQLE 1624
Cdd:PRK01156 541 LKDK--------HDKYEEIKNRYKSLK-LEDLDSKRTSWLNALAVISLIDIEtnrSRSNEIKKQLNDLESRLQEIEIGFP 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1625 EEYEDKQKALrekRELESKLSTLSDQVNQrdFESEKRLRKDLKRTkalladaqimLDHLKNNAPSKREIAQLKNQLeese 1704
Cdd:PRK01156 612 DDKSYIDKSI---REIENEANNLNNKYNE--IQENKILIEKLRGK----------IDNYKKQIAEIDSIIPDLKEI---- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1705 ftcaaAVKARKaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMnELMKKHKAAVAQAS--RDMA 1782
Cdd:PRK01156 673 -----TSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETL-ESMKKIKKAIGDLKrlREAF 745
|
570 580
....*....|....*....|....*..
gi 600971660 1783 QMNDLQAQIEES------NKEKQELQE 1803
Cdd:PRK01156 746 DKSGVPAMIRKSasqamtSLTRKYLFE 772
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1526-1925 |
5.67e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.46 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1526 SLEAELQDISSQESKDEAS---LAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMermrqthsKEMESRD 1602
Cdd:PRK01156 177 MLRAEISNIDYLEEKLKSSnleLENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL--------NELSSLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1603 EEVeearqscqkklKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRkDLKRTKALLADAQIMLDH 1682
Cdd:PRK01156 249 DMK-----------NRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIN-DYFKYKNDIENKKQILSN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1683 LKNNAPSKREIAQLKNQLEE--SEFTcaaavkarkAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ 1760
Cdd:PRK01156 317 IDAEINKYHAIIKKLSVLQKdyNDYI---------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1761 EDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM-----------------VDKS 1823
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgEEKS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1824 L---------VSRQEAKIRELEtrlefekTQVKRLENLASRLKETMEKLTEERDQRAAAENRekeQNKRLQRQLRDTKEE 1894
Cdd:PRK01156 468 NhiinhynekKSRLEEKIREIE-------IEVKDIDEKIVDLKKRKEYLESEEINKSINEYN---KIESARADLEDIKIK 537
|
410 420 430
....*....|....*....|....*....|..
gi 600971660 1895 MSELARKEAEASRKKHELE-MDLESLEAANQS 1925
Cdd:PRK01156 538 INELKDKHDKYEEIKNRYKsLKLEDLDSKRTS 569
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1378-1719 |
6.40e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 61.29 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1378 EWRLKYE-RAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRlgdlqadsdeSQRALQQLKKKCQRltaELQDTKLHLEG 1456
Cdd:pfam17380 255 EYTVRYNgQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM----------EQERLRQEKEEKAR---EVERRRKLEEA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1457 QQVRNHELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMLLAEAFSLK-QQMEEKDLDIAGFTQKVVSLEAELQDI 1534
Cdd:pfam17380 322 EKARQAEMDRQAAIYAEQERMAMErERELERIRQEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1535 SSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQagsIQMLEQAKLRlemEMERMRQTHSKEMES----RDEEVEEARQ 1610
Cdd:pfam17380 402 RKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE---VRRLEEERAR---EMERVRLEEQERQQQverlRQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1611 SCQKKLKQMEVQLEEEY----------EDKQKALREKR-------ELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALL 1673
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQrrkilekeleERKQAMIEEERkrkllekEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 600971660 1674 ADAQIMLDHLKNNAPSKREiAQLKNQLEESEftcaaavKARKAMEV 1719
Cdd:pfam17380 556 EQMRKATEERSRLEAMERE-REMMRQIVESE-------KARAEYEA 593
|
|
| PDZ |
pfam00595 |
PDZ domain; PDZ domains are found in diverse signaling proteins. |
220-308 |
7.95e-09 |
|
PDZ domain; PDZ domains are found in diverse signaling proteins.
Pssm-ID: 395476 [Multi-domain] Cd Length: 81 Bit Score: 54.21 E-value: 7.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPTGDFGFSLRRttMLDRAPEGQAYRRVVHFaepGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:pfam00595 1 QVTLEKDGRGGLGFSLKG--GSDQGDPGIFVSEVLPG---GAAEAG---GLKVGDRILSINGQDVENMTHEEAVLALKGS 72
|
....*....
gi 600971660 300 GDSVRLKVQ 308
Cdd:pfam00595 73 GGKVTLTIL 81
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1691-1872 |
8.26e-09 |
|
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: 58.40 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1691 REIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkh 1770
Cdd:COG1579 17 SELDRLEHRLKELP-------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1771 kaavaqasRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEKtqvKRLE 1850
Cdd:COG1579 86 --------RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE------LAELEAELAELEAELEEKK---AELD 148
|
170 180
....*....|....*....|..
gi 600971660 1851 NLASRLKETMEKLTEERDQRAA 1872
Cdd:COG1579 149 EELAELEAELEELEAEREELAA 170
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1261-1862 |
8.31e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.07 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1261 EEQIRNKDEEIQQLRSKLEKVEKernELRLSSDRLEtRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTq 1340
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEK---SHSITLKEIE-RLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAES- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1341 yDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYeravrevDFTKKRlqqELEDKMEVEQQSRRQLERRLG 1420
Cdd:PRK01156 264 -DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKN-------DIENKK---QILSNIDAEINKYHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1421 DLQADSDEsqraLQQLKKKCQRLTAELQDTKLHLEGQQ--VRNHELEKKQRRfdselsqahEETQREKLQREKLQREKDM 1498
Cdd:PRK01156 333 VLQKDYND----YIKKKSRYDDLNNQILELEGYEMDYNsyLKSIESLKKKIE---------EYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1499 LLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR------DL-EAKVKDQEEELDEQAG 1571
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLgEEKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1572 SiqmLEQAKLRLEMEMERM--RQTHSKEMESR--DEEVEEARQScQKKLKQMEVQLeEEYEDKQKALREKrelESKLSTL 1647
Cdd:PRK01156 480 R---LEEKIREIEIEVKDIdeKIVDLKKRKEYleSEEINKSINE-YNKIESARADL-EDIKIKINELKDK---HDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1648 SDQVNQRDFESekrlrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavKARKAMEVEMEDLHLQ 1727
Cdd:PRK01156 552 KNRYKSLKLED-----LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLE----------SRLQEIEIGFPDDKSY 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1728 IDDIAKaktALEEQLSRLQREKNEIQNrLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ- 1806
Cdd:PRK01156 617 IDKSIR---EIENEANNLNNKYNEIQE-NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDd 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1807 ALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLaSRLKETMEK 1862
Cdd:PRK01156 693 AKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDL-KRLREAFDK 747
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1397-1811 |
1.07e-08 |
|
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: 60.43 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1397 LQQELEDKMEVEQQSrrqLERRLGDLQADSDESQRALQQLKkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELS 1476
Cdd:pfam05667 216 LAAAQEWEEEWNSQG---LASRLTPEEYRKRKRTKLLKRIA---EQLRSAALAGTEATSGASRSAQDLAELLSSFSGSST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1477 QAHEETQREKLQR-EKLQREKDMLLAEAFSLKQQMEEKDLDIAGfTQKVVSLEAELQDISSqeskdeaSLAKVKKQLRDL 1555
Cdd:pfam05667 290 TDTGLTKGSRFTHtEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLES-------SIQELEKEIKKL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1556 EAKVKDQEEELDEQagsiqmlEQAKLRLEMEMERMRQTHsKEMESRDEEVEEARQSCQKKLKQMeVQLEEEYEDKQKAL- 1634
Cdd:pfam05667 362 ESSIKQVEEELEEL-------KEQNEELEKQYKVKKKTL-DLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLi 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1635 REKRELESKLSTlsdqvnqRDFESEKRLR--KDLK-RTKALLADAQimldhlknnapSKRE-IAQLKNQLEE-------S 1703
Cdd:pfam05667 433 EEYRALKEAKSN-------KEDESQRKLEeiKELReKIKEVAEEAK-----------QKEElYKQLVAEYERlpkdvsrS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1704 EFTcaaavkaRKAMEVeMEDLHLQIDDIAKaktALEEQLSrLQREKNEIQNRLEEDQEDMNELM---KKHKAAVAQASRD 1780
Cdd:pfam05667 495 AYT-------RRILEI-VKNIKKQKEEITK---ILSDTKS-LQKEINSLTGKLDRTFTVTDELVfkdAKKDESVRKAYKY 562
|
410 420 430
....*....|....*....|....*....|....*...
gi 600971660 1781 MAQMNDLQAQ----IEESNK---EKQELQEKLQALQSQ 1811
Cdd:pfam05667 563 LAALHENCEQliqtVEETGTimrEIRDLEEQIETESGK 600
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1389-1889 |
1.11e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 60.14 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1389 EVDFTKKRLQQELEDKMEVEQQSRRQLerrlgdlqadsDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQ 1468
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRAR-----------IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1469 RrfdsELSQAHEETQREKLQREKLQREKDMLLAEA----FSLKQQMEEKDLDIAGFTQKVVSLEAELQDIS--------- 1535
Cdd:pfam05557 72 R----EQAELNRLKKKYLEALNKKLNEKESQLADAreviSCLKNELSELRRQIQRAELELQSTNSELEELQerldllkak 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1536 -SQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRL----EMEME----RMRQTHSKEMESRDEEVE 1606
Cdd:pfam05557 148 aSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELaripELEKElerlREHNKHLNENIENKLLLK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1607 EARQSCQKKLKQME------VQLEEEYEDKQKAL---------------------REKRELESKLSTLSDQV-------- 1651
Cdd:pfam05557 228 EEVEDLKRKLEREEkyreeaATLELEKEKLEQELqswvklaqdtglnlrspedlsRRIEQLQQREIVLKEENssltssar 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1652 ----NQRDFESEKR--------LRKDLKRTKALLADAQimldhlKNNAPSKREIAQLKNQLE--ESEFTCAAAVKARKAM 1717
Cdd:pfam05557 308 qlekARRELEQELAqylkkiedLNKKLKRHKALVRRLQ------RRVLLLTKERDGYRAILEsyDKELTMSNYSPQLLER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1718 EVEMEDLhlqIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelMKKHKAAVAQASRDMAQMNDLQAQIEESNKE 1797
Cdd:pfam05557 382 IEEAEDM---TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--ALRQQESLADPSYSKEEVDSLRRKLETLELE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1798 KQELQEKLQALQSQVEFLE----QSMVDKSLVSRQEAKIRELEtrlEFEKTQVKRLENLASRLKETMEKLTEERDQRAAA 1873
Cdd:pfam05557 457 RQRLREQKNELEMELERRClqgdYDPKKTKVLHLSMNPAAEAY---QQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRL 533
|
570
....*....|....*.
gi 600971660 1874 ENREKEQNKRLQRQLR 1889
Cdd:pfam05557 534 PETTSTMNFKEVLDLR 549
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1721-1947 |
1.21e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.77 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1721 MEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQE 1800
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1801 LQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFE-KTQVKRLEN---LASRLKETMEKLteerdQRAAAENR 1876
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRqQTEVLSPEEekeLVEKIKELEKEL-----EKAKKALE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 600971660 1877 EKEQNKRLQRQLRDTKEEMSELARKEAEASRK--KHELEMDlESLEAANQsLQADLKLAFKRIGDLQAAIEDE 1947
Cdd:COG1340 158 KNEKLKELRAELKELRKEAEEIHKKIKELAEEaqELHEEMI-ELYKEADE-LRKEADELHKEIVEAQEKADEL 228
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1393-1812 |
1.33e-08 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 59.92 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1393 TKKRLQQELEDKMEVEQQSRRQLerrlgdlqadSDESQR---ALQQLKKKCQRLT-AELQDTKLHLEGQQVRNhELEKKQ 1468
Cdd:pfam15964 301 TIERLTKERDDLMSALVSVRSSL----------AEAQQRessAYEQVKQAVQMTEeANFEKTKALIQCEQLKS-ELERQK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1469 RRFDSEL-SQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAK 1547
Cdd:pfam15964 370 ERLEKELaSQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1548 VKKQLRDLEAKVKDQEEELdeqagsiqmleqaklrlEMEMERMRQTHSKEMESRDEEVEEARQscqkKLKQMEVQLEEEY 1627
Cdd:pfam15964 450 VCGEMRYQLNQTKMKKDEA-----------------EKEHREYRTKTGRQLEIKDQEIEKLGL----ELSESKQRLEQAQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1628 EDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQLEESEFTC 1707
Cdd:pfam15964 509 QDAARAREECLKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELT------QKMQQMEAQHDKTVNEQ 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1708 AAAVKARKAMEVEMED----LHLQIDDIAKAKTALEEQLSR----LQREKNEIQNRLEEDQED------MNELMK----- 1768
Cdd:pfam15964 583 YSLLTSQNTFIAKLKEecctLAKKLEEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQcvqhgrMHERMKqrlrq 662
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 600971660 1769 --KHKAAVAQasrdmaQMNDLQAQIEESNKEKQELQEKLQALQSQV 1812
Cdd:pfam15964 663 ldKHCQATAQ------QLVQLLSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1378-1817 |
1.37e-08 |
|
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: 60.35 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1378 EWRLKYERAV--REVDFTKKRLQQELEDKM-----EVEQQSRRQ--LERrlgDLQADSDESQRALQ--QLKKKCQRLTAE 1446
Cdd:COG3096 279 ERRELSERALelRRELFGARRQLAEEQYRLvemarELEELSAREsdLEQ---DYQAASDHLNLVQTalRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1447 LQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDML-------------LAEAfslKQQMEEK 1513
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqaLEKA---RALCGLP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1514 DLDIAGFTQKVVSLEAELQDISSQeskdeaslakvkkqLRDLEAKVKDQEEELDEQAGSIQMLEqaklRLEMEMERmrqt 1593
Cdd:COG3096 433 DLTPENAEDYLAAFRAKEQQATEE--------------VLELEQKLSVADAARRQFEKAYELVC----KIAGEVER---- 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1594 hSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSdqvnqrdfeseKRLRKDLkrtkall 1673
Cdd:COG3096 491 -SQAWQTARELLRRYRS--QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFC-----------QRIGQQL------- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1674 aDAQIMLDHLKnnapskreiAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID---DIAKAKTALEEQLSRLQREKN 1750
Cdd:COG3096 550 -DAAEELEELL---------AELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKelaARAPAWLAAQDALERLREQSG 619
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1751 EiqnrleedqedmnelmkkhkaAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQ 1817
Cdd:COG3096 620 E---------------------ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1185-1601 |
1.49e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1185 LARLEEQRDEQTSRHLTLFQAacRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRP-LIQVQLSEEQ 1263
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1264 IRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELT-SELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYD 1342
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1343 ALKKQMEVMEMEVMEARLIRAAEINGEV------DDDDAGGEWRLK---------------YERAVREVDFTKKRLQQEL 1401
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALlallglGGSLLSLILTIAgvlflvlgllallflLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1402 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE---LEKKQRRFDSELSQA 1478
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1479 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAgfTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-- 1556
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEed 468
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 600971660 1557 -------AKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESR 1601
Cdd:COG4717 469 gelaellQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1254-1657 |
2.07e-08 |
|
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: 59.14 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1254 LIQVQLsEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgESASQLLDAETaerlRTEKE 1333
Cdd:pfam07888 31 LLQNRL-EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK---EELRQSREKHE----ELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1334 MKELQTQYDALKKQMevmemevmearliraaeingevdddDAGGEWRLKYERAVREVDFTKKRLQQ---ELEDKMEVEQQ 1410
Cdd:pfam07888 103 YKELSASSEELSEEK-------------------------DALLAQRAAHEARIRELEEDIKTLTQrvlERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1411 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETqreklqre 1490
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKE-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1491 klqrekdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQA 1570
Cdd:pfam07888 230 ----------AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1571 GSIQMlEQAKLRLEMEMERMR-QTHSKEMESRDEEVEEARQSCQKklkqMEVQLEEEYEDKQKALRE-KRELESKLSTLs 1648
Cdd:pfam07888 300 ARWAQ-ERETLQQSAEADKDRiEKLSAELQRLEERLQEERMEREK----LEVELGREKDCNRVQLSEsRRELQELKASL- 373
|
....*....
gi 600971660 1649 dQVNQRDFE 1657
Cdd:pfam07888 374 -RVAQKEKE 381
|
|
| PDZ_SNX27-like |
cd23070 |
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ... |
231-307 |
2.15e-08 |
|
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SNX27-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467283 [Multi-domain] Cd Length: 93 Bit Score: 53.57 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 231 FGFSLRRTTMLD---RAPEGQAYRRVVHFA---EPGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVR 304
Cdd:cd23070 12 FGFNVRGQVSEGgqlRSINGELYAPLQHVSavlEGGAADKA---GVRKGDRILEVNGVNVEGATHKQVVDLIKSGGDELT 88
|
...
gi 600971660 305 LKV 307
Cdd:cd23070 89 LTV 91
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1462-1820 |
2.26e-08 |
|
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: 59.10 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1462 HELEKKQRRFDSELSQ--AHEETQREKLQ--REKLQREKDMLLAEAFS-------LKQQMEEKDLDIAGFTQKVVS---L 1527
Cdd:pfam06160 96 DDIEEDIKQILEELDEllESEEKNREEVEelKDKYRELRKTLLANRFSygpaideLEKQLAEIEEEFSQFEELTESgdyL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1528 EAE--LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGSIQMLEQ----AKLRLEMEMERMRQTHSKEMES- 1600
Cdd:pfam06160 176 EARevLEKLEEETDALEELMEDIPPLYEELKTELPDQLEEL--KEGYREMEEEgyalEHLNVDKEIQQLEEQLEENLALl 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1601 ---RDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQ----------------------VNQRD 1655
Cdd:pfam06160 254 enlELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnkelkeelervqqsytlnenelERVRG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1656 FESE-KRLRKDLKRTKALLADAQI----MLDHLKnnapskreiaQLKNQLEEseftcaaavkarkaMEVEMEDLHLQIDD 1730
Cdd:pfam06160 334 LEKQlEELEKRYDEIVERLEEKEVayseLQEELE----------EILEQLEE--------------IEEEQEEFKESLQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1731 IAKAKTALEEQLSRLQREKNEIQNRLEEDQ-----EDMNELMKKHKAAVAQASRDMAQ----MNDLQAQIEESNKEKQEL 1801
Cdd:pfam06160 390 LRKDELEAREKLDEFKLELREIKRLVEKSNlpglpESYLDYFFDVSDEIEDLADELNEvplnMDEVNRLLDEAQDDVDTL 469
|
410
....*....|....*....
gi 600971660 1802 QEKLQALQSQVEFLEQSMV 1820
Cdd:pfam06160 470 YEKTEELIDNATLAEQLIQ 488
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1687-1882 |
2.73e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1687 APSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNEL 1766
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1767 ---MKKHKAAVAQ-----------------------ASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV 1820
Cdd:COG3883 92 araLYRSGGSVSYldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 600971660 1821 D-KSLVSRQEAKIRELETRlefEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNK 1882
Cdd:COG3883 172 ElEAQQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1637-1902 |
3.17e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 59.15 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1637 KRELESKLSTLSDQvnqRDFESEKrlrkdlkrtKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaAAVKARKA 1716
Cdd:PRK11281 38 EADVQAQLDALNKQ---KLLEAED---------KLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ------APAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1717 MEvEMEDlhLQIDDIAKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESN 1795
Cdd:PRK11281 100 QA-ELEA--LKDDNDEETRETLSTLsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1796 K---------------EKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELET----RLEfekTQVKRLENLAS-- 1854
Cdd:PRK11281 177 NllkggkvggkalrpsQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTariqRLE---HQLQLLQEAINsk 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 600971660 1855 RLKETMEKLTEERDQRAAAEN-------REKEQNKRLQRQLRDTKEEMSELARKE 1902
Cdd:PRK11281 254 RLTLSEKTVQEAQSQDEAARIqanplvaQELEINLQLSQRLLKATEKLNTLTQQN 308
|
|
| cpPDZ_CPP-like |
cd06782 |
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ... |
269-309 |
6.02e-08 |
|
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.
Pssm-ID: 467623 [Multi-domain] Cd Length: 88 Bit Score: 52.10 E-value: 6.02e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 600971660 269 GLVPGDRLVEINGQNVENKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:cd06782 31 GIKPGDVIVAVDGESVRGMSLDEVVKLLRgPKGTKVKLTIRR 72
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1694-1958 |
6.19e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 56.47 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1694 AQLKNQLEESEFTCAAAVKARKAM-EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedmnELMKKHKA 1772
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED------ELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1773 AvaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFEKTQVK----R 1848
Cdd:pfam00038 102 E--------NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN---------HEEEVRELQAQVSDTQVNVEmdaaR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1849 LENLASRLKETMEKLTEE-RDQRAAAENREKEQNKRLQRQ-------LRDTKEEMSELarkeaeaSRKKHELEMDLESLE 1920
Cdd:pfam00038 165 KLDLTSALAEIRAQYEEIaAKNREEAEEWYQSKLEELQQAaarngdaLRSAKEEITEL-------RRTIQSLEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1921 AANQSLQA-----------DLKLAFKRIGDLQAA---IEDEMES--DENEDLIN 1958
Cdd:pfam00038 238 KQKASLERqlaeteeryelQLADYQELISELEAElqeTRQEMARqlREYQELLN 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1690-1906 |
6.23e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1690 KREIAQLKNQLEESEftcaAAVKARKAmEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedMNELMKK 1769
Cdd:COG3206 181 EEQLPELRKELEEAE----AALEEFRQ-KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1770 HKAAVAQASRDmAQMNDLQAQIEESNKEKQELQEKL-------QALQSQVEFLEQSmvdksLVSRQEAKIRELETRLEFE 1842
Cdd:COG3206 252 GPDALPELLQS-PVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-----LQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1843 KTQVKRLENLASRLKETMEKLTEERDQRAaaenrekeqnkRLQRQLRDTKEEMSELARKEAEAS 1906
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR-----------RLEREVEVARELYESLLQRLEEAR 378
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1268-1889 |
1.11e-07 |
|
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: 57.14 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1268 DEEIQQLRSKLEKVEKERNELRLSSDRLETRIS--ELTSELTDE-----------RNTGESASQLLDAETAERLRTEKEM 1334
Cdd:pfam10174 115 EENFRRLQSEHERQAKELFLLRKTLEEMELRIEtqKQTLGARDEsikkllemlqsKGLPKKSGEEDWERTRRIAEAEMQL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1335 KELQTQYD-------ALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgewrlKYERAVREVDFTKKRLQQELEDKMEV 1407
Cdd:pfam10174 195 GHLEVLLDqkekeniHLREELHRRNQLQPDPAKTKALQTVIEMKDTKIS-----SLERNIRDLEDEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1408 EQQSRRQLE----------RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEgqqVRNHELEKKQRRFD----- 1472
Cdd:pfam10174 270 REEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIE---VLKESLTAKEQRAAilqte 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1473 -SELSQAHEETQR------EKLQRekLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDissqesKDeasl 1545
Cdd:pfam10174 347 vDALRLRLEEKESflnkktKQLQD--LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD------KD---- 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1546 akvkKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQsCQKKLKQMEVQLEE 1625
Cdd:pfam10174 415 ----KQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKK-ENKDLKEKVSALQP 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1626 EYEDKQKALREKRE-----------LESKLSTLSDQVNQRdFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIA 1694
Cdd:pfam10174 490 ELTEKESSLIDLKEhasslassglkKDSKLKSLEIAVEQK-KEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVA 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1695 QLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDiakaktaLEEQLSRLQREkneiQNRLEEDQEDMNELMKKHKAAV 1774
Cdd:pfam10174 569 RYKEESGKAQAEVERLLGILREVENEKNDKDKKIAE-------LESLTLRQMKE----QNKKVANIKHGQQEMKKKGAQL 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1775 AQASR---DMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKS--LVSRQEAKIRELETRLEF-------- 1841
Cdd:pfam10174 638 LEEARrreDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghLTNLRAERRKQLEEILEMkqeallaa 717
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1842 --EK-TQVKRLENLASRLKETMEKLteerdqraAAENREKEqnkRLQRQLR 1889
Cdd:pfam10174 718 isEKdANIALLELSSSKKKKTQEEV--------MALKREKD---RLVHQLK 757
|
|
| PDZ_tamalin_CYTIP-like |
cd06713 |
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ... |
223-307 |
1.23e-07 |
|
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This tamalin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467197 [Multi-domain] Cd Length: 91 Bit Score: 51.08 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 223 LQRRPTGDFGF-------------SLRRTTMLDRapegqayrrvVHFAEPGagtkDLAlGLVPGDRLVEINGQNVENKSR 289
Cdd:cd06713 8 LEKQDNETFGFeiqtyglhhknsnEVEMCTYVCR----------VHEDSPA----YLA-GLTAGDVILSVNGVSVEGASH 72
|
90
....*....|....*...
gi 600971660 290 DEIVEMIRQSGDSVRLKV 307
Cdd:cd06713 73 QEIVELIRSSGNTLRLET 90
|
|
| PDZ_SYNJ2BP-like |
cd06709 |
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ... |
220-308 |
1.56e-07 |
|
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNJ2BP-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467193 [Multi-domain] Cd Length: 86 Bit Score: 50.75 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPTGdFGFSLRRTTMLDRAPEGQA-YrrVVHFAEPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIR 297
Cdd:cd06709 2 EITLKRGPSG-LGFNIVGGTDQPYIPNDSGiY--VAKIKEDGAAAID---GrLQEGDKILEINGQSLENLTHQDAVELFR 75
|
90
....*....|.
gi 600971660 298 QSGDSVRLKVQ 308
Cdd:cd06709 76 NAGEDVKLKVQ 86
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1260-1933 |
1.67e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1260 SEEQIRNKDEEIQQLRSKLEKVEKERNEL----RLSSDRL------------ETRISELTSELTDERNTGESASQLLDAE 1323
Cdd:PRK04863 298 SRRQLAAEQYRLVEMARELAELNEAESDLeqdyQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1324 TAER----LRTEKEMKELQTQ-------YDALkkQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAvREVDF 1392
Cdd:PRK04863 378 QEENearaEAAEEEVDELKSQladyqqaLDVQ--QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQA-KEQEA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1393 TKKRLQqeLEDKMEVEQQSRRQLERRLGDLQ--ADSDESQRALQQLKKKCQRLTAE-LQDTKLhlegQQVRNHElekkqr 1469
Cdd:PRK04863 455 TEELLS--LEQKLSVAQAAHSQFEQAYQLVRkiAGEVSRSEAWDVARELLRRLREQrHLAEQL----QQLRMRL------ 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1470 rfdSELSQAHEETQR-EKLQREKLQREKDMLLAEAFsLKQQMEEkdldiagftqkvvsLEAELQDISSQeskdeaslakv 1548
Cdd:PRK04863 523 ---SELEQRLRQQQRaERLLAEFCKRLGKNLDDEDE-LEQLQEE--------------LEARLESLSES----------- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1549 KKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRdEEVEEARQSCQKKLKQMEVQlEEEYE 1628
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-QDVTEYMQQLLERERELTVE-RDELA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1629 dkqkalREKRELESKLSTLSdqvnQRDFESEKRLRKDLKRTKA-LLAD--AQIMLDhlknNAP----------------- 1688
Cdd:PRK04863 652 ------ARKQALDEEIERLS----QPGGSEDPRLNALAERFGGvLLSEiyDDVSLE----DAPyfsalygparhaivvpd 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1689 ---SKREIAQLKNQLEE------------------SEFTCAAAVK-----------------ARKAMEVEMEDLHLQIDD 1730
Cdd:PRK04863 718 lsdAAEQLAGLEDCPEDlyliegdpdsfddsvfsvEELEKAVVVKiadrqwrysrfpevplfGRAAREKRIEQLRAEREE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1731 IAkaktaleEQLSRLQREKNEIQnRLeedQEDMNELMKKHkAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQS 1810
Cdd:PRK04863 798 LA-------ERYATLSFDVQKLQ-RL---HQAFSRFIGSH-LAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRS 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1811 QVEFLEQSMV-------------DKSLVSRQEAkIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEnRE 1877
Cdd:PRK04863 866 QLEQAKEGLSalnrllprlnllaDETLADRVEE-IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLK-QD 943
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1878 KEQNKRLQRQLRDTKEEMSEL-ARKEAEASrkkHELEMDLESLEAANQSLQADLKLA 1933
Cdd:PRK04863 944 YQQAQQTQRDAKQQAFALTEVvQRRAHFSY---EDAAEMLAKNSDLNEKLRQRLEQA 997
|
|
| PDZ2_L-delphilin-like |
cd06744 |
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ... |
224-308 |
2.65e-07 |
|
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which it is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467226 [Multi-domain] Cd Length: 75 Bit Score: 49.58 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 224 QRRPTGDFGFSLRrttmlDRAPegqAYRRVVhfaEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSV 303
Cdd:cd06744 4 VYRGNGSFGFTLR-----GHAP---VYIESV---DPG-SAAERA-GLKPGDRILFLNGLDVRNCSHDKVVSLLQGSGSMP 70
|
....*
gi 600971660 304 RLKVQ 308
Cdd:cd06744 71 TLVVE 75
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1631-1807 |
2.94e-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: 53.78 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1631 QKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESEFTCAAA 1710
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELE-DELAALEARLEAAKTELEDLEKEIKRLEL------EIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1711 VKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdmaqmnDLQ 1788
Cdd:COG1579 86 RNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA----------ELE 155
|
170
....*....|....*....
gi 600971660 1789 AQIEESNKEKQELQEKLQA 1807
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1727-1962 |
3.36e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.41 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1727 QIDDIAKAKT-ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdmaqmnDLQAQIEESNKEKQELQEKL 1805
Cdd:PHA02562 167 EMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA----------RKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1806 QALQSQVEFLEQSMVDkslVSRQEAKIRELETRLefeKTQVKRLENLASRLKE------TMEKLTEERDQRAAAENREKE 1879
Cdd:PHA02562 237 EELTDELLNLVMDIED---PSAALNKLNTAAAKI---KSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1880 QNKRLqRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMES-----DENE 1954
Cdd:PHA02562 311 LQHSL-EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEElaklqDELD 389
|
....*...
gi 600971660 1955 DLINSEGD 1962
Cdd:PHA02562 390 KIVKTKSE 397
|
|
| PDZ4_GRIP1-2-like |
cd06686 |
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
220-308 |
3.95e-07 |
|
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467174 [Multi-domain] Cd Length: 99 Bit Score: 50.04 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPTGDFGFSLR----RTTMLDRAPegqayrrVVHFAEPGAGTKDLALgLVPGDRLVEINGQNVENKSRDEIVEM 295
Cdd:cd06686 9 EVILRGDPLKGFGIQLQggvfATETLSSPP-------LISFIEPDSPAERCGV-LQVGDRVLSINGIPTEDRTLEEANQL 80
|
90
....*....|...
gi 600971660 296 IRQSGDSVRLKVQ 308
Cdd:cd06686 81 LRDSASKVTLEIE 93
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1799-1984 |
4.16e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1799 QELQEKLQALQSQVEFLeqsmvdkslvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREK 1878
Cdd:COG1196 216 RELKEELKELEAELLLL---------------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1879 EQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLIN 1958
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180
....*....|....*....|....*.
gi 600971660 1959 SEGDSDVDSELEDRVDGVKSWLSKNK 1984
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAE 386
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1542-1904 |
4.87e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1542 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQ----AKLRLEMEMERMRQThskemesrdeeveEARQSCQKKLK 1617
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQdyqaASDHLNLVQTALRQQ-------------EKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1618 QMEVQLEEEYEDKQKALREKRELESKLSTLSDQVnqrdfesekrlrkdlKRTKALLADAQIMLDHLKnnapsKREIA--Q 1695
Cdd:PRK04863 359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEV---------------DELKSQLADYQQALDVQQ-----TRAIQyqQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1696 LKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQreknEIQNRLEEdqedmneLMKKHKAAVA 1775
Cdd:PRK04863 419 AVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ----AAHSQFEQ-------AYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1776 QASRDMAQmNDLQAQIEESNKEKQELQeKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASR 1855
Cdd:PRK04863 488 EVSRSEAW-DVARELLRRLREQRHLAE-QLQQLRMRLSELEQ---RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 600971660 1856 LKETMEKLTEErdQRAAAENREkeqnkRLQRQLRDTKEEMSELARKEAE 1904
Cdd:PRK04863 563 LEARLESLSES--VSEARERRM-----ALRQQLEQLQARIQRLAARAPA 604
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1690-1921 |
5.04e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.76 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1690 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedMNELMKK 1769
Cdd:COG1340 21 REEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNE----LREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1770 HKAAVAQASRDMAQMNDLQAQIEE----------SNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRL 1839
Cdd:COG1340 97 LRKELAELNKAGGSIDKLRKEIERlewrqqtevlSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1840 EFEKTQVKRLENLASRLKETMEKLTEERDQ-RAAAE-------------NREKEQNKRLQRQLRDTKEEMSELARKEAEA 1905
Cdd:COG1340 177 EEIHKKIKELAEEAQELHEEMIELYKEADElRKEADelhkeiveaqekaDELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
250
....*....|....*.
gi 600971660 1906 SRKKHELEMDLESLEA 1921
Cdd:COG1340 257 KREKEKEELEEKAEEI 272
|
|
| PDZ2-PTPN13_FRMPD2-like |
cd06792 |
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ... |
273-308 |
5.28e-07 |
|
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467254 [Multi-domain] Cd Length: 87 Bit Score: 49.13 E-value: 5.28e-07
10 20 30
....*....|....*....|....*....|....*.
gi 600971660 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06792 51 GDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLVLE 86
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1427-1641 |
5.33e-07 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 52.36 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1427 DESQRALQQLKK----KCQRLTAELQDTKLHLEGQQVRNHELEKKqrrfdselSQAHEETQREKlqreklQREKDMLLAE 1502
Cdd:pfam15665 10 DEHEAEIQALKEaheeEIQQILAETREKILQYKSKIGEELDLKRR--------IQTLEESLEQH------ERMKRQALTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1503 AFSLKQQMEEKDL-DIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL-RDLEAKVKDQEEELDEQAGSIQMLEQAK 1580
Cdd:pfam15665 76 FEQYKRRVEERELkAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFeQEKRKALEELRAKHRQEIQELLTTQRAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 600971660 1581 LRLEM-EMERMRQTHSKEMESRDEEVEEarqscqkkLKQMEVQLEEEYEDK---QKALREkRELE 1641
Cdd:pfam15665 156 SASSLaEQEKLEELHKAELESLRKEVED--------LRKEKKKLAEEYEQKlskAQAFYE-RELE 211
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1622-1996 |
5.62e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1622 QLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQimldhlknnapskREIAQLKNQLE 1701
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------------EELEQLEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1702 ESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAvaqasrdM 1781
Cdd:COG4372 70 QAR-------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL-------E 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1782 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSlvsrQEAKIRELETRLEFEKTQVKRLENLASRLKETME 1861
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS----EAEAEQALDELLKEANRNAEKEEELAEAEKLIES 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1862 KLTEERDQRAAAENREKEQNkRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQ 1941
Cdd:COG4372 212 LPRELAEELLEAKDSLEAKL-GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 600971660 1942 AAIEDEMESDENEDLINSEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDDGSL 1996
Cdd:COG4372 291 AALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1529-1712 |
5.91e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.64 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1529 AELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMER------MRQTH------SK 1596
Cdd:PHA02562 216 ARKQNKYDELVEEAKTI---KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQfqkvikMYEKGgvcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1597 EMESRDEEVEEARQS---CQKKLKQMEVQLEEEYE---DKQKALREKRELESKLSTLsDQVNQRDFESEKRLRKDLKRTK 1670
Cdd:PHA02562 293 QISEGPDRITKIKDKlkeLQHSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTN-KQSLITLVDKAKKVKAAIEELQ 371
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 600971660 1671 ALLADaqimldhlknnapSKREIAQLKNQLEESEFTCAAAVK 1712
Cdd:PHA02562 372 AEFVD-------------NAEELAKLQDELDKIVKTKSELVK 400
|
|
| PDZ2_DLG5-like |
cd06765 |
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
270-308 |
8.55e-07 |
|
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PSZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467246 [Multi-domain] Cd Length: 77 Bit Score: 48.50 E-value: 8.55e-07
10 20 30
....*....|....*....|....*....|....*....
gi 600971660 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06765 35 LTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLM 73
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1581-1931 |
9.12e-07 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 54.09 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1581 LRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQmevQLEEEYEDKQKALrekrELESKLSTLSDqvnqrdfESEK 1660
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKK---EIDLEYTEAVIAM----GLQERLENLRE-------EFSK 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1661 RLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavkarkamevemedlhlQIDDIAKAKTALEE 1740
Cdd:PLN03229 498 ANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLD-------------------------MLNEFSRAKALSEK 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1741 QlSRLQREKNEIQNRLEE--DQEDMNELMKKHKAAVAQ--ASRDMAQMNDLQAQIEESNKEKQ-ELQEKLQALQSQVEFL 1815
Cdd:PLN03229 553 K-SKAEKLKAEINKKFKEvmDRPEIKEKMEALKAEVASsgASSGDELDDDLKEKVEKMKKEIElELAGVLKSMGLEVIGV 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1816 EQsmvdKSLVSRQEAKIRELETRLEFEKTQV-KRLENL--ASRLKETMEKLTEERDQRAAAEN-REKEQNKRLQRQLRDT 1891
Cdd:PLN03229 632 TK----KNKDTAEQTPPPNLQEKIESLNEEInKKIERVirSSDLKSKIELLKLEVAKASKTPDvTEKEKIEALEQQIKQK 707
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 600971660 1892 -KEEMSELARKEaeasrKKHELEMDLESLEAANQSLQADLK 1931
Cdd:PLN03229 708 iAEALNSSELKE-----KFEELEAELAAARETAAESNGSLK 743
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1598-1811 |
1.25e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1598 MESRDEEVEEARQSCQKKLKQMEVQLEEeyedKQKALREKRElESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQ 1677
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQ-KNGLVDLSEEAKLLL-QQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1678 IMLDHLKNNAPSKRE----------IAQLKNQLEESEFTCAAAVK-------ARKAMEVEMEDLHLQIDD-IAKAKTALE 1739
Cdd:COG3206 240 ARLAALRAQLGSGPDalpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQeAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 600971660 1740 EQLSRLQREKNEIQNRLEEdqedmnelmkkHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1811
Cdd:COG3206 320 AELEALQAREASLQAQLAQ-----------LEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1504-1888 |
1.28e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 53.30 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1504 FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEqagSIQMLEQaklRL 1583
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGP---ALDELEK---QL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1584 EmEMERMRQTHSKEMESRDeeVEEAR---QSCQKKLKQMEVQLEE---EYEDKQKALREK-RELESKLSTLSDQ---VNQ 1653
Cdd:PRK04778 175 E-NLEEEFSQFVELTESGD--YVEAReilDQLEEELAALEQIMEEipeLLKELQTELPDQlQELKAGYRELVEEgyhLDH 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1654 RDFESE-KRLRKDLKRTKALLADAQimLDHLK-NNAPSKREIAQLKNQLEeseftcaAAVKARKAMEVEMEDLHLQIDDI 1731
Cdd:PRK04778 252 LDIEKEiQDLKEQIDENLALLEELD--LDEAEeKNEEIQERIDQLYDILE-------REVKARKYVEKNSDTLPDFLEHA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1732 AKAKTALEEQLSRLQ-----------------REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEES 1794
Cdd:PRK04778 323 KEQNKELKEEIDRVKqsytlneselesvrqleKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1795 N-------KEKQELQEKLQALQSQVE----FLEQS---------MVDKSLVSRQeakIRELETRLE---FEKTQVKRLEN 1851
Cdd:PRK04778 403 SemlqglrKDELEAREKLERYRNKLHeikrYLEKSnlpglpedyLEMFFEVSDE---IEALAEELEekpINMEAVNRLLE 479
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 600971660 1852 LASRLKETMEKLTEE-RDQRAAAE------NREKEQNKRLQRQL 1888
Cdd:PRK04778 480 EATEDVETLEEETEElVENATLTEqliqyaNRYRSDNEEVAEAL 523
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1547-1895 |
1.60e-06 |
|
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: 52.93 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1547 KVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQaklrlememermrqthsKEMESRdEEVEEAR---QSCQKKLKQMEVQL 1623
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLE-----------------SEEKNR-EEVEELKdkyRELRKTLLANRFSY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1624 EEEYEDKQKALrekRELESKLSTLSDQVNQRDFESEK----RLRKDLKRTKALLADAQIMLDHLKNNAPskREIAQLKN- 1698
Cdd:pfam06160 145 GPAIDELEKQL---AEIEEEFSQFEELTESGDYLEARevleKLEEETDALEELMEDIPPLYEELKTELP--DQLEELKEg 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1699 --QLEESEFtcaaaVKARKAMEVEMEDLHlqiDDIAKAKTALEE-QLSRLQREKNEIQNRLEEDQEDM-------NELMK 1768
Cdd:pfam06160 220 yrEMEEEGY-----ALEHLNVDKEIQQLE---EQLEENLALLENlELDEAEEALEEIEERIDQLYDLLekevdakKYVEK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1769 KHKAAVAQASRDMAQMNDLQAQIEESNK----------EKQELQEKLQALQSQVEFLEQSMVDKSLV-SRQEAKIRELET 1837
Cdd:pfam06160 292 NLPEIEDYLEHAEEQNKELKEELERVQQsytlneneleRVRGLEKQLEELEKRYDEIVERLEEKEVAySELQEELEEILE 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 1838 RLE-FEKTQVKrlenlasrLKETMEKLTEErdqraaaENREKEQNKRLQRQLRDTKEEM 1895
Cdd:pfam06160 372 QLEeIEEEQEE--------FKESLQSLRKD-------ELEAREKLDEFKLELREIKRLV 415
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1261-1701 |
2.13e-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: 52.90 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1261 EEQIRNKDEEIQQLRSKLEKVEKERNE-------LRLSSDRLETRISELTSELTderntgesasqlldaetaerlRTEKE 1333
Cdd:pfam10174 246 ERNIRDLEDEVQMLKTNGLLHTEDREEeikqmevYKSHSKFMKNKIDQLKQELS---------------------KKESE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1334 MKELQTQYDALK------KQMEVMEMEVMEARLIRAAEINGEVDdddaggEWRLKYERAVREVDFTKKRLQQELEDKmev 1407
Cdd:pfam10174 305 LLALQTKLETLTnqnsdcKQHIEVLKESLTAKEQRAAILQTEVD------ALRLRLEEKESFLNKKTKQLQDLTEEK--- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1408 eqqsrRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE---ETQR 1484
Cdd:pfam10174 376 -----STLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEalsEKER 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1485 --EKLQREKlQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ 1562
Cdd:pfam10174 451 iiERLKEQR-EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1563 EEEldeqagSIQMLEQAKLRLEMEM-ERMRQTHSKEMESRDEEV----EEARQsCQKKLKQM-----EVQLEEEYEDKQK 1632
Cdd:pfam10174 530 KEE------CSKLENQLKKAHNAEEaVRTNPEINDRIRLLEQEVarykEESGK-AQAEVERLlgilrEVENEKNDKDKKI 602
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 1633 ALREKRELESKLSTLSDQVNQRDFESEKRlrkdlKRTKALLADAQIMLDHLKNNApSKREIAQLKNQLE 1701
Cdd:pfam10174 603 AELESLTLRQMKEQNKKVANIKHGQQEMK-----KKGAQLLEEARRREDNLADNS-QQLQLEELMGALE 665
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1256-1949 |
2.33e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.03 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1256 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNEL------------RLSSDRLETRISELTSELTDERNTGESASQllDAE 1323
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqALEKARALCGLPDLTPENAEDYLAAFRAKE--QQA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1324 TAERLRTEKEM---KELQTQYDAlkkqmevmemevmEARLIRAaeINGEVDDDDAggewrlkYERAvREVdftkkrLQQE 1400
Cdd:COG3096 454 TEEVLELEQKLsvaDAARRQFEK-------------AYELVCK--IAGEVERSQA-------WQTA-REL------LRRY 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1401 LEDKMEVEQQSrrQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhlegqqvrNHELEKKQRRFDSELSQAHE 1480
Cdd:COG3096 505 RSQQALAQRLQ--QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-----------AEELEELLAELEAQLEELEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1481 ETQREKLQREKLQREKDMLLAEAFSLKQQmeekdldiAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK 1560
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAAR--------APAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREAT 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1561 DQEEEldeqagsiqmLEQAKLRLEMEMERMRQTHSkemesrdeeVEEARqscqkkLKQME-----VQLEEEYEDkqKALR 1635
Cdd:COG3096 644 VERDE----------LAARKQALESQIERLSQPGG---------AEDPR------LLALAerlggVLLSEIYDD--VTLE 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1636 EKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKRE-----IAQLKN-QLEESEFTcAA 1709
Cdd:COG3096 697 DAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEGDPDSFDDSVFDAEEledavVVKLSDrQWRYSRFP-EV 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1710 AVKARKAMEVEMEDLHLQIDDIAK--AKTAL----------------------------EEQLSRLQREKNEIQNRLEED 1759
Cdd:COG3096 776 PLFGRAAREKRLEELRAERDELAEqyAKASFdvqklqrlhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQH 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1760 QEDmnelMKKHKAAVAQASRDMAQMNDLQAQIEESNKEkqELQEKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRL 1839
Cdd:COG3096 856 RAQ----EQQLRQQLDQLKEQLQLLNKLLPQANLLADE--TLADRLEELREELDAAQE---AQAFIQQHGKALAQLEPLV 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1840 ----------EFEKTQVKRLENLASRLKETMEKLTEERDQRAA----------AENRekEQNKRLQRQLRDTKEEMSElA 1899
Cdd:COG3096 927 avlqsdpeqfEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyedavgllGENS--DLNEKLRARLEQAEEARRE-A 1003
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1900 RKEAEASRKKH-ELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEME 1949
Cdd:COG3096 1004 REQLRQAQAQYsQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAE 1054
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1713-1909 |
2.78e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1713 ARKAMEVEMEDLHLQIDDIAKA-------KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQ-----ASRD 1780
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEieelkekRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelkEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1781 M--AQMNDLQAQIEESNKEKQELQEK---LQALQSQVEFLEQSMVDKSLVSRQE----AKIRELETRLEfektQVKRLEN 1851
Cdd:COG1340 82 ElnEKLNELREELDELRKELAELNKAggsIDKLRKEIERLEWRQQTEVLSPEEEkelvEKIKELEKELE----KAKKALE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 600971660 1852 LASRLKETMEKLTEERDQRAAAENREKEQNKRLQRqlrdTKEEMSELaRKEAEASRKK 1909
Cdd:COG1340 158 KNEKLKELRAELKELRKEAEEIHKKIKELAEEAQE----LHEEMIEL-YKEADELRKE 210
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1262-1667 |
3.34e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1262 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQY 1341
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1342 DALKKQMEVMEMEVMEARLIRAA----EINGEVDDD---DAGGEWRLKYEravrevdftkkRLQQELEDkMEVEQQSRRQ 1414
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLEAgkcpECGQPVEGSphvETIEEDRERVE-----------ELEAELED-LEEEVEEVEE 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1415 LERRLGDLQADSDESQRALQQLKKKCQRLT---AELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREK 1491
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAerrETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1492 LQREKDMLLAEAFSLkQQMEEKDLDIAGFTQKVVSLEAELQDIssQESKDEAslakvKKQLRDLEAKVKDQEEELDEQAg 1571
Cdd:PRK02224 577 LNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREAL--AELNDER-----RERLAEKRERKRELEAEFDEAR- 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1572 sIQMLEQAKLRLEMEMErmrqthskEMESRDEEVEEARQSCQKKLKQMEVQLE--EEYEDKQKALREKRElesKLSTLSD 1649
Cdd:PRK02224 648 -IEEAREDKERAEEYLE--------QVEEKLDELREERDDLQAEIGAVENELEelEELRERREALENRVE---ALEALYD 715
|
410
....*....|....*...
gi 600971660 1650 QVNQRDfESEKRLRKDLK 1667
Cdd:PRK02224 716 EAEELE-SMYGDLRAELR 732
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1268-1569 |
3.64e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1268 DEEIQQLRSKLEKVEKERNELRLSSDRLEtrisELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQ 1347
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1348 MEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMeveqqsrRQLERRLGDLQADSD 1427
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAM-------RAFNREWPAETADLD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1428 ESQRALQQLKKKCQRLTAElqdtklHLEGQQVRNHELEKKQ-----RRFDSELSQAHEETqreklqREKLQREKDMLLAE 1502
Cdd:COG4913 809 ADLESLPEYLALLDRLEED------GLPEYEERFKELLNENsiefvADLLSKLRRAIREI------KERIDPLNDSLKRI 876
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 600971660 1503 AFS----LKQQMEE-KDLDIAGFTQkvvsleaELQDISSQESKDEASLAKVK-KQLRDLEAKVKDQEEELDEQ 1569
Cdd:COG4913 877 PFGpgryLRLEARPrPDPEVREFRQ-------ELRAVTSGASLFDEELSEARfAALKRLIERLRSEEEESDRR 942
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1773-1947 |
3.90e-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: 50.31 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1773 AVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKTQVKRLEN 1851
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAaKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1852 LASRLK-----ETMEK-LTEERDQRAAAENREKEQNKRLqrqlrDTKEEmsELARKEAEASRKKHELEMDLESLEAANQS 1925
Cdd:COG1579 81 QLGNVRnnkeyEALQKeIESLKRRISDLEDEILELMERI-----EELEE--ELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|..
gi 600971660 1926 LQADLKLAFKRIGDLQAAIEDE 1947
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPE 175
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1552-1902 |
3.92e-06 |
|
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: 51.07 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1552 LRDLEAKV------KDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEE-VEEARQSCQKKLKQMEVQLE 1624
Cdd:pfam13868 8 LRELNSKLlaakcnKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEErKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1625 EEYEDKQKALREKRELesklstLSDQVNQRDFESEKRLRKDLKRTKAlladaqimldhlknnapsKREIAQLKNQLEese 1704
Cdd:pfam13868 88 KRQEEYEEKLQEREQM------DEIVERIQEEDQAEAEEKLEKQRQL------------------REEIDEFNEEQA--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1705 ftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQ----REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRD 1780
Cdd:pfam13868 141 -------EWKELEKEEEREEDERILEYLKEKAEREEEREAEReeieEEKEREIARLRAQQEKAQDEKAERDELRAKLYQE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1781 MAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV-----DKSLVSRQEAKIRELEtRLEFEKTQVKRLENLasR 1855
Cdd:pfam13868 214 EQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAeeaerEEEEFERMLRKQAEDE-EIEQEEAEKRRMKRL--E 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 600971660 1856 LKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKE 1902
Cdd:pfam13868 291 HRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1402-1824 |
4.24e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1402 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKkkcqRLTAelqdTKLHLEGQQVRNHELEKKQRR---FDSELSQA 1478
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFS----RFIG----SHLAVAFEADPEAELRQLNRRrveLERALADH 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1479 HEETQREKLQREKLQREKDML--LAEAFSLkqqmeekdLDIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLrdle 1556
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALnrLLPRLNL--------LADETLADRVEEIREQLD----EAEEAKRFVQQHGNAL---- 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1557 akvkdqeEELDEQAGSIQMLEQaklrlemEMERMRQthskemesrdeEVEEARQScQKKLKQ--------MEVQLEEEYE 1628
Cdd:PRK04863 921 -------AQLEPIVSVLQSDPE-------QFEQLKQ-----------DYQQAQQT-QRDAKQqafaltevVQRRAHFSYE 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1629 DKQKALREKRELESKLSTLSDQVNQ-RDfesekRLRKDLKRTKALLADAQIMLDHLKNNAPSKREI-AQLKNQLEesEFT 1706
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQeRT-----RAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMlQELKQELQ--DLG 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1707 CAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA--QASRDMAQM 1784
Cdd:PRK04863 1048 VPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwCAVLRLVKD 1127
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 600971660 1785 NDLqaqieesnkEKQELQEKLQALQSQVeflEQSMVDKSL 1824
Cdd:PRK04863 1128 NGV---------ERRLHRRELAYLSADE---LRSMSDKAL 1155
|
|
| PDZ_Par6-like |
cd06718 |
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ... |
222-297 |
4.76e-06 |
|
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par6-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467202 [Multi-domain] Cd Length: 84 Bit Score: 46.41 E-value: 4.76e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 222 ELQRRPTGDFGFSLRRTTMLDRAPeGQAYRRVVhfaePGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIR 297
Cdd:cd06718 4 ELIKPPGKPLGFYIRDGNGVERVP-GIFISRLV----LG-SLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMV 73
|
|
| PDZ4_PTPN13-like |
cd06696 |
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ... |
220-307 |
4.99e-06 |
|
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)] and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467182 [Multi-domain] Cd Length: 85 Bit Score: 46.53 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPTGDFGFSLRRTTMldraPEGQAYRRVVHfaEPgagtkdlALG---LVPGDRLVEINGQNVENKSRDEIVEMI 296
Cdd:cd06696 5 EVTLTKSEKGSLGFTVTKGKD----DNGCYIHDIVQ--DP-------AKSdgrLRPGDRLIMVNGVDVTNMSHTEAVSLL 71
|
90
....*....|.
gi 600971660 297 RQSGDSVRLKV 307
Cdd:cd06696 72 RAAPKEVTLVL 82
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1539-1654 |
5.09e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 51.68 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1539 SKDEASLAKVkkqLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthskemESRDEEVEEARQSCQKKLKQ 1618
Cdd:COG1193 510 GEESIDVEKL---IEELERERRELEEEREEAERLREELEKLREELEEKLEELE-------EEKEEILEKAREEAEEILRE 579
|
90 100 110
....*....|....*....|....*....|....*....
gi 600971660 1619 MEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQR 1654
Cdd:COG1193 580 ARKEAEElirELREAQAEEEELKEARKKLEELKQELEEK 618
|
|
| PDZ3_Dlg1-2-4-like |
cd06795 |
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ... |
237-312 |
5.31e-06 |
|
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467257 [Multi-domain] Cd Length: 91 Bit Score: 46.58 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 237 RTTMLDRAPEGQAYRRV---------VHFAEPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06795 3 RKIVLHKGSTGLGFNIVggedgegifISFILAG-GPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTIIA 81
|
....*
gi 600971660 308 QPIPE 312
Cdd:cd06795 82 QYKPE 86
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1483-1673 |
5.36e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1483 QREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQK--VVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK 1560
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1561 DQEEELDE---------QAGSIQMLEQAKLRLEMEMERMRQTHSKE---MESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1628
Cdd:COG3206 244 ALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 600971660 1629 DKQKALREKRELESKLSTLSDQVNQRDFESEkRLRKDLKRTKALL 1673
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELR-RLEREVEVARELY 367
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1413-1569 |
5.38e-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: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1413 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLhlegqQVRNHELEKKQrrfdselSQAHEETQREKLQREKL 1492
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK-----EIKRLELEIEE-------VEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1493 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1569
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1474-1664 |
5.48e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1474 ELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQlR 1553
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1554 DLEAKVKdqeeELDEQAGSIQMLEQAKLRLEMEMERMRqthskemesrdEEVEEARQSCQKKLKQMEvQLEEEYEDKQKA 1633
Cdd:COG1579 90 EYEALQK----EIESLKRRISDLEDEILELMERIEELE-----------EELAELEAELAELEAELE-EKKAELDEELAE 153
|
170 180 190
....*....|....*....|....*....|..
gi 600971660 1634 LREKRE-LESKLSTLSDQVNQRDFESEKRLRK 1664
Cdd:COG1579 154 LEAELEeLEAEREELAAKIPPELLALYERIRK 185
|
|
| PDZ1_PTPN13_FRMPD2-like |
cd06694 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ... |
258-305 |
6.02e-06 |
|
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467180 [Multi-domain] Cd Length: 92 Bit Score: 46.62 E-value: 6.02e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 600971660 258 EPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRL 305
Cdd:cd06694 38 IPG-GPADKDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVEL 84
|
|
| PDZ4_Scribble-like |
cd06701 |
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ... |
220-307 |
6.23e-06 |
|
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467185 [Multi-domain] Cd Length: 98 Bit Score: 46.45 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPTGDFGFSLR------RTTMLDRAPEGQAYRRVVHfaePGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEI 292
Cdd:cd06701 6 ELTIVKEPGEKLGISIRggakghAGNPLDPTDEGIFISKINP---DGAAARD---GrLKVGQRILEVNGQSLLGATHQEA 79
|
90
....*....|....*
gi 600971660 293 VEMIRQSGDSVRLKV 307
Cdd:cd06701 80 VRILRSVGDTLTLLV 94
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1322-1570 |
7.08e-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: 50.53 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1322 AETAERLRTEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDDDDaggewrlkyeravREVDFTKKRLqQEL 1401
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK--------EEKALLKQLAALE-------------RRIAALARRI-RAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1402 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLtAELQDTKLHLEGQQVRnhELEKKQRRFDSELSQAHEE 1481
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1482 TQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1561
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
....*....
gi 600971660 1562 QEEELDEQA 1570
Cdd:COG4942 232 LEAEAAAAA 240
|
|
| PDZ_MPP-like |
cd06726 |
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ... |
273-309 |
7.21e-06 |
|
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467208 [Multi-domain] Cd Length: 80 Bit Score: 45.72 E-value: 7.21e-06
10 20 30
....*....|....*....|....*....|....*..
gi 600971660 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06726 44 GDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLIP 80
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1547-1702 |
7.39e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1547 KVKKQLRDLEAKVKDQEEELDEQAGSIQmlEQAKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEE 1626
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKL----EKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1627 YEDKQKALREKRELESKLSTLSDQVNQRDFESEK---RLRKDLKRTKALLAD--AQIMLDHLKNNApsKREIAQLKNQLE 1701
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEElieEQLQELERISGLTAEeaKEILLEKVEEEA--RHEAAVLIKEIE 179
|
.
gi 600971660 1702 E 1702
Cdd:PRK12704 180 E 180
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1657-1956 |
8.01e-06 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 50.19 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1657 ESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMevemedlhlqiddiAKAKT 1736
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSL--------------SASVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1737 ALEEQLSRLQREKNEIQNRLEED--QEDMN----ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQS 1810
Cdd:pfam15905 126 SLEKQLLELTRVNELLKAKFSEDgtQKKMSslsmELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1811 QVEFLEQSMVDkslvsrqeakireletrlefEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD 1890
Cdd:pfam15905 206 KLVSTEKEKIE--------------------EKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQS 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1891 TKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKlafKRIGDLQAAIedEMESDENEDL 1956
Cdd:pfam15905 266 LEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN---AELEELKEKL--TLEEQEHQKL 326
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1613-1954 |
8.27e-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: 50.73 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1613 QKKLKQMEVQ-LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLR--KDLKRTKALLadaQIMLDHLKNNAPS 1689
Cdd:COG5185 165 FGKLTQELNQnLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGseSTLLEKAKEI---INIEEALKGFQDP 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1690 KREIAQLKNQLEESEFtcaaAVKARKamEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE-----DQEDMN 1764
Cdd:COG5185 242 ESELEDLAQTSDKLEK----LVEQNT--DLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSidikkATESLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1765 ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqSMVDKSLVSRQEAKIRELETRLEFEKT 1844
Cdd:COG5185 316 EQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIE----NIVGEVELSKSSEELDSFKDTIESTKE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1845 ----QVKRLENLASRLKETMEKLTEERDQraaaenrekeQNKRLQRQLRDTKEEMSELARK--EAEASRKKHELEMDLES 1918
Cdd:COG5185 392 sldeIPQNQRGYAQEILATLEDTLKAADR----------QIEELQRQIEQATSSNEEVSKLlnELISELNKVMREADEES 461
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 600971660 1919 LE-------AANQSLQADLKLAFKRIGDLQAAIEDEMESDENE 1954
Cdd:COG5185 462 QSrleeaydEINRSVRSKKEDLNEELTQIESRVSTLKATLEKL 504
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
550-829 |
8.69e-06 |
|
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: 50.90 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 550 LLEAFGNSPTIMNGSATRFSQILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEA------TFNVFYYLLACGD 618
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 619 A-----TLRTELHLNHL----------AENNVFGIVplSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYH 683
Cdd:cd14894 335 AfpfmrLLAKELHLDGIdcsaltylgrSDHKLAGFV--SKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLW 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 684 LGaaGATKEAAEAGRKQFARHEWAQKAAYLLgCSLEELSSAifkHQLKGGTLQRSTSFRQGPE--ESGLGEGtklSALEC 761
Cdd:cd14894 413 LG--NIELDYREVSGKLVMSSTGALNAPQKV-VELLELGSV---EKLERMLMTKSVSLQSTSEtfEVTLEKG---QVNHV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 762 LEGMASGLYSELFTLLISLVNRALKSS-------QHSLCS----------MMIVDTPGFQNpewggsARGASFEELCHNY 824
Cdd:cd14894 484 RDTLARLLYQLAFNYVVFVMNEATKMSalstdgnKHQMDSnasapeavslLKIVDVFGFED------LTHNSLDQLCINY 557
|
....*
gi 600971660 825 AQDRL 829
Cdd:cd14894 558 LSEKL 562
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1542-1902 |
8.91e-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: 51.11 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1542 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQ----AKLRLEMEMERMRQThsKEMESRDEEVEEArqscQKKLK 1617
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQdyqaASDHLNLVQTALRQQ--EKIERYQEDLEEL----TERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1618 QMEVQLEEEYEDKQKAlREKRElesklstlsdqvnqrdfesekRLRKDLKRTKALLADAQIMLDHLKNNAPSKReiaQLK 1697
Cdd:COG3096 365 EQEEVVEEAAEQLAEA-EARLE---------------------AAEEEVDSLKSQLADYQQALDVQQTRAIQYQ---QAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1698 NQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEedqedmneLMKKHKAAVaqa 1777
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE--------LVCKIAGEV--- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1778 srDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELEtrlEFEKTQVKRLENlASRLK 1857
Cdd:COG3096 489 --ERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQ------RLRQQQNAERLLE---EFCQRIGQQLDA-AEELE 556
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 600971660 1858 ETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKE 1902
Cdd:COG3096 557 ELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1696-1930 |
1.19e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1696 LKNQLEESEFTCAAAVKARKAMEVEMEDlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1775
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREK---EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1776 QASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKTQVKRLENLAS 1854
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERmKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1855 RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD----------TKEEMSELARKEAEASRKKHELEMDLESLEAANQ 1924
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTahrkeaeneaLLEELRSLQERLNASERKVEGLGEELSSMAAQRD 268
|
....*.
gi 600971660 1925 SLQADL 1930
Cdd:pfam07888 269 RTQAEL 274
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1409-1742 |
1.37e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1409 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQ 1488
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1489 REKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR-----DLEAKVKDQE 1563
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1564 EELDEQAGSIQMLEQAKLRLEMEMERMRQTHS--KEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELE 1641
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1642 SKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEM 1721
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
|
330 340
....*....|....*....|.
gi 600971660 1722 EDLHLQIDDIAKAKTALEEQL 1742
Cdd:COG4372 350 LLDNDVLELLSKGAEAGVADG 370
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1400-1775 |
1.39e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1400 ELEDKMEVEQQSRRQLERRLGDLQADSDESQRA----LQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSEL 1475
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKalfeLDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1476 SQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEkdldiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDL 1555
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1556 EAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEearqscqKKLKQMEVQLEEEYEDKQKALR 1635
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE-------KLIESLPRELAEELLEAKDSLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1636 EKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARK 1715
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1716 AMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1775
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1261-1930 |
1.46e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1261 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQ 1340
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1341 YDALKKQMEVMEMEVmeARLIRAAEINGE-VDDDDAGGEWRLKYERAVREVDFTKKRLQQEledKMEVEQQSRRQLerrl 1419
Cdd:COG3096 594 IKELAARAPAWLAAQ--DALERLREQSGEaLADSQEVTAAMQQLLEREREATVERDELAAR---KQALESQIERLS---- 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1420 gdlQADSDESQRaLQQLkkkCQRLTAEL-----QDTKLH-------LEGQQ-----VRNHELEKKQ-------------- 1468
Cdd:COG3096 665 ---QPGGAEDPR-LLAL---AERLGGVLlseiyDDVTLEdapyfsaLYGPArhaivVPDLSAVKEQlagledcpedlyli 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1469 ----RRFDSELSQAHEETQREKLQREKLQ----------------REK--DMLLAEAFSLKQQMEEKDLDIagftQKVVS 1526
Cdd:COG3096 738 egdpDSFDDSVFDAEELEDAVVVKLSDRQwrysrfpevplfgraaREKrlEELRAERDELAEQYAKASFDV----QKLQR 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1527 LEAELQDISSQ------ESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAgsiQMLEQAKLRLEMEMERMRQTHSKEMES 1600
Cdd:COG3096 814 LHQAFSQFVGGhlavafAPDPEAELAALRQRRSELERELAQHRAQEQQLR---QQLDQLKEQLQLLNKLLPQANLLADET 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1601 RDEEVEEARqscqkklkqmevqleEEYEDKQKALREKRELESKLSTLSDQVN--QRDFESEKRLRKDLKRTKALLADAQI 1678
Cdd:COG3096 891 LADRLEELR---------------EELDAAQEAQAFIQQHGKALAQLEPLVAvlQSDPEQFEQLQADYLQAKEQQRRLKQ 955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1679 MLDHLKNnapskreiaqlknqleeseftcaaaVKARKAmevemedlHLQIDDIAKaktaleeqlsrlqrekneiqnRLEE 1758
Cdd:COG3096 956 QIFALSE-------------------------VVQRRP--------HFSYEDAVG---------------------LLGE 981
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1759 DQeDMNELMKkHKAAVAQASRDMA--QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA 1830
Cdd:COG3096 982 NS-DLNEKLR-ARLEQAEEARREAreQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqADAEAEERARI 1059
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1831 KIRELETRL--------EFEKTQVKR---LENLASRLKETMEKLTEERDQRAAAenreKEQNKRLQRQLRDTKEE----M 1895
Cdd:COG3096 1060 RRDELHEELsqnrsrrsQLEKQLTRCeaeMDSLQKRLRKAERDYKQEREQVVQA----KAGWCAVLRLARDNDVErrlhR 1135
|
730 740 750
....*....|....*....|....*....|....*
gi 600971660 1896 SELARKEAEASRkkhelEMDLESLEAANQSlQADL 1930
Cdd:COG3096 1136 RELAYLSADELR-----SMSDKALGALRLA-VADN 1164
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1477-1703 |
1.50e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1477 QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagfTQKVVSLEAELQDIssqeskdEASLAKVKKQLRDLE 1556
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEEL-------NEEYNELQAELEAL-------QAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1557 AKVKDQEEELDEQAGSIQMLEQAKLRLEM---------------EMERMRQTHSKEMesrdEEVEEARQSCQKKLKQMEV 1621
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDVllgsesfsdfldrlsALSKIADADADLL----EELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1622 QLEEEYEDKQKALREKRELESKLSTLSDQVNQrdfesekrLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLE 1701
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQ--------LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
..
gi 600971660 1702 ES 1703
Cdd:COG3883 227 AA 228
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1256-1813 |
1.55e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 50.60 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1256 QVQLSEEQIRNkdeEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESasqllDAETAERLRTEKEMK 1335
Cdd:PTZ00440 788 TILNKENKISN---DINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPT-----EDENLNLKELEKEFN 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1336 ELQTQYDALKKQMEvmemevmearliraaEINGEVDdddaggewrlkyerAVREVDFTKKRL---QQELEDKMEVEQQSR 1412
Cdd:PTZ00440 860 ENNQIVDNIIKDIE---------------NMNKNIN--------------IIKTLNIAINRSnsnKQLVEHLLNNKIDLK 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1413 RQLERRLGDLQADS----DESQRALQQLKKKCQRLTAELQDTK---LHLEGQQVRNHeLEKKQRRFDSELSQAHEETQRE 1485
Cdd:PTZ00440 911 NKLEQHMKIINTDNiiqkNEKLNLLNNLNKEKEKIEKQLSDTKinnLKMQIEKTLEY-YDKSKENINGNDGTHLEKLDKE 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1486 KLQREKLQREKDMLLAEAFSLKQQM-------------------EEKDLDIAGFTQKVVSLEAELQD-ISSQESKDEASL 1545
Cdd:PTZ00440 990 KDEWEHFKSEIDKLNVNYNILNKKIddlikkqhddiielidkliKEKGKEIEEKVDQYISLLEKMKTkLSSFHFNIDIKK 1069
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1546 ---AKVKKQLRDLEAKVKDQEEELDEQAGSIqmlEQAKLRLEMEMERMRqthsKEMESRDEEVEEARQSCQKKLKQMEVQ 1622
Cdd:PTZ00440 1070 yknPKIKEEIKLLEEKVEALLKKIDENKNKL---IEIKNKSHEHVVNAD----KEKNKQTEHYNKKKKSLEKIYKQMEKT 1142
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1623 LEE--EYEDKQKALRE--KRELESKLSTLSDQVNQRDFESEKR--LRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQL 1696
Cdd:PTZ00440 1143 LKEleNMNLEDITLNEvnEIEIEYERILIDHIVEQINNEAKKSktIMEEIESYKKDIDQVKKNMSKERNDHLTTFEYNAY 1222
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1697 KNQLEESEFTCAAAVKARKAMEVEMEDlHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdQEDMNELMK--KHKAAV 1774
Cdd:PTZ00440 1223 YDKATASYENIEELTTEAKGLKGEANR-STNVDELKEIKLQVFSYLQQVIKENNKMENALHE-IKNMYEFLIsiDSEKIL 1300
|
570 580 590
....*....|....*....|....*....|....*....
gi 600971660 1775 AQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVE 1813
Cdd:PTZ00440 1301 KEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAK 1339
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1467-1874 |
1.69e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.29 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1467 KQRRFDSElsqaheETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLD-IAGFTQKVVSLEAELQDISSQesKDEASL 1545
Cdd:PLN02939 38 RRRGFSSQ------QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtVMELPQKSTSSDDDHNRASMQ--RDEAIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1546 AKVKKQLRdleaKVKDQEEELDEQAGS-IQMLEQAklrlEMEMERMRQTHSKEMESRDEEVEEaRQSCQKKLKQMEVQLE 1624
Cdd:PLN02939 110 AIDNEQQT----NSKDGEQLSDFQLEDlVGMIQNA----EKNILLLNQARLQALEDLEKILTE-KEALQGKINILEMRLS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1625 EEYEDKQKALREKRELEsklsTLSDQVNQRDFESEKRLRKDLKRTKALLADaqimLDHLK-NNAPSKREIAQLKNQL--- 1700
Cdd:PLN02939 181 ETDARIKLAAQEKIHVE----ILEEQLEKLRNELLIRGATEGLCVHSLSKE----LDVLKeENMLLKDDIQFLKAELiev 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1701 EESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEIqnrLEEDQEDMNELMKKHKAAVAQASRD 1780
Cdd:PLN02939 253 AETEERVFKLEKERSLLDASLRELESKF-------IVAQEDVSKLSPLQYDC---WWEKVENLQDLLDRATNQVEKAALV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1781 MAQMNDLQAQI---EESNKEKQELQEKLQalqsQVEFLEQSMvdKSLVSRQEAKIRELETrlefektQVKRLENLASRLK 1857
Cdd:PLN02939 323 LDQNQDLRDKVdklEASLKEANVSKFSSY----KVELLQQKL--KLLEERLQASDHEIHS-------YIQLYQESIKEFQ 389
|
410
....*....|....*..
gi 600971660 1858 ETMEKLTEERDQRAAAE 1874
Cdd:PLN02939 390 DTLSKLKEESKKRSLEH 406
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1412-1836 |
2.08e-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: 49.64 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1412 RRQLERRLGDLQADSDESQRALQ-------QLKKKCQRLTAELQDTKLHLEGQQVrnhelEKKQRRFDSELSQ------- 1477
Cdd:pfam05701 37 RKLVELELEKVQEEIPEYKKQSEaaeaakaQVLEELESTKRLIEELKLNLERAQT-----EEAQAKQDSELAKlrveeme 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1478 ---AHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEkdldiagfTQKVVSLEAELQDISSQESKDEASLAK-VKKQLR 1553
Cdd:pfam05701 112 qgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELES--------LRKEYASLVSERDIAIKRAEEAVSASKeIEKTVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1554 DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKlKQMEVQLEEEYEdkqKA 1633
Cdd:pfam05701 184 ELTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQLLSA-KDLKSKLETASA---LL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1634 LREKREL----ESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIA-QLKNQLEEsEFTCA 1708
Cdd:pfam05701 260 LDLKAELaaymESKLKEEADG-EGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAaSLRSELEK-EKAEL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1709 AAVKARKAMEvemedlhlqiddiAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKhkaaVAQASRDMAQMNDLQ 1788
Cdd:pfam05701 338 ASLRQREGMA-------------SIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQ----LQQAAQEAEEAKSLA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 600971660 1789 AQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvSRQEAKIRELE 1836
Cdd:pfam05701 401 QAAREELRKAKEEAEQAKAAASTVE------------SRLEAVLKEIE 436
|
|
| CtpA |
COG0793 |
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
269-309 |
2.15e-05 |
|
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440556 [Multi-domain] Cd Length: 341 Bit Score: 48.71 E-value: 2.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 600971660 269 GLVPGDRLVEINGQNVENKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:COG0793 88 GIKPGDIILAIDGKSVAGLTLDDAVKLLRgKAGTKVTLTIKR 129
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1603-1921 |
2.17e-05 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 49.29 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1603 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDF----------ESEKRLRKDLKRTKAL 1672
Cdd:pfam15070 18 ENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAeeeqppagpsEEEQRLQEEAEQLQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1673 LADAQIML-DHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKT---ALEEQLSRLQ-- 1746
Cdd:pfam15070 98 LEALAGQLqAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILEDMQSDRATISRALSqnrELKEQLAELQng 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1747 -----REKNEIQNRLEEDQEDMNELMKKhkaaVAQASRDMAQMNDlqaQIEESNKEKQELQEK----LQALQSQVEFLEQ 1817
Cdd:pfam15070 178 fvkltNENMELTSALQSEQHVKKELAKK----LGQLQEELGELKE---TLELKSQEAQSLQEQrdqyLAHLQQYVAAYQQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1818 SMVDKSLVSRQEAKIRELETRLEFEKTQVK-RLENLASRLKETMEKLTeerdqrAAAenrekEQNKRLQRQLRDTKEEMS 1896
Cdd:pfam15070 251 LASEKEELHKQYLLQTQLMDRLQHEEVQGKvAAEMARQELQETQERLE------ALT-----QQNQQLQAQLSLLANPGE 319
|
330 340
....*....|....*....|....*....
gi 600971660 1897 ----ELARKEAEASRKKHELEMDLESLEA 1921
Cdd:pfam15070 320 gdglESEEEEEEAPRPSLSIPEDFESREA 348
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1495-1817 |
2.77e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1495 EKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEAS-------LAKVKKQLR-------------D 1554
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDyqaasdhLNLVQTALRqqekieryqadleE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1555 LEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMR-------------QTHSKEMESRDEEVEEARQSCQK---KLKQ 1618
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqaldvqQTRAIQYQQAVQALERAKQLCGLpdlTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1619 MEVQLEEeYEDKQKALREK-RELESKLSTLSDQVNQRD------------------FESEKRLRKDLKRTKALLADAQIM 1679
Cdd:PRK04863 440 AEDWLEE-FQAKEQEATEElLSLEQKLSVAQAAHSQFEqayqlvrkiagevsrseaWDVARELLRRLREQRHLAEQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1680 LDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE- 1758
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRl 598
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 600971660 1759 ---------DQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQ 1817
Cdd:PRK04863 599 aarapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| PDZ2_Par3-like |
cd23058 |
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ... |
260-307 |
3.24e-05 |
|
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP, Drosophila Bazooka) and related domains. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include Par3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467271 [Multi-domain] Cd Length: 93 Bit Score: 44.55 E-value: 3.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 600971660 260 GAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQS--GDSVRLKV 307
Cdd:cd23058 43 GAAIQD---GrLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTklGGTVSLVV 90
|
|
| PDZ_6 |
pfam17820 |
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. |
269-308 |
3.33e-05 |
|
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
Pssm-ID: 436067 [Multi-domain] Cd Length: 54 Bit Score: 43.29 E-value: 3.33e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 600971660 269 GLVPGDRLVEINGQNVENKsrDEIVEMIRQSGDS-VRLKVQ 308
Cdd:pfam17820 15 GLRVGDVILAVNGKPVRSL--EDVARLLQGSAGEsVTLTVR 53
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1603-1911 |
3.83e-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: 48.80 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1603 EEVEEARQSCQKKLKQMEvQLEEEYED--------KQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRtkallA 1674
Cdd:COG5185 232 EEALKGFQDPESELEDLA-QTSDKLEKlveqntdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKS-----I 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1675 DAQIMLDHLKNNAPSKREIAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL--EEQLSRLQREKNEI 1752
Cdd:COG5185 306 DIKKATESLEEQLAAAEAEQELEESKRETE---TGIQNLTAEIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDSF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1753 QNRLE----EDQEDMNELMKKHKAAVAQASRDMA----QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSL 1824
Cdd:COG5185 383 KDTIEstkeSLDEIPQNQRGYAQEILATLEDTLKaadrQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1825 VSRQEAK---IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARK 1901
Cdd:COG5185 463 SRLEEAYdeiNRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALE 542
|
330
....*....|
gi 600971660 1902 EAEASRKKHE 1911
Cdd:COG5185 543 NLIPASELIQ 552
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1508-1807 |
3.85e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1508 QQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdqeeELDEQAGSIQMLEQAKLRLEMEM 1587
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK----ELREEAQELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1588 ERMRQTHSKEMESRDEEVEEarqscQKKLKQMEVQLEEEYEDKQKALrekRELESKLstlsdQVNQRDFESEKRLRKDLK 1667
Cdd:COG1340 77 KEERDELNEKLNELREELDE-----LRKELAELNKAGGSIDKLRKEI---ERLEWRQ-----QTEVLSPEEEKELVEKIK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1668 RTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQR 1747
Cdd:COG1340 144 ELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1748 EKNEIQNRLEEDQEDMNELMKKHKAAvaqasRDMAQMNDLQAQIEESNKEKQELQEKLQA 1807
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKL-----RKKQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1520-1587 |
3.88e-05 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 46.46 E-value: 3.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1520 FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQML--EQAKLRLEMEM 1587
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLqdELVALQLQLNM 145
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1402-1955 |
3.90e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1402 EDKMEVEQQSRRQLE----RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNH---------ELEKKQ 1468
Cdd:PRK10246 231 EEKQLLTAQQQQQQSlnwlTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHweriqeqsaALAHTR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1469 RRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDlDIAGFTQKVVSLEAELqdisSQESKDEASLAKV 1548
Cdd:PRK10246 311 QQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHD-RFRQWNNELAGWRAQF----SQQTSDREQLRQW 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1549 KKQLRDLEAKVKDQEE-----ELDEQAGSI-QMLEQAKLRlememERMRQTHSK--EMESRDEEVEEARQSCQKKLKQME 1620
Cdd:PRK10246 386 QQQLTHAEQKLNALPAitltlTADEVAAALaQHAEQRPLR-----QRLVALHGQivPQQKRLAQLQVAIQNVTQEQTQRN 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1621 VQLEEeyedKQKALREKRELESKLSTLSDQvnqrdfesEKRLrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKnqL 1700
Cdd:PRK10246 461 AALNE----MRQRYKEKTQQLADVKTICEQ--------EARI-KDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALE--P 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1701 EESEFTCAAAVKARKAMEVEMEDLHLQIDdiakaktALEEQLsrlQREKNEIQNRLEEDQEdmneLMKKHKAAVAQASRD 1780
Cdd:PRK10246 526 GVNQSRLDALEKEVKKLGEEGAALRGQLD-------ALTKQL---QRDESEAQSLRQEEQA----LTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1781 MAQMNDLQAQIEESNKEKQELQE--KLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFEKTQVK-RLENLASRLK 1857
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHERQLRLlsQRHELQGQIA-------------AHNQQIIQYQQQIEQRQQQLLtALAGYALTLP 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1858 ETMEKLT--EERDQRAAAENREKEQNKRLQRQ------LRDTKEEMSELARKEAEAS----RKKHElemDLESLEAANQS 1925
Cdd:PRK10246 659 QEDEEASwlATRQQEAQSWQQRQNELTALQNRiqqltpLLETLPQSDDLPHSEETVAldnwRQVHE---QCLSLHSQLQT 735
|
570 580 590
....*....|....*....|....*....|
gi 600971660 1926 LQADLKLAFKRIGDLQAAIEDEMESDENED 1955
Cdd:PRK10246 736 LQQQDVLEAQRLQKAQAQFDTALQASVFDD 765
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1601-1942 |
3.95e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1601 RDEEVEEArQSCQKKLKQMEVQLEEEyedkQKALREkreLESKLSTLSdqvnqrdfESEKRLRKDLKRTKALLADAQIML 1680
Cdd:PRK04863 281 RRVHLEEA-LELRRELYTSRRQLAAE----QYRLVE---MARELAELN--------EAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1681 DHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKA----KTALEEQLSRLQREKNEIQnRL 1756
Cdd:PRK04863 345 RQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladyQQALDVQQTRAIQYQQAVQ-AL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1757 EEDQEdMNELMKkhkAAVAQASRDMAQmndLQAQIEESNKEKQELQEKL---QALQSQVEF---LEQSMVDKslVSRQEA 1830
Cdd:PRK04863 424 ERAKQ-LCGLPD---LTADNAEDWLEE---FQAKEQEATEELLSLEQKLsvaQAAHSQFEQayqLVRKIAGE--VSRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1831 K--IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDqraaAENREKEQNKRLQRQLRDtkEEMSELARKEAEASRK 1908
Cdd:PRK04863 495 WdvARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQR----AERLLAEFCKRLGKNLDD--EDELEQLQEELEARLE 568
|
330 340 350
....*....|....*....|....*....|....
gi 600971660 1909 KHELEmdLESLEAANQSLQADLKLAFKRIGDLQA 1942
Cdd:PRK04863 569 SLSES--VSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1587-1933 |
4.15e-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: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1587 MERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQ----LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFE----- 1657
Cdd:pfam07111 21 LERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEgsqaLSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRleaqa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1658 --------SEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEMEDLHLQID 1729
Cdd:pfam07111 101 meldalavAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLT-QAHEEALSSLTSKAEGLEKSLN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1730 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMN---ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ 1806
Cdd:pfam07111 180 SLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEaqvTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1807 ALQSQVEFLE---QSMVdKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEerdQRAAAENREKEQNKR 1883
Cdd:pfam07111 260 DLQATVELLQvrvQSLT-HMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---QLKAQDLEHRDSVKQ 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 600971660 1884 LQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLA 1933
Cdd:pfam07111 336 LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRA 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1402-1611 |
4.82e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1402 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEE 1481
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1482 TQREKLQREKLqrekDMLL-AEAFS--------LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL 1552
Cdd:COG3883 95 LYRSGGSVSYL----DVLLgSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 1553 RDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS 1611
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1613-1928 |
4.93e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 48.21 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1613 QKKLKQMEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS 1689
Cdd:pfam09731 124 QEKEKALEEVLKEaisKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1690 KREIAQLKNQLEESEFTCAAAVKARKAME--VEMEDLHLQIDDIAKAKTALEEQLSRLQREK--NEIQNRLEEDQEDMNE 1765
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEekVEKAQSLAKLVDQYKELVASERIVFQQELVSifPDIIPVLKEDNLLSND 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1766 lmkKHKAAVAQASRDMAQmndLQAQIEEsnKEKQELQEKLQALQSQVEFLEQSmvDKSLVSRQEAKIRELET--RLEFEK 1843
Cdd:pfam09731 284 ---DLNSLIAHAHREIDQ---LSKKLAE--LKKREEKHIERALEKQKEELDKL--AEELSARLEEVRAADEAqlRLEFER 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1844 TQVKRLENLASRLKETMEKLTEERDQRaaAENREKEQNKRLQR-QLRDTKEEMSE----LARKEAEASRKKHELEMDLES 1918
Cdd:pfam09731 354 EREEIRESYEEKLRTELERQAEAHEEH--LKDVLVEQEIELQReFLQDIKEKVEEeragRLLKLNELLANLKGLEKATSS 431
|
330
....*....|.
gi 600971660 1919 -LEAANQSLQA 1928
Cdd:pfam09731 432 hSEVEDENRKA 442
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1266-1591 |
5.26e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.61 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1266 NKDEEIQQLRSKL----EKVEkernELRLSSDRLETRISELTSELTDERN--------TGESASQLLDAETAERLRTEKE 1333
Cdd:pfam00038 1 NEKEQLQELNDRLasyiDKVR----FLEQQNKLLETKISELRQKKGAEPSrlyslyekEIEDLRRQLDTLTVERARLQLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1334 MKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDAGGEWRLKYERAVR----EVDFTKKRLQQELEDKMEVEQ 1409
Cdd:pfam00038 77 LDNLRLAAEDFRQKYEDELNLRTSAE----NDLVGLRKDLDEATLARVDLEAKIEslkeELAFLKKNHEEEVRELQAQVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1410 QSRRQLERRLGdlqadsdesqralqqlkkKCQRLTAELQDTKLHLEGQQVRN-HELEKKQRRFDSELSQAhEETQREKLQ 1488
Cdd:pfam00038 153 DTQVNVEMDAA------------------RKLDLTSALAEIRAQYEEIAAKNrEEAEEWYQSKLEELQQA-AARNGDALR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1489 REKlqrekdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDIssqESKDEASLAKVKKQLRDLEAKVKDQEEELDE 1568
Cdd:pfam00038 214 SAK---------EEITELRRTIQSLEIELQSLKKQKASLERQLAET---EERYELQLADYQELISELEAELQETRQEMAR 281
|
330 340
....*....|....*....|...
gi 600971660 1569 QAGSIQMLEQAKLRLEMEMERMR 1591
Cdd:pfam00038 282 QLREYQELLNVKLALDIEIATYR 304
|
|
| PDZ_syntrophin-like |
cd06801 |
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ... |
270-308 |
5.88e-05 |
|
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntrophin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467262 [Multi-domain] Cd Length: 83 Bit Score: 43.33 E-value: 5.88e-05
10 20 30
....*....|....*....|....*....|....*....
gi 600971660 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06801 44 LFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTLTVK 82
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1427-1804 |
6.16e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.50 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1427 DESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMllaeafs 1505
Cdd:pfam15905 24 EKSQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKElEKEIRALVQERGEQDKRL------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1506 lkQQMEEKdldiagftqkVVSLEAELQDISSQESKDEASLAKVKKQLRDLeAKVKDqeeeldeqagsiqmLEQAKLRLEM 1585
Cdd:pfam15905 97 --QALEEE----------LEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNE--------------LLKAKFSEDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1586 EMERMRQTHSKEMESRDEeVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRkd 1665
Cdd:pfam15905 150 TQKKMSSLSMELMKLRNK-LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLE-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1666 lkrtkalladaqimldhlknnapskrEIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1745
Cdd:pfam15905 227 --------------------------YITELSCVSEQVE-------KYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 1746 QREKNEIQNRLEEDQEDMNELMKKHKAavaQASRDMAQMNDLQAQIEESNKEKQELQEK 1804
Cdd:pfam15905 274 SKQIKDLNEKCKLLESEKEELLREYEE---KEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1398-1897 |
6.25e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 47.98 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1398 QQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhleGQQVRNHELEKKQRrfDSELSQ 1477
Cdd:pfam15964 219 RLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAST----SSRVGGLCLKCAQH--EAVLAQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1478 AHEETQREKLQRekLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSleaelqdisSQESKDEASLAKVKK--QLRDL 1555
Cdd:pfam15964 293 THTNVHMQTIER--LTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQ---------AVQMTEEANFEKTKAliQCEQL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1556 EAKVKDQEEELDEQAGSiqmlEQAKLRLEMEMERmrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqKALR 1635
Cdd:pfam15964 362 KSELERQKERLEKELAS----QQEKRAQEKEALR------KEMKKEREELGATMLALSQNVAQLEAQVE-------KVTR 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1636 EKRELESKLSTLSDQVNQRDFESEK---RLRKDLKRTKALLADAQimLDHLKNNAPSKR-------EIAQLKNQLEESef 1705
Cdd:pfam15964 425 EKNSLVSQLEEAQKQLASQEMDVTKvcgEMRYQLNQTKMKKDEAE--KEHREYRTKTGRqleikdqEIEKLGLELSES-- 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1706 tcaaavkaRKAMEVEMEDLHLQIDDIAKaktaLEEQLSRLQREKNeiqnrleedqedmneLMKKHKAAVAQASRDMAQMN 1785
Cdd:pfam15964 501 --------KQRLEQAQQDAARAREECLK----LTELLGESEHQLH---------------LTRLEKESIQQSFSNEAKAQ 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1786 DLQAQIEEsnkekQELQEKLQALQSQvefleqsmvdkslvsrQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTE 1865
Cdd:pfam15964 554 ALQAQQRE-----QELTQKMQQMEAQ----------------HDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQ 612
|
490 500 510
....*....|....*....|....*....|..
gi 600971660 1866 ERDQRAAAENREKEQNKRLQRQLRDTKEEMSE 1897
Cdd:pfam15964 613 KSRSEVEQLSQEKEYLQDRLEKLQKRNEELEE 644
|
|
| PDZ2_MAGI-1_3-like |
cd06732 |
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
269-308 |
6.79e-05 |
|
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467214 [Multi-domain] Cd Length: 82 Bit Score: 43.31 E-value: 6.79e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 600971660 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQS--GDSVRLKVQ 308
Cdd:cd06732 39 GLQEGDLIVEINGQNVQNLSHAQVVDVLKECpkGSEVTLLVQ 80
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1402-1806 |
7.22e-05 |
|
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: 48.09 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1402 EDKMEVEQQSRRQLERRLGDLQADSDESQ--------RALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQRrfdS 1473
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKhtqnvalnKKLSDIKTEYLYELNVLKEKS---------EAELTSKTK---K 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1474 ELSQAHEETQREKLQREKLQREKDMLLAEA-FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESkdEASLAKVKKQL 1552
Cdd:NF033838 122 ELDAAFEQFKKDTLEPGKKVAEATKKVEEAeKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--ELELVKEEAKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1553 RDLEAKVKDQEEELDEQAGSIQMLEQAKlrlememermrqthskemESRDEEVEEARQSCQKKLKQ-MEVQLEEEYEDKQ 1631
Cdd:NF033838 200 PRDEEKIKQAKAKVESKKAEATRLEKIK------------------TDREKAEEEAKRRADAKLKEaVEKNVATSEQDKP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1632 KAlREKRELESKLSTlsdqvnqrdfesekrlrKDLKRTKALLADAQIMLDHLKNnaPSKREiaqlKNQLEESEFTCAAAV 1711
Cdd:NF033838 262 KR-RAKRGVLGEPAT-----------------PDKKENDAKSSDSSVGEETLPS--PSLKP----EKKVAEAEKKVEEAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1712 KARKAMEVE---------MEDLHLQiddIAKAKTALEE-QLSRLQREKNEIQNrleedQEDMNELMKKHKAAVAQASRdM 1781
Cdd:NF033838 318 KKAKDQKEEdrrnyptntYKTLELE---IAESDVKVKEaELELVKEEAKEPRN-----EEKIKQAKAKVESKKAEATR-L 388
|
410 420
....*....|....*....|....*
gi 600971660 1782 AQMNDLQAQIEESNKEKQELQEKLQ 1806
Cdd:NF033838 389 EKIKTDRKKAEEEAKRKAAEEDKVK 413
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1746-1925 |
8.18e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.64 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1746 QREKNEIQNRLEEDQEDMNELMKKHkaaVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVE----FLEQSMVD 1821
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREE---LELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAqeraRQQQEEFR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1822 KSLVSRQEAKIRELETRLEFEKTQVKRLE-NLASRLKETMEKLTEERDQraaaenrekeqnkrLQRQlrdtKEEMSELAR 1900
Cdd:pfam15709 430 RKLQELQRKKQQEEAERAEAEKQRQKELEmQLAEEQKRLMEMAEEERLE--------------YQRQ----KQEAEEKAR 491
|
170 180
....*....|....*....|....*
gi 600971660 1901 KEAEASRKKHELEMDLESLEAANQS 1925
Cdd:pfam15709 492 LEAEERRQKEEEAARLALEEAMKQA 516
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1384-1933 |
9.03e-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: 48.02 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1384 ERAVREVDFTKKRLQQELEDKMEVE------QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTA------ELQDTK 1451
Cdd:COG3096 532 QNAERLLEEFCQRIGQQLDAAEELEellaelEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDAL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1452 LHLEGQQvrNHELEKKQrrfdsELSQAHEETqrekLQREK-LQREKDMLLAEAFSLKQQMEEkdLDIAG--FTQKVVSLe 1528
Cdd:COG3096 612 ERLREQS--GEALADSQ-----EVTAAMQQL----LEREReATVERDELAARKQALESQIER--LSQPGgaEDPRLLAL- 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1529 AE------LQDISSQESKDEA-----------------SLAKVKKQLRDLEAKVKD------QEEELDEQAGSIQMLEQA 1579
Cdd:COG3096 678 AErlggvlLSEIYDDVTLEDApyfsalygparhaivvpDLSAVKEQLAGLEDCPEDlyliegDPDSFDDSVFDAEELEDA 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1580 KLRLEMEME--------------RMRQTHSKEM-ESRDEEVEE------ARQSCQKKL--------KQMEVQLEEEYEDK 1630
Cdd:COG3096 758 VVVKLSDRQwrysrfpevplfgrAAREKRLEELrAERDELAEQyakasfDVQKLQRLHqafsqfvgGHLAVAFAPDPEAE 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1631 QKALREKR-ELESKLSTLSDQvnqrdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPskreiAQLKNQLEESEFTCAA 1709
Cdd:COG3096 838 LAALRQRRsELERELAQHRAQ--------EQQLRQQLDQLKEQLQLLNKLLPQANLLAD-----ETLADRLEELREELDA 904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1710 AVKARKAMEVEMEDLHlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ---EDMNELM-KKHKAAVAQASRDMAQ-- 1783
Cdd:COG3096 905 AQEAQAFIQQHGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKqqiFALSEVVqRRPHFSYEDAVGLLGEns 983
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1784 -MND-LQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVdkSLVSRQEAKIRELEtrlEFEktqvKRLENLASRLKETME 1861
Cdd:COG3096 984 dLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA--SLKSSRDAKQQTLQ---ELE----QELEELGVQADAEAE 1054
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 600971660 1862 -KLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEmdlESLEAANQSLQADLKLA 1933
Cdd:COG3096 1055 eRARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQER---EQVVQAKAGWCAVLRLA 1124
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1753-1946 |
9.12e-05 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 46.14 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1753 QNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvDKSLVSRQEAKI 1832
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAE-------AAPKEILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1833 RELETRLEFEKTQvkrLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQR------QLRDTKEEMSELARKEAEAS 1906
Cdd:pfam12795 81 EELEQRLLQTSAQ---LQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQirnrlnGPAPPGEPLSEAQRWALQAE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 600971660 1907 RKKHELEMDLESLEAANQSLQADL-----KLAFKRIGDLQAAIED 1946
Cdd:pfam12795 158 LAALKAQIDMLEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQA 202
|
|
| PDZ3_DLG5-like |
cd06767 |
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
9.36e-05 |
|
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467248 [Multi-domain] Cd Length: 82 Bit Score: 42.70 E-value: 9.36e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 600971660 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06767 42 GLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLVQ 81
|
|
| PDZ_MPP3-MPP4-MPP7-like |
cd06799 |
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ... |
269-309 |
9.67e-05 |
|
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467260 [Multi-domain] Cd Length: 81 Bit Score: 42.62 E-value: 9.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 600971660 269 GLV-PGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06799 40 GLIhVGDELREVNGISVEGKDPEEVIQILANSQGPITFKLIP 81
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1248-1623 |
1.01e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 47.59 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1248 FTTVRPLIQV-QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRlssdrletriSELTSELTDERNTGESASQLLDAETAE 1326
Cdd:pfam15964 349 FEKTKALIQCeQLKSELERQKERLEKELASQQEKRAQEKEALR----------KEMKKEREELGATMLALSQNVAQLEAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1327 RLRTEKEMKELQTQYDALKKQMEVMemevmearliraaeingEVDDDDAGGEWR-------LKYERAVREVDFTKKRLQQ 1399
Cdd:pfam15964 419 VEKVTREKNSLVSQLEEAQKQLASQ-----------------EMDVTKVCGEMRyqlnqtkMKKDEAEKEHREYRTKTGR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1400 ELEDKmeveQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDT--KLHLEGQqvrnhELEKKQRRFDSEL-S 1476
Cdd:pfam15964 482 QLEIK----DQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESehQLHLTRL-----EKESIQQSFSNEAkA 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1477 QAHEETQREK----------LQREKLQREKDMLLAEAFSLkqqmeekdldIAGFTQKVVSLEAELQDISSQESKDEASLA 1546
Cdd:pfam15964 553 QALQAQQREQeltqkmqqmeAQHDKTVNEQYSLLTSQNTF----------IAKLKEECCTLAKKLEEITQKSRSEVEQLS 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1547 KVKKQLRDLEAKVKDQEEELDEQAgsIQ---MLEQAKLRLEmEMERMRQTHSK---EMESRDEEVEEARQSCQKKLKQME 1620
Cdd:pfam15964 623 QEKEYLQDRLEKLQKRNEELEEQC--VQhgrMHERMKQRLR-QLDKHCQATAQqlvQLLSKQNQLFKERQNLTEEVQSLR 699
|
...
gi 600971660 1621 VQL 1623
Cdd:pfam15964 700 SQV 702
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1442-1807 |
1.07e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1442 RLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFT 1521
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAAL---SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1522 QKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMErMRQTHSKEMESR 1601
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA-EREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1602 DEEVEEARQSCQKKLKQMEVQleEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLD 1681
Cdd:COG4372 159 LESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1682 HLKNNAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE 1761
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIE-ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 600971660 1762 DM----NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQA 1807
Cdd:COG4372 316 ALlaalLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1825-1942 |
1.07e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1825 VSRQEAKIRELEtrlefekTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRDTKEEMSELARKEAE 1904
Cdd:COG2433 408 LTEEEEEIRRLE-------EQVERLEAEVEELEAELEEK--------------DERIERLERELSEARSEERREIRKDRE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 600971660 1905 ASRKKHE---LEMDLESLEAANQSLQADLKLaFKRIGDLQA 1942
Cdd:COG2433 467 ISRLDREierLERELEEERERIEELKRKLER-LKELWKLEH 506
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1692-1921 |
1.20e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.60 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1692 EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK 1771
Cdd:pfam19220 91 RLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1772 AAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKT-QVKRL 1849
Cdd:pfam19220 171 LLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAeQAERERAEAQLEEAVEAHRAERAsLRMKL 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 600971660 1850 ENLASRLKETMEKLTEERDqraaaenrekeqnkrlqrQLRDTKEEMSELARKEAEASRKKHELEMDLESLEA 1921
Cdd:pfam19220 251 EALTARAAATEQLLAEARN------------------QLRDRDEAIRAAERRLKEASIERDTLERRLAGLEA 304
|
|
| PDZ_SYNPO2-like |
cd10820 |
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ... |
269-308 |
1.24e-04 |
|
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNPO2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467264 [Multi-domain] Cd Length: 78 Bit Score: 42.30 E-value: 1.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 600971660 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd10820 39 GLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
|
|
| PDZ_rhophilin-like |
cd06712 |
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
225-307 |
1.27e-04 |
|
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This rhophilin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467196 [Multi-domain] Cd Length: 78 Bit Score: 42.19 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 225 RRPTGDFGFSLRrttmlDRAPegqayrrV-VHFAEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIVEMIRQSG-DS 302
Cdd:cd06712 7 TKEEGGFGFTLR-----GDSP-------VqVASVDPG-SCAAEA-GLKEGDYIVSVGGVDCKWSKHSEVVKLLKSAGeEG 72
|
....*
gi 600971660 303 VRLKV 307
Cdd:cd06712 73 LELQV 77
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1738-1985 |
1.34e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1738 LEEQLSRLQREKNeiQNRLEEDQEdMNELMKKHKAAVAQASRDMAQMNDLQAQIeeSNKEKQElQEKLQALQSQVEfleq 1817
Cdd:pfam05557 7 SKARLSQLQNEKK--QMELEHKRA-RIELEKKASALKRQLDRESDRNQELQKRI--RLLEKRE-AEAEEALREQAE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1818 smvdkslVSRQEAKIRELETRLEFEKTQvkrLENLASRLKETMEKLTEERDQRAaaeNREKEQNKRLQRQLRDTKEEMSE 1897
Cdd:pfam05557 77 -------LNRLKKKYLEALNKKLNEKES---QLADAREVISCLKNELSELRRQI---QRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1898 LARKEAEASRKKHELEMDLESLEAANQ---------SLQADLKLAFKRIGDLQAAIEdEMES------DENEDLINSEGD 1962
Cdd:pfam05557 144 LKAKASEAEQLRQNLEKQQSSLAEAEQrikelefeiQSQEQDSEIVKNSKSELARIP-ELEKelerlrEHNKHLNENIEN 222
|
250 260
....*....|....*....|...
gi 600971660 1963 SDVdseLEDRVDGVKSWLSKNKG 1985
Cdd:pfam05557 223 KLL---LKEEVEDLKRKLEREEK 242
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1690-1900 |
1.56e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.61 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1690 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEiQNRLEEDQEDMNELMKK 1769
Cdd:PRK11637 67 QQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQI-------DELNASIAKLEQQQAA-QERLLAAQLDAAFRQGE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1770 HKAAVAQASRDMAQ-------------------MNDLQAQIEESNKEKQELQEKlQALQSQVEFLEQSMVDKSLVSRQEA 1830
Cdd:PRK11637 139 HTGLQLILSGEESQrgerilayfgylnqarqetIAELKQTREELAAQKAELEEK-QSQQKTLLYEQQAQQQKLEQARNER 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 1831 K--IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD-------TKEEMSELAR 1900
Cdd:PRK11637 218 KktLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREAREAARVRDKQKQAKRkgstykpTESERSLMSR 296
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1657-1930 |
1.67e-04 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 46.11 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1657 ESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREIAQLKNQL-EESEFTCAAAVKARKAMEVEMEDLHLQIDdiaKAK 1735
Cdd:pfam09311 16 EQEAETRDQVKKLQEMLRQAN---DQLEKTMKDKKELEDKMNQLsEETSNQVSTLAKRNQKSETLLDELQQAFS---QAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1736 TALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqaSRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFL 1815
Cdd:pfam09311 90 RNFQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHV---SLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADHM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1816 EQSMVDKSLVSRQEAKiRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLqRQLRDTKEEM 1895
Cdd:pfam09311 167 EEKLKAEILFLKEQIQ-AEQCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQLENGLTEKI-RQLEDLQTTK 244
|
250 260 270
....*....|....*....|....*....|....*
gi 600971660 1896 SELARKEAEASRKKHELEMDLESLEAANQSLQADL 1930
Cdd:pfam09311 245 GSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTEL 279
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1394-1592 |
1.72e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.90 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1394 KKRLQQELEDKMEVEQ-QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhLEGQqvrnHELEKKQRRfd 1472
Cdd:pfam09787 23 KEKLIASLKEGSGVEGlDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE----LEAQ----QQEEAESSR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1473 SELSQAHEETQREKLQREKLQrekdmllAEAFSLKQQM----EEKDLDIAGFTQKVVSLEAELQDISSQ-ESKDEASLAK 1547
Cdd:pfam09787 93 EQLQELEEQLATERSARREAE-------AELERLQEELryleEELRRSKATLQSRIKDREAEIEKLRNQlTSKSQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 600971660 1548 vkkqlRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQ 1592
Cdd:pfam09787 166 -----SELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQ 205
|
|
| PDZ1_L-delphilin-like |
cd06743 |
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ... |
269-299 |
1.85e-04 |
|
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467225 [Multi-domain] Cd Length: 76 Bit Score: 41.88 E-value: 1.85e-04
10 20 30
....*....|....*....|....*....|.
gi 600971660 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:cd06743 36 GLQPGDQILELDGQDVSSLSCEAIIALARRC 66
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1427-1570 |
2.02e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1427 DESQRALQQLKKKCQrLTA--ELQDTKLHLEGQ-QVRNHELEKKQRRFdselsQAHEETQREKLqrEKLQREKDMLLAEA 1503
Cdd:PRK12704 45 EEAKKEAEAIKKEAL-LEAkeEIHKLRNEFEKElRERRNELQKLEKRL-----LQKEENLDRKL--ELLEKREEELEKKE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1504 FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQeSKDEAS---LAKVKKQLR-DLEAKVKDQEEELDEQA 1570
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEEQLQELERISGL-TAEEAKeilLEKVEEEARhEAAVLIKEIEEEAKEEA 186
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1512-1671 |
2.13e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1512 EKDLDIAGFTQKVVSLEAELQDIssqeskdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEmemERMR 1591
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAEL-------EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1592 QTHS-KEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKALRE-KRELESKLSTLSDQVNQRDfESEKRLRKDLKRT 1669
Cdd:COG1579 84 NVRNnKEYEALQKEIESLKRR-ISDLEDEILELMERIEELEEELAElEAELAELEAELEEKKAELD-EELAELEAELEEL 161
|
..
gi 600971660 1670 KA 1671
Cdd:COG1579 162 EA 163
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
1566-1918 |
2.17e-04 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 45.59 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1566 LDEQAGSIQMLEQAKLRLEMEMERMRqTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKREleskls 1645
Cdd:pfam09755 23 REQLQKRIESLQQENRVLKMELETYK-LRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKE------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1646 TLSDQVNQRdfesEKRLRKDLKRTkalladaqimLDHLKnnapskREIAQLKNQLEeseftcaaavkarKAMEVEMEDLH 1725
Cdd:pfam09755 96 TLAMNYEQE----EEFLTNDLSRK----------LTQLR------QEKVELEQTLE-------------QEQEYQVNKLM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1726 LQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM-NELMKKhkaavaqasrdmaqMNDLQAqieesnkEKQELQEK 1804
Cdd:pfam09755 143 RKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQEALvNRLWKR--------------MDKLEA-------EKRLLQEK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1805 LQALQSQVEFLEQSMVDKSLVSRQEAKIRELEtrlefektqvKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRL 1884
Cdd:pfam09755 202 LDQPVSAPPSPRDSTSEGDTAQNLTAHIQYLR----------KEVERLRRQLATAQQEHTEKMAQYAQEERHIREENLRL 271
|
330 340 350
....*....|....*....|....*....|....
gi 600971660 1885 QRQLRDTKEEMSELARKEAEAsrkKHELEMDLES 1918
Cdd:pfam09755 272 QRKLQLEMERREALCRHLSES---ESSLEMDEER 302
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1740-1961 |
2.18e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1740 EQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM 1819
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1820 VDKSLVSRQEAKIRELETRLEFEK------------TQV-KRLENLASRLKETMEKLTEERDQRAA--AENREKEQNKRL 1884
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERINRARkaaplaahikavTQIeQQAQRIHTELQSKMRSRAKLLMKRAAhvKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1885 QRQLRDTKEEMSELARKEA---EASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDL-----QAAIEDEMESDENEDL 1956
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATsirEISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILqreqaTIDTRTSAFRDLQGQL 426
|
....*
gi 600971660 1957 INSEG 1961
Cdd:TIGR00618 427 AHAKK 431
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1736-1921 |
2.39e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.52 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1736 TALEEQLSRLQREKN----EIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1811
Cdd:pfam09787 43 TALTLELEELRQERDllreEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1812 VEFLEQSMVdKSLVSRQEaKIRELETRLEFEKTQVK--------------RLENLASRL--KETM-EKLTEERDQRAAAE 1874
Cdd:pfam09787 123 LRYLEEELR-RSKATLQS-RIKDREAEIEKLRNQLTsksqssssqselenRLHQLTETLiqKQTMlEALSTEKNSLVLQL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 600971660 1875 NREKEQNKRLQ-RQLRDTKEEMSELARKEAEASRKKHELEMDLESLEA 1921
Cdd:pfam09787 201 ERMEQQIKELQgEGSNGTSINMEGISDGEGTRLRNVPGLFSESDSDRA 248
|
|
| DUF1633 |
pfam07794 |
Protein of unknown function (DUF1633); This family contains sequences derived from a group of ... |
1549-1745 |
2.57e-04 |
|
Protein of unknown function (DUF1633); This family contains sequences derived from a group of hypothetical proteins expressed by Arabidopsis thaliana. These sequences are highly similar and the region concerned is about 100 residues long.
Pssm-ID: 116408 [Multi-domain] Cd Length: 698 Bit Score: 46.03 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1549 KKQLRDLEAKVK-DQEEELDEQAgsiQMLEQAKLRLEMEMermrqTHSKEMESRDEEveearqscqkKLKQMEVQLEEEY 1627
Cdd:pfam07794 457 ERAIREEDPHLGaDQDREVRFGA---EGIVPGIERLKIEL-----STSKDLEKGYAE----------KIGFMEMEFGGLE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1628 EDKQKALREKRELESKLSTLSDQVnqRDFESEKR-LRKDLKRTKALLADAQI-MLDHLKNNAPSKREIAQLKNQLEESEF 1705
Cdd:pfam07794 519 ADKQMARNQIHRLEEKKDELSKKV--LDLTSIAQgAKKAVHDAKVELAAAYLkLLAGIKDKWVAKKEFTVLEGQAAEVES 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 600971660 1706 TCA---AAVKARKAMEVEMEDLHLQIDDIaKAKTALEE----QLSRL 1745
Cdd:pfam07794 597 NLAlidQITKAAIDLTLEKPRFQAEIDDL-EARCKLKEvsdfTLSKL 642
|
|
| PDZ5_MUPP1-like |
cd06669 |
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ... |
269-311 |
2.62e-04 |
|
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467157 [Multi-domain] Cd Length: 98 Bit Score: 41.83 E-value: 2.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 600971660 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSG-DSVRLKV-QPIP 311
Cdd:cd06669 54 RLLPGDRLVFVNDVSLENASLDEAVQALKSAPpGTVRIGVaKPLP 98
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1421-1916 |
3.02e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.84 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1421 DLQADSDESQralqQLKKKCQRL---TAELQDTKLHLegqQVRNHELEKKQRRFDSELSQA--------HEETQREKLQR 1489
Cdd:pfam05622 1 DLSEAQEEKD----ELAQRCHELdqqVSLLQEEKNSL---QQENKKLQERLDQLESGDDSGtpggkkylLLQKQLEQLQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1490 EKLQREKDmllAEAFSLKQQMEEKD-LDIAGFTQKVVSLEAElqdisSQESKDE-----ASLAKVKKqlrdLEAKV---K 1560
Cdd:pfam05622 74 ENFRLETA---RDDYRIKCEELEKEvLELQHRNEELTSLAEE-----AQALKDEmdilrESSDKVKK----LEATVetyK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1561 DQEEELDEQAGSIQMLEqaklrlEMEMERMRQTHSKEMESRDEEVEEAR-QSCQKKLKQMEVQLEEEYEDKQKALREKRE 1639
Cdd:pfam05622 142 KKLEDLGDLRRQVKLLE------ERNAEYMQRTLQLEEELKKANALRGQlETYKRQVQELHGKLSEESKKADKLEFEYKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1640 LESKLSTLsdqvnQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKN------------------QLE 1701
Cdd:pfam05622 216 LEEKLEAL-----QKEKERLIIERDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDnlaaeimpaeireklirlQHE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1702 ESEFTCaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLsRLQREK-NEIQNRLEEDQEDMNELMKKHKAAVAqasrd 1780
Cdd:pfam05622 291 NKMLRL----GQEGSYRERLTELQQLLEDANRRKNELETQN-RLANQRiLELQQQVEELQKALQEQGSKAEDSSL----- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1781 maqmndLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdkSLVSRQEAKIRELETRLefektQVKRLENLA--SRLKE 1858
Cdd:pfam05622 361 ------LKQKLEEHLEKLHEAQSELQKKKEQIEELEP-----KQDSNLAQKIDELQEAL-----RKKDEDMKAmeERYKK 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 1859 TMEKLTEE-RDQRAAAENREKEQNKRLQRQLRDtKEEMSELARKEAEASRKKHELEMDL 1916
Cdd:pfam05622 425 YVEKAKSViKTLDPKQNPASPPEIQALKNQLLE-KDKKIEHLERDFEKSKLQREQEEKL 482
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1262-1885 |
3.08e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.36 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1262 EQIRNKDEEIQQLRSKLEKVEKER------NELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAeRLRTEKEMK 1335
Cdd:PTZ00440 1190 EEIESYKKDIDQVKKNMSKERNDHlttfeyNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEI-KLQVFSYLQ 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1336 ELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEwrlKYER-AVREVDFTKkRLQQELEDKMEVEQQSRRQ 1414
Cdd:PTZ00440 1269 QVIKENNKMENALHEIKNMYEFLISIDSEKILKEILNSTKKAE---EFSNdAKKELEKTD-NLIKQVEAKIEQAKEHKNK 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1415 LERRLGDLQADSDesqraLQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAH------------EET 1482
Cdd:PTZ00440 1345 IYGSLEDKQIDDE-----IKKIEQIKEEISNKRKEINKYLS-------NIKSNKEKCDLHVRNASrgkdkidflnkhEAI 1412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1483 QREKLQREKLQREKDML------LAEAFSLKQQMEEKDLDIAGFTQKVVSLeaeLQD--ISSQESKDEaslaKVKKQLRD 1554
Cdd:PTZ00440 1413 EPSNSKEVNIIKITDNInkckqySNEAMETENKADENNDSIIKYEKEITNI---LNNssILGKKTKLE----KKKKEATN 1485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1555 LEAKVKDQEEELDEQAGSIQmleqaklrlememERMRQTHSKEMESRDEEV------EEARQSCQKKLKQMEVQLEEEYE 1628
Cdd:PTZ00440 1486 IMDDINGEHSIIKTKLTKSS-------------EKLNQLNEQPNIKREGDVlnndksTIAYETIQYNLGRVKHNLLNILN 1552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1629 DKQKA---LREKRELESKLSTLSDQVNQRDFES-EKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEES- 1703
Cdd:PTZ00440 1553 IKDEIetiLNKAQDLMRDISKISKIVENKNLENlNDKEADYVKYLDNILKEKQLMEAEYKKLNEIYSDVDNIEKELKKHk 1632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1704 --------EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL-------EEQLSRLQREKNEIQNRLEEDQEDMNELMK 1768
Cdd:PTZ00440 1633 knyeigllEKVIEINKNIKLYMDSTKESLNSLVNNFSSLFNNFylnkyniNENLEKYKKKLNEIYNEFMESYNIIQEKMK 1712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1769 KhkaavaqASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsMVDKSLVSRQEAKIRELETRLEFEKTQVKR 1848
Cdd:PTZ00440 1713 E-------VSNDDVDYNEAKTLREEAQKEEVNLNNKEEEAKKYLNDIKK-QESFRFILYMKEKLDELSKMCKQQYNIVDE 1784
|
650 660 670
....*....|....*....|....*....|....*..
gi 600971660 1849 LENLASRLKETMEKLTEErDQRAAAENREKEQNKRLQ 1885
Cdd:PTZ00440 1785 GYNYIKKKIEYIKTLNDE-NNLSDSLNQAEDKNKEVA 1820
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1517-1778 |
3.16e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1517 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQaklrlememermrqthsk 1596
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1597 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKAlrekreleSKLSTLSDQVNQRDFesekrLRKDLKRTKALLADA 1676
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSV--------SYLDVLLGSESFSDF-----LDRLSALSKIADADA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1677 QIMLDHlknnapsKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRL 1756
Cdd:COG3883 133 DLLEEL-------KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
250 260
....*....|....*....|..
gi 600971660 1757 EEDQEDMNELMKKHKAAVAQAS 1778
Cdd:COG3883 206 AAAEAAAAAAAAAAAAAAAAAA 227
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1457-1931 |
3.18e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.97 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1457 QQVRNHELEKKQRRFDSE--LSQAHEETQR----EKLQREKLQREkdmLLAEAFSLKQQMEEK------------DLDIA 1518
Cdd:NF041483 76 QLLRNAQIQADQLRADAEreLRDARAQTQRilqeHAEHQARLQAE---LHTEAVQRRQQLDQElaerrqtveshvNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1519 GFTQKVVSLEAE---LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEM-------- 1587
Cdd:NF041483 153 WAEQLRARTESQarrLLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAERLLnaastqaq 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1588 ------ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesEKR 1661
Cdd:NF041483 233 eatdhaEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESAN------EQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1662 LRKdlkrtkalladaqimldhlknnapSKREIAQLKNQ-LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE 1740
Cdd:NF041483 307 TRT------------------------AKEEIARLVGEaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1741 --QLSRLQREKNEIQNRLEEDQEDM-----NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQ--------ELQEKL 1805
Cdd:NF041483 363 aaQLAKAARTAEEVLTKASEDAKATtraaaEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTkeyraktvELQEEA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1806 QALQSQVEFLEQSMVDKSLVSRQEAKireletrlefeKTQVKRLENLASRLKETMEKLTEERDQ--RAAAENREKEQNKR 1883
Cdd:NF041483 443 RRLRGEAEQLRAEAVAEGERIRGEAR-----------REAVQQIEEAARTAEELLTKAKADADElrSTATAESERVRTEA 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 600971660 1884 LQR--QLRDTKEEMSELARKEAEasRKKHELEMDLESLEAANQSLQADLK 1931
Cdd:NF041483 512 IERatTLRRQAEETLERTRAEAE--RLRAEAEEQAEEVRAAAERAARELR 559
|
|
| PDZ_PDLIM-like |
cd06753 |
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
3.45e-04 |
|
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467235 [Multi-domain] Cd Length: 79 Bit Score: 40.98 E-value: 3.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 600971660 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06753 39 NLRPGDVILAINGESTEGMTHLEAQNKIKAATGSLSLTLE 78
|
|
| PDZ2_Dlg1-2-4-like |
cd06724 |
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ... |
258-308 |
3.47e-04 |
|
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467207 [Multi-domain] Cd Length: 85 Bit Score: 41.10 E-value: 3.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 600971660 258 EPGAGTKDLALGLvpGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06724 37 EGGAAQKDGRLQV--GDKLLAVNDVSLEEVTHEEAVAALKNTSDVVYLKVA 85
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1255-1569 |
3.57e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1255 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEM 1334
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1335 KELQTQYDALKKQmevmemevmearlirAAEINGEVDDddaggewrlkyeravrevdftKKRLQQELEDKMEVEQQSRRQ 1414
Cdd:COG4372 104 ESLQEEAEELQEE---------------LEELQKERQD---------------------LEQQRKQLEAQIAELQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1415 LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQR 1494
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 600971660 1495 EKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1569
Cdd:COG4372 228 EAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1268-1447 |
3.84e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1268 DEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQT--QYDALK 1345
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1346 KQmevmemEVMEARLIRAAeingevddddaggewrlkyERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLGDLQAD 1425
Cdd:COG1579 96 KE------IESLKRRISDL-------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 600971660 1426 SDESQRALQQLKKKCQRLTAEL 1447
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| PDZ_MPP1-like |
cd10830 |
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ... |
273-309 |
3.88e-04 |
|
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1, and related domains. MPP1 (also known as MAGUK p55 subfamily member 1, erythrocyte membrane protein p55, EMP55) is a membrane-associated guanylate kinase (MAGUK)-like protein which forms a complex with protein 4.1 and glycophorin C (GPC) at the cytoplasmic face of the plasma membrane; this complex is essential for cytoskeleton-membrane linkage in erythrocytes and many non-erythroid cells, and participates in the determination of membrane stability and cell shape. MPP1, by interacting with various scaffold proteins and cytoskeletal proteins in the postsynaptic density, also plays an important role in organizing synaptic and non-synaptic structures. MPP1 is also a component of the Crumbs protein complex in the mammalian retina and may link the Usher protein network and the Crumbs protein complex. The MPP1 PDZ domain binding partners include GPC, ABCC4, and CADM1/Necl-2/SynCAM1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467266 [Multi-domain] Cd Length: 81 Bit Score: 41.00 E-value: 3.88e-04
10 20 30
....*....|....*....|....*....|....*..
gi 600971660 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd10830 45 GDEILEINGKSVTNHSVDQLQKMLKETKGMVSLKVIP 81
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1549-1729 |
4.01e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.47 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1549 KKQLRDLEAKVKDQEEELDEQAgsiqMLEQAKLRLEMEMERMRqtHSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYE 1628
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEE----KLEAALLEAKELLLRER--NQQRQEARREREELQRE--EERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1629 DKQKALREKRELESKLSTLSDQVNQRdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEsEFTCA 1708
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEEL----EKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE-EADLE 173
|
170 180
....*....|....*....|.
gi 600971660 1709 AAVKARKAMEVEMEDLHLQID 1729
Cdd:PRK12705 174 AERKAQNILAQAMQRIASETA 194
|
|
| PDZ4_DLG5-like |
cd06766 |
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
237-308 |
4.03e-04 |
|
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467247 [Multi-domain] Cd Length: 81 Bit Score: 40.84 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 237 RTTMLDRAPE--------GQAYRRVVHFAEPGAGTKDLAlGLVPGDRLVEINGQNVENKSRDEI-VEMIRQSgDSVRLKV 307
Cdd:cd06766 3 RLVFLKKSQVelgiqlcgGNLHGIFVEDVEDDSPAKGPD-GLVPGDLILEYNSVDMRNKTAEEAyLEMLKPA-ETVTLKV 80
|
.
gi 600971660 308 Q 308
Cdd:cd06766 81 Q 81
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1256-1477 |
4.11e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1256 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNElRLSSDRLETRISELTSELTDERNT-GESASQLLDAETAERlRTEKEM 1334
Cdd:PRK11281 88 QLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLESRLAQTLDQLQNAQNDlAEYNSQLVSLQTQPE-RAQAAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1335 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQQELEDKMEVEQQsrrQ 1414
Cdd:PRK11281 166 YANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNA----QNDLQRKSLEGNTQLQDLLQKQRDYLTARIQ---R 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 600971660 1415 LERRLGDLQADSdeSQRALQQLKKKCQRltAELQDtklhlEGQQVRNHELEKKQRRFDSELSQ 1477
Cdd:PRK11281 239 LEHQLQLLQEAI--NSKRLTLSEKTVQE--AQSQD-----EAARIQANPLVAQELEINLQLSQ 292
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1660-1946 |
4.44e-04 |
|
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: 44.91 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1660 KRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE-----MEDLHLQIDDIAKA 1734
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEerkryRQELEEQIEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1735 KtalEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQE-KLQALQSQVE 1813
Cdd:pfam13868 89 R---QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRILEYLKEKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1814 FLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKR-----LQRQL 1888
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQelqqaREEQI 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 600971660 1889 RDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRigDLQAAIED 1946
Cdd:pfam13868 246 ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR--ELEKQIEE 301
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1588-1913 |
4.66e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1588 ERMRQTHSKEMESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKalrekrelesklstLSDQVNQRDFESEKRLRKDL 1666
Cdd:pfam02029 18 ERRRQKEEEEPSGQvTESVEPNEHNSYEEDSELKPSGQGGLDEEEA--------------FLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1667 KRTKALLadaqimldhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhlqiddiakaktalEEQLSRlq 1746
Cdd:pfam02029 84 ERQKEFD----------PTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYK----------------EEETEI-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1747 REKNEIQNRLEEDQEDMNELMKKHKAAVAQASR-DMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS------M 1819
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEvPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKsqngeeE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1820 VDKSLVS--RQEAKIRELETRLEFEKTQV---KRLENLASRLKET----MEKLtEERDQRAAAE----NREKEQNKRL-- 1884
Cdd:pfam02029 216 VTKLKVTtkRRQGGLSQSQEREEEAEVFLeaeQKLEELRRRRQEKeseeFEKL-RQKQQEAELEleelKKKREERRKLle 294
|
330 340
....*....|....*....|....*....
gi 600971660 1885 QRQLRDTKEEMSELARKEAEASRKKHELE 1913
Cdd:pfam02029 295 EEEQRRKQEEAERKLREEEEKRRMKEEIE 323
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1255-1565 |
4.78e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1255 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEM 1334
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1335 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDK---MEVEQQS 1411
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1412 RRQLERRlgdlqadSDESQRALQQLKKKCQRLTAELQDTKLHLeGQQVRNHELEKKQRRFDSElsQAHEETQREKLQRE- 1490
Cdd:pfam05483 617 NKALKKK-------GSAENKQLNAYEIKVNKLELELASAKQKF-EEIIDNYQKEIEDKKISEE--KLLEEVEKAKAIADe 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1491 --KLQREKDML----LAEAFSLKQQ--------MEEKDLDIAGFTQK-------VVSLEAELQDIssqeskdEASLAKVK 1549
Cdd:pfam05483 687 avKLQKEIDKRcqhkIAEMVALMEKhkhqydkiIEERDSELGLYKNKeqeqssaKAALEIELSNI-------KAELLSLK 759
|
330
....*....|....*....
gi 600971660 1550 KQL---RDLEAKVKDQEEE 1565
Cdd:pfam05483 760 KQLeieKEEKEKLKMEAKE 778
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
1830-1955 |
5.07e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 41.62 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1830 AKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEnrekEQNKRLQRQLRDTKEEMSELARKEAEASRKK 1909
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELE----AEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 600971660 1910 HELEMDLESLEAANQSLQADLKlafKRIGDLQAAIEDEMESDENED 1955
Cdd:pfam04871 77 DDLLLLLGDLEEKVEKYKARLK---ELGEEVLSDDEDDDEDDEEDD 119
|
|
| PDZ1_PTPN13-like |
cd23072 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ... |
259-309 |
5.13e-04 |
|
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467285 [Multi-domain] Cd Length: 92 Bit Score: 40.94 E-value: 5.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 600971660 259 PGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV-QP 309
Cdd:cd23072 39 PG-GPADLDGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTLVVsQP 89
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1258-1629 |
5.15e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1258 QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSsdrletriseltseltDERNTGESASQLldAETAERLRteKEMKEL 1337
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLE----------------KLGENAESSKRL--NENANNLI--KQFENT 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1338 QTQYDALKKQMEVMEMEVMEARLIRAAEINGEvddddaggewrlkYERAVREVDFTKKRLQQELEdkmeveqQSRRQLER 1417
Cdd:COG5185 295 KEKIAEYTKSIDIKKATESLEEQLAAAEAEQE-------------LEESKRETETGIQNLTAEIE-------QGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1418 RLGDLQADSDESQRALQQlkkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKL-QREKLQREK 1496
Cdd:COG5185 355 NLEAIKEEIENIVGEVEL-----SKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADrQIEELQRQI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1497 DmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAK--VKKQLRDLEAKVKDQEEELDEQAGSiq 1574
Cdd:COG5185 430 E-------QATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINrsVRSKKEDLNEELTQIESRVSTLKAT-- 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 600971660 1575 mLEQAKLRLEMEMERMRQTHSKEMESRDEEvEEARQSCQKKLKQMEVQLEEEYED 1629
Cdd:COG5185 501 -LEKLRAKLERQLEGVRSKLDQVAESLKDF-MRARGYAHILALENLIPASELIQA 553
|
|
| PDZ2_MUPP1-like |
cd06667 |
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ... |
259-307 |
5.19e-04 |
|
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467155 [Multi-domain] Cd Length: 80 Bit Score: 40.73 E-value: 5.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 600971660 259 PGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06667 31 PG-GVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSHVRLVV 78
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1384-1641 |
5.57e-04 |
|
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: 44.52 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1384 ERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRlgdlqadsdESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnHE 1463
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERKRYRQELEEQIEER---------EQKRQEEYEEKLQEREQMDEIVERIQEEDQAEA-EE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1464 LEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftqkvvsLEAELQDIssqeskdEA 1543
Cdd:pfam13868 121 KLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEE-------------REAEREEI-------EE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1544 SLAKVKKQLRDLEAKVKDQEEELDEQagsiqmleQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQK----KLKQM 1619
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDEL--------RAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEqielKERRL 252
|
250 260
....*....|....*....|..
gi 600971660 1620 EVQLEEEYEDKQKALREKRELE 1641
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDE 274
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1559-1893 |
5.66e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 44.67 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1559 VKDQEEELDEQAGSIQMLEQAKLRL---------EMEMER-----MRQTHSKEMESRDEEVEEARQSCQKKL--KQMEVQ 1622
Cdd:pfam15742 1 VSSGEKLKYQQQEEVQQLRQNLQRLqilctsaekELRYERgknldLKQHNSLLQEENIKIKAELKQAQQKLLdsTKMCSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1623 LEEEYEDKQKALREkRELESKLSTLSDQvnqrdfeSEKRLRKDLKRTKALLADAQIMldhlknnapskreIAQLKNQLEE 1702
Cdd:pfam15742 81 LTAEWKHCQQKIRE-LELEVLKQAQSIK-------SQNSLQEKLAQEKSRVADAEEK-------------ILELQQKLEH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1703 SEFTCAAAVKA--RKAMEVEMEDLhlqIDDIAKAKTAL-EEQLSR--LQREKNEIQNRLEEDQEDMNELMKKHKAAVAQA 1777
Cdd:pfam15742 140 AHKVCLTDTCIleKKQLEERIKEA---SENEAKLKQQYqEEQQKRklLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1778 SRDMAQMNDLQAQI---EESNKEKQELQEKLQALQSQVEFL--EQSMVDKSL----------VSRQEAKIRELETRLEFE 1842
Cdd:pfam15742 217 QQQEAQLKQLENEKrksDEHLKSNQELSEKLSSLQQEKEALqeELQQVLKQLdvhvrkynekHHHHKAKLRRAKDRLVHE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 600971660 1843 KTQ----VKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKE 1893
Cdd:pfam15742 297 VEQrderIKQLENEIGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQEE 351
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1697-1871 |
5.69e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1697 KNQLEESEFTCAAAVK-ARKAMEVEMEDLHLQI-DDIAKAKTALEEQLsrlqREKNEIQNRLEEDQEDMNELMKKHKAAV 1774
Cdd:PRK12704 30 EAKIKEAEEEAKRILEeAKKEAEAIKKEALLEAkEEIHKLRNEFEKEL----RERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1775 AQASRDMAQMNDLQAQIEESNKEKQELQEKLQalQSQVEFLEQSMvdkSLvSRQEAK---IRELETRLEFEKtqvkrlen 1851
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELI--EEQLQELERIS---GL-TAEEAKeilLEKVEEEARHEA-------- 171
|
170 180
....*....|....*....|
gi 600971660 1852 lASRLKETMEKLTEERDQRA 1871
Cdd:PRK12704 172 -AVLIKEIEEEAKEEADKKA 190
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1433-1650 |
6.10e-04 |
|
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: 44.74 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1433 LQQLKKKCQRLTAELQdTKLHLEGQQV-RNHELEKKQRRFDSELSQAHEetqreklqrEKLQREKDMLLaeafSLKQQME 1511
Cdd:pfam07111 483 LEQLREERNRLDAELQ-LSAHLIQQEVgRAREQGEAERQQLSEVAQQLE---------QELQRAQESLA----SVGQQLE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1512 EKDLDIAGFTQKVVSLEAEL---QDISSQESKDEasLAKVKKQLRDLEAKVKDQ-EEELDEQAGSIQMLEQAKLRLEMEM 1587
Cdd:pfam07111 549 VARQGQQESTEEAASLRQELtqqQEIYGQALQEK--VAEVETRLREQLSDTKRRlNEARREQAKAVVSLRQIQHRATQEK 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 600971660 1588 ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQ 1650
Cdd:pfam07111 627 ERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDK 689
|
|
| secA |
PRK12903 |
preprotein translocase subunit SecA; Reviewed |
1779-1955 |
6.47e-04 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237258 [Multi-domain] Cd Length: 925 Bit Score: 45.05 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1779 RDMAQMNDLQAQIEESNKEKQELQEKLqALQSQVEFLEQSMVDKSLvsrqeaKIRELETRLEFEKTQVKRLENLASRLKE 1858
Cdd:PRK12903 741 VQYSQKNPYQVYTEEGTKKFNILLQEI-AYDVIVSLFNNPNAEKIL------IITEILSDGINNSDINDRPQELIDQIIE 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1859 T-MEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFK-R 1936
Cdd:PRK12903 814 SeEERLKALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEFKNDPKKLNKLIIAKdV 893
|
170
....*....|....*....
gi 600971660 1937 IGDLQAAIEDEMESDENED 1955
Cdd:PRK12903 894 LIKLVISSDEIKQDEKTTK 912
|
|
| PDZ5_DrPTPN13-like |
cd23060 |
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ... |
220-307 |
7.48e-04 |
|
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of Danio rerio Ptpn13, and related domains. Protein-tyrosine phosphatases (PTPs) dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases (PTKs). Danio rerio Ptpn13 is a classical non-receptor-like PTP. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467273 [Multi-domain] Cd Length: 80 Bit Score: 40.03 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPTGDFGFSLRRttmldrAPEGQAYRrvVHFAEPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:cd23060 1 QIELEKPANGGLGFSLVG------GEGGSGIF--VKSISPG-GVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKA 71
|
....*...
gi 600971660 300 GDSVRLKV 307
Cdd:cd23060 72 KGTVQLTV 79
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1551-1865 |
7.86e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1551 QLRDLeaKVKDQEEELDEQAGSIQMLEQA--KLRLEMEMERMRQthSKEMESRDEEVEEARQSCQKKLKQmevqLEEEYE 1628
Cdd:PRK05771 32 HIEDL--KEELSNERLRKLRSLLTKLSEAldKLRSYLPKLNPLR--EEKKKVSVKSLEELIKDVEEELEK----IEKEIK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1629 DKQKALR----EKRELESKLSTLSdqvNQRDFESEKRLRKDLKRTKALLADAQimldhlKNNAPSKREIAQLKNQLEESE 1704
Cdd:PRK05771 104 ELEEEISelenEIKELEQEIERLE---PWGNFDLDLSLLLGFKYVSVFVGTVP------EDKLEELKLESDVENVEYIST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1705 F----TCAAAVKARKAMEV--EMEDLHLQIDDIAKAKTALEEqLSRLQREKNEIQNRLEEDQEDMNELMKKHKaavaqas 1778
Cdd:PRK05771 175 DkgyvYVVVVVLKELSDEVeeELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELAKKYL------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1779 rdmaqmNDLQAQIEESNKEKQELQEKLQALQS----QVE-FLEQSMVD--KSLVSRQEAK---IRELETRLEFEKTQVKr 1848
Cdd:PRK05771 247 ------EELLALYEYLEIELERAEALSKFLKTdktfAIEgWVPEDRVKklKELIDKATGGsayVEFVEPDEEEEEVPTK- 319
|
330
....*....|....*..
gi 600971660 1849 LENlaSRLKETMEKLTE 1865
Cdd:PRK05771 320 LKN--PKFIKPFESLTE 334
|
|
| PDZ_RGS12-like |
cd06710 |
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ... |
222-308 |
8.57e-04 |
|
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467194 [Multi-domain] Cd Length: 76 Bit Score: 39.92 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 222 ELQRRPTGdFGFSLRrttmldrapeGQAYRRVVHFaepGAGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGD 301
Cdd:cd06710 4 EIARGRAG-YGFTIS----------GQAPCVLSCV---VRGSPADVAGLKAGDQILAVNGINVSKASHEDVVKLIGKCTG 69
|
....*..
gi 600971660 302 SVRLKVQ 308
Cdd:cd06710 70 VLRLVIA 76
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1733-2026 |
8.79e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.65 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1733 KAKTALEEQLSRLQ--REKNEIQNRLEEDQedmnelmkkhkaavAQASRDMAQMNDLQAQIEESNKEKQELQEKLqaLQS 1810
Cdd:PTZ00108 1031 AKKKDLVKELKKLGyvRFKDIIKKKSEKIT--------------AEEEEGAEEDDEADDEDDEEELGAAVSYDYL--LSM 1094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1811 QVEFLEQSMVDKsLVSRQEAKIRELEtrlEFEKTQVKR--LENLAsRLKETMEKlTEERDQRAAAENREKEQNKRL-QRQ 1887
Cdd:PTZ00108 1095 PIWSLTKEKVEK-LNAELEKKEKELE---KLKNTTPKDmwLEDLD-KFEEALEE-QEEVEEKEIAKEQRLKSKTKGkASK 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1888 LRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDS 1967
Cdd:PTZ00108 1169 LRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKN 1248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 1968 ELEDRVDGVKSWLSKNKGPSKAPSDDgsLKSSSPTSHWKPLAPDPSDDEHDPVDSISRP 2026
Cdd:PTZ00108 1249 NSSKSSEDNDEFSSDDLSKEGKPKNA--PKRVSAVQYSPPPPSKRPDGESNGGSKPSSP 1305
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1260-1346 |
9.05e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1260 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldAETAERLRTEKEMKELQT 1339
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKDREISRLDR 472
|
....*..
gi 600971660 1340 QYDALKK 1346
Cdd:COG2433 473 EIERLER 479
|
|
| RseP |
COG0750 |
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ... |
269-308 |
1.02e-03 |
|
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];
Pssm-ID: 440513 [Multi-domain] Cd Length: 349 Bit Score: 43.54 E-value: 1.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 600971660 269 GLVPGDRLVEINGQNVEnkSRDEIVEMIRQS-GDSVRLKVQ 308
Cdd:COG0750 145 GLQPGDRIVAINGQPVT--SWDDLVDIIRASpGKPLTLTVE 183
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1412-1629 |
1.06e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1412 RRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTK-----LHLEGQQvrnHELEKKQRRFDSELSQAHEETQREK 1486
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEA---KLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1487 LQREKLQREKDMLLAEAFSLKQqmeekDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ---- 1562
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaqri 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1563 ----EEELDEQAGSIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQ---SCQKKLKQMEVQLEEEYED 1629
Cdd:COG3206 315 laslEAELEALQAREASLQAQLAQLEARLAELPEL-EAELRRLEREVEVARElyeSLLQRLEEARLAEALTVGN 387
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1709-1900 |
1.08e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1709 AAVKARKAMEVEMEDLHlqiDDIAKAKTALEEQLSRLQRekneIQNRLEEDQEDMNELMKKHKAAVAQASRDMA------ 1782
Cdd:COG1842 20 KAEDPEKMLDQAIRDME---EDLVEARQALAQVIANQKR----LERQLEELEAEAEKWEEKARLALEKGREDLArealer 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1783 ------QMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFEKTQVKRLENLAS-- 1854
Cdd:COG1842 93 kaeleaQAEALEAQLAQLEEQVEKLKEALRQLESKLE-------------ELKAKKDTLKARAKAAKAQEKVNEALSGid 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 600971660 1855 -----RLKETMEKLTEERDQRAAAEnREKEQNKRLQRQLRDTKEEMS---ELAR 1900
Cdd:COG1842 160 sddatSALERMEEKIEEMEARAEAA-AELAAGDSLDDELAELEADSEvedELAA 212
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1721-1812 |
1.11e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 43.52 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1721 MEDLHLQIDDIAKAKTALE--------EQLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRDMAQMNDLQA 1789
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAkrgfpldvDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKE 80
|
90 100
....*....|....*....|...
gi 600971660 1790 QIEESNKEKQELQEKLQALQSQV 1812
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRI 103
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1637-1811 |
1.11e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1637 KRELESKLSTLSdqvnqrdfESEKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQleeseftcaaavkarka 1716
Cdd:smart00787 146 KEGLDENLEGLK--------EDYKLLMKELELLNSIKPKLRDRKDALE------EELRQLKQL----------------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1717 mEVEMEDLHLQIDDIAKAKtaleeqLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEE--- 1793
Cdd:smart00787 195 -EDELEDCDPTELDRAKEK------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQcrg 267
|
170
....*....|....*....
gi 600971660 1794 -SNKEKQELQEKLQALQSQ 1811
Cdd:smart00787 268 fTFKEIEKLKEQLKLLQSL 286
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1738-1927 |
1.19e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 43.90 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1738 LEEQLSRLQREKNEIQNRLEEDQEDMNELmkKHKAAVAQASRDM------AQMNDLQAQIEESNKEKQELQEKLQAlqsQ 1811
Cdd:pfam15070 34 LSEQVRTLREEKERSVSQVQELETSLAEL--KNQAAVPPAEEEQppagpsEEEQRLQEEAEQLQKELEALAGQLQA---Q 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1812 VEFLEQSmvdKSLVSRQEAKIRELETRLEFEKTQVKRLEnlasRLKETME--KLTeerDQRAAAENRE-KEQNKRLQRQ- 1887
Cdd:pfam15070 109 VQDNEQL---SRLNQEQEQRLLELERAAERWGEQAEDRK----QILEDMQsdRAT---ISRALSQNRElKEQLAELQNGf 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 600971660 1888 LRDTKEEM-------------SELARKEAEASRKKHEL--EMDLESLEAanQSLQ 1927
Cdd:pfam15070 179 VKLTNENMeltsalqseqhvkKELAKKLGQLQEELGELkeTLELKSQEA--QSLQ 231
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1733-1858 |
1.19e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.13 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1733 KAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQV 1812
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 600971660 1813 EFLEQSMVDKslvsrqEAKIRELETRLEFEKTQVKRLENLASRLKE 1858
Cdd:pfam10473 83 ENLTKELQKK------QERVSELESLNSSLENLLEEKEQEKVQMKE 122
|
|
| PDZ5_GRIP1-2-like |
cd06682 |
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
270-308 |
1.28e-03 |
|
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family domain PDZ5 is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467170 [Multi-domain] Cd Length: 85 Bit Score: 39.64 E-value: 1.28e-03
10 20 30
....*....|....*....|....*....|....*....
gi 600971660 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06682 46 LEPGDKLLAIDNIRLDNCSMEDAAQILQQAEDIVKLKIR 84
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1850-1959 |
1.33e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1850 ENLASRLKETMEKLTEERDQRAaaenREKEQNKRLQRQLRDTKEEMSELArKEAEAsrKKHELEMDLESLEAANQSLQAD 1929
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQA----REKAQSQALAEAQQQELVALEGLA-AELEE--KQQELEAQLEQLQEKAAETSQE 213
|
90 100 110
....*....|....*....|....*....|
gi 600971660 1930 LKLAFKRIGDlQAAIEDEMESDENEDLINS 1959
Cdd:PRK11448 214 RKQKRKEITD-QAAKRLELSEEETRILIDQ 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1268-1448 |
1.34e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1268 DEEIQQLRSKLEKVEKERNELRLSSDrletriseltseLTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQ 1347
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNG------------LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1348 MEVMEMEVMEAR--------LIRAAEINGEVDdddaggEWRLKY-------ERAVREVDFTKKRLQQELEDKMEVEQQSR 1412
Cdd:COG3206 249 LGSGPDALPELLqspviqqlRAQLAELEAELA------ELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190
....*....|....*....|....*....|....*.
gi 600971660 1413 RQLERRLGDLQADSDESQRALQQLKKKCQRLtAELQ 1448
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAEL-RRLE 357
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1256-1625 |
1.46e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1256 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRIseltseLTDERNTGESASQLldaetaerlrtEKEMK 1335
Cdd:PRK04778 113 LLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL------LANRFSFGPALDEL-----------EKQLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1336 ELQTQYDalkkqmevmemevmearliRAAEINGEVDDDDAggewRLKYERAVREVDFTK----------KRLQQELEDKM 1405
Cdd:PRK04778 176 NLEEEFS-------------------QFVELTESGDYVEA----REILDQLEEELAALEqimeeipellKELQTELPDQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1406 EVEQQSRRQLER---RLGDLQADSDesqraLQQLKKKCQRLTAELQDtkLHLEGQQVRNHELEKK--------QRRFDSE 1474
Cdd:PRK04778 233 QELKAGYRELVEegyHLDHLDIEKE-----IQDLKEQIDENLALLEE--LDLDEAEEKNEEIQERidqlydilEREVKAR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1475 lSQAHEETQREKLQREKLQREKDMLLAEAFSLKQ--QMEEKDLDIA-GFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1551
Cdd:PRK04778 306 -KYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsyTLNESELESVrQLEKQLESLEKQYDEITERIAEQEIAYSELQEE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1552 LRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQ---THSKEMESRD-----EEVEEARQSCQKKLKQMEVQL 1623
Cdd:PRK04778 385 LEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklhEIKRYLEKSNlpglpEDYLEMFFEVSDEIEALAEEL 464
|
..
gi 600971660 1624 EE 1625
Cdd:PRK04778 465 EE 466
|
|
| PDZ2_GRIP1-2-like |
cd06681 |
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
220-308 |
1.50e-03 |
|
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467169 [Multi-domain] Cd Length: 89 Bit Score: 39.52 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPtGDFGFSLR----RTTMLDRA-------PEGQAYRRvvhfaepgaGTkdlalgLVPGDRLVEINGQNVENKS 288
Cdd:cd06681 4 EVTLEKEG-NSFGFVIRggahEDRNKSRPltvthvrPGGPADRE---------GT------IKPGDRLLSVDGISLHGAT 67
|
90 100
....*....|....*....|
gi 600971660 289 RDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06681 68 HAEAMSILKQCGQEATLLIE 87
|
|
| PDZ3_MUPP1-like |
cd06791 |
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ... |
272-307 |
1.59e-03 |
|
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467253 [Multi-domain] Cd Length: 89 Bit Score: 39.52 E-value: 1.59e-03
10 20 30
....*....|....*....|....*....|....*.
gi 600971660 272 PGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06791 52 VNDQIIAVDGVNLQGFTNQEAVEVLRNTGQVVHLTL 87
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1828-1936 |
1.61e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1828 QEAKIRELETRLEFEKTQVKRLENLASRLKETMEklteERDQRAAaenREKEQNKRLQRQLRDTKEEMSELARKEAEASR 1907
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELE----EKDERIE---RLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|..
gi 600971660 1908 KKHELE---MDLESLEAANQSLQADLKLAFKR 1936
Cdd:COG2433 477 LERELEeerERIEELKRKLERLKELWKLEHSG 508
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1410-1653 |
1.67e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1410 QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLT-AELQdtklhlEGQQVrnhELEKKQRRfdseLSQAheetqrEKLq 1488
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELEaAALQ------PGEEE---ELEEERRR----LSNA------EKL- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1489 REKLQREKDML----------LAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESK-------DEASLAKVKK- 1550
Cdd:COG0497 225 REALQEALEALsggeggaldlLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRyldslefDPERLEEVEEr 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1551 --QLRDLEAKVKDQEEELdeqagsIQMLEQAKLRLEmemermrqthskEMESRDEEVEEarqscqkkLKQMEVQLEEEYE 1628
Cdd:COG0497 305 laLLRRLARKYGVTVEEL------LAYAEELRAELA------------ELENSDERLEE--------LEAELAEAEAELL 358
|
250 260
....*....|....*....|....*
gi 600971660 1629 DKQKALREKRELESKlsTLSDQVNQ 1653
Cdd:COG0497 359 EAAEKLSAARKKAAK--KLEKAVTA 381
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1320-1586 |
1.77e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1320 LDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVMEARliraaEINGEV-----------DDDDAGGEWRLKYERAVR 1388
Cdd:pfam05622 199 LSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLR-----ETNEELrcaqlqqaelsQADALLSPSSDPGDNLAA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1389 EV---DFTKKRLQQELEDKMEVEQQSrRQLERRLGDLQADSDESQRALQQL----KKKCQR---LTAELQDTKLHLEGQQ 1458
Cdd:pfam05622 274 EImpaEIREKLIRLQHENKMLRLGQE-GSYRERLTELQQLLEDANRRKNELetqnRLANQRileLQQQVEELQKALQEQG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1459 VRNHELEKKQRRFDS---ELSQAHEETQREKLQREKLQREKDMLLAE-AFSLKQQMEEKDLDIAGFTQK----------- 1523
Cdd:pfam05622 353 SKAEDSSLLKQKLEEhleKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEERykkyvekaksv 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 600971660 1524 VVSLEAELQDISSQEskdeasLAKVKKQLRDLEAKVKDQEEEldeqagsiqmLEQAKLRLEME 1586
Cdd:pfam05622 433 IKTLDPKQNPASPPE------IQALKNQLLEKDKKIEHLERD----------FEKSKLQREQE 479
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1652-1923 |
1.78e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.29 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1652 NQRDFESEKRLRKDLKRTKALLADAQImldhlknnapSKREIAQLKNQLEEseftcaAAVKARKAMEvemEDLHLQIDDI 1731
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDA----------SKQRAAAYQKALDD------APAELRELRQ---ELAALQAKAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1732 AKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNELMKkhkaavaqasrdmaQMNDLQAQIEESNKEKQELQEKLQALQS 1810
Cdd:pfam12795 69 AAPKEILASLsLEELEQRLLQTSAQLQELQNQLAQLNS--------------QLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1811 QvefLEQSMVDKSLVSrqEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRaaaenreKEQNKRLQRQLRD 1890
Cdd:pfam12795 135 R---LNGPAPPGEPLS--EAQRWALQAELAALKAQIDMLEQELLSNNNRQDLLKARRDLL-------TLRIQRLEQQLQA 202
|
250 260 270
....*....|....*....|....*....|...
gi 600971660 1891 TKEEMSELARKEAEASRKkhELEMDLESLEAAN 1923
Cdd:pfam12795 203 LQELLNEKRLQEAEQAVA--QTEQLAEEAAGDH 233
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1757-1907 |
1.82e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1757 EEDQEDMNELMKKHKAAVAQASRDMAQ-MNDLQAQIEESNKEKQELQEKLQalqsqvefleqsmvdkslvsRQEAKIREL 1835
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEeIRRLEEQVERLEAEVEELEAELE--------------------EKDERIERL 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 600971660 1836 ETRLEFEKTQVKRlenlasrlketmekltEERDQRaAAENREKEqNKRLQRQLRDTKEEMSELARKEAEASR 1907
Cdd:COG2433 447 ERELSEARSEERR----------------EIRKDR-EISRLDRE-IERLERELEEERERIEELKRKLERLKE 500
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1782-1957 |
1.93e-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: 41.94 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1782 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETrlEFEKTQvKRLENLASRLKEtME 1861
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAE------VAALNRRIQLLEE--ELERTE-ERLAEALEKLEE-AE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1862 KLTEERDQ-RAAAENREKEQNKR---LQRQLRDTKEEMSELARKEAEASRKKHELEMDLE-------SLEAANQSLQADL 1930
Cdd:pfam00261 71 KAADESERgRKVLENRALKDEEKmeiLEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraeeraeLAESKIVELEEEL 150
|
170 180
....*....|....*....|....*...
gi 600971660 1931 KLAFKRIGDLQAAIEDEMES-DENEDLI 1957
Cdd:pfam00261 151 KVVGNNLKSLEASEEKASEReDKYEEQI 178
|
|
| PDZ1_harmonin |
cd06737 |
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ... |
220-310 |
1.96e-03 |
|
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467219 [Multi-domain] Cd Length: 85 Bit Score: 39.16 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 220 ELELQRRPTGDFGFSLRR---------TTMLDraPEGQAYRRvvhfaepgagtkdlalGLVPGDRLVEINGQNVENKSRD 290
Cdd:cd06737 4 LVRLDRRGPESLGFSVRGglehgcglfVSHVS--PGSQADNK----------------GLRVGDEIVRINGYSISQCTHE 65
|
90 100
....*....|....*....|
gi 600971660 291 EIVEMIRQSgDSVRLKVQPI 310
Cdd:cd06737 66 EVINLIKTK-KTVSLKVRHV 84
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1845-1970 |
2.21e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1845 QVKRLENLASRLKETMEKLTEERDQRAAAENREKEqnkrLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQ 1924
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 600971660 1925 SLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSELE 1970
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ 139
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1267-1572 |
2.29e-03 |
|
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: 43.02 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1267 KDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAE---TAERLRTEKEMKELQTQYDA 1343
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEaeqELEESKRETETGIQNLTAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1344 LKKQMEVMEmevmearliRAAEINGEVDDDDAGGEWRLKYER---AVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLG 1420
Cdd:COG5185 346 EQGQESLTE---------NLEAIKEEIENIVGEVELSKSSEEldsFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1421 DLQADSDESQRALQQLKKKcqrlTAELQDTKLHLEgqqvrnHELEKKQRRFDSELSQAHEETQREKLQR-----EKLQRE 1495
Cdd:COG5185 417 AADRQIEELQRQIEQATSS----NEEVSKLLNELI------SELNKVMREADEESQSRLEEAYDEINRSvrskkEDLNEE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1496 KDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLE---AELQDISSQESKDEASLAKVKKQlRDLEAKvKDQEEELDEQAGS 1572
Cdd:COG5185 487 LTQIESRVSTLKATLEKLRAKLERQLEGVRSKLdqvAESLKDFMRARGYAHILALENLI-PASELI-QASNAKTDGQAAN 564
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1485-1636 |
2.32e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.43 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1485 EKLQREKLQREKDMLLAEAFSLKQQMEEKdldIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLRDLEAKVKDQEE 1564
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEP---LQKAQEEVEELRKQLE----NYEKDKQSLKNLKARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 600971660 1565 ELDeqagsiqMLEQAKLRLEMEMErmrqthskEMESRDEE-VEEARQSCQKK---LKQMEVQLEEEYEDKQKALRE 1636
Cdd:pfam13851 107 EHE-------VLEQRFEKVERERD--------ELYDKFEAaIQDVQQKTGLKnllLEKKLQALGETLEKKEAQLNE 167
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1768-1915 |
2.37e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1768 KKHKAAVAQASRDMAQMndlqaqIEESNKEKQELQeKLQALQSQVEFLE-QSMVDKSLVSRqEAKIRELETRLEFEKTQV 1846
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRI------LEEAKKEAEAIK-KEALLEAKEEIHKlRNEFEKELRER-RNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1847 KRLENLASRLKETMEKLTEERDQR--------AAAENREKEQNKRLQRQLRDTKEE-----MSELARK-EAEASRKKHEL 1912
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKqqelekkeEELEELIEEQLQELERISGLTAEEakeilLEKVEEEaRHEAAVLIKEI 178
|
...
gi 600971660 1913 EMD 1915
Cdd:PRK12704 179 EEE 181
|
|
| PDZ1_Scribble-like |
cd06704 |
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ... |
226-308 |
2.80e-03 |
|
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467188 [Multi-domain] Cd Length: 87 Bit Score: 38.80 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 226 RPTGDFGFSL---RRTTMLDRAPEGQAYRRVvhfAEPGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDS 302
Cdd:cd06704 7 RQTGGLGISIaggKGSTPYKGDDEGIFISRV---TEGGPAAKA---GVRVGDKLLEVNGVDLVDADHHEAVEALKNSGNT 80
|
....*.
gi 600971660 303 VRLKVQ 308
Cdd:cd06704 81 VTMVVL 86
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1260-1478 |
2.95e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1260 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDerntgesasqlldaetaerlrTEKEMKELQT 1339
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA---------------------LQAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1340 QYDALKKQmeVMEMEVMEARLIRAAEINGEVDDDDA---GGE------WRLKYERAVREVDFTKKRLQQELEDKMEVEQQ 1410
Cdd:COG3883 73 EIAEAEAE--IEERREELGERARALYRSGGSVSYLDvllGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 600971660 1411 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQA 1478
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1397-1534 |
3.00e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.89 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1397 LQQELEDKmEVEQQSRRQLERRLgdlqadsDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnheLEKKQRRFDSELS 1476
Cdd:pfam02841 178 LQEFLQSK-EAVEEAILQTDQAL-------TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQM---MEAQERSYQEHVK 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 600971660 1477 QAHEETQREklqREKLQREKDMLLAeafslKQQMEEKDLDIAGFTQKVVSLEAELQDI 1534
Cdd:pfam02841 247 QLIEKMEAE---REQLLAEQERMLE-----HKLQEQEELLKEGFKTEAESLQKEIQDL 296
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1771-1913 |
3.25e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.14 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1771 KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFEKTqvKRLE 1850
Cdd:TIGR02794 39 QAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAA---------EQARQKELEQRAAAEKA--AKQA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 600971660 1851 NLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELE 1913
Cdd:TIGR02794 108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEE 170
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1792-1910 |
3.34e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1792 EESNKEKQELQEKLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKL------TE 1865
Cdd:pfam20492 2 EEAEREKQELEERLKQYEEETKKAQEEL------EESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLeesaemEA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 600971660 1866 ERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKH 1910
Cdd:pfam20492 76 EEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| PDZ_Lin-7-like |
cd06796 |
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ... |
259-311 |
3.65e-03 |
|
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Lin-7-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467258 [Multi-domain] Cd Length: 86 Bit Score: 38.57 E-value: 3.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 600971660 259 PGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQPIP 311
Cdd:cd06796 35 PG-GVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVRYTP 86
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1665-1921 |
3.80e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1665 DLKRTKALladaqIMLDHLKNNAPSKREiaQLKNQLE-ESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLS 1743
Cdd:pfam15964 348 NFEKTKAL-----IQCEQLKSELERQKE--RLEKELAsQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1744 RLQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDMA-QMNDLQAQIEESNKEKQELQEKlqaLQSQVEFLEQsmvdk 1822
Cdd:pfam15964 421 KVTREKNSLVSQLEEAQKQ----LASQEMDVTKVCGEMRyQLNQTKMKKDEAEKEHREYRTK---TGRQLEIKDQ----- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1823 slvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDqraaaenrEKEQNKRLQRQLRDTKEE-MSELARK 1901
Cdd:pfam15964 489 --------EIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG--------ESEHQLHLTRLEKESIQQsFSNEAKA 552
|
250 260
....*....|....*....|.
gi 600971660 1902 EA-EASRKKHELEMDLESLEA 1921
Cdd:pfam15964 553 QAlQAQQREQELTQKMQQMEA 573
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1773-1906 |
3.84e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1773 AVAQASRDMAQMNDLQAQIEESNKEKQ-ELQEKL--QALQSQVEFLEQsmvdkslVSRQEAKIRELEtrlefektqvKRL 1849
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALNKQKLlEAEDKLvqQDLEQTLALLDK-------IDRQKEETEQLK----------QQL 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 600971660 1850 ENLASRLKETMEKLT--EERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAS 1906
Cdd:PRK11281 90 AQAPAKLRQAQAELEalKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYN 148
|
|
| PDZ_MAST1 |
cd23073 |
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 ... |
225-314 |
3.90e-03 |
|
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST family kinase MAST1, and related domains. MAST1 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain; MAST family member MASTL is a shorter protein lacking the PDZ domain. MAST1 functions as a scaffold protein to link the dystrophin/utrophin network with microfilaments via syntrophin, and it has been identified as a main driver of cisplatin resistance in human cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST1 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467286 [Multi-domain] Cd Length: 95 Bit Score: 38.47 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 225 RRPTGDFGFSLRRTTMLDRAPEGQAYRRVVHFAEPGAGTKDLalGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVR 304
Cdd:cd23073 8 QRSGKKYGFTLRAIRVYMGDSDVYSVHHIVWHVEEGGPAQEA--GLCAGDLITHVNGEPVHGMVHPEVVELILKSGNKVA 85
|
90
....*....|
gi 600971660 305 LKVQPIPELS 314
Cdd:cd23073 86 VTTTPFENTS 95
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1741-1930 |
4.35e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1741 QLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRdmaQMNDLQAQIEESNKEKQELQEKLQALQSQvefleQ 1817
Cdd:PRK11637 48 QLKSIQQDIAAKEKSVRQQQQQRASLlaqLKKQEEAISQASR---KLRETQNTLNQLNKQIDELNASIAKLEQQ-----Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1818 SMVDKSLVSRQEAKIRE-----LETRLEFEKTQVK-RLENLASRL----KETMEKLTEERDQrAAAENREKEQNKRLQRQ 1887
Cdd:PRK11637 120 AAQERLLAAQLDAAFRQgehtgLQLILSGEESQRGeRILAYFGYLnqarQETIAELKQTREE-LAAQKAELEEKQSQQKT 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 600971660 1888 LRDTKEEmSELARKEAEASRKKhelemDLESLEAANQSLQADL 1930
Cdd:PRK11637 199 LLYEQQA-QQQKLEQARNERKK-----TLTGLESSLQKDQQQL 235
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1549-1636 |
4.42e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.48 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1549 KKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1628
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQ 97
|
....*....
gi 600971660 1629 DK-QKALRE 1636
Cdd:pfam03938 98 DKiNKAIKE 106
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1688-1888 |
4.44e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1688 PSKREIaqlKNQLEeseftcaaAVKARKAMEVE-------MEDLHLQIDDIAKAK---TALEEQLSRLQREKNEIQNRLE 1757
Cdd:PRK11281 36 PTEADV---QAQLD--------ALNKQKLLEAEdklvqqdLEQTLALLDKIDRQKeetEQLKQQLAQAPAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1758 EdqedmnelMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQvefleqsmvdksLVSRQEAKIReLET 1837
Cdd:PRK11281 105 A--------LKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQ------------LVSLQTQPER-AQA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1838 RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQL 1888
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKS 214
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1697-1921 |
4.57e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 41.74 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1697 KNQLEESEFTCAAAVKARKAMEVEMEDLHLQ--IDDIAKAKTALEEQLS---RLQREKNEIQNRLEEDQEdmnelmkkhk 1771
Cdd:pfam15066 329 KQQMQIQDLQCSNLYLEKKVKELQMKITKQQvfVDIINKLKENVEELIEdkyNVILEKNDINKTLQNLQE---------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1772 aavaqasrdmaQMNDLQAQIEESNKEKQELQEKLQALQ-SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLE 1850
Cdd:pfam15066 399 -----------ILANTQKHLQESRKEKETLQLELKKIKvNYVHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQ 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 600971660 1851 nlasRLKETMEKLTEerdqrAAAENREKEQNKRLQRQLRDTKeemsELARKEAEASRKKHELEMDLESLEA 1921
Cdd:pfam15066 468 ----QLKGELEKATT-----SALDLLKREKETREQEFLSLQE----EFQKHEKENLEERQKLKSRLEKLVA 525
|
|
| PDZ_CASK-like |
cd10831 |
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ... |
273-309 |
4.63e-03 |
|
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CASK, Caenorhabditis elegans Lin-2, and related domains. CASK and Lin-2 are membrane-associated guanylate kinase (MAGUK)-like proteins. CASK (also known as Calcium/calmodulin-dependent protein kinase, CAKI, and Camguk) has a role in synaptic transmembrane protein anchoring and ion channel trafficking. CASK may regulate transmembrane proteins that bind calcium, calmodulin, or nucleotides; it regulates the Drosophila ether a go-go (eag) potassium channel, and also regulates autophosphorylation of CaMKII. CASK binding partners include the transcription factor TBR1, and cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. Lin-2, as a component of the CLin-10-Lin-2-Lin-7 complex, plays a role in controlling the basolateral localization of the EGF receptor Let-23; this complex also associates with the neuron-specific motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. CASK may also function in targeting or scaffolding of the protein parkin which is selectively truncated by a Parkinson's disease-causing mutation; the C-terminus of parkin functions as a class II PDZ-binding motif that binds CASK. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP6-MPP2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467267 [Multi-domain] Cd Length: 81 Bit Score: 37.85 E-value: 4.63e-03
10 20 30
....*....|....*....|....*....|....*..
gi 600971660 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd10831 45 GDEIREINGISVANQTVEQLQKMLREARGSITFKIVP 81
|
|
| PDZ3_MAGI-1_3-like |
cd06733 |
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
223-300 |
5.17e-03 |
|
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467215 [Multi-domain] Cd Length: 85 Bit Score: 37.98 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 223 LQRRPTGdFGFSLrrttmLDRAPEG-QAYrrVVHFAEPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQSG 300
Cdd:cd06733 6 LRRQETG-FGFRI-----LGGTEEGsQVS--IGAIVPGGAADLD---GrLRTGDELLSVDGVNVVGASHHKVVDLMGNAA 74
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1526-1827 |
5.39e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1526 SLEAeLQDISSQESKDEASLAKVKKQLRDLeAKVKDQEEELDEqagsiqmLEQaklRLEMEMERMRQThSKEMES-RDEE 1604
Cdd:PRK11281 44 QLDA-LNKQKLLEAEDKLVQQDLEQTLALL-DKIDRQKEETEQ-------LKQ---QLAQAPAKLRQA-QAELEAlKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1605 VEEARQSCQK-KLKQMEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL---RKDLKRT----KALL 1673
Cdd:PRK11281 111 DEETRETLSTlSLRQLESRLAQtldQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLqqiRNLLKGGkvggKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1674 ADAQIMLdhlknNApskrEIAQLKNQLEESEFTCAAAVKarkameveMEDLHLQIDDIAKAKTA-LEEQLSRLQREKNei 1752
Cdd:PRK11281 191 PSQRVLL-----QA----EQALLNAQNDLQRKSLEGNTQ--------LQDLLQKQRDYLTARIQrLEHQLQLLQEAIN-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1753 QNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQI--------EESNK-EKQELQEKLQ---ALQSQVEFLEQSMV 1820
Cdd:PRK11281 252 SKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLsqrllkatEKLNTlTQQNLRVKNWldrLTQSERNIKEQISV 331
|
....*....
gi 600971660 1821 DK-SLV-SR 1827
Cdd:PRK11281 332 LKgSLLlSR 340
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1420-1564 |
5.85e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1420 GDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAhEETQREKLQREKLQREKDML 1499
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQ---AAEQERLKQLEKERLAAQEQKKQA-EEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 600971660 1500 LAEAFSLKQQMEEKDLDIAGftqKVVSLEAELQDISSQESKDEaslAKVKKQLrDLEAKVKDQEE 1564
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAA---KKAAAEAKKKAEAEAAKKAA---AEAKKKA-EAEAAAKAAAE 198
|
|
| PDZ2_APBA1_3-like |
cd06793 |
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ... |
273-309 |
5.88e-03 |
|
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, APBA3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of APBA1, APBA2, APBA3, and related domains. The APBA/X11/Mint protein family includes three members: neuron specific APBA1 (also known as X11alpha and Mint1) and APBA2 (also known as X11beta and Mint2), and the ubiquitously expressed APBA3 (also known as X12gamma and Mint3). They are involved in regulating neuronal signaling, trafficking, and plasticity. They contain two PDZ domains (PDZ1 and PDZ2) which bind a variety of proteins: Arf GTPases (APBA1 and APBA2 PDZ2) and neurexin (APBA1 and APBA2 PDZ1 and 2) which are involved in vesicle docking and exocytosis; alpha1B subunit of N-type Ca2+ channel (APBA1 PDZ1) that is involved in ion channels; KIF17 (APBA1 PDZ1) that is involved in transport and traffic; and Alzheimer's disease related proteins, APP (APBA3 PDZ2), CCS (APBA1 PDZ2), NF-kappa-B/p65 (APBA2 PDZ2), presenilin-1 (APBA1 and APBA2 PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This APBA1,3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467255 [Multi-domain] Cd Length: 78 Bit Score: 37.38 E-value: 5.88e-03
10 20 30
....*....|....*....|....*....|....*..
gi 600971660 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06793 42 GHRIIEINGQSVVATPHEKIVQLLSNSVGEIHMKTMP 78
|
|
| PDZ_ZASP52-like |
cd23068 |
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ... |
269-308 |
6.20e-03 |
|
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Drosophila melanogaster Zasp52 and related domains. Drosophila melanogaster Zasp52 (also known as Z band alternatively spliced PDZ-motif protein or Zasp) colocalizes with integrins at myotendinous junctions and with alpha-actinin at Z-disks and is required for muscle attachment as well as Z-disk assembly and maintenance. The Zasp52 actin-binding site includes the extended PDZ domain and the ZM region. The Zasp52-PDZ domain is required for myofibril assembly. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Zasp52-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467281 [Multi-domain] Cd Length: 82 Bit Score: 37.51 E-value: 6.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 600971660 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd23068 42 GLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQ 81
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1537-1901 |
6.50e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.58 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1537 QESKD-EASLAKVKKQLRDLEAKVKDQEEELdeqagsiqmlEQAKLRLEMEMERMRQTHSKEMESR-DEEVEEARQSCQK 1614
Cdd:pfam13166 89 EESIEiQEKIAKLKKEIKDHEEKLDAAEANL----------QKLDKEKEKLEADFLDECWKKIKRKkNSALSEALNGFKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1615 KLKQMEVQLEE--EYEDKQKALREKRELESKLSTLSDQ---------VNQRDFESEKRLRKDLKRTKALLADAQIMLDHL 1683
Cdd:pfam13166 159 EANFKSRLLREieKDNFNAGVLLSDEDRKAALATVFSDnkpeiapltFNVIDFDALEKAEILIQKVIGKSSAIEELIKNP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1684 KNNAPSKREIAQLKNQLEESEFtC--------AAAVKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQL----------S 1743
Cdd:pfam13166 239 DLADWVEQGLELHKAHLDTCPF-CgqplpaerKAALEAHfdDEFTEFQNRLQKLIEKVESAISSLLAQLpavsdlasllS 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1744 RLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASR---------DMAQMNDLQAQIEES----NKEKQELQEKLQALQS 1810
Cdd:pfam13166 318 AFELDVEDIESEAEVLNSQLDGLRRALEAKRKDPFKsieldsvdaKIESINDLVASINELiakhNEITDNFEEEKNKAKK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1811 QVEfleqsmvdKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRD 1890
Cdd:pfam13166 398 KLR--------LHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKL--------------REEIKELEAQLRD 455
|
410
....*....|....
gi 600971660 1891 TK---EEMSELARK 1901
Cdd:pfam13166 456 HKpgaDEINKLLKA 469
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1586-1759 |
7.64e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1586 EMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQV-NQRDFES-EKRLr 1663
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEAlQKEI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1664 KDLKRTKALLADaqimldhlknnapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAktaLEEQLS 1743
Cdd:COG1579 99 ESLKRRISDLED----------------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELE 159
|
170
....*....|....*.
gi 600971660 1744 RLQREKNEIQNRLEED 1759
Cdd:COG1579 160 ELEAEREELAAKIPPE 175
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1691-1920 |
7.94e-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: 40.01 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1691 REIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1770
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1771 KAAVAQASRDMAQMNDLQAQI-------EESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEK 1843
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLkeakeiaEEADRKYEEVARKLVVVEGDLERAEER------AELAESKIVELEEELKVVG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1844 TQVKRLEnlasrlketmekLTEErdqrAAAENREKEQNkrlqrQLRDTKEEMSELARKEAEASRKKHELEMDLESLE 1920
Cdd:pfam00261 155 NNLKSLE------------ASEE----KASEREDKYEE-----QIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLE 210
|
|
| PDZ10_MUPP1-PDZ8_PATJ-like |
cd06673 |
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ... |
258-307 |
8.03e-03 |
|
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 10 of MUPP1, PDZ domain 8 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ10 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467161 [Multi-domain] Cd Length: 86 Bit Score: 37.27 E-value: 8.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 600971660 258 EPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06673 37 EDGAAAKD---GrLWAGDQILEVNGEDLRKATHDEAINVLRQTPQKVRLLV 84
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1396-1587 |
9.12e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1396 RLQQELEDKMEVEQQSRRQLE-RRLGDLQADSDESQRAlqQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRR---F 1471
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEqRRLQQEQLERAEKMRE--ELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLqlqA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1472 DSELSQAHEETQREKLQreKLQREKDMLLAE-AFSLKQQMEEKDLDIAGfTQKVVSLEAELQDISSQESKDEAslakvkK 1550
Cdd:pfam15709 417 AQERARQQQEEFRRKLQ--ELQRKKQQEEAErAEAEKQRQKELEMQLAE-EQKRLMEMAEEERLEYQRQKQEA------E 487
|
170 180 190
....*....|....*....|....*....|....*..
gi 600971660 1551 QLRDLEAKVKDQEEEldeqagsiqmlEQAKLRLEMEM 1587
Cdd:pfam15709 488 EKARLEAEERRQKEE-----------EAARLALEEAM 513
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1269-1763 |
9.29e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 40.82 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1269 EEIQQLRSKLEKVEKERnelrlssDRLETRISELTSELTDERNTGESASQLLDAETA----ERLRTEKEMKELQTQYDAL 1344
Cdd:pfam15070 29 QKMQQLSEQVRTLREEK-------ERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgpseEEQRLQEEAEQLQKELEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1345 kkqmevmemevmearlirAAEINGEVDDDDagGEWRLKYERAVREVDftkkrLQQELEDKMEVEQQSRRQLErrlgDLQA 1424
Cdd:pfam15070 102 ------------------AGQLQAQVQDNE--QLSRLNQEQEQRLLE-----LERAAERWGEQAEDRKQILE----DMQS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1425 DSDESQRALQQLKKKCQRLtAELQD-------------TKLHLEgQQVRNhELEKKQRRFDSELSQAHEETQREKLQREK 1491
Cdd:pfam15070 153 DRATISRALSQNRELKEQL-AELQNgfvkltnenmeltSALQSE-QHVKK-ELAKKLGQLQEELGELKETLELKSQEAQS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1492 LQREKDMLLAE----AFSLKQQMEEKDLdiagfTQKVVSLEAELQD-ISSQESKDEASLAKVKKQLRD----LEAKVKDQ 1562
Cdd:pfam15070 230 LQEQRDQYLAHlqqyVAAYQQLASEKEE-----LHKQYLLQTQLMDrLQHEEVQGKVAAEMARQELQEtqerLEALTQQN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1563 EEEldeQAGSIQMLEQAK---LRLEMEMERMRQTH---SKEMESRDEEVE---EARQSCQKKLKQMEVQLEEEYedkqka 1633
Cdd:pfam15070 305 QQL---QAQLSLLANPGEgdgLESEEEEEEAPRPSlsiPEDFESREAMVAffnSALAQAEEERAELRRQLKEQK------ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1634 lREKRELESKLSTLSDQvnQRDFESEKRLRKD---LKRTKALladaQIMLDHLKNNAPS-KREIAQLKNQLEESEFTCAa 1709
Cdd:pfam15070 376 -RRCRRLAQQAAPAQEE--PEHEAHAPGTGGDsvpVEVHQAL----QVAMEKLQSRFTElMQEKADLKERVEELEHRCI- 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 600971660 1710 avkarkamevemeDLHLQIDDIAKAKTALEEQ---LSRLQREKNEIQNRLEEDQEDM 1763
Cdd:pfam15070 448 -------------QLSGETDTIGEYIALYQSQraiLKQRHREKEEYISRLAQDKEEM 491
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1451-1636 |
9.52e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.71 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1451 KLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQK-VVSLEA 1529
Cdd:pfam15709 337 RLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKqRLQLQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1530 ELQDISSQESKDEASLAKVKKQLRDLEAKvKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEAR 1609
Cdd:pfam15709 417 AQERARQQQEEFRRKLQELQRKKQQEEAE-RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAE 495
|
170 180
....*....|....*....|....*..
gi 600971660 1610 QSCQKKLKQMEVQLEEEYEDKQKALRE 1636
Cdd:pfam15709 496 ERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1397-1558 |
9.56e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1397 LQQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRrfds 1473
Cdd:pfam13851 27 LIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELK---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1474 ELSQAHEEtqreKLQR-EKLQREKDMLLAE----AFSLKQQMEEKDLDIAgftQKVVSL-------EAELQDISSQESKD 1541
Cdd:pfam13851 103 DLKWEHEV----LEQRfEKVERERDELYDKfeaaIQDVQQKTGLKNLLLE---KKLQALgetlekkEAQLNEVLAAANLD 175
|
170
....*....|....*...
gi 600971660 1542 EASLAKVKKQLRD-LEAK 1558
Cdd:pfam13851 176 PDALQAVTEKLEDvLESK 193
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1772-1888 |
9.58e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1772 AAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMvdkSLVSRQeakIRELETRLEfektqvkRLEN 1851
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAI---SQASRK---LRETQNTLN-------QLNK 103
|
90 100 110
....*....|....*....|....*....|....*..
gi 600971660 1852 LASRLKETMEKLteerdqraaaENREKEQNKRLQRQL 1888
Cdd:PRK11637 104 QIDELNASIAKL----------EQQQAAQERLLAAQL 130
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1713-1817 |
9.73e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 37.93 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600971660 1713 ARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIE 1792
Cdd:pfam13863 11 VQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIE 90
|
90 100
....*....|....*....|....*
gi 600971660 1793 ESNKEKQELQEKLQALQSQVEFLEQ 1817
Cdd:pfam13863 91 ELKSEISKLEEKLEEYKPYEDFLEK 115
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