|
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 ... |
323-1069 |
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: 1128.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTSGtKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 482
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVG-GVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 483 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEE 562
Cdd:cd01386 160 LLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 563 QKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFRQGPEESGLG 639
Cdd:cd01386 240 QRAIWSILAAIYHLGAAGATKaasAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQESPARSSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 640 EGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGSARGASFEELCHNYAQDRLQR 719
Cdd:cd01386 320 GGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERLQL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 720 LFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASH--LVRSLAHADEARGLLWLLEEEALVPGATEDALLDRL 797
Cdd:cd01386 400 LFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqaLVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFLERL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 798 FSYYGPQEGDkKGQSPLLRSSKPRHFLLGHSHGTNWVEYNVAGWLNYTKQNPATQNAPRLLQDSQKKiisnlflgragsa 877
Cdd:cd01386 480 FSHYGDKEGG-KGHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE------------- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 878 tvlsgsiagleggsqlalrratsmrktfttgMAAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGEPRsa 957
Cdd:cd01386 546 -------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDERS-- 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 958 ssrrvsssseldlppGDPCEAGLLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYI 1037
Cdd:cd01386 593 ---------------TSSPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSE 657
|
730 740 750
....*....|....*....|....*....|..
gi 1907082237 1038 VVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd01386 658 VADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
324-1069 |
1.07e-143 |
|
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: 463.22 E-value: 1.07e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTSGTKVFS-----VEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 477
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSSsassiEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 478 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAEN---NVFGIVPLSKPEEKQKAAQQFSKLQAAMK 554
Cdd:cd00124 162 SIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYyylNDYLNSSGCDRIDGVDDAEEFQELLDALD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 555 VLAISPEEQKTCWLILASIYHLG-----AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTlqrstsf 629
Cdd:cd00124 242 VLGFSDEEQDSIFRILAAILHLGniefeEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGG------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 630 rqgpeESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSS--QHSLCSMMIVDTPGFQNPEWggsargASFEE 707
Cdd:cd00124 315 -----ETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTdaAESTSFIGILDIFGFENFEV------NSFEQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 708 LCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDLEPVAD------DSV-AAVDQASHLvrslahadeargllw 777
Cdd:cd00124 384 LCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSfidFPDNQDCLDliegkpLGIlSLLDEECLF--------------- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 778 lleeealvPGATEDALLDRLFSYYGPQEGDKKGqspllRSSKPRHFllGHSHGTNWVEYNVAGWLNYTKQNpatqnaprl 857
Cdd:cd00124 449 --------PKGTDATFLEKLYSAHGSHPRFFSK-----KRKAKLEF--GIKHYAGDVTYDADGFLEKNKDT--------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 858 lqdsqkkiisnlflgragsatvLSGSIAGLeggsqlaLRRATSMRKtfttgmaavkkkslciqiklQVDALIDTIKRSKM 937
Cdd:cd00124 505 ----------------------LPPDLVDL-------LRSGSQFRS--------------------QLDALMDTLNSTQP 535
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 938 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1017
Cdd:cd00124 536 HFVRCIKPNDEKKPG-----------------------------LFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1907082237 1018 RRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd00124 587 LKRYRILAPGATEKA-----SDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
304-1081 |
2.39e-113 |
|
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: 377.27 E-value: 2.39e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 304 NAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQ 383
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 384 TAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGtSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFS 461
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG-SNTEVGSVED-QILESnpILEAFGNAKTLRNNNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 462 QILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFgivpLSKPEEKQK 541
Cdd:smart00242 159 KFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRY----LNQGGCLTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 542 A----AQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG----AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAI 613
Cdd:smart00242 234 DgiddAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGniefEEGRNDNAASTVKDKEELSNAAELLGVDPEELEKAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 614 fkhqlkggtLQRSTSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQ- 692
Cdd:smart00242 314 ---------TKRKIKTGGEVITKPL---NVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEi 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 693 ---NpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVRS- 765
Cdd:smart00242 382 fevN----------SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDwtfIDFFDNQDCID-----------LIEKk 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 766 ----LAHADEArgllwlleeeALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEYNV 838
Cdd:smart00242 441 ppgiLSLLDEE----------CRFPKGTDQTFLEKLNQHH--------KKHPHFSKPKKKgrtEFIIKHYAGD--VTYDV 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 839 AGWLnytKQN--PATQNAPRLLQDSQKKIISNLFlgragsatvlsGSIAGleggsqlalrRATSMRKTFTTGMaavkkks 916
Cdd:smart00242 501 TGFL---EKNkdTLSDDLIELLQSSKNPLIASLF-----------PSGVS----------NAGSKKRFQTVGS------- 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 917 lciQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSR 996
Cdd:smart00242 550 ---QFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPG-----------------------------DFDSSLVLHQLRYLG 597
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 997 LLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFRAGTLARL 1076
Cdd:smart00242 598 VLENIRIRRAGFPYRLPFDEFLQRYRVLLPD-TWPPWGG----DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAEL 672
|
....*
gi 1907082237 1077 EEQRD 1081
Cdd:smart00242 673 EELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
285-1795 |
7.60e-110 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 386.74 E-value: 7.60e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 285 KLDHDGAILDVDEDDIEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMH 364
Cdd:COG5022 42 KEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 365 MFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKwQALST--L 442
Cdd:COG5022 122 SYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEK-QILATnpI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 443 LEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL--- 519
Cdd:COG5022 201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLqnp 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 520 ---NHLAENNVFGIVPLSKPEEkqkaaqqFSKLQAAMKVLAISPEEQKTCWLILASIYHLG--AAGATKAGRKQFARHEW 594
Cdd:COG5022 281 kdyIYLSQGGCDKIDGIDDAKE-------FKITLDALKTIGIDEEEQDQIFKILAAILHIGniEFKEDRNGAAIFSDNSV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 595 AQKAAYLLGCSLEELSSAIFKHQLKGG--TLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRA 672
Cdd:COG5022 354 LDKACYLLGIDPSLFVKWLVKRQIKTGgeWIVVPLNLEQ--------------ALAIRDSLAKALYSNLFDWIVDRINKS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 673 LKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVA 749
Cdd:COG5022 420 LDHSAAASNFIGVLDIYGFEIFEKN------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEwsfIDYFDNQPCI 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 750 DDSvaavdQASHLVRSLAHADEArgllwlleeeALVPGATEDALLDRLFSYYgPQEGDKKGQSPLLRSSKprhFLLGHSH 829
Cdd:COG5022 494 DLI-----EKKNPLGILSLLDEE----------CVMPHATDESFTSKLAQRL-NKNSNPKFKKSRFRDNK---FVVKHYA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 830 GTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvlsgsiaglEGGSQLALRRATSMrktfttgm 909
Cdd:COG5022 555 GD--VEYDVEGFLDKNK-DPLNDDLLELLKASTNEFVSTLFDDEE-------------NIESKGRFPTLGSR-------- 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 910 aavkkkslciqIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLR 989
Cdd:COG5022 611 -----------FKESLNSLMSTLNSTQPHYIRCIKPNEEKSPW-----------------------------TFDNQMVL 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 990 AQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNYIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:COG5022 651 SQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPS-KSWTGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFK 729
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1070 AGTLARLEEQRDEQTSRHLTLFQAACRGYLARQHF-KKRKIQDlAIRCVQKNIKKNKGVKDWPWWKLFTTVRPLIQVQLS 1148
Cdd:COG5022 730 AGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYlQALKRIK-KIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGS 808
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1149 EEQIRNKDEEIQQLRSKLEKV----EKERNELRLSSDRLETRISEltSELTDERNTGESASQLLDAETAERLRTEKEMKE 1224
Cdd:COG5022 809 RKEYRSYLACIIKLQKTIKREkklrETEEVEFSLKAEVLIQKFGR--SLKAKKRFSLLKKETIYLQSAQRVELAERQLQE 886
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1225 LQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDF----TKKRLQQELEDKMEVEQQSR 1300
Cdd:COG5022 887 LKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLeegpSIEYVKLPELNKLHEVESKL 966
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1301 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRrfdsELSQAHEETQREKLQREKL 1380
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPV----EVAELQSASKIISSESTEL 1042
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1381 QREKDMLLAEAFSLKQQME-EKDLdiagftqKVVSLEAELQDIssqESKDEASLAKVKKQLRDLEAK---VKDQEEELDE 1456
Cdd:COG5022 1043 SILKPLQKLKGLLLLENNQlQARY-------KALKLRRENSLL---DDKQLYQLESTENLLKTINVKdleVTNRNLVKPA 1112
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1457 QAGSIQMLEQAKLRLEMEMERM--RQTHSKEMESRDEEVEEARQSCQKKLKQMEvqlEEEYEDKQKALREKRELESKL-- 1532
Cdd:COG5022 1113 NVLQFIVAQMIKLNLLQEISKFlsQLVNTLEPVFQKLSVLQLELDGLFWEANLE---ALPSPPPFAALSEKRLYQSALyd 1189
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1533 --STLSDQVNQ---RDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLknqleESEFTCAAAVKarkamev 1607
Cdd:COG5022 1190 ekSKLSSSEVNdlkNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNL-----NKKFDTPASMS------- 1257
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1608 eMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLeeDQEDMNEL-MKKHKAAVAQASRDmaqmnDLQAQIEESNKEK 1686
Cdd:COG5022 1258 -NEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYI--NVGLFNALrTKASSLRWKSATEV-----NYNSEELDDWCRE 1329
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1687 QELQEklqaLQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKT-QVKRLENlasrlketmeklteeRDQRAAAENR- 1764
Cdd:COG5022 1330 FEISD----VDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPaEIQNLKS---------------RYDPADKENNl 1390
|
1530 1540 1550
....*....|....*....|....*....|.
gi 1907082237 1765 EKEQNKRLQRQLRDTKEEMSELARKEAEASR 1795
Cdd:COG5022 1391 PKEILKKIEALLIKQELQLSLEGKDETEVHL 1421
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
312-1069 |
4.63e-107 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 358.90 E-value: 4.63e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 312 EDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLM 391
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 392 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGT-SGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDF 468
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSgSAGNVGRLEE-QILQSnpILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 469 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL---------NHLAENNVFGIvplskpeek 539
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyhylSQSGCYTIDGI--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 540 qKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFA---RHEWAQKAAYLLGCSLEELSSAIFKH 616
Cdd:pfam00063 232 -DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAvpdDTENLQKAASLLGIDSTELEKALCKR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 617 QLKGGTLQRSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPE 695
Cdd:pfam00063 311 RIKTGRETVSKPQ------------NVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIgVLDIYGFEIFE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 696 WGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVRS-----LA 767
Cdd:pfam00063 379 KN------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEwtfIDFGDNQPCID-----------LIEKkplgiLS 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 768 HADEArgllwlleeeALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLNY 844
Cdd:pfam00063 442 LLDEE----------CLFPKATDQTFLDKLYSTF--------SKHPHFQKPRLQgetHFIIKHYAGD--VEYNVEGFLEK 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 845 TKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvLSGSIAGLEGGSQLALRRATSMRKtfTTGMaavkkkslciQIKLQ 924
Cdd:pfam00063 502 NK-DPLNDDLVSLLKSSSDPLLAELFPDYE-----TAESAAANESGKSTPKRTKKKRFI--TVGS----------QFKES 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 925 VDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMY 1004
Cdd:pfam00063 564 LGELMKTLNSTNPHYIRCIKPNEKKRAG-----------------------------VFDNSLVLHQLRCNGVLEGIRIR 614
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1005 RQGYPDHMVFSEFRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:pfam00063 615 RAGFPNRITFQEFVQRYRILAPKTWPK-----WKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
324-1069 |
9.42e-100 |
|
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: 337.13 E-value: 9.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPyKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW-----QALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 475
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledQILQAnpILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 476 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFgIVPLSKPEEKQKAAQQFSKLQAAMKV 555
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFF-LSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 556 LAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRSTSFR 630
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAEldgTEEADKAAHLLGVNSSDLLKALLKPRIKVGRewVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 631 QgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQ----NpewggsargaSFE 706
Cdd:cd01377 320 Q--------------VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN----------SFE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 707 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF----DDLEPVADdsvaavdqashLVRS-----LAHADEargllw 777
Cdd:cd01377 376 QLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgLDLQPTID-----------LIEKpnmgiLSILDE------ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 778 lleeEALVPGATEDALLDRLFSYygpQEGDKKGQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLnyTK-QNPATQNAPR 856
Cdd:cd01377 439 ----ECVFPKATDKTFVEKLYSN---HLGKSKNFKKPKPKKSEAHFILKHYAGD--VEYNIDGWL--EKnKDPLNENVVA 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 857 LLQDSQKKIISNLFlgragsatvlsgSIAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSK 936
Cdd:cd01377 508 LLKKSSDPLVASLF------------KDYEESGGGGGKKKKKGGSFRT----VSQLHKEQL--------NKLMTTLRSTH 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 937 MHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSE 1016
Cdd:cd01377 564 PHFVRCIIPNEEKKPGK-----------------------------IDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAE 614
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1907082237 1017 FRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd01377 615 FKQRYSILAPNAIPK-----GFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
323-1069 |
3.31e-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: 306.94 E-value: 3.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIA-----GTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 475
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAsshkgRKDHNIPGELER-QLLQAnpILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 476 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF--GIVPLSkpeeKQKAAQQFSKLQAAM 553
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsnGYIPIP----GQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 554 KVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRSTs 628
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmpeNTVAQKLCHLLGMNVMEFTRAILTPRIKVGRdyVQKAQ- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 629 frqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEE 707
Cdd:cd14920 315 -------------TKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIgILDIAGFEIFELN------SFEQ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 708 LCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFD----DLEPVADdsvaAVDQASHLVRSLAHADEargllwlleeEA 783
Cdd:cd14920 376 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIdfglDLQPCID----LIERPANPPGVLALLDE----------EC 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 784 LVPGATEDALLDRLfsyygpqEGDKKGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQD 860
Cdd:cd14920 442 WFPKATDKTFVEKL-------VQEQGSHSKFQKPRQLKdkaDFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVATLLHQ 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 861 SQKKIISNLFlgRAGSATVlsgSIAGLEGGSQLALRRATSMRKTFTTGMAAVKKKSLciqiklqvDALIDTIKRSKMHFV 940
Cdd:cd14920 512 SSDRFVAELW--KDVDRIV---GLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESL--------TKLMATLRNTNPNFV 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 941 HCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1020
Cdd:cd14920 579 RCIIPNHEKRAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 629
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1907082237 1021 FDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14920 630 YEILTPNAIPK-----GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
323-1069 |
2.02e-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: 2.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIA----GTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 476
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAsshkGKKDTSITGELEKQLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 477 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNV--FGIVPLSkpeeKQKAAQQFSKLQAAMK 554
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFlsNGFVPIP----AAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 555 VLAISPEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTSFRQ 631
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKernTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVG-----RDVVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 632 GPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEELCH 710
Cdd:cd14921 312 KAQ-------TKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEIFEVN------SFEQLCI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 711 NYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPGATE 790
Cdd:cd14921 379 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDE----------ECWFPKATD 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 791 DALLDRLFSyygPQEGDKKGQSPLLRSSKPRHFLLghsHGTNWVEYNVAGWLNyTKQNPATQNAPRLLQDSQKKIISNLF 870
Cdd:cd14921 449 KSFVEKLCT---EQGNHPKFQKPKQLKDKTEFSII---HYAGKVDYNASAWLT-KNMDPLNDNVTSLLNASSDKFVADLW 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 871 LGragsatvlSGSIAGLEGGSQLALRRATSMRKTfTTGMAavkkKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGW 950
Cdd:cd14921 522 KD--------VDRIVGLDQMAKMTESSLPSASKT-KKGMF----RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKR 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 951 PGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTK 1030
Cdd:cd14921 589 SG-----------------------------KLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIP 639
|
730 740 750
....*....|....*....|....*....|....*....
gi 1907082237 1031 KHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14921 640 KG-----FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
323-1069 |
9.99e-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: 288.03 E-value: 9.99e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIA-----GTSGTKVFSV-------EKWQAL---STLLEAFGNSPTIMNGSATRFSQILSLD 467
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpkGSGAVPHPAVnpavligELEQQLlqaNPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 468 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVF---GIVPLSKPEEkqkaAQ 544
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDD-VKSYAFlsnGSLPVPGVDD----YA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 545 QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGG 621
Cdd:cd14911 236 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQernNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 622 tlqrstsfRQGPEESGLGEGTKLSalecLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsa 700
Cdd:cd14911 316 --------RDFVTKAQTKEQVEFA----VEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIgILDMAGFEIFELN--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 701 rgaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFD----DLEPVADdsvaavdqashLVrslahaDEARGLL 776
Cdd:cd14911 381 ---SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIdfglDLQPTID-----------LI------DKPGGIM 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 777 WLLEEEALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLnYTKQNPATQN 853
Cdd:cd14911 441 ALLDEECWFPKATDKTFVDKLVSAH--------SMHPKFMKTDFRgvaDFAIVHYAGR--VDYSAAKWL-MKNMDPLNEN 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 854 APRLLQDSQKKIISNLFlgraGSATVLSGSIAGLeGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQVDALIDTIK 933
Cdd:cd14911 510 IVSLLQGSQDPFVVNIW----KDAEIVGMAQQAL-TDTQFGARTRKGMFRTVSH------------LYKEQLAKLMDTLR 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 934 RSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMV 1013
Cdd:cd14911 573 NTNPNFVRCIIPNHEKRAG-----------------------------KIDAPLVLDQLRCNGVLEGIRICRQGFPNRIP 623
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082237 1014 FSEFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14911 624 FQEFRQRYELLTPNVIPKG-----FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
323-1069 |
5.59e-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: 282.69 E-value: 5.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTSGTK------VFS---VEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQA 471
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKkdqssiALShgeLEK-QLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 472 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQA 551
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDK--ELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 AMKVLAISPEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTS 628
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKernSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVG-----RD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 629 FRQGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEE 707
Cdd:cd14932 313 YVQKAQ-------TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN------SFEQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 708 LCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPG 787
Cdd:cd14932 380 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDE----------ECWFPK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 788 ATEDALLDRLFSYYGpqeGDKKGQSPlLRSSKPRHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKIIS 867
Cdd:cd14932 450 ATDKSFVEKVVQEQG---NNPKFQKP-KKLKDDADFCIIHYAGK--VDYKANEWL-MKNMDPLNENVATLLNQSTDKFVS 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 868 NLFlgRAGSATVLSGSIAGLEGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQVDALIDTIKRSKMHFVHCFLPVA 947
Cdd:cd14932 523 ELW--KDVDRIVGLDKVAGMGESLHGAFKTRKGMFRTVGQ------------LYKEQLMNLMTTLRNTNPNFVRCIIPNH 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 948 EGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1027
Cdd:cd14932 589 EKKAG-----------------------------KLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1907082237 1028 LTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14932 640 AIPKG-----FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
323-1069 |
3.85e-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: 277.36 E-value: 3.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQAL---STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASI 479
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLlqaNPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 480 QTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQAAMKVLAIS 559
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK--DMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 560 PEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTSFRQGPEes 636
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKernTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG-----RDYVQKAQ-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 637 glgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEELCHNYAQD 715
Cdd:cd14919 312 -----TKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIgILDIAGFEIFDLN------SFEQLCINYTNE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 716 RLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPGATEDALLD 795
Cdd:cd14919 381 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDE----------ECWFPKATDKSFVE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 796 RLFSYYGPQegdKKGQSPLLRSSKPrHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKIISNLFlgRAG 875
Cdd:cd14919 451 KVVQEQGTH---PKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWL-MKNMDPLNDNIATLLHQSSDKFVSELW--KDV 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 876 SATVLSGSIAGLeggSQLALRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDTIKRSKMHFVHCFLPVAEGWPGepr 955
Cdd:cd14919 522 DRIIGLDQVAGM---SETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIPNHEKKAG--- 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 956 sassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHgrn 1035
Cdd:cd14919 588 --------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG--- 638
|
730 740 750
....*....|....*....|....*....|....
gi 1907082237 1036 yiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14919 639 --FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
323-1069 |
1.07e-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: 272.62 E-value: 1.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTSGTKvfsvEKWQAL-------STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 475
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESK----KKLGALedqimqaNPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 476 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDATLRTELHLN------HLAENNVFGIvplskpeEKQKAAQQFSKL 549
Cdd:cd14929 157 SADIDIYLLEKSRVIFQQPGERNYHIFYQILS-GKKELRDLLLVSanpsdfHFCSCGAVAV-------ESLDDAEELLAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 550 QAAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARH---EWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQ 624
Cdd:cd14929 229 EQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEAdgtENADKAAFLMGINSSELVKGLIHPRIKVGNeyVT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 625 RSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaS 704
Cdd:cd14929 309 RSQNIEQVTYAVG--------------ALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYN------S 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 705 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELafddlepvaddsvAAVDQASHLVRSLAHADEARGLLWLLEEEAL 784
Cdd:cd14929 369 LEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDW-------------VSIDFGLDLQACIDLIEKPMGIFSILEEECM 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 785 VPGATEDALLDRLFSYYgpqegdkKGQSPLLRSSKPR------HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLL 858
Cdd:cd14929 436 FPKATDLTFKTKLFDNH-------FGKSVHFQKPKPDkkkfeaHFELVHYAGV--VPYNISGWLEKNK-DLLNETVVAVF 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 859 QDSQKKIISNLFlgragSATVLSGSiaGLEGGSQlALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKMH 938
Cdd:cd14929 506 QKSSNRLLASLF-----ENYISTDS--AIQFGEK-KRKKGASFQT-----VASLHKENL--------NKLMTNLKSTAPH 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 939 FVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1018
Cdd:cd14929 565 FVRCINPNVNKIPG-----------------------------VLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFK 615
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1019 RRFDVLAPHLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14929 616 QRYCILNPRTFPKSK----FVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
323-1069 |
2.02e-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: 2.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAG 472
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELekqllqanpiLEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 473 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQAA 552
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDK--DLFTETMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 553 MKVLAISPEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRST 627
Cdd:cd15896 239 FRIMGIPEDEQIGMLKVVASVLQLGNMSFKKerhTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRdyVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 628 SFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFE 706
Cdd:cd15896 319 TQEQ--------------AEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN------SFE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 707 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVP 786
Cdd:cd15896 379 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDE----------ECWFP 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 787 GATEDALLDRLFSYYGPQEGDKKGQspllRSSKPRHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKII 866
Cdd:cd15896 449 KATDKSFVEKVLQEQGTHPKFFKPK----KLKDEADFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVATLLNQSTDKFV 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 867 SNLFLGragsatvlSGSIAGLEGGSQLA-LRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDTIKRSKMHFVHCFLP 945
Cdd:cd15896 522 SELWKD--------VDRIVGLDKVSGMSeMPGAFKTRKGMFRTVGQLYKE--------QLSKLMATLRNTNPNFVRCIIP 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 946 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1025
Cdd:cd15896 586 NHEKKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082237 1026 PHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd15896 637 PNAIPKG-----FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
323-1069 |
9.94e-73 |
|
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: 258.35 E-value: 9.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIA--GTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQ 470
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalGDGPGKKAQFLATKTGGTLedqiieanpaMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 471 AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLN------HLAENNVFGIVPLSKPEEkqkaaq 544
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmnpydyHFCSQGVTTVDNMDDGEE------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 545 qFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARH---EWAQKAAYLLGCSLEELSSAIFKHQLKGG 621
Cdd:cd14927 235 -LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAdgtESADKAAYLMGVSSADLLKGLLHPRVKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 622 tlQRSTSFRQGPEESGLGEGtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsar 701
Cdd:cd14927 314 --NEYVTKGQSVEQVVYAVG----------ALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFN---- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 702 gaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQASHLVRSLAHADEargllwllee 781
Cdd:cd14927 378 --SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDF---GLDLQACIDLIEKPLGILSILEE---------- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 782 EALVPGATEDALLDRLFSYYgpqegdkKGQSPLLRSSKP-------RHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNA 854
Cdd:cd14927 443 ECMFPKASDASFKAKLYDNH-------LGKSPNFQKPRPdkkrkyeAHFEVVHYAGV--VPYNIVGWLDKNK-DPLNETV 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 855 PRLLQDSQKKIISNLFLGRAGSAtvlsgSIAGLEGGSQLALRRATSmrktFTTgMAAVKKKSLciqiklqvDALIDTIKR 934
Cdd:cd14927 513 VAIFQKSQNKLLATLYENYVGSD-----STEDPKSGVKEKRKKAAS----FQT-VSQLHKENL--------NKLMTNLRA 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 935 SKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVF 1014
Cdd:cd14927 575 TQPHFVRCIIPNETKTPG-----------------------------VMDPFLVLHQLRCNGVLEGIRICRKGFPNRILY 625
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1015 SEFRRRFDVLAPHLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14927 626 ADFKQRYRILNPSAIPDDK----FVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
323-1069 |
9.45e-72 |
|
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: 255.15 E-value: 9.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW----QALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 476
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGsledQVVQTnpVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 477 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlaeNNVFGIVPLSKPE---EKQKAAQQFSKLQAAM 553
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLS----DNIYDYYIVSQGKvtvPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 554 KVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARH---EWAQKAAYLLGCSLEELSSAIFKHQLKGGTlQRSTSFR 630
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQdgeEEGGRVSKLFGCDTAELYKNLLKPRIKVGN-EFVTQGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 631 QgpeesglgegtKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGsargasFEELCH 710
Cdd:cd14909 316 N-----------VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------FEQLCI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 711 NYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPGATE 790
Cdd:cd14909 379 NFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDF---GMDLLACIDLIEKPMGILSILEE----------ESMFPKATD 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 791 DALLDRLFSyygpqegDKKGQSPLLRSSKP-------RHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQK 863
Cdd:cd14909 446 QTFSEKLTN-------THLGKSAPFQKPKPpkpgqqaAHFAIAHYAGC--VSYNITGWLEKNK-DPLNDTVVDQFKKSQN 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 864 KIISNLFLGRAGSatvlSGSIAGLEGGsqlalrratsmRKTFTTGMAAVKKkslciQIKLQVDALIDTIKRSKMHFVHCF 943
Cdd:cd14909 516 KLLIEIFADHAGQ----SGGGEQAKGG-----------RGKKGGGFATVSS-----AYKEQLNSLMTTLRSTQPHFVRCI 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 944 LPvaegwpgeprsassrrvsssSELDLPpgdpceaGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1023
Cdd:cd14909 576 IP--------------------NEMKQP-------GV--VDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKI 626
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1907082237 1024 LAPHLTKKHgrnyivVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14909 627 LNPAGIQGE------EDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
324-1069 |
9.72e-70 |
|
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: 249.58 E-value: 9.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 403
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLATIAGT------SGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 475
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdlakkKDSKMKGTLEDQIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 476 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA---A 552
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILS----NKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLAtdsA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 553 MKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGTlqrstsf 629
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKTAYLMGLNSSDLLKALCFPRVKVGN------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 630 rqgpEESGLGEgTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELC 709
Cdd:cd14913 311 ----EYVTKGQ-TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN------SLEQLC 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 710 HNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALVPGAT 789
Cdd:cd14913 380 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPMGIFSILEEECMFPKAT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 790 EDALLDRLFSYYGPQEGDKkgQSPLLRSSKPR-HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISN 868
Cdd:cd14913 447 DTSFKNKLYDQHLGKSNNF--QKPKVVKGRAEaHFSLIHYAGT--VDYSVSGWLEKNK-DPLNETVVGLYQKSSNRLLAH 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 869 LFLGRAGS-ATVLSGSIAGLEGGSqlalrratsmrktFTTgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLPVA 947
Cdd:cd14913 522 LYATFATAdADSGKKKVAKKKGSS-------------FQT-VSALFRENL--------NKLMSNLRTTHPHFVRCIIPNE 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 948 EGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1027
Cdd:cd14913 580 TKTPGA-----------------------------MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 630
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1907082237 1028 LTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14913 631 AIPE-GQ---FIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
323-1069 |
1.07e-69 |
|
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: 249.24 E-value: 1.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGT-SGTKVFSV-----EKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 476
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSpKGRKEPGVpgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 477 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQkaaQQFSKLQAAMKVL 556
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER---ELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 557 AISPEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTSFRQGP 633
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRernTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG-----RDYVQKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 634 EesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEELCHNY 712
Cdd:cd14930 313 Q-------TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFEIFQLN------SFEQLCINY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 713 AQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPGATEDA 792
Cdd:cd14930 380 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDE----------ECWFPKATDKS 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 793 LLDRLfsyygpqeGDKKGQSPllRSSKPRH------FLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKII 866
Cdd:cd14930 450 FVEKV--------AQEQGGHP--KFQRPRHlrdqadFSVLHYAGK--VDYKANEWL-MKNMDPLNDNVAALLHQSTDRLT 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 867 SNLFLGRAGsatvlsgsIAGLEGGSQL--ALRRATSMRKTFTTgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFL 944
Cdd:cd14930 517 AEIWKDVEG--------IVGLEQVSSLgdGPPGGRPRRGMFRT-VGQLYKESL--------SRLMATLSNTNPSFVRCIV 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 945 PVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1024
Cdd:cd14930 580 PNHEKRAG-----------------------------KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082237 1025 APHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14930 631 TPNAIPKG-----FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
324-1026 |
9.29e-69 |
|
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: 246.07 E-value: 9.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 403
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLATIAGTSGtkvfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 481
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSS----GIEN-EILQTnpILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 482 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKpeekqkaAQQFSKLQAAMKV 555
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLksaseyKYLNQSNCLTIDGVDD-------AKKFHELKEALDT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 556 LAISPEEQKTCWLILASIYHLGAAGATKAGRKQF---ARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFrqg 632
Cdd:cd01383 228 VGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHvevVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKL--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 633 peesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQH-SLCSMMIVDTPGFQnpewggSARGASFEELCHN 711
Cdd:cd01383 305 ---------TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRrTGRSISILDIYGFE------SFQKNSFEQLCIN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 712 YAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEpvadDSVAAVDqashLVRS-----LAHADEargllwlleeEALVP 786
Cdd:cd01383 370 YANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFE----DNQECLD----LIEKkplglISLLDE----------ESNFP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 787 GATEDALLDRLFSYYGPQEGDKKGQSpllrsskpRHFLLGHSHGTnwVEYNVAGWLNytkqnpatQNAPRLLQDsqkkiI 866
Cdd:cd01383 432 KATDLTFANKLKQHLKSNSCFKGERG--------GAFTIRHYAGE--VTYDTSGFLE--------KNRDLLHSD-----L 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 867 SNLFLGRAGSATVLSGSIAGLEGGSQLALRRATSMRKTfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPV 946
Cdd:cd01383 489 IQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQ---------KQSVATKFKGQLFKLMQRLENTTPHFIRCIKPN 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 947 AEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1026
Cdd:cd01383 560 NKQLPGV-----------------------------FDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLP 610
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
324-1069 |
1.78e-66 |
|
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: 239.62 E-value: 1.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 403
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLATIAG---------TSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQV 474
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 475 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA--- 551
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILS----NKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMAtdn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRS 626
Cdd:cd14917 237 AFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEpdgTEEADKSAYLMGLNSADLLKGLCHPRVKVGNeyVTKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 627 TSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFE 706
Cdd:cd14917 317 QNVQQVIYATG--------------ALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 707 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQAshlvrslahaDEARGLLWLLEEEALVP 786
Cdd:cd14917 377 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---GMDLQACIDLI----------EKPMGIMSILEEECMFP 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 787 GATEDALLDRLFSYYGPQEGDKkgQSPLLRSSKPR-HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKI 865
Cdd:cd14917 444 KATDMTFKAKLFDNHLGKSNNF--QKPRNIKGKPEaHFSLIHYAGT--VDYNIIGWLQKNK-DPLNETVVGLYQKSSLKL 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 866 ISNLFLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLP 945
Cdd:cd14917 519 LSNLFANYAGADAPIEKGKGKAKKGS------------SFQT-VSALHRENL--------NKLMTNLRSTHPHFVRCIIP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 946 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1025
Cdd:cd14917 578 NETKSPG-----------------------------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082237 1026 PHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14917 629 PAAIPE-GQ---FIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
323-1069 |
3.36e-66 |
|
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: 238.77 E-value: 3.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTS-----GTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 477
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGkqssdGKGSLEDQIIQA-NPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 478 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKPEEKQKAaqqfsklQA 551
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvpnpkeYHWVSQGVTVVDNMDDGEELQIT-------DV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRS 626
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEvdtTEVADKVAHLMGLNSGELQKGITRPRVKVGNefVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 627 TSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFE 706
Cdd:cd14934 313 QNMEQCNNSIG--------------ALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN------SFE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 707 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQashlvrslahADEARGLLWLLEEEALVP 786
Cdd:cd14934 373 QLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDF---GLDLQACIDL----------LEKPMGIFSILEEQCVFP 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 787 GATE--------DALLDRLFSYYGPQEGDKKGQSPllrsskprHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLL 858
Cdd:cd14934 440 KATDatfkaalyDNHLGKSSNFLKPKGGKGKGPEA--------HFELVHYAGT--VGYNITGWLEKNK-DPLNETVVGLF 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 859 QDSQkKIISNLFLGRAGSAtvlsgsiagleGGSQLALRRATSMrktfttgmaavkkkSLCIQIKLQVDALIDTIKRSKMH 938
Cdd:cd14934 509 QKSS-LGLLALLFKEEEAP-----------AGSKKQKRGSSFM--------------TVSNFYREQLNKLMTTLHSTAPH 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 939 FVHCFLpvaegwpgeprsassrrvsssseldlpPGDPCEAGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1018
Cdd:cd14934 563 FVRCIV---------------------------PNEFKQSGV--VDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFK 613
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1019 RRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14934 614 QRYQVLNPNVIPQG-----FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
323-1069 |
9.84e-66 |
|
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: 237.22 E-value: 9.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGpSLLVlstrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 394
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTG-SILV-------AVnpykelpiYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 395 DQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTkvFSVEKwQAL--STLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 472
Cdd:cd14883 73 NQSVIISGESGAGKTETTKLILQYLC--AVTNNH--SWVEQ-QILeaNTILEAFGNAKTVRNDNSSRFGKFIEVCFDASG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 473 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACG--DATLRTELHL---NHLAENNVFGIVPLSKPEEKQKaaqqFS 547
Cdd:cd14883 148 HIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLgepEDYHYLNQSGCIRIDNINDKKD----FD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 548 KLQAAMKVLAISPEEQKTCWLILASIYHLGAAgatkagrkQFARHEWAQkaayllgCSLEELSSAIFKH-----QLKGGT 622
Cdd:cd14883 224 HLRLAMNVLGIPEEMQEGIFSVLSAILHLGNL--------TFEDIDGET-------GALTVEDKEILKIvakllGVDPDK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 623 LQRSTSFRQgpeESGLGEGT----KLS-ALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWG 697
Cdd:cd14883 289 LKKALTIRQ---INVRGNVTeiplKVQeARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 698 gsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDLEPVADdsvaAVDQASHLVRSLAhADEARg 774
Cdd:cd14883 366 ------SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWShivFTDNQECLD----LIEKPPLGILKLL-DEECR- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 775 llwlleeealVPGATEDALLDRLFSYYGPQEGDKKgqsPLLRSSKPRhFLLGHSHGTnwVEYNVAGWLNytkQNPATQ-- 852
Cdd:cd14883 434 ----------FPKGTDLTYLEKLHAAHEKHPYYEK---PDRRRWKTE-FGVKHYAGE--VTYTVQGFLD---KNKDTQqd 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 853 NAPRLLQDSQKKIISNLFLGRAgsatvlsgsiagleggsQLALRRATSMRKTFTTGMAAVKKK-SLCIQIKLQVDALIDT 931
Cdd:cd14883 495 DLFDLMSRSKNKFVKELFTYPD-----------------LLALTGLSISLGGDTTSRGTSKGKpTVGDTFKHQLQSLVDV 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 932 IKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDH 1011
Cdd:cd14883 558 LSATQPWYVRCIKPNSLKEPN-----------------------------VFDDELVLAQLRYAGMLEIIRIRKEGFPIH 608
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1012 MVFSEFRRRFDVLAPHLTKKHGRnyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14883 609 LTFKEFVDRYLCLDPRARSADHK-----ETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
324-1069 |
1.34e-64 |
|
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: 234.19 E-value: 1.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 403
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLATIAgTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 473
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIA-VTGDKKKEQQPGKMQGTLedqiiqanplLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 474 VASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 551
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMS----NKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLAtd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELssaifkhqLKGGTLQRst 627
Cdd:cd14923 237 nAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAGYLMGLNSAEM--------LKGLCCPR-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 628 sFRQGPEESGLGEGTKlSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEE 707
Cdd:cd14923 307 -VKVGNEYVTKGQNVQ-QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 708 LCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALVPG 787
Cdd:cd14923 379 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFSILEEECMFPK 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 788 ATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIIS 867
Cdd:cd14923 446 ATDTSFKNKLYDQHLGKSNNFQKPKPA-KGKAEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSSLKLLS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 868 NLFLGRAGSAtvlsgsiAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLPVA 947
Cdd:cd14923 522 FLFSNYAGAE-------AGDSGGSKKGGKKKGSSFQT----VSAVFRENL--------NKLMTNLRSTHPHFVRCLIPNE 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 948 EGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1027
Cdd:cd14923 583 TKTPG-----------------------------VMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNAS 633
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1907082237 1028 LTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14923 634 AIPEGQ----FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
324-1069 |
3.46e-64 |
|
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: 233.08 E-value: 3.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 403
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 473
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLedqiisanplLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 474 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 551
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQR 625
Cdd:cd14910 238 sAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAAYLQNLNSADLLKALCYPRVKVGNeyVTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 626 STSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSF 705
Cdd:cd14910 318 GQTVQQ--------------VYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 706 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALV 785
Cdd:cd14910 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFSILEEECMF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 786 PGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKI 865
Cdd:cd14910 445 PKATDTSFKNKLYEQHLGKSNNFQKPKPA-KGKVEAHFSLIHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSSMKT 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 866 ISNLFLGrAGSATVLSGsiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLP 945
Cdd:cd14910 521 LALLFSG-AAAAEAEEG------GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTHPHFVRCIIP 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 946 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1025
Cdd:cd14910 581 NETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082237 1026 PHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14910 632 ASAIPE-GQ---FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
325-1031 |
3.76e-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: 232.18 E-value: 3.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 325 VLHTLRQRYGASLLHTYAGPSLL-VLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 403
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIaVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 481
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQ-QVLESnpLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 482 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKPEEkqkaaqqFSKLQAAMKV 555
Cdd:cd01384 162 YLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 556 LAISPEEQKTCWLILASIYHLG------AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQlkggtlqrstsf 629
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGniefskGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRV------------ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 630 RQGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQnpewggSARGASFEELC 709
Cdd:cd01384 303 IVTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE------SFKTNSFEQFC 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 710 HNYAQDRLQRLFHERTFLQELERYKEDNIELAF----------DDLEPVADDSVAAVDQASHLVRSlahadeargllwll 779
Cdd:cd01384 377 INLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYiefvdnqdvlDLIEKKPGGIIALLDEACMFPRS-------------- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 780 eeealvpgaTEDALLDRLFSYYgpqeGDKKgqspllRSSKPR----HFLLGHSHGTnwVEYNVAGWLNYTKQN--PATQN 853
Cdd:cd01384 443 ---------THETFAQKLYQTL----KDHK------RFSKPKlsrtDFTIDHYAGD--VTYQTDLFLDKNKDYvvAEHQA 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 854 aprLLQDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKtFTtgmaavkkkSLCIQIKLQVDALIDTIK 933
Cdd:cd01384 502 ---LLNASKCPFVAGLF--------------------PPLPREGTSSSSK-FS---------SIGSRFKQQLQELMETLN 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 934 RSKMHFVHCFLPVAEgwpgeprsassrrvsssseldLPPGDPCEAGLLQldvsllraQLRGSRLLDAMRMYRQGYPDHMV 1013
Cdd:cd01384 549 TTEPHYIRCIKPNNL---------------------LKPGIFENANVLQ--------QLRCGGVLEAVRISCAGYPTRKP 599
|
730
....*....|....*...
gi 1907082237 1014 FSEFRRRFDVLAPHLTKK 1031
Cdd:cd01384 600 FEEFLDRFGLLAPEVLKG 617
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
325-1069 |
1.41e-63 |
|
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: 231.16 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 325 VLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSS 404
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 405 GSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQ--------ALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 476
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 477 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA---AM 553
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtdsAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 554 KVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGTlqrstsfr 630
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAAYLQSLNSADLLKALCYPRVKVGN-------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 631 qgpEESGLGEgTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCH 710
Cdd:cd14918 311 ---EYVTKGQ-TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 711 NYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALVPGATE 790
Cdd:cd14918 381 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPLGIFSILEEECMFPKATD 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 791 DALLDRLFSYYGPQEGDKKgQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLF 870
Cdd:cd14918 448 TSFKNKLYDQHLGKSANFQ-KPKVVKGKAEAHFSLIHYAGT--VDYNITGWLDKNK-DPLNDTVVGLYQKSAMKTLASLF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 871 LGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTGMAAVKKkslciqiklQVDALIDTIKRSKMHFVHCFLPVAEGW 950
Cdd:cd14918 524 STYASAEADSGAKKGAKKKGS------------SFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCIIPNETKT 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 951 PGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTK 1030
Cdd:cd14918 583 PG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIP 633
|
730 740 750
....*....|....*....|....*....|....*....
gi 1907082237 1031 KhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14918 634 E-GQ---FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
324-1069 |
1.57e-63 |
|
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: 231.16 E-value: 1.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 403
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLATIA---------GTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 472
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAvtgekkkeeAASGKMQGTLED-QIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 473 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA- 551
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMAt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 --AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQ 624
Cdd:cd14915 237 dsAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAAYLTSLNSADLLKALCYPRVKVGNeyVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 625 RSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaS 704
Cdd:cd14915 317 KGQTVQQVYNSVG--------------ALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------S 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 705 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEAL 784
Cdd:cd14915 377 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFSILEEECM 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 785 VPGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKK 864
Cdd:cd14915 444 FPKATDTSFKNKLYEQHLGKSNNFQKPKPA-KGKAEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSGMK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 865 IISNLFLGraGSATVLSGSiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFL 944
Cdd:cd14915 520 TLAFLFSG--GQTAEAEGG-----GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTHPHFVRCLI 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 945 PVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1024
Cdd:cd14915 580 PNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082237 1025 APHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14915 631 NASAIPE-GQ---FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
324-1069 |
1.41e-62 |
|
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: 228.46 E-value: 1.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 403
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 473
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLedqiisanplLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 474 VASASIQTMLLEKLRVARRPASEATFNVFYYLlacgDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 551
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQI----TSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQR 625
Cdd:cd14912 238 sAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEpdgTEVADKAAYLQSLNSADLLKALCYPRVKVGNeyVTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 626 STSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSF 705
Cdd:cd14912 318 GQTVEQVTNAVG--------------ALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 706 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALV 785
Cdd:cd14912 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPMGIFSILEEECMF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 786 PGATEDALLDRLFSYYGPQEGDKKgQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKI 865
Cdd:cd14912 445 PKATDTSFKNKLYEQHLGKSANFQ-KPKVVKGKAEAHFSLIHYAGV--VDYNITGWLDKNK-DPLNETVVGLYQKSAMKT 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 866 ISNLFLGragsATVLSGSIAGleGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLP 945
Cdd:cd14912 521 LAYLFSG----AQTAEGASAG--GGAKKGGKKKGSSFQT----VSALFRENL--------NKLMTNLRSTHPHFVRCIIP 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 946 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1025
Cdd:cd14912 583 NETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 633
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082237 1026 PHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14912 634 ASAIPE-GQ---FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
324-1026 |
8.25e-62 |
|
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: 226.09 E-value: 8.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 403
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLATIA--GTSGTKVFSVEKWQAL-------STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQV 474
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAaiGDRSKKENPNANKGTLedqiiqaNPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 475 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA--- 551
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILS----NKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLAtds 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRS 626
Cdd:cd14916 238 AFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEpdgTEDADKSAYLMGLNSADLLKGLCHPRVKVGNeyVTKG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 627 TSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFE 706
Cdd:cd14916 318 QSVQQ--------------VYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 707 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQAshlvrslahaDEARGLLWLLEEEALVP 786
Cdd:cd14916 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---GMDLQACIDLI----------EKPMGIMSILEEECMFP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 787 GATEDALLDRLF-SYYGPQEGDKKGQSplLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKI 865
Cdd:cd14916 445 KASDMTFKAKLYdNHLGKSNNFQKPRN--VKGKQEAHFSLVHYAGT--VDYNILGWLEKNK-DPLNETVVGLYQKSSLKL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 866 ISNLFLGRAGSATvlsgsiaGLEGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLP 945
Cdd:cd14916 520 MATLFSTYASADT-------GDSGKGKGGKKKGSSFQT-----VSALHRENL--------NKLMTNLKTTHPHFVRCIIP 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 946 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1025
Cdd:cd14916 580 NERKAPG-----------------------------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 630
|
.
gi 1907082237 1026 P 1026
Cdd:cd14916 631 P 631
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
323-1026 |
2.11e-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: 2.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMS----RQDQS 397
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPyKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSgvldPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 398 IVLLGSSGSGKTTSFQHLVQYLATIagTSGTKVFSVEKWQALST------------------LLEAFGNSPTIMNGSATR 459
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARI--TSGFAQGASGEGEAASEaieqtlgsledrvlssnpLLESFGNAKTLRNDNSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 460 FSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLnhlaENNVFGIVPLSK--PE 537
Cdd:cd14890 159 FGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKL----QTPVEYFYLRGEcsSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 538 EKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG-----AAGATKAGRKQfARHEWAQKAAYLLGCSLEELSSA 612
Cdd:cd14890 235 PSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGnvdfeSENDTTVLEDA-TTLQSLKLAAELLGVNEDALEKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 613 IFKHQL--KGGTLQRstsfrqgPEESGLGEgTKLSALeclegmASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPG 690
Cdd:cd14890 314 LLTRQLfvGGKTIVQ-------PQNVEQAR-DKRDAL------AKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 691 FQNPEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADDSVAAVDQASHLVRSLa 767
Cdd:cd14890 380 FEKFEWNT------FEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDwqyITFNDNQACLELIEGKVNGKPGIFITL- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 768 haDEARGLLWLLEEEALVpgatedALLDRLF--SYYGPQEGDKKGQSPLLRSSK---PRHFLLGHSHGTnwVEYNVAGwl 842
Cdd:cd14890 453 --DDCWRFKGEEANKKFV------SQLHASFgrKSGSGGTRRGSSQHPHFVHPKfdaDKQFGIKHYAGD--VIYDASG-- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 843 nYTKQNPATqnaprlLQDSQKKIIsnlflgragsatvlsgsiagleggsqlalrrATSMRktfttgmaAVKKKSLCIQIK 922
Cdd:cd14890 521 -FNEKNNET------LNAEMKELI-------------------------------KQSRR--------SIREVSVGAQFR 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 923 LQVDALIDTIKRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagLLQLDVSLlraQLRGSRLLDAMR 1002
Cdd:cd14890 555 TQLQELMAKISLTNPRYVRCIKPNETKAPGK--------------------------FDGLDCLR---QLKYSGMMEAIQ 605
|
730 740
....*....|....*....|....*..
gi 1907082237 1003 MYRQGYP---DHMVFseFrRRFDVLAP 1026
Cdd:cd14890 606 IRQQGFAlreEHDSF--F-YDFQVLLP 629
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
323-945 |
7.20e-60 |
|
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: 219.72 E-value: 7.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPslLVLST---RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIV 399
Cdd:cd01378 1 EAINENLKKRFENDEIYTYIGH--VLISVnpfKDLG-IYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 400 LLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVeKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 477
Cdd:cd01378 78 ISGESGAGKTEASKRIMQYIAAVSGGSESEVERV-KDMLLASnpLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 478 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKpeekqkaAQQFSKLQA 551
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLqrpeqyYYYSKSGCFDVDGIDD-------AADFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 AMKVLAISPEEQKTCWLILASIYHLGAAG--ATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRST-S 628
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQfaEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGRSVyE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 629 FRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGF----QNpewggsarga 703
Cdd:cd01378 310 VPLNVEQ----------AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIgVLDIYGFeifeKN---------- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 704 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA----FDDlEPVADdsvaavdqashLVRS-----LAHADEArg 774
Cdd:cd01378 370 SFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTpikyFNN-KIICD-----------LIEEkppgiFAILDDA-- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 775 llwlleeEALVPGATEDALLDRLFSYYGPQEGDKKGQSPllRSSKPRHFLLGHSHGTnwVEYNVAGwlnYTKQNPAT--Q 852
Cdd:cd01378 436 -------CLTAGDATDQTFLQKLNQLFSNHPHFECPSGH--FELRRGEFRIKHYAGD--VTYNVEG---FLDKNKDLlfK 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 853 NAPRLLQDSQKKIISNLFlgragsatvlsgsiagLEGGSQLALRRATsmrktfTTGMaavkkkslciQIKLQVDALIDTI 932
Cdd:cd01378 502 DLKELMQSSSNPFLRSLF----------------PEGVDLDSKKRPP------TAGT----------KFKNSANALVETL 549
|
650
....*....|...
gi 1907082237 933 KRSKMHFVHCFLP 945
Cdd:cd01378 550 MKKQPSYIRCIKP 562
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
324-1029 |
1.39e-58 |
|
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: 215.81 E-value: 1.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGpSLL--VLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 401
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIG-SILasVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 402 GSSGSGKTTSFQHLVQYLATIAGTS-----GTKVFSVEKWQALST-LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 475
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelslKEKTSCVEQAILESSpIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 476 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhLAEN----NVFGIVPLSKPEEKqkaaQQFSKLQA 551
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENyhylNQSGCVEDKTISDQ----ESFREVIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRq 631
Cdd:cd14873 236 AMEVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPTQLTDAL---------TQRSMFLR- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 632 GPEESglgegTKLS---ALECLEGMASGLYSELFTLLISLVNRALKSSQHsLCSMMIVDTPGFQNPEWGgsargaSFEEL 708
Cdd:cd14873 306 GEEIL-----TPLNvqqAVDSRDSLAMALYARCFEWVIKKINSRIKGKED-FKSIGILDIFGFENFEVN------HFEQF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 709 CHNYAQDRLQRLFHERTF-LQELERYKEDnieLAFDDLEPVadDSVAAVDQASHLVRSLAHADEargllwlleeEALVPG 787
Cdd:cd14873 374 NINYANEKLQEYFNKHIFsLEQLEYSREG---LVWEDIDWI--DNGECLDLIEKKLGLLALINE----------ESHFPQ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 788 ATEDALLDRLFSyygpqeGDKKGQSPLlrssKPR--HFLLGHSHGTNWVEYNVAGWLnytKQNPAT--QNAPRLLQDSQK 863
Cdd:cd14873 439 ATDSTLLEKLHS------QHANNHFYV----KPRvaVNNFGVKHYAGEVQYDVRGIL---EKNRDTfrDDLLNLLRESRF 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 864 KIISNLFlgragsatvlsgsiagleggsqlalRRATSMRKTFTTGMAAVKKK-SLCIQIKLQVDALIDTIKRSKMHFVHC 942
Cdd:cd14873 506 DFIYDLF-------------------------EHVSSRNNQDTLKCGSKHRRpTVSSQFKDSLHSLMATLSSSNPFFVRC 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 943 FLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 1022
Cdd:cd14873 561 IKPNMQKMPD-----------------------------QFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYK 611
|
....*..
gi 1907082237 1023 VLAPHLT 1029
Cdd:cd14873 612 VLMRNLA 618
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
324-744 |
6.55e-58 |
|
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: 213.17 E-value: 6.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYG-ASLLHTYAGpslLVLStrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 394
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCG---IVLV-----AInpyedlpiYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 395 DQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 472
Cdd:cd01380 74 NQSIIVSGESGAGKTVSAKYAMRYFATVGGSSSGET-QVEE-KVLASnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 473 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFGIVPLSKPEEKQKAAQQFSKLQAA 552
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGS-AEDFFYTNQGGSPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 553 MKVLAISPEEQKTCWLILASIYHLGAAGATKAGRK---QFARHEWAQKAAYLLGCSLEELSSAIFKHQLK--GGTLQRST 627
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDsasISPDDEHLQIACELLGIDESQLAKWLCKRKIVtrSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 628 SFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQ-HSLCSMM-IVDTPGFQNPEWGgsargaSF 705
Cdd:cd01380 311 TLQQ--------------AIVARDALAKHIYAQLFDWIVDRINKALASPVkEKQHSFIgVLDIYGFETFEVN------SF 370
|
410 420 430
....*....|....*....|....*....|....*....
gi 1907082237 706 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDD 744
Cdd:cd01380 371 EQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFID 409
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
323-1026 |
8.73e-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: 213.87 E-value: 8.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 401
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPyQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 402 GSSGSGKTTSFQHLVQYLATIAGtsGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 481
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 482 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAennVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 561
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANEC---AYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 562 EQKTCWLILASIYHLGAAGATKAG---RKQFARHEW--AQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFRqgpees 636
Cdd:cd14903 236 KQEVLFEVLAGILHLGQLQIQSKPnddEKSAIAPGDqgAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 637 glgegtKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCHNYAQDR 716
Cdd:cd14903 310 ------KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHN------SFEQFCINYANEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 717 LQRLFHERTFLQELERYKEDNIELAFDDLepvADDS-VAAVDQASHLVRSLAHADEARgllwlleeealvPGATEDALLD 795
Cdd:cd14903 378 LQQKFTQDVFKTVQIEYEEEGIRWAHIDF---ADNQdVLAVIEDRLGIISLLNDEVMR------------PKGNEESFVS 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 796 RLFSYYgpqeGDKKGQSPLLRSSKPRhFLLGHSHGTnwVEYNVAGWLNYTKQNpatqnaprLLQD-------SQKKIISN 868
Cdd:cd14903 443 KLSSIH----KDEQDVIEFPRTSRTQ-FTIKHYAGP--VTYESLGFLEKHKDA--------LLPDlsdlmrgSSKPFLRM 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 869 LFLGRAGSATVLSGSIAGLEGgsqlalRRATSMRKTFTTGMaavkkkslciQIKLQVDALIDTIKRSKMHFVHCFLPVAE 948
Cdd:cd14903 508 LFKEKVESPAAASTSLARGAR------RRRGGALTTTTVGT----------QFKDSLNELMTTIRSTNVHYVRCIKPNSI 571
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 949 GWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1026
Cdd:cd14903 572 KSPTE-----------------------------LDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLP 620
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
323-1026 |
9.37e-58 |
|
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: 213.27 E-value: 9.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGpSLLVlstrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 394
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTG-SILV-------AVnpyqilpiYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 395 DQSIVLLGSSGSGKTTSFQHLVQYLATIAGtsgtKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 472
Cdd:cd01381 73 DQCVVISGESGAGKTESTKLILQYLAAISG----QHSWIEQ-QILEAnpILEAFGNAKTIRNDNSSRFGKYIDIHFNKNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 473 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNH------LAENNVFGIvplskpeEKQKAAQQF 546
Cdd:cd01381 148 VIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDasdyyyLTQGNCLTC-------EGRDDAAEF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 547 SKLQAAMKVLAISPEEQKTCWLILASIYHLG-----AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQL--K 619
Cdd:cd01381 221 ADIRSAMKVLMFTDEEIWDIFKLLAAILHLGnikfeATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIftR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 620 GGTLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRAL---KSSQHSLCSMMIVDTPGFQNPEW 696
Cdd:cd01381 301 GETVVSPLSAEQ--------------ALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENFEV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 697 GgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsVAAVDQAShlvrSLAHADEar 773
Cdd:cd01381 367 N------SFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINwqhIEFVDNQDVLD--LIALKPMN----IMSLIDE-- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 774 gllwlleeEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLLRSSKPRHFLlghshGTnwVEYNVAGWLNytKQNPA-TQ 852
Cdd:cd01381 433 --------ESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFA-----GV--VFYDTRGFLE--KNRDTfSA 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 853 NAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsQLALRRATSMRKtfttgmaavKKKSLCIQIKLQVDALIDTI 932
Cdd:cd01381 496 DLLQLVQSSKNKFLKQLF---------------------NEDISMGSETRK---------KSPTLSSQFRKSLDQLMKTL 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 933 KRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHM 1012
Cdd:cd01381 546 SACQPFFVRCIKPNEYKKPML-----------------------------FDRELCVRQLRYSGMMETIRIRKAGYPIRH 596
|
730
....*....|....
gi 1907082237 1013 VFSEFRRRFDVLAP 1026
Cdd:cd01381 597 TFEEFVERYRVLVP 610
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
324-871 |
8.72e-57 |
|
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: 210.32 E-value: 8.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTSGTkvFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 482
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPSDDS--DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 483 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNH----------LAENNVFGIVplskpEEKQKAAQQFSKLQAA 552
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDpdchrilrddNRNRPVFNDS-----EELEYYRQMFHDLTNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 553 MKVLAISPEEQKTCWLILASIYHLG---------AAGATKAGRKQFarhewaQKAAYLLGCSLEELSSAIF--KHQLKGG 621
Cdd:cd14897 235 MKLIGFSEEDISVIFTILAAILHLTnivfipdedTDGVTVADEYPL------HAVAKLLGIDEVELTEALIsnVNTIRGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 622 TLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQ-----HSLCSMMIVDTPGFQNpew 696
Cdd:cd14897 309 RIQSWKSLRQ--------------ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKdfqimTRGPSIGILDMSGFEN--- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 697 ggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAfdDLEPVADDSV------------AAVDQASHLvr 764
Cdd:cd14897 372 ---FKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR--DIEYHDNDDVlelffkkplgilPLLDEESTF-- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 765 slahadeargllwlleeealvPGATEDALLDRLFSYYGPqegdkkgqSPLLRSSKPRHFLLGHSHGTNWVEYNVAGWLNY 844
Cdd:cd14897 445 ---------------------PQSTDSSLVQKLNKYCGE--------SPRYVASPGNRVAFGIRHYAEQVTYDADGFLEK 495
|
570 580
....*....|....*....|....*..
gi 1907082237 845 TKQNpATQNAPRLLQDSQKKIISNLFL 871
Cdd:cd14897 496 NRDN-LSSDIVGCLLNSNNEFISDLFT 521
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
324-750 |
4.32e-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: 207.90 E-value: 4.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 403
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLaTIAGTSGTKVFSvEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTML 483
Cdd:cd01379 82 SGAGKTESANLLVQQL-TVLGKANNRTLE-EKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 484 LEKLRVARRPASEATFNVFYYLLA-------CGDATLRTELHLNHLAEnnvFGIVPLSKpEEKQKAAQQFSKLQAAMKVL 556
Cdd:cd01379 160 LEKSRVVHQAIGERNFHIFYYIYAglaedkkLAKYKLPENKPPRYLQN---DGLTVQDI-VNNSGNREKFEEIEQCFKVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 557 AISPEEQKTCWLILASIYHLG-------AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQL--KGGTLQRST 627
Cdd:cd01379 236 GFTKEEVDSVYSILAAILHIGdieftevESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVvtRGETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 628 SFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHS---LCSMMIVDTPGFQNpewggsARGAS 704
Cdd:cd01379 316 TVEE--------------ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAsdePLSIGILDIFGFEN------FQKNS 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907082237 705 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL---AFDDLEPVAD 750
Cdd:cd01379 376 FEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVdliEYEDNRPLLD 424
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
320-748 |
1.63e-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: 203.55 E-value: 1.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 320 LNESSVLHTLRQRYGASLLHTYAGPS-LLVLSTRGAPAVYSEKVMHMFK-------GCRREDMAPHIYAVAQTAYRAMLM 391
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 392 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTS--GTKVfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFD 469
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSkkGTKL--SSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 470 QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF---GIVPL-SKPEEKQkaAQQ 545
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLpLGPGSDD--AEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 546 FSKLQAAMKVLAISPEEQKTCWLILASIYHLgaagatkaGRKQFA-----RHEWA--------QKAAYLLGCSLEELSSA 612
Cdd:cd14879 237 FQELKTALKTLGFKRKHVAQICQLLAAILHL--------GNLEFTydhegGEESAvvkntdvlDIVAAFLGVSPEDLETS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 613 I-FKHQLKGGtlQRSTSFrqgpeesgLG-EGTKLSALEclegMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTP 689
Cdd:cd14879 309 LtYKTKLVRK--ELCTVF--------LDpEGAAAQRDE----LARTLYSLLFAWVVETINQKLCAPEDDFATFIsLLDFP 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082237 690 GFQNPewgGSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA----FDDLEPV 748
Cdd:cd14879 375 GFQNR---SSTGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPatsyFDNSDCV 434
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
323-1025 |
6.45e-54 |
|
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: 201.93 E-value: 6.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIagtsGTKVFSVEKWQALSTL--LEAFGNSPTIMNGSATRFSQILSLDFdQAGQVASASIQ 480
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVLpiLESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 481 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAEN----NVFGIVPLSKPEEkqkaAQQFSKLQAAMKVL 556
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETyyylNQGGACRLQGKED----AQDFEGLLKALQGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 557 AISPEEQKTCWLILASIYHLGAAGATKAGRKQF---ARHEWA--QKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFrq 631
Cdd:cd14896 231 GLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAeiHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPL-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 632 gPEEsglgegtklSALECLEGMASGLYSELFTLLISLVNRAL--KSSQHSLCSMMIVDTPGFQnpewggSARGASFEELC 709
Cdd:cd14896 309 -PVE---------GAIDARDALAKTLYSRLFTWLLKRINAWLapPGEAESDATIGVVDAYGFE------ALRVNGLEQLC 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 710 HNYAQDRLQRLFHERTFLQELERYKEDniELAFDDLEPVADDSVA--AVDQASHLVRSLahadeargllwllEEEALVPG 787
Cdd:cd14896 373 INLASERLQLFSSQTLLAQEEEECQRE--LLPWVPIPQPPRESCLdlLVDQPHSLLSIL-------------DDQTWLSQ 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 788 ATEDALLDRLFSYYGPQEGDKKGQSPLlrsskPRhFLLGHSHGTnwVEYNVAGWLNYTKQ--NPATQNaprLLQDSQKKI 865
Cdd:cd14896 438 ATDHTFLQKCHYHHGDHPSYAKPQLPL-----PV-FTVRHYAGT--VTYQVHKFLNRNRDqlDPAVVE---MLAQSQLQL 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 866 ISNLFlgragsatvlsgsiagLEGGSQLALRRatsmrktfttgmaavKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLP 945
Cdd:cd14896 507 VGSLF----------------QEAEPQYGLGQ---------------GKPTLASRFQQSLGDLTARLGRSHVYFIHCLNP 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 946 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1025
Cdd:cd14896 556 NPGKLPG-----------------------------LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG 606
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
323-1069 |
1.30e-53 |
|
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: 201.13 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTSGTKVfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQaGQVASASIQTM 482
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLV--TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 483 LLEKLRVARRPASEATFNVFYYLLACGDATLRTE---------LHLNHLAENNVFGivplskpeekQKAAQQFSKLQAAM 553
Cdd:cd01387 158 LLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKyglqeaekyFYLNQGGNCEIAG----------KSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 554 KVLAISPEEQKTCWLILASIYHLGAAgatkagrkQFARHEW--AQKAAyLLGcSLEELSSAIFKHQLKGGTLQRSTSFR- 630
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNV--------YFHKRQLrhGQEGV-SVG-SDAEIQWVAHLLQISPEGLQKALTFKv 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 631 -QGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELC 709
Cdd:cd01387 298 tETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN------SFEQLC 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 710 HNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVAddsvaavdqasHLVrslahADEARGLLWLLEEEALVP 786
Cdd:cd01387 372 INYANENLQYYFNKHVFKLEQEEYIREQIDwteIAFADNQPVI-----------NLI-----SKKPVGILHILDDECNFP 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 787 GATEDALLDRLFSYYGPQEgdkkgqspllRSSKPR----HFLLGHSHGTNWveYNVAGWLNYTKqNPATQNAPRLLQDSQ 862
Cdd:cd01387 436 QATDHSFLEKCHYHHALNE----------LYSKPRmplpEFTIKHYAGQVW--YQVHGFLDKNR-DQLRQDVLELLVSSR 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 863 KKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAAVKKKSLCIQIKLQ--VDALIDTIKRSKMHFV 940
Cdd:cd01387 503 TRVVAHLF--------------------SSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQdsLLQLLEKMERCNPWFV 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 941 HCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1020
Cdd:cd01387 563 RC---------------------------LKPNHKKEPMLFDMDVVM--AQLRYSGMLETIRIRKEGYPVRLPFQVFIDR 613
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1907082237 1021 FDvlapHLTKKHGRNYIVVDEKRAVeELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd01387 614 YR----CLVALKLPRPAPGDMCVSL-LSRLCTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
325-1024 |
1.18e-52 |
|
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: 198.21 E-value: 1.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 325 VLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAML----MSRQDQSIVL 400
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 401 LGSSGSGKTTSFQHLVQYLATIAgtSGTKVFSVEKWQaLSTLLEAFGNSPTIMNGSATRFSQILSLDFdQAGQVASASIQ 480
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC--RGNSQLEQQILQ-VNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 481 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL----NHLAENNVFGivplsKPEEKQKAAQQFSKLQAAMKVL 556
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLldpgKYRYLNNGAG-----CKREVQYWKKKYDEVCNAMDMV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 557 AISPEEQKTCWLILASIYHLG----AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSsaifkhqlkgGTLQRSTSFRQG 632
Cdd:cd14889 234 GFTEQEEVDMFTILAGILSLGnitfEMDDDEALKVENDSNGWLKAAAGQFGVSEEDLL----------KTLTCTVTFTRG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 633 peESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHS---LCSMMIVDTPGFQNPEWGgsargaSFEELC 709
Cdd:cd14889 304 --EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSsveLREIGILDIFGFENFAVN------RFEQAC 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 710 HNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDLEPVADDSVAA-------VDQASHLvrslahadeargllwll 779
Cdd:cd14889 376 INLANEQLQYFFNHHIFLMEQKEYKKEGIdwkEITYKDNKPILDLFLNKpigilslLDEQSHF----------------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 780 eeealvPGATEDALLDRLFSYYGPQEGDKKGQspllrsSKPRHFLLGHSHGTnwVEYNVAGWLNYTKQN-PATQNAprLL 858
Cdd:cd14889 439 ------PQATDESFVDKLNIHFKGNSYYGKSR------SKSPKFTVNHYAGK--VTYNASGFLEKNRDTiPASIRT--LF 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 859 QDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSQlalrratsmrktfttGMAAVKKKSLCIQIKLQVDALIDTIKRSKMH 938
Cdd:cd14889 503 INSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD---------------NFNSTRKQSVGAQFKHSLGVLMEKMFAASPH 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 939 FVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1018
Cdd:cd14889 568 FVRCIKPNHVKVPG-----------------------------QLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFA 618
|
....*.
gi 1907082237 1019 RRFDVL 1024
Cdd:cd14889 619 ERYKIL 624
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
324-1026 |
1.28e-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: 198.24 E-value: 1.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPyKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGtsGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 482
Cdd:cd14904 82 ESGAGKTETTKIVMNHLASVAG--GRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 483 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEE 562
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 563 QKTCWLILASIYHLGAAGATKAGRK--QFARHEWAQKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRQgpeESGLGE 640
Cdd:cd14904 240 QRTLFKILSGVLHLGEVMFDKSDENgsRISNGSQLSQVAKMLGLPTTRIEEAL---------CNRSVVTRN---ESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 641 GTKLSALECLEGMASGLYSELFTLLISLVNRALkSSQHSLCSMMI--VDTPGFQNPEWGGsargasFEELCHNYAQDRLQ 718
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAI-STDDDRIKGQIgvLDIFGFEDFAHNG------FEQFCINYANEKLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 719 RLFHERTFLQELERYKEDNieLAFDDLEPVADDSVAAVDQASHLVRSLAHaDEARGllwlleeealvPGATEDALLDRLF 798
Cdd:cd14904 381 QKFTTDVFKTVEEEYIREG--LQWDHIEYQDNQGIVEVIDGKMGIIALMN-DHLRQ-----------PRGTEEALVNKIR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 799 SYYGPQEGDKKGQSPllrSSKPRHFLLGHSHGTnwVEYNVAGWLNytKQNPATQN-APRLLQDSQKKIISNLFlgraGSA 877
Cdd:cd14904 447 TNHQTKKDNESIDFP---KVKRTQFIINHYAGP--VTYETVGFME--KHRDTLQNdLLDLVLLSSLDLLTELF----GSS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 878 TVLSGSIAGLEGGSQLAlrratsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGEprsa 957
Cdd:cd14904 516 EAPSETKEGKSGKGTKA-------------------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTE---- 572
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 958 ssrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1026
Cdd:cd14904 573 -------------------------FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP 616
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
324-1069 |
5.55e-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: 196.15 E-value: 5.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVM--HMFKGCRRedMAPHIYAVAQTAYRAMLMSRQDQSIVLL 401
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMdqYMHKGPKE--MPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 402 GSSGSGKTTSFQHLVQYLATIAGTSGtkvfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASI 479
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTN----GVEQ-RVLLAnpILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 480 QTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlaenNVFGIVPLSKPEEKQKA--AQQFSKLQAAMKVLA 557
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSS-----AAYGYLSLSGCIEVEGVddVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 558 ISPEEQKTCWLILASIYHLG------AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QLKGgtlQRSTSF 629
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGniefasGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRlmEIKG---CDPTRI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 630 RQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSL-CSMMIVDTPGFQNPEWGgsargaSFEEL 708
Cdd:cd14872 307 PLTPAQ----------ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKtTFIGVLDIFGFEIFEKN------SFEQL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 709 CHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVrslahadEAR--GLLWLLEEEA 783
Cdd:cd14872 371 CINFTNEKLQQHFNQYTFKLEEALYQSEGVKfehIDFIDNQPVLD-----------LI-------EKKqpGLMLALDDQV 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 784 LVPGATEDALLDRLfsyyGPQEGDKKGQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQK 863
Cdd:cd14872 433 KIPKGSDATFMIAA----NQTHAAKSTFVYAEVRTSRTEFIVKHYAGD--VTYDITGFLEKNK-DTLQKDLYVLLSSSKN 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 864 KIISNLFlgragsatvlsgsiagleggSQLALRRATSmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCf 943
Cdd:cd14872 506 KLIAVLF--------------------PPSEGDQKTS-------------KVTLGGQFRKQLSALMTALNATEPHYIRC- 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 944 lpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1023
Cdd:cd14872 552 --------------------------VKPNQEKRARLFDGFMSL--EQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRF 603
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1907082237 1024 LAPHLTKKHGRnyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1069
Cdd:cd14872 604 LVKTIAKRVGP-----DDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
324-1026 |
1.03e-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: 196.06 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 403
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLaTIAGTSGTKVfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 481
Cdd:cd01385 82 SGSGKTESTNFLLHHL-TALSQKGYGS-GVEQ-TILGAgpVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 482 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 561
Cdd:cd01385 159 YLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 562 EQKTCWLILASIYHLgaaGATKAGRKQFARHEWAQKA--------AYLLGCSLEELSSAIF--KHQLKGGTLQRSTSFrq 631
Cdd:cd01385 238 TQRQIFSVLSAVLHL---GNIEYKKKAYHRDESVTVGnpevldiiSELLRVKEETLLEALTtkKTVTVGETLILPYKL-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 632 gPEesglgegtklsALECLEGMASGLYSELFTLLISLVNRAL---KSSQHSLC-SMMIVDTPGFQNPEWGgsargaSFEE 707
Cdd:cd01385 313 -PE-----------AIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEAKGlSIGVLDIFGFEDFGNN------SFEQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 708 LCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLEPVadDSVAAVdqasHLVRSLAHadearGLLWLLEEEALVPG 787
Cdd:cd01385 375 FCINYANEHLQYYFNQHIFKLEQEEYKKEGIS--WHNIEYT--DNTGCL----QLISKKPT-----GLLCLLDEESNFPG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 788 ATEDALLDRLFS-------YYGPQEgdkkgqspllrssKPRHFLLGHSHGTnwVEYNVAGW----LNYTKQNPATqnapr 856
Cdd:cd01385 442 ATNQTLLAKFKQqhkdnkyYEKPQV-------------MEPAFIIAHYAGK--VKYQIKDFreknLDLMRPDIVA----- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 857 LLQDSQKKIISNL-----------------FLGRAGSATVLSGSIAGLEGGSQLALRRATSMRktfttGMAAVKKKSLCI 919
Cdd:cd01385 502 VLRSSSSAFVRELigidpvavfrwavlrafFRAMAAFREAGRRRAQRTAGHSLTLHDRTTKSL-----LHLHKKKKPPSV 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 920 QIKLQV--DALIDTIKRSKMHFVHCFLPVAEGWPgeprsassrrvsssseldlppgdpceaglLQLDVSLLRAQLRGSRL 997
Cdd:cd01385 577 SAQFQTslSKLMETLGQAEPFFIRCIKSNAEKKP-----------------------------LRFDDELVLRQLRYTGM 627
|
730 740
....*....|....*....|....*....
gi 1907082237 998 LDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1026
Cdd:cd01385 628 LETVRIRRSGYSVRYTFQEFITQFQVLLP 656
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
324-1031 |
1.40e-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: 196.27 E-value: 1.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFK--------GCRREDMAPHIYAVAQTAYRAMLMS-R 393
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPlKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 394 QDQSIVLLGSSGSGKTTSFQHLVQYLATI-----AGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSL 466
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLTSVgrdqsSTEQEGSDAVEIGKRILQTnpILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 467 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAE---NNVFGIVPLSKPEEKQKAA 543
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKyelLNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 544 QQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG------AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQ 617
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGnvnftaENGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSRE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 618 LKGGtlQRSTSFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVN---------RALKSSQHSLCSMMIVDT 688
Cdd:cd14902 322 IKAG--VEVMVLKLTPEQ----------AKEICGSLAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGILDI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 689 PGFQNPEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVaddsVAAVDqashlvrs 765
Cdd:cd14902 390 FGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDwknISYPSNAAC----LALFD-------- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 766 lahaDEARGLLWLLEEEALVPGATEDALLDRLFSYYGPQEgdkkgqspllrsskprHFLLGHSHGTnwVEYNVAGWLNyT 845
Cdd:cd14902 452 ----DKSNGLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAGR--VCYNVEQFVE-K 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 846 KQNPATQNAPRLLQDSQKKIISNLFL-GRAGSATVLSGSiagleggsqlALRRATSMrktfttgmaaVKKKSLCIQIKLQ 924
Cdd:cd14902 509 NTDALPADASDILSSSSNEVVVAIGAdENRDSPGADNGA----------AGRRRYSM----------LRAPSVSAQFKSQ 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 925 VDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMY 1004
Cdd:cd14902 569 LDRLIVQIGRTEAHYVRCLKPNEVKKPG-----------------------------IFDRERMVEQMRSVGVLEAVRIA 619
|
730 740
....*....|....*....|....*..
gi 1907082237 1005 RQGYPDHMVFSEFRRRFDVLAPHLTKK 1031
Cdd:cd14902 620 RHGYSVRLAHASFIELFSGFKCFLSTR 646
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
324-1026 |
3.77e-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: 3.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLL-VLSTRGAPAVYSEKVM--HMFKGcrrEDMAPHIYAVAQTAYRAMLMSRQDQSIVL 400
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIaVNPFKTIPGLYSDEMLlkFIQPS---ISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 401 LGSSGSGKTTSFQHLVQYLATiAGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQ-------- 470
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLAC-AGSEDIKKRSLVEAQVLESnpLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 471 -AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIV--PLSKPEEKQKAAQQFS 547
Cdd:cd14888 158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADakPISIDMSSFEPHLKFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 548 KLQ--------------------AAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARH------EWAQKAAYL 601
Cdd:cd14888 238 YLTksschelpdvddleefestlYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVvsasctDDLEKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 602 LGCSLEELSSAifkhqLKGGTLQRSTSFRQGPEESGLGEGTKlsaleclEGMASGLYSELFTLLISLVNRAL-KSSQHSL 680
Cdd:cd14888 318 LGVDAEDLLNA-----LCYRTIKTAHEFYTKPLRVDEAEDVR-------DALARALYSCLFDKVVERTNESIgYSKDNSL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 681 CSMMIVDTPGFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLE-PVADDSVAAVDQA 759
Cdd:cd14888 386 LFCGVLDIFGFE------CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIS--WNPLDfPDNQDCVDLLQEK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 760 SHLVrsLAHADEargllwlleeEALVPGATEDALLDRLFSYYGpqeGDKKGQSPllrSSKPRHFLLGHSHGTnwVEYNVA 839
Cdd:cd14888 458 PLGI--FCMLDE----------ECFVPGGKDQGLCNKLCQKHK---GHKRFDVV---KTDPNSFVIVHFAGP--VKYCSD 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 840 GWLNYTKqNPATQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsqlalrrATSMRKTFTTGMAAVKKKSLCI 919
Cdd:cd14888 518 GFLEKNK-DQLSVDAQEVIKNSKNPFISNLF---------------------------SAYLRRGTDGNTKKKKFVTVSS 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 920 QIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPgeprsassrrvsssSELDlppgdpceagllQLDVSllrAQLRGSRLLD 999
Cdd:cd14888 570 EFRNQLDVLMETIDKTEPHFIRCIKPNSQNVP--------------DLFD------------RISVN---EQLKYGGVLQ 620
|
730 740
....*....|....*....|....*..
gi 1907082237 1000 AMRMYRQGYPDHMVFSEFRRRFDVLAP 1026
Cdd:cd14888 621 AVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
326-1025 |
1.09e-50 |
|
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: 192.28 E-value: 1.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 326 LHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSekVMHMFKGCRREDMA----PHIYAVAQTAYRAMLMSR----QDQ 396
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPyKSIPLLYD--VPGFDSQRKEEATAssppPHVFSIAERAYRAMKGVGkgqgTPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 397 SIVLLGSSGSGKTTSFQHLVQYLATI----AGTSGTKVF-----SVEKWQALS-TLLEAFGNSPTIMNGSATRFSQILSL 466
Cdd:cd14892 82 SIVVSGESGAGKTEASKYIMKYLATAsklaKGASTSKGAanaheSIEECVLLSnLILEAFGNAKTIRNDNSSRFGKYIQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 467 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAEnnvFGIVPLSKPEEKQKA--AQ 544
Cdd:cd14892 162 HYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAES---FLFLNQGNCVEVDGVddAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 545 QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGA----AGATKAGRK-QFARHEWAQKAAYLLGCSLEELSSAIFKHQLK 619
Cdd:cd14892 239 EFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNvrfeENADDEDVFaQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 620 GGtlqRSTSFRQ--GPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRAlkSSQHSLCSMMIVDTP-------- 689
Cdd:cd14892 319 TA---RGSVLEIklTARE----------AKNALDALCKYLYGELFDWLISRINAC--HKQQTSGVTGGAASPtfspfigi 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 690 ----GFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaaVDQASHL 762
Cdd:cd14892 384 ldifGFE------IMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDvsaIEFQDNQDCLD-----LIQKKPL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 763 vrslahadeargllwlleeeALVPGATEDALLDR-------LFSYYgpQEGDKKGQSpllrSSKPR----HFLLGHSHGT 831
Cdd:cd14892 453 --------------------GLLPLLEEQMLLKRkttdkqlLTIYH--QTHLDKHPH----YAKPRfecdEFVLRHYAGD 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 832 nwVEYNVAGWLnyTKQNPATQNAPRLLQDSQKKiisnlflgragsatvlsgsiagleggsqlalrratsmrktFTTgmaa 911
Cdd:cd14892 507 --VTYDVHGFL--AKNNDNLHDDLRDLLRSSSK----------------------------------------FRT---- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 912 vkkkslciqiklQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvsssSELDLPPGDPCEagllqldvsLLRAQ 991
Cdd:cd14892 539 ------------QLAELMEVLWSTTPSYIKCIKP--------------------NNLKFPGGFSCE---------LVRDQ 577
|
730 740 750
....*....|....*....|....*....|....
gi 1907082237 992 LRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1025
Cdd:cd14892 578 LIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLA 611
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
324-1067 |
8.06e-50 |
|
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: 189.61 E-value: 8.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSE--KVMHMFKGCRRED----MAPHIYAVAQTAYRAMLMSR---- 393
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDetKEAYYEHGERRAAgerkLPPHVYAVADKAFRAMLFASrgqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 394 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW----QALST--LLEAFGNSPTIMNGSATRFSQILSLD 467
Cdd:cd14901 82 CDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATEREnvrdRVLESnpILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 468 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFS 547
Cdd:cd14901 162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 548 KLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRK----QFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTL 623
Cdd:cd14901 242 KTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEggtfSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 624 QRSTSFRqgPEESGLGEgtklsaleclEGMASGLYSELFTLLISLVNRALK--SSQHSLCSMMIVDTPGF----QNpewg 697
Cdd:cd14901 322 YITMPLS--VEQALLTR----------DVVAKTLYAQLFDWLVDRINESIAysESTGASRFIGIVDIFGFeifaTN---- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 698 gsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLePVADDSVAAVDQASHLVRSLahADEargllw 777
Cdd:cd14901 386 ------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-PNNDACVAMFEARPTGLFSL--LDE------ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 778 lleeEALVPGATEDALLDrlfSYYgpqegDKKGQSPLLRSSK----PRHFLLGHSHGTnwVEYNVAGWLNYTKQNPATqN 853
Cdd:cd14901 451 ----QCLLPRGNDEKLAN---KYY-----DLLAKHASFSVSKlqqgKRQFVIHHYAGA--VCYATDGFCDKNKDHVHS-E 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 854 APRLLQDSqkkiiSNLFLgragSATVLSgsiagleggsqlalrratsmrktfttgmaavkkkslciQIKLQVDALIDTIK 933
Cdd:cd14901 516 ALALLRTS-----SNAFL----SSTVVA--------------------------------------KFKVQLSSLLEVLN 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 934 RSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDpcEAGLLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMV 1013
Cdd:cd14901 549 ATEPHFIRC---------------------------IKPND--VLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1014 FSEFRRRFDVLAPHLTKKHGRNYIVVDEKRAVEELLESLDLEKSSCCLGLSRVF 1067
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
323-1024 |
2.90e-48 |
|
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: 185.23 E-value: 2.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRRE--------DMAPHIYAVAQTAYRAMLMSR 393
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPyKQIDNLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 394 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAG----------------TSGTKVFSVEKwQALST--LLEAFGNSPTIMNG 455
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssirATSKSTKSIEQ-KILSCnpILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 456 SATRFSQILSLDFD-QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL-NHLAENNVFgivPL 533
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLkNQLSGDRYD---YL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 534 SKPE----EKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG-----AAGATKAGRKQFARHEWAQKAAYLLGC 604
Cdd:cd14907 237 KKSNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGnlqfdDSTLDDNSPCCVKNKETLQIIAKLLGI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 605 SLEELSSAIFKHQLKGGTlQRSTSfrqgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRAL-------- 673
Cdd:cd14907 317 DEEELKEALTTKIRKVGN-QVITS--------------PLSKKECinnRDSLSKELYDRLFNWLVERLNDTImpkdekdq 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 674 KSSQHSLCSMMIVDTPGFQNPEwggsarGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE-----LAFDDLEPV 748
Cdd:cd14907 382 QLFQNKYLSIGLLDIFGFEVFQ------NNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdylnqLSYTDNQDV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 749 AD--DS-----VAAVDQASHLvrslahadeargllwlleeealvPGATEDALLDRLFSYYGpqeGDKKGQSPllRSSKPR 821
Cdd:cd14907 456 IDllDKppigiFNLLDDSCKL-----------------------ATGTDEKLLNKIKKQHK---NNSKLIFP--NKINKD 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 822 HFLLGHSHGTnwVEYNVAGWL--NYTKQNPATQNaprLLQDSQKKIISNLFLGRAGSATVLSGSIAGleggsqlalrrat 899
Cdd:cd14907 508 TFTIRHTAKE--VEYNIEGFRekNKDEISQSIIN---CIQNSKNRIISSIFSGEDGSQQQNQSKQKK------------- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 900 smrktfttgmAAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGwpgeprsassrrvsssseldlppgdpcEAG 979
Cdd:cd14907 570 ----------SQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEK---------------------------KAD 612
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082237 980 LLQLDVSLLraQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1024
Cdd:cd14907 613 LFIQGYVLN--QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
324-734 |
7.06e-45 |
|
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: 174.74 E-value: 7.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIAGTSGTKVFS--VEKwqalSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQ 480
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIEQriLEA----NPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 481 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENnvfgivplskpeekqkaAQQFSKLQAAMKVLAISP 560
Cdd:cd01382 158 HYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLDD-----------------VGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 561 EEQKTCWLILASIYHLG------AAGATKAGRKQFARHEWA-QKAAYLLGCSLEELSSAI---FKHQLKGGTlqRSTSFR 630
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGniefeeNGSDSGGGCNVKPKSEQSlEYAAELLGLDQDELRVSLttrVMQTTRGGA--KGTVIK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 631 QG--PEESGlgegtklSALECLegmASGLYSELFTLLISLVNRAL--KSSQHSLCsmmIVDTPGFQ----Npewggsarg 702
Cdd:cd01382 299 VPlkVEEAN-------NARDAL---AKAIYSKLFDHIVNRINQCIpfETSSYFIG---VLDIAGFEyfevN--------- 356
|
410 420 430
....*....|....*....|....*....|..
gi 1907082237 703 aSFEELCHNYAQDRLQRLFHERTFLQELERYK 734
Cdd:cd01382 357 -SFEQFCINYCNEKLQQFFNERILKEEQELYE 387
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
324-1040 |
1.26e-43 |
|
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: 170.49 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF-------------KGcrREDMAPHIYAVAQTAYRAM 389
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfQKLPGLYSSDTMAKYllsfearssstrnKG--SDPMPPHIYQVAGEAYKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 390 LMSR----QDQSIVLLGSSGSGKTTSFQHLVQYLA---------TIAGTSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGS 456
Cdd:cd14900 80 MLGLngvmSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQT-NILLESFGNARTLRNDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 457 ATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDAtlrtelhlnhlaennvfgivplskp 536
Cdd:cd14900 159 SSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAI-GAS------------------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 537 eEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKqfarHEWAQKAAYLLGCSLEELSSAIFKH 616
Cdd:cd14900 213 -EAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENS----DRLGQLKSDLAPSSIWSRDAAATLL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 617 QLKGGTLQRSTS---FRQGPEESGLgegtKLSALEC---LEGMASGLYSELFTLLISLVNRALK-----SSQHSLCSMMI 685
Cdd:cd14900 288 SVDATKLEKALSvrrIRAGTDFVSM----KLSAAQAnnaRDALAKALYGRLFDWLVGKMNAFLKmddssKSHGGLHFIGI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 686 VDTPGF----QNpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEpvadDSVAAVDQ 758
Cdd:cd14900 364 LDIFGFevfpKN----------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDwkyVEFCDNQ----DCVNLISQ 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 759 ASHLVRSLahADEargllwlleeEALVPGATEDALLDRLFSyygpqegdKKGQSPLLRSSKPRH----FLLGHSHGTnwV 834
Cdd:cd14900 430 RPTGILSL--IDE----------ECVMPKGSDTTLASKLYR--------ACGSHPRFSASRIQRarglFTIVHYAGH--V 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 835 EYNVAGWLNytkqnpatQNAPRLLQDsqkkiISNLFLGragsatvlsgsiagleggsqlalrratsmrktfttgmaavkk 914
Cdd:cd14900 488 EYSTDGFLE--------KNKDVLHQE-----AVDLFVY------------------------------------------ 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 915 kslCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRG 994
Cdd:cd14900 513 ---GLQFKEQLTTLLETLQQTNPHYVRC---------------------------LKPNDLCKAGIYERERVL--NQLRC 560
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1907082237 995 SRLLDAMRMYRQGYPDHMVFSEFRRRFDVL----APHLTKKHGrnYIVVD 1040
Cdd:cd14900 561 NGVMEAVRVARAGFPIRLLHDEFVARYFSLarakNRLLAKKQG--TSLPD 608
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
324-1025 |
1.89e-43 |
|
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: 171.29 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSekvMHMFkgcrREDM------APHIYAVAQTAYRAMLM----- 391
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPfKHIPGLYD---LHKY----REEMpgwtalPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 392 --SRQDQSIVLLGSSGSGKTTSFQHLVQYLA-----TIAGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQ 462
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskhTTATSSSKRRRAISGSELLSAnpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 463 ILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNvFGIVPLSKPE 537
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQE-FQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 538 EKQKAAQ---QFSKLQAAMKVLAISPEEQKTCWLILASIYHLG-----AAGATKAGRKQFARHEWAQKA----------- 598
Cdd:cd14895 234 QRNDGVRddkQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvASSEDEGEEDNGAASAPCRLAsaspssltvqq 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 599 -----AYLLGCSLEELSSAIFKHQLKGGtlqrstsfrqgpEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRAL 673
Cdd:cd14895 314 hldivSKLFAVDQDELVSALTTRKISVG------------GETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 674 KSSQHSLCS-----------MMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 742
Cdd:cd14895 382 PQRQFALNPnkaankdttpcIAVLDIFGFEEFEVN------QFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 743 DDLEpvaDDSVA--AVDQASHLVRSLAhaDEargllwlleeEALVPGATEDALLDRLFSYYGpqegDKKGQSPLLRSSKP 820
Cdd:cd14895 456 VDYE---DNSVCleMLEQRPSGIFSLL--DE----------ECVVPKGSDAGFARKLYQRLQ----EHSNFSASRTDQAD 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 821 RHFLLGHSHGTnwVEYNVAGWLNYTKQNPaTQNAPRLLQDSQKKIISNLFlgragsaTVLSGSIAGLEGGSQLALRRATS 900
Cdd:cd14895 517 VAFQIHHYAGA--VRYQAEGFCEKNKDQP-NAELFSVLGKTSDAHLRELF-------EFFKASESAELSLGQPKLRRRSS 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 901 MRKTFTTGMaavkkkslciQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGl 980
Cdd:cd14895 587 VLSSVGIGS----------QFKQQLASLLDVVQQTQTHYIRC---------------------------IKPNDESASD- 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082237 981 lQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1025
Cdd:cd14895 629 -QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1120-1814 |
3.06e-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: 170.36 E-value: 3.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1120 NIKKNKGVKDWPWWKLFTTVRPLIQVQLSEEQIRNKDE-EIQQLRSKLEKVEKERNELrlssdrlETRISELTSELtder 1198
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESERQRAEL-------AEKLSKLQSEL---- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1199 ntgESASQLLDAETAERLRTEKEMKELQTQ-YDALKKQMEVMEMEVMEARLIRA--AEINGEVDDDDAGGEWRLKYERAV 1275
Cdd:pfam01576 443 ---ESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQleDERNSLQEQLEEEEEAKRNVERQL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1276 REVDF----TKKRLQQELEdKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE 1351
Cdd:pfam01576 520 STLQAqlsdMKKKLEEDAG-TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1352 LEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSqeSKDEA 1431
Cdd:pfam01576 599 LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVS--SKDDV 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1432 --SLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEV 1509
Cdd:pfam01576 677 gkNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1510 QLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLrKDLKRTKALLADAQIMLDHLKNN-----APSKREIAQL 1584
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV-KQLKKLQAQMKDLQRELEEARASrdeilAQSKESEKKL 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1585 KN------QLEESeftCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1658
Cdd:pfam01576 836 KNleaellQLQED---LAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL 912
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1659 KAAVAQ---------ASRDMAQMND-LQAQIEESNKekqELQEKLQALQSQVEFLEqsmvdKSLVSRQEAKIRELETRLE 1728
Cdd:pfam01576 913 RKSTLQveqlttelaAERSTSQKSEsARQQLERQNK---ELKAKLQEMEGTVKSKF-----KSSIAALEAKIAQLEEQLE 984
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1729 FEKTQ----VKRLENLASRLKETMEKLTEER---DQRAAAENREKEQNKRLQRQLRDTKEEMSelarkEAEASRKKheLE 1801
Cdd:pfam01576 985 QESRErqaaNKLVRRTEKKLKEVLLQVEDERrhaDQYKDQAEKGNSRMKQLKRQLEEAEEEAS-----RANAARRK--LQ 1057
|
730
....*....|...
gi 1907082237 1802 MDLESLEAANQSL 1814
Cdd:pfam01576 1058 RELDDATESNESM 1070
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
363-739 |
3.34e-42 |
|
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: 166.37 E-value: 3.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 363 MHMFKGCRREDMAPHIYAVAQTAYRAMLMSR---QDQSIVLLGSSGSGKTTSFQHLVQYLAT-----IAGTSGTKVFSVE 434
Cdd:cd14891 40 KSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQSIVISGESGAGKTETSKIILRFLTTravggKKASGQDIEQSSK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 435 KWQALST-----------LLEAFGNSPTIMNGSATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVF 502
Cdd:cd14891 120 KRKLSVTslderlmdtnpILESFGNAKTLRNHNSSRFGKFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 503 YYLLACGDATLRTELHlnhlaennvfgivpLSKPEEKQKAAQ-------------QFSKLQAAMKVLAISPEEQKTCWLI 569
Cdd:cd14891 200 YQLLAGASAELLKELL--------------LLSPEDFIYLNQsgcvsddniddaaNFDNVVSALDTVGIDEDLQLQIWRI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 570 LASIYHLG-------------AAGATKAGRKQFArhewaqKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRqgpees 636
Cdd:cd14891 266 LAGLLHLGniefdeedtsegeAEIASESDKEALA------TAAELLGVDEEALEKVI---------TQREIVTR------ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 637 GLGEGTKLSALECL---EGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEwggsaRGASFEELCHNYA 713
Cdd:cd14891 325 GETFTIKRNAREAVysrDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFE-----TKNDFEQLLINYA 399
|
410 420
....*....|....*....|....*.
gi 1907082237 714 QDRLQRLFHERTFLQELERYKEDNIE 739
Cdd:cd14891 400 NEALQATFNQQVFIAEQELYKSEGID 425
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
324-1037 |
1.75e-40 |
|
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: 162.07 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 401
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 402 GSSGSGKTTSFQHLVQYLATiagTSGTKVF----------SVEKWQALST-LLEAFGNSPTIMNGSATRFSQILSLDFDQ 470
Cdd:cd14906 82 GESGSGKTEASKTILQYLIN---TSSSNQQqnnnnnnnnnSIEKDILTSNpILEAFGNSRTTKNHNSSRFGKFLKIEFRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 471 A-GQVASASIQTMLLEKLRVARRP-ASEATFNVFYYLLACGDATLRTELHLNH--------LAENNVFGIV------PLS 534
Cdd:cd14906 159 SdGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNdpskyrylDARDDVISSFksqssnKNS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 535 KPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG-------AAGATKAGRKQFARHEWAQkAAYLLGCSLE 607
Cdd:cd14906 239 NHNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGniefeedSDFSKYAYQKDKVTASLES-VSKLLGYIES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 608 ELSSAIFKHQLKGGTlqRSTSFRQgPEESGLGEGTKlsaleclEGMASGLYSELFTLLISLVNR-----------ALKSS 676
Cdd:cd14906 318 VFKQALLNRNLKAGG--RGSVYCR-PMEVAQSEQTR-------DALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 677 QHSLCSMMIVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDlepvADDSV 753
Cdd:cd14906 388 KKNNLFIGVLDIFGFEN------LSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSnsnFID----NKECI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 754 AAVDQASHLVRSLAHaDEArgllwlleeeaLVPGATEDALLDRLFSYYgpqegdKKGQSPLLRSSKPRHFLLGHSHGTnw 833
Cdd:cd14906 458 ELIEKKSDGILSLLD-DEC-----------IMPKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGD-- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 834 VEYNVAGWLNYTKQNPATqNAPRLLQDSQKKIISNLFLGRAGSATvlsgsiagleggsqlalrrATSMRKTFTTGMAAvk 913
Cdd:cd14906 518 VTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT-------------------NTTKKQTQSNTVSG-- 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 914 kkslciQIKLQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvssssELDLPPGDpceagllqLDVSLLRAQLR 993
Cdd:cd14906 576 ------QFLEQLNQLIQTINSTSVHYIRCIKP---------------------NQTMDCNN--------FNNVHVLSQLR 620
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082237 994 GSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYI 1037
Cdd:cd14906 621 NVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPK 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
323-1025 |
7.48e-39 |
|
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: 156.51 E-value: 7.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMF---KGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIV 399
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 400 LLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSveKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDF-DQAGQVASAS 478
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDS--RFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 479 IQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVfgiVPLSKPEEKQKAA-----QQFSKLQAAM 553
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRY---LNQTMREDVSTAErslnrEKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 554 KVLAISPEEQKTCWLILASIYHLGAAG---ATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFK--HQLKGGTLQRSTS 628
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRftaLTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTdiQYFKGDMIIRRHT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 629 FRQGPEESGLgegtklsaleclegMASGLYSELFTLLISLVNRALKsSQHSLCSMM-----IVDTPGFQNpewggsARGA 703
Cdd:cd14878 316 IQIAEFYRDL--------------LAKSLYSRLFSFLVNTVNCCLQ-SQDEQKSMQtldigILDIFGFEE------FQKN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 704 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE-------------LAFDDLEPVADDSVaaVDQASHLVRSLAHAD 770
Cdd:cd14878 375 EFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTmetayspgnqtgvLDFFFQKPSGFLSL--LDEESQMIWSVEPNL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 771 EARgllwlleeealVPGATEDALLDRLFSYYGPQEGD--KKGQSPLlrsskprhFLLGHSHGTnwVEYNVAGWLNYTKqN 848
Cdd:cd14878 453 PKK-----------LQSLLESSNTNAVYSPMKDGNGNvaLKDQGTA--------FTVMHYAGR--VMYEIVGAIEKNK-D 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 849 PATQNAPRLLQDSQKKIISNLFlgRAGSATVlsgsiaglegGSQLalrratsmrktfttgmaavkKKSLC-IQIKLQvda 927
Cdd:cd14878 511 SLSQNLLFVMKTSENVVINHLF--QSKLVTI----------ASQL--------------------RKSLAdIIGKLQ--- 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 928 lidtikRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQG 1007
Cdd:cd14878 556 ------KCTPHFIHCIKPNNSKLPD-----------------------------TFDNFYVSAQLQYIGVLEMVKIFRYG 600
|
730
....*....|....*...
gi 1907082237 1008 YPDHMVFSEFRRRFDVLA 1025
Cdd:cd14878 601 YPVRLSFSDFLSRYKPLA 618
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
324-1036 |
4.50e-38 |
|
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: 152.74 E-value: 4.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGpsLLVLSTRGAPAVYSEKVMHMFKGCRREdMAPHIYAVAQTAYRAMLMSrQDQSIVLLGS 403
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSG--LVFLALNPYETIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 404 SGSGKTTSFQHLVQYLatIAGTSGTKvfSVEK-WQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDqaGQVASASIQTM 482
Cdd:cd14898 78 SGSGKTENAKLVIKYL--VERTASTT--SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 483 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSkpeekqkaaQQFSKLQAAMKVLAI-SPE 561
Cdd:cd14898 152 LLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFIDTSSTAGNKESIVQLS---------EKYKMTCSAMKSLGIaNFK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 562 EQKTCwliLASIYHLGAAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QLKGGTLQRSTSFRQgpeesglg 639
Cdd:cd14898 223 SIEDC---LLGILYLGSIQFVNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFsiQVKGETIEVFNTLKQ-------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 640 egtklsALECLEGMASGLYSELFTLLISLVNRALK-SSQHSLCsmmIVDTPGFQNPEWGGsargasFEELCHNYAQDRLQ 718
Cdd:cd14898 292 ------ARTIRNSMARLLYSNVFNYITASINNCLEgSGERSIS---VLDIFGFEIFESNG------LDQLCINWTNEKIQ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 719 RLFHERTFLQELERYKEDNIElaFDDLEPVADDSVaavdqashlvrsLAHADEARGLLWLLEEEALVPGATEDALLDRLF 798
Cdd:cd14898 357 NDFIKKMFRAKQGMYKEEGIE--WPDVEFFDNNQC------------IRDFEKPCGLMDLISEESFNAWGNVKNLLVKIK 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 799 SYYGPQEGDKKGQSPLLrsskprhfllghSHGTNWVEYNVAGWLNYTKQNpatqnaprllqdSQKKIISNLFLGRAGSat 878
Cdd:cd14898 423 KYLNGFINTKARDKIKV------------SHYAGDVEYDLRDFLDKNREK------------GQLLIFKNLLINDEGS-- 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 879 vlsgsiagleggsqlalrratsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPgeprsas 958
Cdd:cd14898 477 -----------------------------------KEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRP------- 514
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 959 srrvsssseldlppgdpceaglLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTK----KHGR 1034
Cdd:cd14898 515 ----------------------WCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLFEvvdyRKGR 572
|
..
gi 1907082237 1035 NY 1036
Cdd:cd14898 573 TR 574
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
326-1069 |
6.37e-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: 151.34 E-value: 6.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 326 LHTLRQRYGA--------SLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQS 397
Cdd:cd14887 4 LENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 398 IVLLGSSGSGKTTSFQHLVQYLATI------AGTSGTKvfsvEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQA 471
Cdd:cd14887 84 ILISGESGAGKTETSKHVLTYLAAVsdrrhgADSQGLE----ARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 472 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLlaCGDATLRTELHlnhlaennvfgivplSKPEEKQKAAQQFSKLQA 551
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYAL--CNAAVAAATQK---------------SSAGEGDPESTDLRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARH-----------EWAQKAAYLLgcSLEELSSAIFKHQLKG 620
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKrkltsvsvgceETAADRSHSS--EVKCLSSGLKVTEASR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 621 GTLQRSTSFRQGPEESGLGEGTKLS-----------------ALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSM 683
Cdd:cd14887 301 KHLKTVARLLGLPPGVEGEEMLRLAlvsrsvretrsffdldgAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSESD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 684 MIVDTP--------------GFQNPEWGGSARgasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL-----AFDD 744
Cdd:cd14887 381 SDEDTPsttgtqtigildlfGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQnqdcsAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 745 LEPVADDSVAAVDQASHLvrSLAHADEARGLLWLLEEEALVPGATEDALLdrlfsyygpqegdkkgQSPLLRSSKPRHFL 824
Cdd:cd14887 458 SFPLASTLTSSPSSTSPF--SPTPSFRSSSAFATSPSLPSSLSSLSSSLS----------------SSPPVWEGRDNSDL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 825 LGHShgtnwVEYNVAGWLNYTKQNPAtqnaprlLQDSQKKIISNLFLGRA---------GSATVLSGSIAGLEGGSQLAL 895
Cdd:cd14887 520 FYEK-----LNKNIINSAKYKNITPA-------LSRENLEFTVSHFACDVtydardfcrANREATSDELERLFLACSTYT 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 896 RRATSMRKTFTTGMAAvKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGwpgeprsassrrvsssseldlppgdp 975
Cdd:cd14887 588 RLVGSKKNSGVRAISS-RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQ-------------------------- 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 976 cEAGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHgrnyivVDEKRAVEELLESLDLE 1055
Cdd:cd14887 641 -EAGI--FEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREA------LTPKMFCKIVLMFLEIN 711
|
810
....*....|....
gi 1907082237 1056 KSSCCLGLSRVFFR 1069
Cdd:cd14887 712 SNSYTFGKTKIFFR 725
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
324-742 |
3.21e-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: 148.52 E-value: 3.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFK--GCRRE-------DMAPHIYAVAQTAYRAMLM-SR 393
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiespqALGPHVFAIADRSYRQMMSeIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 394 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL---------LEAFGNSPTIMNGSATRFSQIL 464
Cdd:cd14908 82 ASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSIMdrvlqsnpiLEAFGNARTLRNDNSSRFGKFI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 465 SLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGivplskPEEKQKAAQ 544
Cdd:cd14908 162 ELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQL------PNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 545 -------------QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGA---AGATKAGRKQFAR---HEWAQKAAYLLGCS 605
Cdd:cd14908 236 ggapdlreftdedGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQlefESKEEDGAAEIAEegnEKCLARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 606 LEELSSAIFKHQLKGGTLQRSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALK--SSQHSLCSM 683
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKL------------TPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRSSV 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 684 MIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 742
Cdd:cd14908 384 GVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAF 436
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
258-1125 |
1.67e-35 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 147.48 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 258 LVHRDgfSLASQLKSEELSLPEGKarvkldhdgaILDVDEDDIEKANAP-SCDRLEDLASLVYLNESSVLHTLRQRYGAS 336
Cdd:PTZ00014 56 LVLPG--STGEKLTLKQIDPPTNS----------TFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 337 LLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHL 415
Cdd:PTZ00014 124 QIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 416 VQYLAtiAGTSGTKVFSVEK--WQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRP 493
Cdd:PTZ00014 204 MRYFA--SSKSGNMDLKIQNaiMAA-NPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 494 ASEATFNVFYYLLACGDATLRTELHLNHLAENNVfgIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASI 573
Cdd:PTZ00014 281 DDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKY--INPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 574 YHLG--------AAGATKAGRKQFARHEWAQKAAYLLGCSLEELS-SAIFKHQLKGGTLQRStsfRQGPEESglgEGTKL 644
Cdd:PTZ00014 359 LLLGnveiegkeEGGLTDAAAISDESLEVFNEACELLFLDYESLKkELTVKVTYAGNQKIEG---PWSKDES---EMLKD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 645 SaleclegMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQ----NpewggsargaSFEELCHNYAQDRLQRL 720
Cdd:PTZ00014 433 S-------LSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEvfknN----------SLEQLFINITNEMLQKN 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 721 FHERTFLQELERYKEDNI---ELAFDDLEPVAD------DSVAAV--DQashlvrSLAhadeargllwlleeealvPGAT 789
Cdd:PTZ00014 496 FVDIVFERESKLYKDEGIsteELEYTSNESVIDllcgkgKSVLSIleDQ------CLA------------------PGGT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 790 EDALLDRLFSYYGPQEGDKKGqspllRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNL 869
Cdd:PTZ00014 552 DEKFVSSCNTNLKNNPKYKPA-----KVDSNKNFVIKHTIGD--IQYCASGFLFKNK-DVLRPELVEVVKASPNPLVRDL 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 870 FLGragsATVLSGSIAgleggsqlalrratsmrktfttgmaavKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPvaeg 949
Cdd:PTZ00014 624 FEG----VEVEKGKLA---------------------------KGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKP---- 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 950 wpgeprsassrrvssssELDLPPGDPCEAGLLqldvsllrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLT 1029
Cdd:PTZ00014 669 -----------------NENKKPLDWNSSKVL--------IQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVS 723
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1030 KKHGrnyivVDEKRAVEELLESLDLEKSSCCLGLSRVFFR---AGTLARLEEQRDEQTSRHLTLFQAACRGYLARQHFKK 1106
Cdd:PTZ00014 724 NDSS-----LDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRK 798
|
890
....*....|....*....
gi 1907082237 1107 RkIQDLAIrcVQKNIKKNK 1125
Cdd:PTZ00014 799 N-IKSLVR--IQAHLRRHL 814
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
323-742 |
1.77e-35 |
|
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: 146.15 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQ--DQSI 398
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPfKPVPQLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 399 VLLGSSGSGKTTSFQHLVQYLATIAG--TSGTKVFSVEKWQAL----STLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 472
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAspTSWESHKIAERIEQRilnsNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 473 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLnhlAENNVFGIVPLSkpeEKQKAAQQFSKLQAA 552
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHL---PEGAAFSWLPNP---ERNLEEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 553 MKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFA------RHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRS 626
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpmddTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 627 tsFRQgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQN-PEwggsar 701
Cdd:cd14880 315 --FKK-----------PCSRAECdtrRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIgLLDVYGFESfPE------ 375
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1907082237 702 gASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 742
Cdd:cd14880 376 -NSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSF 415
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
323-1021 |
9.18e-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: 144.47 E-value: 9.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF----------KGCRREDMAPHIYAVAQTAYRAMLM 391
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPfQDLPQLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 392 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW-------------QALST--LLEAFGNSPTIMNGS 456
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESIsppaspsrttieeQVLQSnpILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 457 ATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLA----CGDATLRTELHLNHLAEN-NVFGI 530
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSadnnCVSKEQKQVLALSGGPQSfRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 531 VPLSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGA---------------AGATKAGRKQFARHEWA 595
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNvdfeqiphkgddtvfADEARVMSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 596 QKAAYLLGCSLEELSSAIFKHQLKGGtlqrSTSFRQGPEESGLGEGTKLSALEClegmasglYSELFTLLISLVNRALK- 674
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHAS----NETLVVGVDVAHARNTRNALTMEC--------YRLLFEWLVARVNNKLQr 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 675 --------------SSQHSLCSMMIVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL 740
Cdd:cd14899 389 qasapwgadesdvdDEEDATDFIGLLDIFGFED------MAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 741 AFDDLEpvadDSVAAVDQASHlvrslahadEARGLLWLLEEEALVPGATEDALLDRlfsYYgpQEGDKKGQSPLLRSS-- 818
Cdd:cd14899 463 SFVDFP----NNRACLELFEH---------RPIGIFSLTDQECVFPQGTDRALVAK---YY--LEFEKKNSHPHFRSApl 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 819 --KPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLflgRAGSATVLSGSIAGLEGGSQLALR 896
Cdd:cd14899 525 iqRTTQFVVAHYAGC--VTYTIDGFLAKNK-DSFCESAAQLLAGSSNPLIQAL---AAGSNDEDANGDSELDGFGGRTRR 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 897 RATSmrktfttgmaAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPC 976
Cdd:cd14899 599 RAKS----------AIAAVSVGTQFKIQLNELLSTVRATTPRYVRC---------------------------IKPNDSH 641
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082237 977 EAGLLQldVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRF 1021
Cdd:cd14899 642 VGSLFQ--STRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
324-758 |
4.86e-32 |
|
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: 135.25 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKvMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQE-FHAKYRCKsRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLATIA-GTSGTkvfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 481
Cdd:cd14882 81 ESYSGKTTNARLLIKHLCYLGdGNRGA----TGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 482 MLLEKLRVARRPASEATFNVFYYLLACGDATLRteLHLNHLAENNVFGIVPLSKPEEKQKA----------AQQFSKLQA 551
Cdd:cd14882 157 YQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNR--LKEYNLKAGRNYRYLRIPPEVPPSKLkyrrddpegnVERYKEFEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 552 AMKVLAISPEEQKTCWLILASIYHLGAAGATKA-GRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQL-KGGTLQRStsf 629
Cdd:cd14882 235 ILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNgGYAELENTEIASRVAELLRLDEKKFMWALTNYCLiKGGSAERR--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 630 RQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVN------RALKSSQHSLcsmMIVDTPGFQNPEWGGsarga 703
Cdd:cd14882 312 KHTTEE----------ARDARDVLASTLYSRLVDWIINRINmkmsfpRAVFGDKYSI---SIHDMFGFECFHRNR----- 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 704 sFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIelafddlePVAD----DSVAAVDQ 758
Cdd:cd14882 374 -LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDI--------PTINlrfyDNKTAVDQ 423
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
323-1027 |
1.54e-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: 134.33 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRRE----------DMAPHIYAVAQTAYRAMLMS 392
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 393 RQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALS----------TLLEAFGNSPTIMNGSATRFSQ 462
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHpigqqilhafTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 463 ILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAC--GDATLRTELHLNHLAENnvFGIVPLSKPEEKQ 540
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKCVNE--FVMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 541 KA--AQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG---------AAGATKAGRKQFARHEWA----QKAAYLLGCS 605
Cdd:cd14893 239 FAldARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGnvdfvpdpeGGKSVGGANSTTVSDAQScalkDPAQILLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 606 LEELSSAIFKHQLKggtLQRSTSFRQGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVN--------RALKS-- 675
Cdd:cd14893 319 LLEVEPVVLDNYFR---TRQFFSKDGNKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNgilggifdRYEKSni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 676 ---SQhslcSMMIVDTPGFQNPEwggsARGASFEELCHNYAQDRLQRLFHERTfLQELERYKEDNIELAFDDLepvADDS 752
Cdd:cd14893 396 vinSQ----GVHVLDMVGFENLT----PSQNSFDQLCFNYWSEKVHHFYVQNT-LAINFSFLEDESQQVENRL---TVNS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 753 VAAVDQASHLVRSLAHaDEARGLLWLLEEEALVPGATEDALLDRLFS-------YYGPQEGDKKGQSPLLRSSKPR-HFL 824
Cdd:cd14893 464 NVDITSEQEKCLQLFE-DKPFGIFDLLTENCKVRLPNDEDFVNKLFSgneavggLSRPNMGADTTNEYLAPSKDWRlLFI 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 825 LGHSHGTnwVEYNVAGwlnYTKQNPATQNA--PRLLQDSQkkiisNLFLGRAGSATVLSGSIAglEGGSQLALRRATS-- 900
Cdd:cd14893 543 VQHHCGK--VTYNGKG---LSSKNMLSISStcAAIMQSSK-----NAVLHAVGAAQMAAASSE--KAAKQTEERGSTSsk 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 901 MRKTFTTGMAAVK-KKSLCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAG 979
Cdd:cd14893 611 FRKSASSARESKNiTDSAATDVYNQADALLHALNHTGKNFLVC---------------------------IKPNETLEEG 663
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1907082237 980 LlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1027
Cdd:cd14893 664 V--FDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1159-1877 |
1.91e-31 |
|
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: 135.58 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1159 IQQLRSKLEKVEKERNELRLSSDRLETRISELTSE---LTDERNTGESASQLL----DAETAERLR----TEKEMKELQT 1227
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerLRREREKAERYQALLkekrEYEGYELLKekeaLERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1228 QYDALKKQMEVMEMEVM------EARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTK-KRLQQELEDKMEVEQQSR 1300
Cdd:TIGR02169 245 QLASLEEELEKLTEEISelekrlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1301 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKL 1380
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1381 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDE-------ASLAKVKKQLRDLEAKVKDQEEE 1453
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1454 LDEQAGSIQMLEqAKLRLEMEMERMRQTHSKEMESRDEEV---------------------------------EEARQSC 1500
Cdd:TIGR02169 485 LSKLQRELAEAE-AQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgeryataievaagnrlnnvvvedDAVAKEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1501 QKKLKQME----------------------------------VQLEEEYEDKQK----------ALREKREL--ESKLST 1534
Cdd:TIGR02169 564 IELLKRRKagratflplnkmrderrdlsilsedgvigfavdlVEFDPKYEPAFKyvfgdtlvveDIEAARRLmgKYRMVT 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1535 L-------------------SDQVNQR-DFESEKRLRKDLKRTKALLADAQIMLDHLKNNA--------PSKREIAQLKN 1586
Cdd:TIGR02169 644 LegelfeksgamtggsraprGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIENRLdelsqelsDASRKIGEIEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1587 QLEESEFTcAAAVKAR--------KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEI-----QNRLEEDQEDMNE 1653
Cdd:TIGR02169 724 EIEQLEQE-EEKLKERleeleedlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1654 LMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLE----F 1729
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------IENLNGKKEELEEELEeleaA 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1730 EKTQVKRLENLAS---RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHElEMDLES 1806
Cdd:TIGR02169 877 LRDLESRLGDLKKerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLED 955
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1807 LEAANQSLQADLklafKRIGDLQAAIEDEMEsdENEDLINSLQDmvtkyqkKKNKLEGDSDvdsELEDRVD 1877
Cdd:TIGR02169 956 VQAELQRVEEEI----RALEPVNMLAIQEYE--EVLKRLDELKE-------KRAKLEEERK---AILERIE 1010
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1283-1863 |
2.52e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.60 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1283 KRLQQELED-KMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1361
Cdd:COG1196 216 RELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1362 ELSQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR 1441
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLE-------ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1442 DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMEsRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKA 1521
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1522 LREKRELESKLSTLSDQVnqrdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESeftcAAAVKA 1601
Cdd:COG1196 448 AEEEAELEEEEEALLELL--------AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG----VKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1602 RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQReknEIQNRLEEDQEDMNELMKKHKAAVA-------QASRDMAQMND 1674
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ---NIVVEDDEVAAAAIEYLKAAKAGRAtflpldkIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1675 LQAQIEESNKEKQELQEKLQALQSQveFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEE 1754
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYV--LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1755 RDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED 1834
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
570 580 590
....*....|....*....|....*....|
gi 1907082237 1835 EMESDENEDL-INSLQDMVTKYQKKKNKLE 1863
Cdd:COG1196 751 EALEELPEPPdLEELERELERLEREIEALG 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1143-1865 |
3.31e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 131.33 E-value: 3.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1143 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldaetAERLRTEKEM 1222
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--------------LEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1223 KELQTQYDALKkqmevmemevmearliraAEINgevddddaggewrlkyeRAVREVDFTKKRLQQeLEDKMEVEQQSRRQ 1302
Cdd:TIGR02168 284 EELQKELYALA------------------NEIS-----------------RLEQQKQILRERLAN-LERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1303 LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQR 1382
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1383 EKDMLLAEAFSLKQQMEEKDLDIAgftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQ 1462
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLE---------EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1463 M----LEQAKLRLEMeMERMRQTHSKEMESRDEEVEEARQ------------SCQKKLKQ-MEVQL-----------EEE 1514
Cdd:TIGR02168 479 AaereLAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAaIEAALggrlqavvvenLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1515 YEDKQKALREKRELESKLSTLsDQVNQRDFESEKRLRKDLKRTKALLAD--------AQIMLDHLKNN---APSKREIAQ 1583
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVTFLPL-DSIKGTEIQGNDREILKNIEGFLGVAKdlvkfdpkLRKALSYLLGGvlvVDDLDNALE 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1584 LKNQLEESE----------FTCAAAVKARK-------AMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE 1646
Cdd:TIGR02168 637 LAKKLRPGYrivtldgdlvRPGGVITGGSAktnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1647 DQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV-DKSLVSRQEAKIRELET 1725
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAeAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1726 RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLE 1805
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1806 SLEAANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINSLQDMVTKYQKKKNKLEGD 1865
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRElESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1157-1864 |
5.89e-30 |
|
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: 130.30 E-value: 5.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1157 EEI-QQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDErntgESASQLLDAEtaeRLRTEKEMKELQTQYDALKKQ 1235
Cdd:pfam01576 74 EEIlHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE----EAARQKLQLE---KVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1236 MEVMEMEVMEARLiRAAEINGEVDDDDAG----GEWRLKYERAVREVDftkKRLQQELEDKMEVEQqSRRQLERRLGDLQ 1311
Cdd:pfam01576 147 NSKLSKERKLLEE-RISEFTSNLAEEEEKakslSKLKNKHEAMISDLE---ERLKKEEKGRQELEK-AKRKLEGESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1312 ADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEA 1391
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1392 FSLKQQMEEkdldiagfTQKVVSLEAELQdissqeSKDEASLAKVKK-----------QLRDLEAKVKDQEEELDEQags 1460
Cdd:pfam01576 302 EALKTELED--------TLDTTAAQQELR------SKREQEVTELKKaleeetrsheaQLQEMRQKHTQALEELTEQ--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1461 iqmLEQAKlRLEMEMERMRQTHSKEMESRDEEV---EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLS- 1536
Cdd:pfam01576 365 ---LEQAK-RNKANLEKAKQALESENAELQAELrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQs 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1537 --DQVNQRDFESEK---RLRKDLKRTKALLADAQIML-------------------------DHLKNNAPSKREI----- 1581
Cdd:pfam01576 441 elESVSSLLNEAEGkniKLSKDVSSLESQLQDTQELLqeetrqklnlstrlrqledernslqEQLEEEEEAKRNVerqls 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1582 ------AQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQRE----------KNEIQNRLE 1645
Cdd:pfam01576 521 tlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElddllvdldhQRQLVSNLE 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1646 EDQEDMNELMKKHKAAVAQAS--RDMAQMN---------DLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM--VDKSL 1712
Cdd:pfam01576 601 KKQKKFDQMLAEEKAISARYAeeRDRAEAEareketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKddVGKNV 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1713 VSRQEAKiRELETRLEFEKTQVKRL-------ENLASRLKETME--KLTEERDQRAAAENREkEQNKRLQRQLRDTKEEM 1783
Cdd:pfam01576 681 HELERSK-RALEQQVEEMKTQLEELedelqatEDAKLRLEVNMQalKAQFERDLQARDEQGE-EKRRQLVKQVRELEAEL 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1784 SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMEsdENEDLINSLQDMVTKYQKKKNKLE 1863
Cdd:pfam01576 759 EDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQR--ELEEARASRDEILAQSKESEKKLK 836
|
.
gi 1907082237 1864 G 1864
Cdd:pfam01576 837 N 837
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1168-1811 |
2.41e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 128.13 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1168 KVEKERNELRLSS--DRLEtRISELTSELtdERNTGESASQlldAETAERLRtekemkELQTQYDALKKQMEVMEMEVME 1245
Cdd:COG1196 171 KERKEEAERKLEAteENLE-RLEDILGEL--ERQLEPLERQ---AEKAERYR------ELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1246 ARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQ-QELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQL 1324
Cdd:COG1196 239 AELEELEAELEELEAELE----ELEAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1325 KKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLD 1404
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1405 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSK 1484
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1485 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLrkdlkrtkALLADA 1564
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL--------EAALAA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1565 QIMLDHLKNNAPSKREIAQLK-NQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR 1643
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1644 LEEDQEDM-NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvSRQEAKIRE 1722
Cdd:COG1196 627 LVAARLEAaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA------------ERLAEEELE 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1723 LETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEM 1802
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....*....
gi 1907082237 1803 DLESLEAAN 1811
Cdd:COG1196 775 EIEALGPVN 783
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
376-1031 |
2.58e-29 |
|
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: 126.85 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 376 PHIYAVAQTAYRAMLM-SRQDQSIVLLGSSGSGKTTSFQHLVQYLA---------TIAGTSGTKVFSVEKWQalSTLLEA 445
Cdd:cd14875 56 PHIWQVAHKAFNAIFVqGLGNQSVVISGESGSGKTENAKMLIAYLGqlsymhssnTSQRSIADKIDENLKWS--NPVMES 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 446 FGNSPTIMNGSATRFSQILSLDFDQA-GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDAT-------LRTEL 517
Cdd:cd14875 134 FGNARTVRNDNSSRFGKYIKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEekkelggLKTAQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 518 HLNHLAENNVF---GI--VPLSKPEEkqkaaqqFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKagrKQFARH 592
Cdd:cd14875 214 DYKCLNGGNTFvrrGVdgKTLDDAHE-------FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES---DQNDKA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 593 EWAQKAAYLLGCSLEELSSAifkhQLKGGTLQRS-----TSFRQGPEESGLgegtklsalecLEGMASGLYSELFTLLIS 667
Cdd:cd14875 284 QIADETPFLTACRLLQLDPA----KLRECFLVKSktslvTILANKTEAEGF-----------RNAFCKAIYVGLFDRLVE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 668 LVNRALKSSQH-SLCSMM-IVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAF 742
Cdd:cd14875 349 FVNASITPQGDcSGCKYIgLLDIFGFEN------FTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQipkIEF 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 743 DDlepvADDSVAAVDQASHLVRSLahADEargllwlleeEALVPGATEDALLDRLFSYYGpqegdkkGQSPLL---RSSK 819
Cdd:cd14875 423 PD----NSECVNMFDQKRTGIFSM--LDE----------ECNFKGGTTERFTTNLWDQWA-------NKSPYFvlpKSTI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 820 PRHFllGHSHGTNWVEYNVAGWLNytKQNPA-TQNAPRLLQDSQKKIISNLFLGRAGSAtvlsgsiagleggsqlalRRa 898
Cdd:cd14875 480 PNQF--GVNHYAAFVNYNTDEWLE--KNTDAlKEDMYECVSNSTDEFIRTLLSTEKGLA------------------RR- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 899 tsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpcea 978
Cdd:cd14875 537 ---------------KQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPS-------------------------- 575
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1907082237 979 gllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKK 1031
Cdd:cd14875 576 ---FLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTAS 625
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
325-739 |
3.46e-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: 126.15 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 325 VLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRRE-----DMAPHIYAVAQTAYRAMLMSRQDQSI 398
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfKQIRNLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 399 VLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVekwqALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 476
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSL----ILGSnpLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 477 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF-GIVPLSKPE-EKQKaaqQFSKLQAAMK 554
Cdd:cd14886 159 GKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLnASKCYDAPGiDDQK---EFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 555 VLaISPEEQKTCWLILASIYHLG--------AAGATKAGRkqFARHEWAQKAAYLLGCSLEELSSAIfkhqlkggtLQRS 626
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGniefseegDMGVINAAK--ISNDEDFGKMCELLGIESSKAAQAI---------ITKV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 627 TSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFE 706
Cdd:cd14886 304 VVINNETIISPV---TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN------TYE 374
|
410 420 430
....*....|....*....|....*....|...
gi 1907082237 707 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIE 739
Cdd:cd14886 375 QLLINYANERLQQYFINQVFKSEIQEYEIEGID 407
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
324-758 |
1.73e-28 |
|
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: 124.25 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF-------KGCRREDMAPHIYAVAQTAYRAMLMSRQD 395
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPyKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 396 QSIVLLGSSGSGKTTSFQHLVQYLATIAGTSgTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQ----- 470
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTDS-QMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 471 ----AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLL-ACGDATLRT-----ELHLNHLAENNVFGIVPLSK----- 535
Cdd:cd14884 161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLrGLSDEDLARrnlvrNCGVYGLLNPDESHQKRSVKgtlrl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 536 --------PEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGaagatkagrkqfarhEWAQKAAyllgCSLE 607
Cdd:cd14884 241 gsdsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLG---------------NRAYKAA----AECL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 608 ELSSAIFKHQLKGGTLQ-RSTSFRQgpeesglgEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSM--- 683
Cdd:cd14884 302 QIEEEDLENVIKYKNIRvSHEVIRT--------ERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDned 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 684 ---------MIVDTPGFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIeLAFDDLEPVADDSVA 754
Cdd:cd14884 374 iysineaiiSILDIYGFE------ELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCSDVAPSYSDTLI 446
|
....
gi 1907082237 755 AVDQ 758
Cdd:cd14884 447 FIAK 450
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1143-1874 |
3.19e-28 |
|
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: 124.90 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1143 IQVQLSE--EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldaetAERLRTEK 1220
Cdd:pfam01576 227 LQAQIAElrAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESER--------------AARNKAEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1221 EMKELQTQYDALKkqmevmemevmearliraAEINGEVDDDDAGGEWRLKYERAVREVdftKKRLQQELEDKMEVEQQSR 1300
Cdd:pfam01576 293 QRRDLGEELEALK------------------TELEDTLDTTAAQQELRSKREQEVTEL---KKALEEETRSHEAQLQEMR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1301 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKL 1380
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1381 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGS 1460
Cdd:pfam01576 432 AEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1461 IQMLEQAKLRLEMEMERMRQtHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLS-DQV 1539
Cdd:pfam01576 512 KRNVERQLSTLQAQLSDMKK-KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvDLD 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1540 NQRDFES--EKRLRK---DLKRTKALLADAQIMLDHLKNNAPSKREIA-QLKNQLEESEFTCAAAVKARKAMEVEMEDLH 1613
Cdd:pfam01576 591 HQRQLVSnlEKKQKKfdqMLAEEKAISARYAEERDRAEAEAREKETRAlSLARALEEALEAKEELERTNKQLRAEMEDLV 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1614 LQIDDIAK-------AKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDmaqmndLQAQIEESnkek 1686
Cdd:pfam01576 671 SSKDDVGKnvhelerSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERD------LQARDEQG---- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1687 qelQEKLQALQSQVefleqsmvdkslvsrqeakiRELETRLEFEKTQvkRLENLASRLKETMEKLTEERDQRAAAENREK 1766
Cdd:pfam01576 741 ---EEKRRQLVKQV--------------------RELEAELEDERKQ--RAQAVAAKKKLELDLKELEAQIDAANKGREE 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1767 --EQNKRLQRQLRDTKEEMSE--LARKEAEASRKkhELEMDLESLEAANQSLQADLKLAFKrigdlqAAIEDEMESDENE 1842
Cdd:pfam01576 796 avKQLKKLQAQMKDLQRELEEarASRDEILAQSK--ESEKKLKNLEAELLQLQEDLAASER------ARRQAQQERDELA 867
|
730 740 750
....*....|....*....|....*....|...
gi 1907082237 1843 DLINSLQDMVTKYQKKKNKLEGD-SDVDSELED 1874
Cdd:pfam01576 868 DEIASGASGKSALQDEKRRLEARiAQLEEELEE 900
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
325-945 |
2.22e-27 |
|
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: 120.48 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 325 VLHTLRQRYGASLLHTYAGPSLLVLST---------------RGAPAVysekvmhmfkgcrrEDMAPHIYAVAQTAYRAM 389
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirkyRDAPDL--------------TKLPPHVFYTARRALENL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 390 LMSRQDQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTKVFSVEKW-QALSTLLEAFGNSPTIMNGSATRFSQILSLDF 468
Cdd:cd14876 69 HGVNKSQTIIVSGESGAGKTEATKQIMRYFA--SAKSGNMDLRIQTAiMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 469 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENN--------VFGIVPLskpeekq 540
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKflnpkcldVPGIDDV------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 541 kaaQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG---AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQ 617
Cdd:cd14876 220 ---ADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGnvkITGKTEQGVDDAAAISNESLEVFKEACSLLFLDPEALKRE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 618 L------KGGtlQRSTSFRQGPEesglGEGTKLSaleclegMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGF 691
Cdd:cd14876 297 LtvkvtkAGG--QEIEGRWTKDD----AEMLKLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 692 ---QNpewggsargASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDLEPVAD------DSVAAV--D 757
Cdd:cd14876 364 evfKN---------NSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIptaELEYTSNAEVIDvlcgkgKSVLSIleD 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 758 QAshlvrsLAhadeargllwlleeealvPGATEDALLDRLFSyygpQEGDKKGQSPLLRSSKpRHFLLGHSHGTnwVEYN 837
Cdd:cd14876 435 QC------LA------------------PGGSDEKFVSACVS----KLKSNGKFKPAKVDSN-INFIVVHTIGD--IQYN 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 838 VAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGragsATVLSGSIA-GLEGGSQLalrratsMRktfttgmaavkkks 916
Cdd:cd14876 484 AEGFLFKNK-DVLRAELVEVVQASTNPVVKALFEG----VVVEKGKIAkGSLIGSQF-------LK-------------- 537
|
650 660
....*....|....*....|....*....
gi 1907082237 917 lciqiklQVDALIDTIKRSKMHFVHCFLP 945
Cdd:cd14876 538 -------QLESLMGLINSTEPHFIRCIKP 559
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
323-1026 |
2.14e-26 |
|
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: 117.28 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVmhmFKGCrredmapHIYAVAQTAYRAML-MSRQDQSIVLL 401
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLV---IKKC-------HISGVAENALDRIKsMSSNAESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 402 GSSGSGKTTSFQHLVQYLATIAGTSGTKVFSvekwQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 481
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHS----SAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 482 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLaeNNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 561
Cdd:cd14874 147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 562 EQKTCWLILASIYHLGAAgATKAGRKQFARHE-----------WaqkAAYLLGCSLEELSSAIFKHQLKGGTLQRStsfr 630
Cdd:cd14874 225 HCISIYKIISTILHIGNI-YFRTKRNPNVEQDvveignmsevkW---VAFLLEVDFDQLVNFLLPKSEDGTTIDLN---- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 631 qgpeesglgegtklSALECLEGMASGLYSELFTLLISLVNRALKSSQHSlCSMMIVDTPGFQNPEWGGsargasFEELCH 710
Cdd:cd14874 297 --------------AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHT-GVISILDHYGFEKYNNNG------VEEFLI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 711 NYAQDRLQRLFHERTFLQELERYKEDNIELafddlepvaDDSVAAVDQASHLVRSLAHADEarGLLWLLEEEALVPGATE 790
Cdd:cd14874 356 NSVNERIENLFVKHSFHDQLVDYAKDGISV---------DYKVPNSIENGKTVELLFKKPY--GLLPLLTDECKFPKGSH 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 791 DALLDRL------FSYYGPQegdkkgqspllRSSKPRHFLLGHSHGTNWveYNVAGWLNYTKQNpATQNAPRLLQDSQKK 864
Cdd:cd14874 425 ESYLEHCnlnhtdRSSYGKA-----------RNKERLEFGVRHCIGTTW--YNVTDFFSRNKRI-ISLSAVQLLRSSKNP 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 865 IISNLFLGRAGSATVLSGSIAgleggsQLALRRATSmrktfttgmaavkkkslciqiklqvdaLIDTIKRSKMHFVHCFL 944
Cdd:cd14874 491 IIGLLFESYSSNTSDMIVSQA------QFILRGAQE---------------------------IADKINGSHAHFVRCIK 537
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 945 PVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1024
Cdd:cd14874 538 SNNERQPK-----------------------------KFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
..
gi 1907082237 1025 AP 1026
Cdd:cd14874 589 LP 590
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1149-1811 |
3.17e-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: 118.24 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1149 EEQIRNKDEEIQQLRSKLEKVEKERNELR-----LSSD--RLETRISELTSELTDERNTGESASQLLDAETAERLRTEKE 1221
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQkelyaLANEisRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1222 MKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQeLEDKMEVEQQSRR 1301
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-LEARLERLEDRRE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1302 QLERRLGDLQADSDESQRALQQLKkkCQRLTAELQDTKLHLEGQQVR----NHELEKKQRRFDSELSQAHEETQR----E 1373
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEAleelREELEEAEQALDAAERELAQLQARldslE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1374 KLQR--EKLQREKDMLLAEAF-------SLKQQME-----EKDLDIA--GFTQKVV--SLEAELQDISSQESKDE---AS 1432
Cdd:TIGR02168 496 RLQEnlEGFSEGVKALLKNQSglsgilgVLSELISvdegyEAAIEAAlgGRLQAVVveNLNAAKKAIAFLKQNELgrvTF 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1433 LAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERM--------------RQTHSKEMESR--------- 1489
Cdd:TIGR02168 576 LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddldnalELAKKLRPGYRivtldgdlv 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1490 ---------DEEVEEARQSCQKKLKQMEVQ---LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL---RKDL 1554
Cdd:TIGR02168 656 rpggvitggSAKTNSSILERRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1555 KRTKALLADAQIMLDHL-KNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1633
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLsKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1634 QREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSL 1712
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALlRSE 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1713 VSRQEAKIRELETRlefektqVKRLENLasrLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARK--- 1789
Cdd:TIGR02168 896 LEELSEELRELESK-------RSELRRE---LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKied 965
|
730 740
....*....|....*....|...
gi 1907082237 1790 -EAEASRKKHELEMDLESLEAAN 1811
Cdd:TIGR02168 966 dEEEARRRLKRLENKIKELGPVN 988
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1147-1851 |
8.03e-26 |
|
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: 117.09 E-value: 8.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1147 LSEEqiRNKDEEIQQLRSKLEKVE------------KERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAE 1214
Cdd:TIGR02169 203 LRRE--REKAERYQALLKEKREYEgyellkekealeRQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1215 -RLRTEKEMKELQTQYDALKKQMEVMEMEVMEA--RLIRAAE--INGEVDDDDAGGEWRlKYERAVREVDFTKKRLQQEL 1289
Cdd:TIGR02169 281 iKDLGEEEQLRVKEKIGELEAEIASLERSIAEKerELEDAEErlAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1290 EDKmeveQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhLEGQQVRnheLEKKQRRFDSELSQAHEE 1369
Cdd:TIGR02169 360 AEL----KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE----LKRELDR---LQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1370 TQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKV-- 1447
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVrg 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1448 -KDQEEELD------------------------EQAGS-----------------IQMLEQAKL-RLE-MEMERMRQTHS 1483
Cdd:TIGR02169 509 gRAVEEVLKasiqgvhgtvaqlgsvgeryataiEVAAGnrlnnvvveddavakeaIELLKRRKAgRATfLPLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1484 -KEMESRD------------------------------EEVEEAR----------------------------------- 1497
Cdd:TIGR02169 589 dLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvvEDIEAARrlmgkyrmvtlegelfeksgamtggsraprggilf 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1498 --------QSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEkRLRKDLKRTKALLADAQIMLD 1569
Cdd:TIGR02169 669 srsepaelQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLS 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1570 HLKNN-APSKREIAQLKNQLEESEftcAAAVKARKAME-VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEED 1647
Cdd:TIGR02169 748 SLEQEiENVKSELKELEARIEELE---EDLHKLEEALNdLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1648 QEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETR 1726
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlKKERDELEAQLRELERK 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1727 LEFEKTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRDTKEEMSELARKEAEASRKKhELEMDLES 1806
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEAL--------------EEELSEIEDPKGEDEEIPEEELSLEDVQAELQ-RVEEEIRA 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1907082237 1807 LEAANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINSLQDM 1851
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKlEEERKAILERIEEYEKK 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1147-1842 |
1.04e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 113.70 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1147 LSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRL--ETRISELTSELTDERNTgESASQLLDAETAERLRTEKEMKE 1224
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaeDARKAEEARKAEDAKRV-EIARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1225 LQTQYDALKKQMEVMEMEVMEARLIRAAEingevddddaggewRLKYERAVREVdftkkrlqQELEDKMEVEQqSRRQLE 1304
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAAR--------------KAEEERKAEEA--------RKAEDAKKAEA-VKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1305 RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK--QRRFDSELSQAHEETQREKLQREKLQR 1382
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1383 EKdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-AKVKDQEEELDEQAGSI 1461
Cdd:PTZ00121 1315 KK----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1462 QMLEQAKLRLEMEMERMRQTHSKEMESRdeEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQ 1541
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1542 RDFESEKRLRKDLKR----TKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCA-AAVKARKAMEVEMEDLHLQI 1616
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKkadeAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkKAEEAKKADEAKKAEEKKKA 1548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1617 DDIAKA---KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL 1693
Cdd:PTZ00121 1549 DELKKAeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1694 QALQSQVEFLEQSMVDKslvSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQ 1773
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1774 R-------------QLRDTKEE----MSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEM 1836
Cdd:PTZ00121 1706 ElkkkeaeekkkaeELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
....*.
gi 1907082237 1837 ESDENE 1842
Cdd:PTZ00121 1786 DEEDEK 1791
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1286-1862 |
1.14e-24 |
|
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: 112.42 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1286 QQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQR--RFDSEL 1363
Cdd:TIGR04523 35 EKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN---------DKLKKNKDKinKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1364 SQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKdeaslakVKKQLRDL 1443
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELN-------KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1444 EAKVKDQEEELDEQAGSIQMLEQAKLRLEMEM---ERMRQTHsKEMESRDEEVEEARQSCQKKLKQmevqLEEEYEDKQK 1520
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKN-KSLESQISELKKQNNQLKDNIEK----KQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1521 ALREKrelESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESeftCAAAVK 1600
Cdd:TIGR04523 247 EISNT---QTQLNQLKDE-QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS------EISDLNNQKEQD---WNKELK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1601 AR-KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKN-------EIQNRLEEDQEDMnELMKKHKAAVAQASRDM-AQ 1671
Cdd:TIGR04523 314 SElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTnsesensEKQRELEEKQNEI-EKLKKENQSYKQEIKNLeSQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1672 MNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQ--------------EAKIRELETRLEFEKTQVKR 1736
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlKETIIKNnseikdltnqdsvkELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1737 LENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQA 1816
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1817 DLKLAF--KRIGDLQAAIEdEMEsDENEDLINS---LQDMVTKYQKKKNKL 1862
Cdd:TIGR04523 553 ELKKENleKEIDEKNKEIE-ELK-QTQKSLKKKqeeKQELIDQKEKEKKDL 601
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1144-1789 |
6.78e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 110.92 E-value: 6.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1144 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLD----AETAERL-RT 1218
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelKELQAELeEL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1219 EKEMKELQTQYDALKKQMEVMEMEVMEARLIR------AAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRL---QQEL 1289
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALdaaereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgiLGVL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1290 EDKMEVEQQSRRQLERRLG-DLQA----DSDESQRALQQLKK--------------KCQRLTAELQDTKLHLEGQQVRNH 1350
Cdd:TIGR02168 526 SELISVDEGYEAAIEAALGgRLQAvvveNLNAAKKAIAFLKQnelgrvtflpldsiKGTEIQGNDREILKNIEGFLGVAK 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1351 ELEKKQRRFDSELS------------QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAE 1418
Cdd:TIGR02168 606 DLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEK 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1419 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERmrqtHSKEMESRDEEVEEArq 1498
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTEL-- 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1499 scQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSK 1578
Cdd:TIGR02168 760 --EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1579 -REIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1657
Cdd:TIGR02168 837 eRRLEDLEEQIEELS-------EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1658 HKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQsQVEFleqsMVDKSLVSRQEAKIRELETRLEFEKTQVKRL 1737
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY-SLTL----EEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1738 E--NLASrlketMEKLTEERdQRAAAENREKEQNKRLQRQLRDTKEEMSELARK 1789
Cdd:TIGR02168 985 GpvNLAA-----IEEYEELK-ERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1144-1773 |
2.52e-23 |
|
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: 108.18 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1144 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMK 1223
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1224 ELQTQYDALKKQMEVMEMEVMEARLIRAaEINgevddddaggewrlKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQL 1303
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKSLES-QIS--------------ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1304 E----------RRLGDLQADSDESQRALQQLKKKCQRLTAELQDtkLHLEGQQVRNHEL-------EKKQRRFDSELSQA 1366
Cdd:TIGR04523 256 NqlkdeqnkikKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELkselknqEKKLEEIQNQISQN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1367 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAK 1446
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEK--------------QNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1447 VKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHS------KEMESRDEEVEEARQSCQKKLKQMEVQLEE---EYED 1517
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVlsrSINK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1518 KQKALREK-RELESKLSTLsDQVNQRDFESEKRLrKDLKRTKALLADAQIMLDHLKNNApsKREIAQLKNQLEESEFTca 1596
Cdd:TIGR04523 480 IKQNLEQKqKELKSKEKEL-KKLNEEKKELEEKV-KDLTKKISSLKEKIEKLESEKKEK--ESKISDLEDELNKDDFE-- 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1597 aavkarkamevemedlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQ 1676
Cdd:TIGR04523 554 -----------------LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1677 AQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA--KIRELETRL-EFEKTQVKRLENLASRLKET 1747
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVkqiketIKEIRNKWPEIikKIKESKTKIdDIIELMKDWLKELSLHYKKY 696
|
650 660
....*....|....*....|....*...
gi 1907082237 1748 MEKLTEERDQRAAAENRE--KEQNKRLQ 1773
Cdd:TIGR04523 697 ITRMIRIKDLPKLEEKYKeiEKELKKLD 724
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
323-738 |
3.24e-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: 107.41 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 323 SSVLHTLRQRYGASLLHTYAGPSLLVLStrgaPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISIN----PYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLatIAGTSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 482
Cdd:cd14937 77 ESGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDS-NFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 483 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISpEE 562
Cdd:cd14937 154 LLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIR--SENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMH-DM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 563 QKTCWLILASIYHLGAA---GATKAGRKQFAR-----HEWAQKAAYLLGCSLEELSSAIfkhqlkggTLQRSTSFRQGPE 634
Cdd:cd14937 231 KDDLFLTLSGLLLLGNVeyqEIEKGGKTNCSEldknnLELVNEISNLLGINYENLKDCL--------VFTEKTIANQKIE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 635 esglgegTKLSALECL---EGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQnpewggSARGASFEELCHN 711
Cdd:cd14937 303 -------IPLSVEESVsicKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFE------IFSKNSLEQLLIN 369
|
410 420
....*....|....*....|....*..
gi 1907082237 712 YAQDRLQRLFHERTFLQELERYKEDNI 738
Cdd:cd14937 370 IANEEIHSIYLYIVYEKETELYKAEDI 396
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1073-1758 |
1.29e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.56 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1073 LARLEEQRdEQTSRHLTLfQAACRGYLARQHFKKRKIQDLAIRCVQKNIKKNKgvkdwpwwklfttvrplIQVQLSEEQI 1152
Cdd:COG1196 202 LEPLERQA-EKAERYREL-KEELKELEAELLLLKLRELEAELEELEAELEELE-----------------AELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1153 RNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDAL 1232
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1233 KKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREvdftkkrlQQELEDKMEVEQQSRRQLERRLGDLQA 1312
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE--------LLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1313 DSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAF 1392
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1393 SLKQQMEEKDLDIAGftqkvvSLEAELQDISSQESKDEASLAKVKKQLRD-----LEAKVKDQEEELDEQAGS-IQMLEQ 1466
Cdd:COG1196 495 LLLEAEADYEGFLEG------VKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaaLAAALQNIVVEDDEVAAAaIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1467 AKL--RLEMEMERMRQTHSKEMESRDEEVEEARqscqkklkqmevqLEEEYEDKQKALREKRELESKLSTLSDQvnqrdf 1544
Cdd:COG1196 569 AKAgrATFLPLDKIRARAALAAALARGAIGAAV-------------DLVASDLREADARYYVLGDTLLGRTLVA------ 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1545 eseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaaVKARKAMEVEMEDLHLQIDDIAKAKT 1624
Cdd:COG1196 630 ---ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL------LEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1625 ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLE 1704
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1705 QsmVDksLVSRQEAKirELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQR 1758
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 ... |
1265-1833 |
1.95e-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: 106.03 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1265 GEWRLKYERAVREVDFTKKRLQQELE-----DKMEVEQQSRRQ-LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDT 1338
Cdd:pfam01576 29 KELEKKHQQLCEEKNALQEQLQAETElcaeaEEMRARLAARKQeLEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1339 KLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMllaeafslkqqmeekdldiagftqkvvsLEAE 1418
Cdd:pfam01576 109 EEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL----------------------------LEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1419 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSkEMESRDEEVEEARQ 1498
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA-ELQAQIAELRAQLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1499 SCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLsdqvnQRDFESEKRLRKDLKRTK-----ALLADAQIMLDHLKN 1573
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISEL-----QEDLESERAARNKAEKQRrdlgeELEALKTELEDTLDT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1574 NAP-----SKR--EIAQLKNQLEESEFTCAAAVKA-RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLE 1645
Cdd:pfam01576 315 TAAqqelrSKReqEVTELKKALEEETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1646 EDQEDMNELMKKHKAAvaqasrdMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLeqsmvdKSLVSRQEAKIRELEt 1725
Cdd:pfam01576 395 TLQQAKQDSEHKRKKL-------EGQLQELQARLSESERQRAELAEKLSKLQSELESV------SSLLNEAEGKNIKLS- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1726 rlefektqvKRLENLASRLKETMEKLTEERDQRAAAENR----EKEQNKrLQRQLRDTKE-------EMSELARKEAEAS 1794
Cdd:pfam01576 461 ---------KDVSSLESQLQDTQELLQEETRQKLNLSTRlrqlEDERNS-LQEQLEEEEEakrnverQLSTLQAQLSDMK 530
|
570 580 590
....*....|....*....|....*....|....*....
gi 1907082237 1795 RKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1833
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1069-1858 |
2.38e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 105.99 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1069 RAGTLARLEEQRDEQTSRHLTLF---QAACRGYLARQHFKKRKIQDlAIRCVQ----KNIKKNKGVKDWPWWKLFTTVRP 1141
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIArkaEDARKAEEARKAEDAKKAEA-ARKAEEvrkaEELRKAEDARKAEAARKAEEERK 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1142 LIQVQLSEEQIR----NKDEEIQQLRSKLEKVEKERNE---LRLSSDRLETRISELTSELTDERNTGESASQLLDAETAE 1214
Cdd:PTZ00121 1214 AEEARKAEDAKKaeavKKAEEAKKDAEEAKKAEEERNNeeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1215 RLRTEKEMKELqtqyDALKKQMEVMEMEVMEARliRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKME 1294
Cdd:PTZ00121 1294 EAKKAEEKKKA----DEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1295 VEQQSRRQLERRLGDLQADSDESQRAlQQLKKKCQrltaelQDTKlhlEGQQVRNHELEKKQRrfdSELSQAHEETQREK 1374
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAE------EDKK---KADELKKAAAAKKKA---DEAKKKAEEKKKAD 1434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1375 LQREKLQREKdmllaEAFSLKQQMEEKDldiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEEL 1454
Cdd:PTZ00121 1435 EAKKKAEEAK-----KADEAKKKAEEAK-------------KAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEA 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1455 DEQAGSIQMLEQAKLRLEmEMERMRQTHSKEMESRDEE---VEEARQSCQKKlKQMEVQLEEEY---EDKQKALREKREL 1528
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEakkADEAKKAEEKK-KADELKKAEELkkaEEKKKAEEAKKAE 1573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1529 ESKLSTL-----SDQVNQRDFESEKRLRKDLKRTKALLA----DAQIMLDHLKNNAPSKREIAQLKNQLEES-------- 1591
Cdd:PTZ00121 1574 EDKNMALrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaeelk 1653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1592 ----EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTalEEQLSRLQREK---NEIQNRLEEDQEDMNELMKKHKAAVAQ 1664
Cdd:PTZ00121 1654 kaeeENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--AEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1665 ASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLAS-- 1742
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANii 1811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1743 --------RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSL 1814
Cdd:PTZ00121 1812 eggkegnlVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1907082237 1815 QADLKlafkrigDLQAAIEDEMESDENEDLINSLQDmVTKYQKK 1858
Cdd:PTZ00121 1892 KIDKD-------DIEREIPNNNMAGKNNDIIDDKLD-KDEYIKR 1927
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1249-1863 |
5.48e-22 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 103.99 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1249 IRAAEINGEVDDDDA---------GGEwrlKYERA-------VREVDFTKKRLQQELEDKMEVEQQSRRQlERRLGDLQA 1312
Cdd:PRK03918 132 IRQGEIDAILESDESrekvvrqilGLD---DYENAyknlgevIKEIKRRIERLEKFIKRTENIEELIKEK-EKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1313 DSDESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRRFDSELSQAhEETQREKLQREKLQREKDMLLA 1389
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIREL-EERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1390 EAfslkQQMEEKDLDIAGFTQKVVSleaELQDISSQESKDEASLAKVKKQLRDLE---AKVKDQEEELDEQAGSIQMLEQ 1466
Cdd:PRK03918 287 EL----KEKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1467 AKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQrdFES 1546
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKL----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE--LKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1547 EKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQidDIAKAKTAL 1626
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR---KELRELEKVLKKESELIKLK--ELAEQLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1627 EEQLSRLQREKNEiqnRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS 1706
Cdd:PRK03918 509 EEKLKKYNLEELE---KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1707 MVDKSlvsrqEAKIRELET---RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEM 1783
Cdd:PRK03918 586 SVEEL-----EERLKELEPfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1784 SElarkeaEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED----EMESDENEDLINSLQDMVTKYQKKK 1859
Cdd:PRK03918 661 YE------ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEErekaKKELEKLEKALERVEELREKVKKYK 734
|
....
gi 1907082237 1860 NKLE 1863
Cdd:PRK03918 735 ALLK 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1270-1792 |
6.17e-22 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 103.99 E-value: 6.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1270 KYERAVREVDFTKKRLQqELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN 1349
Cdd:PRK03918 225 KLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1350 HELEKKQR--RFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFtQKVVSLEAELQDISSQES 1427
Cdd:PRK03918 304 EYLDELREieKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1428 kdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSK----EMESRDEEVEEARQSCQKK 1503
Cdd:PRK03918 383 --GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1504 LKQMEVQLEEEYEDKQKALREKRELESKLstlsdqvnqrdfESEKRLRKDLKrtkalladaqiMLDHLKN--NAPSKREI 1581
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVL------------KKESELIKLKE-----------LAEQLKEleEKLKKYNL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1582 AQLKNQLEESEFTCAAAVKARKAMEVEMEDLHlQIDDIAKAKTALEEQLSRLQREKNEIQNRL--------EEDQEDMNE 1653
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1654 LMKKH------KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLvSRQEAKIRELETRL 1727
Cdd:PRK03918 597 LEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY-EELREEYLELSREL 675
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1728 EFEKTQVKRLENLASRLKETMEKLTEERDQRAAAE------NREKEQNKRLQRQLRDTKEEMSELARKEAE 1792
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKkeleklEKALERVEELREKVKKYKALLKERALSKVG 746
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1150-1808 |
6.38e-21 |
|
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: 100.48 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1150 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESasqlLDAET---AERLRTEKEMK-EL 1225
Cdd:TIGR04523 47 NELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK----LNSDLskiNSEIKNDKEQKnKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1226 QTQYDALKKQMEVMEMEVmearliraAEINGEV-DDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ------Q 1298
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNI--------DKFLTEIkKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKnidkikN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1299 SRRQLERRLGDLQAdsdesqralqqLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFdSELSQAHEETQrEKLQRE 1378
Cdd:TIGR04523 195 KLLKLELLLSNLKK-----------KIQKNKSLESQISELK---KQNNQLKDNIEKKQQEI-NEKTTEISNTQ-TQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1379 KLQREKDmllaeafslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKVKDQEEE 1453
Cdd:TIGR04523 259 KDEQNKI---------KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1454 LDEQAGSIQMLEQAKLRLEMEmermRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLS 1533
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1534 TLSDQVNQRD-----FESEKRLRkdLKRTKALLADaqimldhlknNAPSKREIAQLKNQLEESEftcaaavkarkameve 1608
Cdd:TIGR04523 402 NQEKLNQQKDeqikkLQQEKELL--EKEIERLKET----------IIKNNSEIKDLTNQDSVKE---------------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1609 medlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASrdmaqmnDLQAQIEESNKEKQE 1688
Cdd:TIGR04523 454 -----LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK-------ELEEKVKDLTKKISS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1689 LQEKLQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFE--KTQVKRLENLASRLKETMEKLTEERDQ-RAAAENRE 1765
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDL------EDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEkQELIDQKE 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082237 1766 KEQNK-------------RLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLE 1808
Cdd:TIGR04523 596 KEKKDlikeieekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1416-1874 |
7.19e-21 |
|
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: 100.63 E-value: 7.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1416 EAELQDISSQESKDEASLAKVKKQLRDLEAKVkdqeEELDEQAGSIQMLEQAKLRLEMEMERMRQTHS----------KE 1485
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKH----QQLCEEKNALQEQLQAETELCAEAEEMRARLAarkqeleeilHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1486 MESRDEEVEEARQSCQ---KKLKQ----MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTK 1558
Cdd:pfam01576 80 LESRLEEEEERSQQLQnekKKMQQhiqdLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLE-DQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1559 ALLADAQI----------MLDHLKNNAPSKreIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE 1628
Cdd:pfam01576 159 ERISEFTSnlaeeeekakSLSKLKNKHEAM--ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1629 QLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVE-FLEQSM 1707
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1708 VDKSLVSRQEAKIRELETRLEFE-KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSEL 1786
Cdd:pfam01576 317 AQQELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1787 ARKEAEASRKKHELEMDLESLEA-ANQSLQADLKLAfKRIGDLQAAIEdemesdenedlinSLQDMVTKYQKKKNKLEGD 1865
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQArLSESERQRAELA-EKLSKLQSELE-------------SVSSLLNEAEGKNIKLSKD 462
|
490
....*....|
gi 1907082237 1866 -SDVDSELED 1874
Cdd:pfam01576 463 vSSLESQLQD 472
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
324-765 |
1.10e-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: 99.40 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 402
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPlRYLPFLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 403 SSGSGKTTSFQHLVQYLAT--IAGTSGTKVFSVEKwqalSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQ 480
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTtdLSRSKYLRDYILES----GIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 481 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL---NHLAENNVFGIVPLSKPEEKqkaaQQFSKLQAAMKVLA 557
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLgdiNSYHYLNQGGSISVESIDDN----RVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 558 ISPEEQKTCWLILASIYHLGAAG-ATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKhqlkggtlQRSTSFRQgpees 636
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTfFQKNGKTEVKDRTLIESLSHNITFDSTKLENILIS--------DRSMPVNE----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 637 glgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLcSMMIVDTPGFQNPEWGGsargasFEELCHNYAQDR 716
Cdd:cd14905 299 ---------AVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNG------YEQFSINFLEER 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082237 717 LQRLFHERTFLQELERYKEDNI----ELAFDDLE---PVADDSVAAVDQASHLVRS 765
Cdd:cd14905 363 LQQIYLQTVLKQEQREYQTERIpwmtPISFKDNEesvEMMEKIINLLDQESKNINS 418
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1142-1782 |
1.67e-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: 99.66 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1142 LIQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLE-----TRISELTSELTDERNTGESASQLLDAETAERl 1216
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1217 rtekeMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgeWRLKYERAVREVDFTKKrLQQELEDKMEVE 1296
Cdd:TIGR00618 324 -----AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS--IREISCQQHTLTQHIHT-LQQQKTTLTQKL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1297 QQSRRQLE--RRLGDLQADSDESQRALQQlkkkcqrltaelqdTKLHLEGQQVRNHELEKKQRRFDSElsQAHEETQREK 1374
Cdd:TIGR00618 396 QSLCKELDilQREQATIDTRTSAFRDLQG--------------QLAHAKKQQELQQRYAELCAAAITC--TAQCEKLEKI 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1375 LQREKLQ--REKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISS---QESKDEASLAKVKKQLRDLEAKVKD 1449
Cdd:TIGR00618 460 HLQESAQslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnPARQDIDNPGPLTRRMQRGEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1450 QEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRD---EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR 1526
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNrskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1527 ELESKLSTLSDQVNQRDFESEKRLRK-DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAM 1605
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1606 EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKE 1685
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1686 KQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQvKRLENLASRLKETMEKLTEERDQRAAAENRE 1765
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-QEEEQFLSRLEEKSATLGEITHQLLKYEECS 858
|
650
....*....|....*..
gi 1907082237 1766 KEQNKRLQRQLRDTKEE 1782
Cdd:TIGR00618 859 KQLAQLTQEQAKIIQLS 875
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1140-1896 |
1.91e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 99.28 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1140 RPLIQVQLSEEQIRNKDEEIQqlRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTE 1219
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELK--LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1220 KEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQS 1299
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1300 RRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREK 1379
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1380 LQREKDMLLAEAFSL--KQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1457
Cdd:pfam02463 414 ARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1458 AG-SIQMLEQ------AKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELES 1530
Cdd:pfam02463 494 KLeERSQKESkarsglKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1531 KLStlSDQVNQRDFESEKRLRKDLK------RTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaavKARKA 1604
Cdd:pfam02463 574 PLG--ARKLRLLIPKLKLPLKSIAVleidpiLNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKE-------SAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1605 MEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNK 1684
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1685 EKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENR 1764
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1765 E--KEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENE 1842
Cdd:pfam02463 805 AleEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKL 884
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082237 1843 DLINS---------LQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDD 1896
Cdd:pfam02463 885 KDELEskeekekeeKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADE 947
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1148-1854 |
9.81e-20 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 96.63 E-value: 9.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1148 SEEQIRNKDEEIQQLRSKL----EKVEKERNELRLSSDRLETR---ISELTSELTDERNTGESASQLLDAETAERLRTEK 1220
Cdd:TIGR04523 73 SNNKIKILEQQIKDLNDKLkknkDKINKLNSDLSKINSEIKNDkeqKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1221 EMKELQTQYDALKKQmevmemevmearliraaeingevddddaggewrlkyeraVREVDFTKKRLQQELEDKMEVEQQSR 1300
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQ---------------------------------------KEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1301 RQLERrlgdlqadsdeSQRALQQLKKKCQRLTaELQDTKLHLEGQQ-VRNHELEKKQRRFdSELSQAHEETQrEKLQREK 1379
Cdd:TIGR04523 194 NKLLK-----------LELLLSNLKKKIQKNK-SLESQISELKKQNnQLKDNIEKKQQEI-NEKTTEISNTQ-TQLNQLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1380 LQREKDmllaeafslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKVKDQEEEL 1454
Cdd:TIGR04523 260 DEQNKI---------KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQNQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1455 DEQAGSIQMLEQAKLRLEMEmermRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLST 1534
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1535 LSDQVNQRD-----FESEKRLRkdLKRTKALLADaqimldhlknNAPSKREIAQLKNQLEESEftcaaavkarkamevem 1609
Cdd:TIGR04523 403 QEKLNQQKDeqikkLQQEKELL--EKEIERLKET----------IIKNNSEIKDLTNQDSVKE----------------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1610 edlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKKHKaavaqasrdmaqmndlqaQIEESNKEKQEL 1689
Cdd:TIGR04523 454 ----LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK---ELKSKEK------------------ELKKLNEEKKEL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1690 QEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKTQVKRlenlaSRLKETMEKLTEERDQRAAAENREKEQ 1768
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKlESEKKEKESKISDLEDELNKDDFELKK-----ENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1769 NKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQ---SLQADLKLAFKRIGDLQAAIEDEMESDENE--D 1843
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEklsSIIKNIKSKKNKLKQEVKQIKETIKEIRNKwpE 663
|
730
....*....|.
gi 1907082237 1844 LINSLQDMVTK 1854
Cdd:TIGR04523 664 IIKKIKESKTK 674
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
354-472 |
1.26e-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: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 354 APAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTK---- 429
Cdd:cd01363 11 LPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgete 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907082237 430 ---------VFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 472
Cdd:cd01363 91 gwvylteitVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1149-1859 |
2.57e-19 |
|
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: 95.17 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1149 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSE---LTDERNTGESASQLLD---AETAERL-RTEKE 1221
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdLIKENNATRHLCNLLKetcARSAEKTkKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1222 MKELQTQYDALKKQMEvmemevmeaRLIRAAEiNGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKmevEQQSRR 1301
Cdd:pfam05483 178 REETRQVYMDLNNNIE---------KMILAFE-ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK---EKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1302 QL------ERRLGDLQADSDESQRALQQLKKKcqrltAELQDTKLHlegqqvrnhELEKKQRRFDSELSQAHEETQREKL 1375
Cdd:pfam05483 245 LLiqitekENKMKDLTFLLEESRDKANQLEEK-----TKLQDENLK---------ELIEKKDHLTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1376 QREKLQREKDMLLAEAFSLKQ----QMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1451
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEekeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1452 EELDEQAG-----SIQMLEQAKLRLEMEM----ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKAL 1522
Cdd:pfam05483 391 SELEEMTKfknnkEVELEELKKILAEDEKlldeKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1523 REKRELESKLstlsdqvnqrdfESEKrlrkdLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaaVKAR 1602
Cdd:pfam05483 471 KEVEDLKTEL------------EKEK-----LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED--------IINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1603 KAMEvemEDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQ 1678
Cdd:pfam05483 526 KKQE---ERMLKQIENLEEKEMNLRDELESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1679 IEESNKEKQELQEKLQALQsqveflEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKE----TMEKLTEE 1754
Cdd:pfam05483 603 IENKNKNIEELHQENKALK------KKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEdkkiSEEKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1755 RDQRAA----AENREKEQNKRLQRQLRD---------------TKEEMSELA---RKEAEASRKKHELEMDLESLEAANQ 1812
Cdd:pfam05483 677 VEKAKAiadeAVKLQKEIDKRCQHKIAEmvalmekhkhqydkiIEERDSELGlykNKEQEQSSAKAALEIELSNIKAELL 756
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1907082237 1813 SLQADLklafkrigdlqaaiedEMESDENEDLINSLQDMVTKYQKKK 1859
Cdd:pfam05483 757 SLKKQL----------------EIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1149-1876 |
2.63e-19 |
|
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: 95.57 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1149 EEQIRNKDEEIQQLRSKL----EKVEKERNELRLSSDRLETRISELTSE---LTDERNTgESASQ----------LLDAE 1211
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLnesnELHEKQKFYLRQSVIDLQTKLQEMQMErdaMADIRRR-ESQSQedlrnqlqntVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1212 TAERLRtEKEMKELQTQYDALKKQMEVMEMEVMEARLIRaaeingeVDDDDAGGEWRLKYERA----VREVDFTKKRLQQ 1287
Cdd:pfam15921 156 AAKCLK-EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL-------VDFEEASGKKIYEHDSMstmhFRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1288 ELEDKMEVEQQSRRQLERRLGDLQADS-DESQRALQQLKKKCQRLTAE--LQDTKLHLEGQQVRNhELEKKQRRFDSELS 1364
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSESqNKIELLLQQHQDRIEQLISEheVEITGLTEKASSARS-QANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1365 QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE 1444
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1445 AKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVeearQSCQKKLKQMEVQLEEEYEDKQKALRE 1524
Cdd:pfam15921 384 ADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLR----RELDDRNMEV----QRLEALLKAMKSECQGQMERQMAAIQG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1525 KRELESKLSTLSDQVnqrdfESEKRLrkdLKRTKALLADAQIMLDHlknnapSKREIAQLKNQLEESE----FTCAAAVK 1600
Cdd:pfam15921 456 KNESLEKVSSLTAQL-----ESTKEM---LRKVVEELTAKKMTLES------SERTVSDLTASLQEKEraieATNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1601 ARKAMEVEMEDL-HLQIDDIAKAKTALEEQLSRLQ-REKNEIQNRLEEDQEDMNELmkkhkaaVAQASRDMAQMNDLQAQ 1678
Cdd:pfam15921 522 LRSRVDLKLQELqHLKNEGDHLRNVQTECEALKLQmAEKDKVIEILRQQIENMTQL-------VGQHGRTAGAMQVEKAQ 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1679 IE-ESNKEKQELQEKlqalqsqvefleqsmvdKSLVSRQEAKIRELETR---LEFEKTqvkRLENLASRLKETMEKLTEE 1754
Cdd:pfam15921 595 LEkEINDRRLELQEF-----------------KILKDKKDAKIRELEARvsdLELEKV---KLVNAGSERLRAVKDIKQE 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1755 RDQ-------RAAAENREKEQNKRLQRQLRDTKEEMSELARK-EAEASRKKHELEM---DLESLEAAN-------QSLQA 1816
Cdd:pfam15921 655 RDQllnevktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQtrnTLKSMEGSDghamkvaMGMQK 734
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1817 DLKLAFKRIGDLQAAI---EDEMESDENEDLI-----NSLQDMVTKYQKKKNKLEGDSDVDSELEDRV 1876
Cdd:pfam15921 735 QITAKRGQIDALQSKIqflEEAMTNANKEKHFlkeekNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1404-1794 |
3.91e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.13 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1404 DIAG---FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEELDEQAGSIQMLEQAKLRLEMEmermrq 1480
Cdd:TIGR02169 161 EIAGvaeFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR-REREKAERYQALLKEKREYEGYELLKEKE------ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1481 thskEMESRDEEVEEARQSCQKKLKQMEVQLEEeyedkqkalREKR--ELESKLSTLSDQVNQRDFESEKRLRKDLKRTK 1558
Cdd:TIGR02169 234 ----ALERQKEAIERQLASLEEELEKLTEEISE---------LEKRleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1559 ALLADAQimldhlknnapskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKN 1638
Cdd:TIGR02169 301 AEIASLE-------------RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1639 EIQNRLEEDQEDMNELMKKHKAAVaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKslvsrqEA 1718
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYR-------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI------EA 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082237 1719 KIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRaaaenreKEQNKRLQRQLRDTKeemSELARKEAEAS 1794
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQ---RELAEAEAQAR 500
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1274-1855 |
1.07e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.57 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1274 AVREVDFTKKRLQQELEDkmEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELE 1353
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKA--QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1354 kkqrrfdsELSQAHEETQREKLQREklqREKDMLLAEAFSLKQQMEEkdldiagftqkvvsLEAELQDISSQESKDEASL 1433
Cdd:PRK02224 255 --------TLEAEIEDLRETIAETE---REREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1434 AKVKKQLRDLEAKVKDQEEELDEQAGSIQML-EQAK------LRLEMEMERMRqTHSKEMESRDEEVEEARQSCQKKLKQ 1506
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHnEEAEslredaDDLEERAEELR-EEAAELESELEEAREAVEDRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1507 MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqRDFESEKRLRKDLKRTKALLADAQIMLDHLKnnAPskrEIAQlkn 1586
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERD-ELREREAELEATLRTARERVEEAEALLEAGK--CP---ECGQ--- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1587 QLEESEFTCAAAVK--ARKAMEVEMEDLHLQIDDIAKAKTALEEqLSRLQREKNeiqnRLEEDQEDMNELMKKHKAAVAQ 1664
Cdd:PRK02224 460 PVEGSPHVETIEEDreRVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIE----RLEERREDLEELIAERRETIEE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1665 ASRdmaqmndlqaQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKslvsRQEAKirELETRLEFEKTQVKRLENLASRL 1744
Cdd:PRK02224 535 KRE----------RAEELRERAAELEAEAEEKREAAAEAEEEAEEA----REEVA--ELNSKLAELKERIESLERIRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1745 ------KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHE-----LEMDLESLEAANQS 1813
Cdd:PRK02224 599 aaiadaEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEeyleqVEEKLDELREERDD 678
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907082237 1814 LQadlklafKRIGDLQAAIEdEMES--DENEDLINSLQDMVTKY 1855
Cdd:PRK02224 679 LQ-------AEIGAVENELE-ELEElrERREALENRVEALEALY 714
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1214-1863 |
2.25e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 92.73 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1214 ERLRTEKEM---KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERA---VREVDFTKKRLQQ 1287
Cdd:pfam02463 154 RRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEkleLEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1288 ELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAH 1367
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1368 EETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLaKVKKQLRDLEAKV 1447
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1448 KDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRE 1527
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEK---KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1528 LESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAM-- 1605
Cdd:pfam02463 470 SEDLLKETQLVKLQEQ-LELLLSRQKLEERSQKESKARSGLK--VLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAis 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1606 ---EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM----NELMKKHKAAVAQASRDMAQMNDLQAQ 1678
Cdd:pfam02463 547 tavIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleiDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1679 IEESNKEKQELQEKLQALQSQVefLEQSMVDKSLVSRQEAKIRELETRLEfekTQVKRLENLASRLKETMEKLTEERDQR 1758
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGL--RKGVSLEEGLAEKSEVKASLSELTKE---LLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1759 AAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRigdLQAAIEDEMES 1838
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS---ELSLKEKELAE 778
|
650 660
....*....|....*....|....*
gi 1907082237 1839 DENEDLINSLQDMVTKYQKKKNKLE 1863
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEEL 803
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1581-1843 |
9.86e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1581 IAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKA 1660
Cdd:COG1196 195 LGELERQLEPLE---RQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1661 AVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSL-VSRQEAKIRELETRLEFEKTQVKRLEN 1739
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEeLAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1740 LASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLK 1819
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260
....*....|....*....|....
gi 1907082237 1820 LAFKRIGDLQAAIEDEMESDENED 1843
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELE 455
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1254-1653 |
1.84e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 89.73 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1254 INGEVDDDDAGgewRLKYERAVREVDFTKKRLQQ---ELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQR 1330
Cdd:TIGR02168 661 ITGGSAKTNSS---ILERRREIEELEEKIEELEEkiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1331 LTAELQdtklhlegqqvrnhELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQ 1410
Cdd:TIGR02168 738 LEAEVE--------------QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1411 KVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRD 1490
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1491 eEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesekRLRKDLKRTK-ALLADAQIMLD 1569
Cdd:TIGR02168 884 -SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE--------GLEVRIDNLQeRLSEEYSLTLE 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1570 HLKNN--------APSKREIAQLKNQLEE---------SEFtcaAAVKARKamevemEDLHLQIDDIAKAKTALEEQLSR 1632
Cdd:TIGR02168 955 EAEALenkieddeEEARRRLKRLENKIKElgpvnlaaiEEY---EELKERY------DFLTAQKEDLTEAKETLEEAIEE 1025
|
410 420
....*....|....*....|.
gi 1907082237 1633 LQReknEIQNRLEEDQEDMNE 1653
Cdd:TIGR02168 1026 IDR---EARERFKDTFDQVNE 1043
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1281-1863 |
2.21e-17 |
|
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: 89.26 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1281 TKKRLQQELEDKMEVEQQSRRQLeRRLGDLQADSDESQRALQQLKKKCQRLTA-----ELQDTKLHLEGQQVRNHELEKK 1355
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAqeavlEETQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1356 QRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQ--MEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1433
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1434 AKVKKQLRDLEAKVK---DQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVEEARQSCQKKLkQMEVQ 1510
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQslcKELDILQREQATIDTRTSAFRDLQGQLAHAK----KQQELQQRYAELCAAAITCTA-QCEKL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1511 LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL-------RKDLKRTKALLADAQIMLDHLKNNAPSKR---E 1580
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeqT 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1581 IAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKKHKA 1660
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE---AEDMLACE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1661 AVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ---------EAKIRELETRLEFEK 1731
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkellasrQLALQKMQSEKEQLT 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1732 TQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEA--------SRKKHELEMD 1803
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkarteahFNNNEEVTAA 773
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082237 1804 L------ESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQdMVTKYQKKKNKLE 1863
Cdd:TIGR00618 774 LqtgaelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCET-LVQEEEQFLSRLE 838
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
324-506 |
1.32e-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: 86.43 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKgCRR--EDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 401
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYK-CIDciEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 402 GSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQAL---------------------STLLEAFGNSPTIMNGSATRF 460
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDnihneentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907082237 461 SQILSLDFDQAgQVASASIQTMLLEKLRVARRPASEATFNVFYYLL 506
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYII 205
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1140-1869 |
2.16e-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: 86.25 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1140 RPLIQVQLSEEQIRNKDEEIQ--QLRSKLEKVEKE-------RNELRLSSDRLETR---ISELTSELTDERNTGESASQL 1207
Cdd:TIGR00606 351 RLQLQADRHQEHIRARDSLIQslATRLELDGFERGpfserqiKNFHTLVIERQEDEaktAAQLCADLQSKERLKQEQADE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1208 LDAETAERLRT--------EKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVR--- 1276
Cdd:TIGR00606 431 IRDEKKGLGRTielkkeilEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQnek 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1277 -EVDFTKKRLQQELE-----------------DKMEVEQQSRRQLERRLGDLQA------DSDESQRALQQLKKKCQRLT 1332
Cdd:TIGR00606 511 aDLDRKLRKLDQEMEqlnhhtttrtqmemltkDKMDKDEQIRKIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTR 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1333 AELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-----------ETQREKLQR--EKLQREKDMLLAEAFSLKQQME 1399
Cdd:TIGR00606 591 DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcgsqdeESDLERLKEeiEKSSKQRAMLAGATAVYSQFIT 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1400 EKDLDIAG---FTQKVVSLEAELQDISsqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME 1476
Cdd:TIGR00606 671 QLTDENQSccpVCQRVFQTEAELQEFI---SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1477 RMRQTHSK------EMESRDEEVEEARQSCQKKLKQMEV---------QLEEEYEDKQKALREK-RELESKLSTLS-DQV 1539
Cdd:TIGR00606 748 ELRNKLQKvnrdiqRLKNDIEEQETLLGTIMPEEESAKVcltdvtimeRFQMELKDVERKIAQQaAKLQGSDLDRTvQQV 827
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1540 NQRDFESEKRLRK---DLKRTKALLADAQIMLDHLKNNApskreiaqlkNQLEESEFTCAAAVKARKAME-------VEM 1609
Cdd:TIGR00606 828 NQEKQEKQHELDTvvsKIELNRKLIQDQQEQIQHLKSKT----------NELKSEKLQIGTNLQRRQQFEeqlvelsTEV 897
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1610 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEED----QEDMNELMKKHKAAVA---------------QASRDMA 1670
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSnkkaQDKVNDIKEKVKNIHGymkdienkiqdgkddYLKQKET 977
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1671 QMNDLQAQIEESNKEKQELQEKLQALQSQVE---FLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLasRLKET 1747
Cdd:TIGR00606 978 ELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVL--QMKQE 1055
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1748 MEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAsrKKHELEMDLESLEAANQSL--------QADLK 1819
Cdd:TIGR00606 1056 HQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE--KYREMMIVMRTTELVNKDLdiyyktldQAIMK 1133
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1820 LAFKRIGDLQAAIED--------------EMESDENEDLinSLQDMVTKYQKKKNKLEGDSDVD 1869
Cdd:TIGR00606 1134 FHSMKMEEINKIIRDlwrstyrgqdieyiEIRSDADENV--SASDKRRNYNYRVVMLKGDTALD 1195
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1105-1694 |
4.62e-16 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 84.69 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1105 KKRKIQDLAIRCVQKNIKKNKgvkdwpwwKLFTTVRPLIQVQLS-EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRL 1183
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNK--------SLESQISELKKQNNQlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1184 ETRISELTSELtderntgESASQLLDaetaerlRTEKEMKELQTQYDALKKQmevmemevmearliRAAEINGEVDDDDA 1263
Cdd:TIGR04523 266 KKQLSEKQKEL-------EQNNKKIK-------ELEKQLNQLKSEISDLNNQ--------------KEQDWNKELKSELK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1264 GGEWRL--------KYERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKkcqrLTAEL 1335
Cdd:TIGR04523 318 NQEKKLeeiqnqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN----LESQI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1336 QDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSL 1415
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-------DLTNQDSVKELIIKNLDNTRESL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1416 EAELQDISSQESKDEASLAKVKKQLrdleakvKDQEEELDeqagsiqMLEQAKLRLEMEMermrqthsKEMESRdeevee 1495
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKEL-------KSKEKELK-------KLNEEKKELEEKV--------KDLTKK------ 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1496 arqscQKKLKQMEVQLEeeyedkqkalREKRELESKLSTLSDQVNQRDFESEKRLRKD-----------LKRTKALLADA 1564
Cdd:TIGR04523 519 -----ISSLKEKIEKLE----------SEKKEKESKISDLEDELNKDDFELKKENLEKeideknkeieeLKQTQKSLKKK 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1565 QIMLDHLKNNapSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR- 1643
Cdd:TIGR04523 584 QEEKQELIDQ--KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKw 661
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1644 ---------LEEDQEDMNELMKKHK----AAVAQASRDMAQMNDLQaQIEESNKEKQELQEKLQ 1694
Cdd:TIGR04523 662 peiikkikeSKTKIDDIIELMKDWLkelsLHYKKYITRMIRIKDLP-KLEEKYKEIEKELKKLD 724
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1166-1637 |
5.31e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 84.05 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1166 LEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVME 1245
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1246 ARLI-RAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQLerrlgdlqadSDESQRALQQL 1324
Cdd:COG4717 128 LPLYqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL----------SLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1325 KKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEtqreklqrEKLQREKDMLLAEA-----FSLKQQME 1399
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--------ERLKEARLLLLIAAallalLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1400 EKDLDIAGFTQKVVSLeaeLQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKL-RLEMEMERM 1478
Cdd:COG4717 270 SLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1479 RQTHSKEMESRDEE----VEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQR--------DFES 1546
Cdd:COG4717 347 EELQELLREAEELEeelqLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgeleellEALD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1547 EKRLRKDLKRTKALLADAQIMLDHLknnapsKREIAQLKNQLE--ESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKT 1624
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEEL------REELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
490
....*....|...
gi 1907082237 1625 ALEEQLSRLQREK 1637
Cdd:COG4717 501 LLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1331-1831 |
6.25e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 84.05 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1331 LTAELQDTKLHLEGQQVRNHELEKKQRRfdsELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQ 1410
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELK---ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1411 KVvsleaELQDISSQESKDEASLAKVKKQLRDLEAkvkdQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRD 1490
Cdd:COG4717 124 LL-----QLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1491 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQvnqrdfesekrlrKDLKRTKALLADAQIMLdh 1570
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-------------ERLKEARLLLLIAAALL-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1571 lknnapskrEIAQLKNQLEESEFTCAAAVKARKAMevemedLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQED 1650
Cdd:COG4717 260 ---------ALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1651 MNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKlQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFE 1730
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED------EEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1731 KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQnkRLQRQLRDTKEEMSELARKEAEASRKKHELEMD--LESLE 1808
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELE--ELEEELEELEEELEELREELAELEAELEQLEEDgeLAELL 475
|
490 500
....*....|....*....|...
gi 1907082237 1809 AANQSLQADLKLAFKRIGDLQAA 1831
Cdd:COG4717 476 QELEELKAELRELAEEWAALKLA 498
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
324-1042 |
1.53e-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: 82.85 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 324 SVLHTLRQRYGASLLHTYAGPSLLVLST---RGAPAVYSEKvmhmfkgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVL 400
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPyrdVGNPLTLTST--------RSSPLAPQLLKVVQEAVRQQSETGYPQAIIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 401 LGSSGSGKTTSFQHLVQYLATIAGtSGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQaGQVASASIQ 480
Cdd:cd14881 74 SGTSGSGKTYASMLLLRQLFDVAG-GGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 481 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLN--------HLAENNVFgivplskpEEKQKAAQQFSKLQAA 552
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgyspanlrYLSHGDTR--------QNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 553 MKVLAISpeeqktcWL----ILASIYHLGAAG-ATKAGRKQFARHEWAQKA-AYLLGCSleelSSAIFKhqlkgGTLQRS 626
Cdd:cd14881 224 LGILGIP-------FLdvvrVLAAVLLLGNVQfIDGGGLEVDVKGETELKSvAALLGVS----GAALFR-----GLTTRT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 627 TSFRQGPEESGLGEGTKLSALECLegmASGLYSElftLLISLVNRAlkSSQHSLCSMM----------IVDTPGFQNPew 696
Cdd:cd14881 288 HNARGQLVKSVCDANMSNMTRDAL---AKALYCR---TVATIVRRA--NSLKRLGSTLgthatdgfigILDMFGFEDP-- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 697 ggsaRGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELafdDLEPVADDSVAAVDqashLVRSLahadeARGLL 776
Cdd:cd14881 358 ----KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQC---EVEVDYVDNVPCID----LISSL-----RTGLL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 777 WLLEEEALVPGATEdalldrlfSYYGPQEGDKKGQSPLLRSSK--PRHFLLGHSHGTnwVEYNVAGWLnytkqnpatqna 854
Cdd:cd14881 422 SMLDVECSPRGTAE--------SYVAKIKVQHRQNPRLFEAKPqdDRMFGIRHFAGR--VVYDASDFL------------ 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 855 prllqDSQKKIISNlflgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAavkkkslciQIKLQVDALIDTIKR 934
Cdd:cd14881 480 -----DTNRDVVPD----------------------DLVAVFYKQNCNFGFATHTQ---------DFHTRLDNLLRTLVH 523
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 935 SKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVF 1014
Cdd:cd14881 524 ARPHFVRCIRSNTTETPN-----------------------------HFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRF 574
|
730 740
....*....|....*....|....*...
gi 1907082237 1015 SEFRRRFDVLAPHLTKKHGRNYIVVDEK 1042
Cdd:cd14881 575 KAFNARYRLLAPFRLLRRVEEKALEDCA 602
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1143-1659 |
1.55e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.19 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1143 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLET---------RISELTSELTDERNTGE-------SASQ 1206
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEkrlsrleEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1207 LLDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEvddddaggewRLKYERAVREVDFTKKRLQ 1286
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE----------RLKKRLTGLTPEKLEKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1287 QELEDKMEVEQQsRRQLERRLGDLQADSDESQRALQQLKK---KCQRLTAELQDtklhlegqqvrnHELEKKQRRFDSEL 1363
Cdd:PRK03918 395 ELEKAKEEIEEE-ISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTE------------EHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1364 SQAHEETQREKLQREKLQREKDMLlaEAFSLKQQMEEKDLDIAgftQKVVSLEAELQDISSQE-SKDEASLAKVKKQLRD 1442
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELA---EQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1443 LEAKVKDQEEELDEQagsiqmleqaklrlememermrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEE----YEDK 1518
Cdd:PRK03918 537 LKGEIKSLKKELEKL--------------------------EELKKKLAELEKKLDELEEELAELLKELEELgfesVEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1519 QKALREKRELESKLSTLSDQVnqRDFESEKRLRKDLKRTkalLADAQIMLDHLKNNAPSKR-EIAQLKNQLEESEFTCAA 1597
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAE--KELEREEKELKKLEEE---LDKAFEELAETEKRLEELRkELEELEKKYSEEEYEELR 665
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082237 1598 AVKARKAMEV-----EMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNrLEEDQEDMNELMKKHK 1659
Cdd:PRK03918 666 EEYLELSRELaglraELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVK 731
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1149-1630 |
1.91e-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: 82.92 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1149 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISEL---TSELTDERNTGESAsqlldaetaeRLRTEKEMKEL 1225
Cdd:pfam01576 656 ERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMktqLEELEDELQATEDA----------KLRLEVNMQAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1226 QTQYDAlkkqmevmemevmearliraaEINGEvddDDAGGEWRLKYERAVREvdftkkrLQQELEDKMEVEQQ---SRRQ 1302
Cdd:pfam01576 726 KAQFER---------------------DLQAR---DEQGEEKRRQLVKQVRE-------LEAELEDERKQRAQavaAKKK 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1303 LERRLGDLQADSDESQR----ALQQLKK---KCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKL 1375
Cdd:pfam01576 775 LELDLKELEAQIDAANKgreeAVKQLKKlqaQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1376 QREKLQREKDmllaeafslkqqmeekdldiagftqkvvsleaELQDISSQESKDEASLAKVKkqlRDLEAKVKDQEEELD 1455
Cdd:pfam01576 855 ARRQAQQERD--------------------------------ELADEIASGASGKSALQDEK---RRLEARIAQLEEELE 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1456 EQAGSIQMLEQAKLRLEMEMERMRQTHSKEmESRDEEVEEARQSCQKKLKQMEVQL-EEEYEDKQKALREKRELESKLST 1534
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLQVEQLTTELAAE-RSTSQKSESARQQLERQNKELKAKLqEMEGTVKSKFKSSIAALEAKIAQ 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1535 LSDQVNQrdfESEKRLR--KDLKRTKALLADAQIMLDHLKNNAPSKREIA--------QLKNQLEESEFTCAAAVKARKA 1604
Cdd:pfam01576 979 LEEQLEQ---ESRERQAanKLVRRTEKKLKEVLLQVEDERRHADQYKDQAekgnsrmkQLKRQLEEAEEEASRANAARRK 1055
|
490 500
....*....|....*....|....*.
gi 1907082237 1605 MEVEMEDLHLQIDDIAKAKTALEEQL 1630
Cdd:pfam01576 1056 LQRELDDATESNESMNREVSTLKSKL 1081
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1523-1879 |
2.67e-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: 82.42 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1523 REKRELESKLSTLS--DQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcaAAVK 1600
Cdd:TIGR02169 153 VERRKIIDEIAGVAefDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGY--ELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1601 ARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM-AQMNDLQAQI 1679
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELeAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1680 EESNKEKQELQEKLQ-------ALQSQVEFLEQSMVDKSL--------VSRQEAKIRELETRLEFEKTQVKRLENLASRL 1744
Cdd:TIGR02169 311 AEKERELEDAEERLAkleaeidKLLAEIEELEREIEEERKrrdklteeYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1745 KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1824
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1825 IGDLQA---AIEDEMESDENEdlinsLQDMVTKYQKKKNKLEGDSDVDSELEDRVDGV 1879
Cdd:TIGR02169 471 LYDLKEeydRVEKELSKLQRE-----LAEAEAQARASEERVRGGRAVEEVLKASIQGV 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1143-1489 |
3.23e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.41 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1143 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLET-------RISELTSELTDERNTGESASQLLDAETAER 1215
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAeveqleeRIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1216 LRTEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDD-DDAGGEWRLKYERAVREVDFTKKRLqQELEDKME 1294
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALRE--------ALDELRAELTLlNEEAANLRERLESLERRIAATERRL-EDLEEQIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1295 VEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREK 1374
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1375 LQREKLQREKDMLLaEAFSLKQQMeekdldiagftqkvvsleaELQDISSQESKDEASLAKVKKQLRDLEAKVK------ 1448
Cdd:TIGR02168 929 LRLEGLEVRIDNLQ-ERLSEEYSL-------------------TLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvn 988
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907082237 1449 --------DQEEELDEQAGSIQMLEQAKLRLEMEMERMrqthSKEMESR 1489
Cdd:TIGR02168 989 laaieeyeELKERYDFLTAQKEDLTEAKETLEEAIEEI----DREARER 1033
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1422-1874 |
3.86e-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: 81.61 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1422 ISSQESKD---EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEmemERMRQTHSKEMESRD-------- 1490
Cdd:TIGR04523 28 ANKQDTEEkqlEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILE---QQIKDLNDKLKKNKDkinklnsd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1491 -----EEVEEARQSCQKK---LKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesekrlrkDLKRTKALLA 1562
Cdd:TIGR04523 105 lskinSEIKNDKEQKNKLeveLNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN------------DLKKQKEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1563 DAQIMLDHLKNNApsKREIAQLKNQLEESEFTCAAAVKARKamevEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQN 1642
Cdd:TIGR04523 173 NELNLLEKEKLNI--QKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1643 RLEEDQEDMNELMKKHKaavaqasRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD------KSLVSRQ 1716
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQN-------KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelKSELKNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1717 EAKIRELETRLEFEKTQVKRLENLASRLKETMEKLT---EERDQRAAAENRE----KEQNKRLQRQLRDTKEEMSELARK 1789
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEieklKKENQSYKQEIKNLESQINDLESK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1790 EAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESD-ENEDLINSLQDMVTKYQKKKNKLEGD-SD 1867
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDsVKELIIKNLDNTRESLETQLKVLSRSiNK 479
|
....*..
gi 1907082237 1868 VDSELED 1874
Cdd:TIGR04523 480 IKQNLEQ 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1284-1789 |
5.16e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.50 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1284 RLQQELEDKMEVEQQSRRQLERR--LGDLQADSDESQRALQQLKkkcqrlTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1361
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIelLEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1362 ELSQAHEETQREKLQREKLQREKDMLLAEAFS--------LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1433
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1434 AKVKKQLR------------------DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKE---------- 1485
Cdd:COG4913 383 AALRAEAAallealeeelealeealaEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlgldeaelpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1486 ----MESRDEE-------------------VEEARQSC------QKKLKQmEVQLEEEYEDKQKALREK-------RELE 1529
Cdd:COG4913 463 vgelIEVRPEEerwrgaiervlggfaltllVPPEHYAAalrwvnRLHLRG-RLVYERVRTGLPDPERPRldpdslaGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1530 SKLSTLSDQVNQ---RDF-----ESEKRLRKDlkrTKALLADAQImldhlKNNApSKREIaQLKNQLEESEFTCAAAVKA 1601
Cdd:COG4913 542 FKPHPFRAWLEAelgRRFdyvcvDSPEELRRH---PRAITRAGQV-----KGNG-TRHEK-DDRRRIRSRYVLGFDNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1602 RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelmkkhkaaVAQASRDMAQMNDLQAQIEE 1681
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID---------VASAEREIAELEAELERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1682 SNKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFEKTQVK----RLENLASRLKETMEKLTEERDQ 1757
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEE------ELDELKGEIGRLEKELEQAEEELDelqdRLEAAEDLARLELRALLEERFA 756
|
570 580 590
....*....|....*....|....*....|..
gi 1907082237 1758 RAAAENREKEQNKRLQRQLRDTKEEMSELARK 1789
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1541-1874 |
6.04e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.26 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1541 QRDFESEKRLRK---DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaavkarkamevemedlhLQID 1617
Cdd:TIGR02168 172 ERRKETERKLERtreNLDRLEDILNELERQLKSLERQAEKAERYKELKAELRE-----------------------LELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1618 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkhkaavaqasrdmaqmndlQAQIEESNKEKQELQEKLQALQ 1697
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQEL---------------------EEKLEELRLEVSELEEEIEELQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1698 SqvEFLEQSmvdkslvsrqeAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLR 1777
Cdd:TIGR02168 288 K--ELYALA-----------NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1778 DTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQK 1857
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
330
....*....|....*..
gi 1907082237 1858 KKNKLEGDSDVDSELED 1874
Cdd:TIGR02168 435 LKELQAELEELEEELEE 451
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1146-1797 |
1.34e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.40 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1146 QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDaetaERLRTEKEMKEL 1225
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ----GKLTEEKEELEK 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1226 QTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELE--DKMEVEQQSRRQL 1303
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggRIISAHGRLGDLG 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1304 ERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEETQREKLQREKLQRE 1383
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK---LPLKSIAVLEIDPILNLAQLDKAT 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1384 KDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQE------SKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1457
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaekSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1458 AGSIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSD 1537
Cdd:pfam02463 693 EILRRQLEIKKKEQREK-EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1538 QVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID 1617
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1618 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqasrdMAQMNDLQAQIEESNKEKQELQEKLQALQ 1697
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEK------EEKKELEEESQKLNLLEEKENEIEERIKE 925
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1698 SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLEN---LASRLKETMEKLTEERDQRAAAENREKEQN----K 1770
Cdd:pfam02463 926 EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLakeELGKVNLMAIEEFEEKEERYNKDELEKERLeeekK 1005
|
650 660
....*....|....*....|....*..
gi 1907082237 1771 RLQRQLRDTKEEMSELARKEAEASRKK 1797
Cdd:pfam02463 1006 KLIRAIIEETCQRLKEFLELFVSINKG 1032
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1153-1758 |
2.12e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1153 RNKDEEIQQLRSKLEkvEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDaETAERLrteKEMKELQTQYDAL 1232
Cdd:PRK02224 183 SDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRD-EADEVL---EEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1233 KkqmevmemevmearliraAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELED---KMEVEQQSRRQLERRLGD 1309
Cdd:PRK02224 257 E------------------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDllaEAGLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1310 LQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDmlla 1389
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE---- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1390 eafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD-------QEEELDEQAGSIQ 1462
Cdd:PRK02224 395 ---ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1463 MLEQAKLRLEMEMERMRQTHskemESRDEEVEEArqscqKKLKQMEVQLEEeyedkqkaLREKRELESKLSTlsdqvNQR 1542
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEV----EEVEERLERA-----EDLVEAEDRIER--------LEERREDLEELIA-----ERR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1543 DFESEKRLRKDLKRTKAlladaqimlDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE----MEDLHLQIDD 1618
Cdd:PRK02224 530 ETIEEKRERAEELRERA---------AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKEriesLERIRTLLAA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1619 IAKAKTALE---EQLSRLQREKNEIQNRLEEDQEDMNELMKKH-KAAVAQASRDMAQMNDLQAQIEEsnkEKQELQEKLQ 1694
Cdd:PRK02224 601 IADAEDEIErlrEKREALAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEE---KLDELREERD 677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082237 1695 ALQSQVefleqSMVDKSLvsrqeAKIRELETRLEFEKTQVKRLENL---ASRLKETMEKLTEERDQR 1758
Cdd:PRK02224 678 DLQAEI-----GAVENEL-----EELEELRERREALENRVEALEALydeAEELESMYGDLRAELRQR 734
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1578-1794 |
6.15e-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: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1578 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1657
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1658 -------HKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdkslvsRQEAKIRELETRLEFE 1730
Cdd:COG4942 113 lyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA---------ELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1731 KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAS 1794
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1150-1786 |
7.33e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.65 E-value: 7.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1150 EQIRNKDEEIQQLRSKLEKVEKERNELRLssDRLETRISELTSELTDERntgesasQLLDAETAERLRTEKEMKELQTQY 1229
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAELEELR-------AELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1230 DALKKQMevmemevmearliraaeingevddDDAGGEwRLkyERAVREVdftkKRLQQELEDKmeveQQSRRQLERRLGD 1309
Cdd:COG4913 326 DELEAQI------------------------RGNGGD-RL--EQLEREI----ERLERELEER----ERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1310 LQADSDESQRALQQLKKKCQRLTAELQDtklHLEGQQVRNHELEKKQRRFDSELSQAHEE----TQREKLQREKLQREKD 1385
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEE---ELEALEEALAEAEAALRDLRRELRELEAEiaslERRKSNIPARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1386 MLlAEAFSLKqqmeEKDLDIAGftqkvvsleaELQDISSQESK------------------DEASLAKVKKQLR--DLEA 1445
Cdd:COG4913 448 AL-AEALGLD----EAELPFVG----------ELIEVRPEEERwrgaiervlggfaltllvPPEHYAAALRWVNrlHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1446 KVKDQEEELDEQAGSIQMLEQAKL--RLEMEMERMRQTHSKEMESRD-----EEVEEARQ-------SCQKKL------K 1505
Cdd:COG4913 513 RLVYERVRTGLPDPERPRLDPDSLagKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRhpraitrAGQVKGngtrheK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1506 QMEVQLEEEY------EDKQKALREKR-ELESKLSTLSDQVNQRdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSK 1578
Cdd:COG4913 593 DDRRRIRSRYvlgfdnRAKLAALEAELaELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1579 REIAQLKNQ---LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE----DQEDM 1651
Cdd:COG4913 668 REIAELEAElerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlARLEL 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1652 NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQveFLEQSMVDKSLVSRQEAKIRELETRLEfek 1731
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA--FNREWPAETADLDADLESLPEYLALLD--- 822
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082237 1732 tqvkRLENlaSRLKETMEKLteeRDQRAAAENREKEQ-NKRLQRQLRDTKEEMSEL 1786
Cdd:COG4913 823 ----RLEE--DGLPEYEERF---KELLNENSIEFVADlLSKLRRAIREIKERIDPL 869
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1462-1863 |
1.19e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 76.73 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1462 QMLEQaklRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQVNQ 1541
Cdd:COG4717 45 AMLLE---RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1542 -RDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS----KREIAQLKNQLEESEFTCAAAVK-ARKAMEVEMEDLHLQ 1615
Cdd:COG4717 121 lEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1616 IDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK-----------AAVA--------------------- 1663
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaAALLallglggsllsliltiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1664 ---------------QASRDMAQMNDLQAQIEESNKEKQELQEKLQALQ----SQVEFLEQSMVDKSLVSRQEAKIRELE 1724
Cdd:COG4717 281 lvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGlppdLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1725 TRLEFEKTQvKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAsrkkhELEMDL 1804
Cdd:COG4717 361 EELQLEELE-QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEEL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 1805 ESLEAANQSLQADLKLAFKRIGDLQAAIEdEMESDEnedlinSLQDMVTKYQKKKNKLE 1863
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELE-QLEEDG------ELAELLQELEELKAELR 486
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1261-1873 |
1.49e-13 |
|
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: 77.01 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1261 DDAGGEWRLKYERAVREVDFTKKRLQQeledkmeveqqsrrQLERRLGDLQADSDESQRALQQLKKKCQRLTaELQDTKL 1340
Cdd:TIGR01612 1099 DDFGKEENIKYADEINKIKDDIKNLDQ--------------KIDHHIKALEEIKKKSENYIDEIKAQINDLE-DVADKAI 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1341 HLEGQQvrnhELEKKQRRFDSELSQA---HEETQreKLQREKLQREKDmllaeafslKQQMEE-KDLDIAgFTQKVVSLE 1416
Cdd:TIGR01612 1164 SNDDPE----EIEKKIENIVTKIDKKkniYDEIK--KLLNEIAEIEKD---------KTSLEEvKGINLS-YGKNLGKLF 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1417 aeLQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEELDEQAGsIQMLEQAklrlemEMERMRQTHSKEM------ESRD 1490
Cdd:TIGR01612 1228 --LEKIDEEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMG-IEMDIKA------EMETFNISHDDDKdhhiisKKHD 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1491 EEVEEARQscqKKLKQMEVQLEE-EYEDKQKAL--------REKRELESKLSTLSDQVNQRDFESEKRLRKDLKR-TKAL 1560
Cdd:TIGR01612 1298 ENISDIRE---KSLKIIEDFSEEsDINDIKKELqknlldaqKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKEyTKEI 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1561 LADAQIMLDHLKNnapSKREIAQLKNQLeeSEFTCAAAVKArkamEVEMEDLHLQIDDIAKAKTALEEQLSRLQ------ 1634
Cdd:TIGR01612 1375 EENNKNIKDELDK---SEKLIKKIKDDI--NLEECKSKIES----TLDDKDIDECIKKIKELKNHILSEESNIDtyfkna 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1635 REKNE----IQNRLEEDQEDMNELMKKHKAavaQASRDMA-QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvd 1709
Cdd:TIGR01612 1446 DENNEnvllLFKNIEMADNKSQHILKIKKD---NATNDHDfNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQY--- 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1710 KSLVSRQEAKIRELETRLEFEKTQvKRLENLASRLKETMEKLTEErdqraaAENREKEQNKRLQRQLRDTKEemselARK 1789
Cdd:TIGR01612 1520 KKDVTELLNKYSALAIKNKFAKTK-KDSEIIIKEIKDAHKKFILE------AEKSEQKIKEIKKEKFRIEDD-----AAK 1587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1790 EAEASRKKHELEMDLESLEaaNQSLQ-ADLKlafKRIGDLQAAIED-------------EMESDENEDLINSLQDMVTKY 1855
Cdd:TIGR01612 1588 NDKSNKAAIDIQLSLENFE--NKFLKiSDIK---KKINDCLKETESiekkissfsidsqDTELKENGDNLNSLQEFLESL 1662
|
650 660
....*....|....*....|..
gi 1907082237 1856 QKKKNKLEGDS----DVDSELE 1873
Cdd:TIGR01612 1663 KDQKKNIEDKKkeldELDSEIE 1684
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1299-1864 |
1.77e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1299 SRRQLERRLGDLQADSDESQRALQqlkkkcQRLTAelqdtKLHLEGQQ--------------------VRNHELEKKQ-- 1356
Cdd:COG4913 156 DIRALKARLKKQGVEFFDSFSAYL------ARLRR-----RLGIGSEKalrllhktqsfkpigdlddfVREYMLEEPDtf 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1357 RRFDS------ELSQAHEETQREKLQREKLQREKDmlLAEAF-SLKQQMEEKDLDIAGFTQKVVSLEAELQdissqeskd 1429
Cdd:COG4913 225 EAADAlvehfdDLERAHEALEDAREQIELLEPIRE--LAERYaAARERLAELEYLRAALRLWFAQRRLELL--------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1430 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKL--------RLEMEMERMRQTHskemesrdEEVEEARQSCQ 1501
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLEREL--------EERERRRARLE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1502 KKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQImLDHLKNNAPskREI 1581
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS-LERRKSNIP--ARL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1582 AQLKNQLEEseftcAAAVKARKA------MEVEMED--------------------------------------LHLQID 1617
Cdd:COG4913 443 LALRDALAE-----ALGLDEAELpfvgelIEVRPEEerwrgaiervlggfaltllvppehyaaalrwvnrlhlrGRLVYE 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1618 DI------AKAKTALEEQLSR-LQREKNEIQNRLE------------EDQEDmnelMKKHKAAVAQA-----SRDMAQMN 1673
Cdd:COG4913 518 RVrtglpdPERPRLDPDSLAGkLDFKPHPFRAWLEaelgrrfdyvcvDSPEE----LRRHPRAITRAgqvkgNGTRHEKD 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1674 DL-------------QAQIEESNKEKQELQEKLQALQSQVEFLEQSMvdKSLVSRQEAKIRELETRleFEKTQVKRLENL 1740
Cdd:COG4913 594 DRrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAEL--DALQERREALQRLAEYS--WDEIDVASAERE 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1741 ASRLKETMEKLTEERDQRAAAENREKEQNKR---LQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEA-ANQSLQA 1816
Cdd:COG4913 670 IAELEAELERLDASSDDLAALEEQLEELEAEleeLEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlARLELRA 749
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1907082237 1817 DLKLAFkrigdlQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEG 1864
Cdd:COG4913 750 LLEERF------AAALGDAVERELRENLEERIDALRARLNRAEEELER 791
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1322-1855 |
4.28e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 75.39 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1322 QQLKKKCQRLTAELQDTKLHLEGQQVRNHElekKQRRFDSELSQAHEETQREKLQREKLQREkDMLLAEAFSLKQQMEEK 1401
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHE---RKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1402 DLDIAGFT--QKVVSLEAELQDISSQESK---DEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME 1476
Cdd:TIGR00618 266 RARIEELRaqEAVLEETQERINRARKAAPlaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1477 RMRQTHSKEMESRDE-EVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFE--SEKRLRKD 1553
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAhEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRtsAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1554 LKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcaaAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1633
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ---SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1634 QREKNE-----------------IQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQAL 1696
Cdd:TIGR00618 503 PCPLCGscihpnparqdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1697 QSQVEFLEQSMVD------------KSLVSRQEAKIRELETRLE------FEKTQVKRLENLASRLKETMEKLTEERDQR 1758
Cdd:TIGR00618 583 KEDIPNLQNITVRlqdlteklseaeDMLACEQHALLRKLQPEQDlqdvrlHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1759 AAAENREKEQNKRLQRQLRDTKEE-------------------MSELARKEAEASRKKHELEMDLESLEaanQSLQADLK 1819
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQsekeqltywkemlaqcqtlLRELETHIEEYDREFNEIENASSSLG---SDLAARED 739
|
570 580 590
....*....|....*....|....*....|....*.
gi 1907082237 1820 LAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKY 1855
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ 775
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1363-1565 |
7.25e-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: 72.87 E-value: 7.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1363 LSQAHEETQREKlQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1442
Cdd:COG4942 16 AAQADAAAEAEA-ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1443 LEAKVKDQEEELDEQAGSIQML-EQAKLRLEM------EMERMRQTHSKEMESRDEEVEEARQScQKKLKQMEVQLEEEY 1515
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgRQPPLALLLspedflDAVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1516 EDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQ 1565
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1620-1824 |
7.51e-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: 72.87 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1620 AKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1699
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1700 VEFLEQSMVD--------------KSLVSRQEAK-----IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAA 1760
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqpplALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1761 AENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1824
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1479-1908 |
9.95e-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: 73.90 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1479 RQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTK 1558
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK-LNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1559 AlladaQIMLD-HLKNNapSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREK 1637
Cdd:TIGR04523 110 S-----EIKNDkEQKNK--LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1638 NEIQN----------RLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSm 1707
Cdd:TIGR04523 183 LNIQKnidkiknkllKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1708 vDKSLVSRQEAKIRELETrlefEKTQVKRLENLASRLKETMEKLteerdqraaaeNREKEQN--KRLQRQLRDTKEEMSE 1785
Cdd:TIGR04523 262 -QNKIKKQLSEKQKELEQ----NNKKIKELEKQLNQLKSEISDL-----------NNQKEQDwnKELKSELKNQEKKLEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1786 LarkeaeasrkkhelemdlesleaanqslqadlklafkrigdlqaaiedEMESDENEDLINSLQDMVTKYQKKKNKLEGD 1865
Cdd:TIGR04523 326 I------------------------------------------------QNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907082237 1866 -SDVDSELEDRVDGVKSWLSKNKGPSKAPSddgSLKSSRTALNS 1908
Cdd:TIGR04523 358 nSEKQRELEEKQNEIEKLKKENQSYKQEIK---NLESQINDLES 398
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1269-1821 |
1.25e-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: 73.70 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1269 LKYERAVREVDFTKKRLqqeLEDKMEVEQQSRRQLERRLGDLQaDSDESQRALQQL----KKKCQRLTAELQDTKLHLEG 1344
Cdd:pfam10174 41 LKKERALRKEEAARISV---LKEQYRVTQEENQHLQLTIQALQ-DELRAQRDLNQLlqqdFTTSPVDGEDKFSTPELTEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1345 QQVRNHELEKKQRRFDSELSQAHEE------TQREKL--QREKLQREKDMLLAEAFSLKQQMEEKDLD--IAGFTQKVVS 1414
Cdd:pfam10174 117 NFRRLQSEHERQAKELFLLRKTLEEmelrieTQKQTLgaRDESIKKLLEMLQSKGLPKKSGEEDWERTrrIAEAEMQLGH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1415 LEAELQDISSQESKDEASLaKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVE 1494
Cdd:pfam10174 197 LEVLLDQKEKENIHLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1495 --EARQSCQKKLKQMEVQLEEEYEDKQKalrEKRELESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLK 1572
Cdd:pfam10174 276 qmEVYKSHSKFMKNKIDQLKQELSKKES---ELLALQTKLETLTNQ-NSDCKQHIEVLKESLTAKEQRAAILQTEVDALR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1573 NNAPSKREIAQLKNQ----LEESEFTCAAA---------VKARKAMEVE--MEDLHLQIDDIAKAKTALEEQLSRLQREK 1637
Cdd:pfam10174 352 LRLEEKESFLNKKTKqlqdLTEEKSTLAGEirdlkdmldVKERKINVLQkkIENLQEQLRDKDKQLAGLKERVKSLQTDS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1638 NEIQNRL---EE---DQEDMNELMKKHKAAVAQASRDmaqmndlqaQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-- 1709
Cdd:pfam10174 432 SNTDTALttlEEalsEKERIIERLKEQREREDRERLE---------ELESLKKENKDLKEKVSALQPELTEKESSLIDlk 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1710 ---KSLVSR---QEAKIRELETRLEFEKTQVKRLENlasRLKETMEKlteERDQRAAAENREKEQNkrLQRqlrdtkeem 1783
Cdd:pfam10174 503 ehaSSLASSglkKDSKLKSLEIAVEQKKEECSKLEN---QLKKAHNA---EEAVRTNPEINDRIRL--LEQ--------- 565
|
570 580 590
....*....|....*....|....*....|....*....
gi 1907082237 1784 sELARKEAEASRKKHELEMDLESL-EAANQSLQADLKLA 1821
Cdd:pfam10174 566 -EVARYKEESGKAQAEVERLLGILrEVENEKNDKDKKIA 603
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1272-1810 |
1.36e-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: 73.72 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1272 ERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRL----GDLQADSDESQRALQQLKkkcQRLTAELQDTKLHLEGQQV 1347
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHG---AFLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1348 RNHELEKKQRRFDSeLSQAHEETQREKLQREKL--QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQ 1425
Cdd:pfam12128 352 WQSELENLEERLKA-LTGKHQDVTAKYNRRRSKikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1426 eSKDEASLAKVKKQLRDLEAKVK-----DQEEELDEQAGSIQMLEQAKLRLEM---EMERMrQTHSKEMESRDEEVEEAR 1497
Cdd:pfam12128 431 -GKLEFNEEEYRLKSRLGELKLRlnqatATPELLLQLENFDERIERAREEQEAanaEVERL-QSELRQARKRRDQASEAL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1498 QSCQKKLKQMEVQLEE-------------EYEDKQKALREK---RELESKLSTLSDQVNQRDFESEKR------LRKDLK 1555
Cdd:pfam12128 509 RQASRRLEERQSALDElelqlfpqagtllHFLRKEAPDWEQsigKVISPELLHRTDLDPEVWDGSVGGelnlygVKLDLK 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1556 RTkallaDAQIMLDHlknNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDiakAKTALEEQLSRLQR 1635
Cdd:pfam12128 589 RI-----DVPEWAAS---EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETF---ARTALKNARLDLRR 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1636 EKNEIQNrleeDQEDMNELMKKHKAAVAQASRDMAQ-----MNDLQAQIEESNKEKQELQ-EKLQALQSQVEFLEQSM-- 1707
Cdd:pfam12128 658 LFDEKQS----EKDKKNKALAERKDSANERLNSLEAqlkqlDKKHQAWLEEQKEQKREARtEKQAYWQVVEGALDAQLal 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1708 VDKSLVSRQEAKIRELETRLEFEKTQVKRL---ENLASRLKETMEKLTE-----ERDQRAAAENRE------KEQNKRLQ 1773
Cdd:pfam12128 734 LKAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIRTLERkieriAVRRQEVLRYFDwyqetwLQRRPRLA 813
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1907082237 1774 RQLRDTKEEMSE----LARKEAEASRKKHELEMDLESLEAA 1810
Cdd:pfam12128 814 TQLSNIERAISElqqqLARLIADTKLRRAKLEMERKASEKQ 854
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1414-1888 |
1.85e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 73.01 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1414 SLEAELQDISSQESKDEAS---LAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMermrqthsKEMESRD 1490
Cdd:PRK01156 177 MLRAEISNIDYLEEKLKSSnleLENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL--------NELSSLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1491 EEVeearqscqkklKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRkDLKRTKALLADAQIMLDH 1570
Cdd:PRK01156 249 DMK-----------NRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIN-DYFKYKNDIENKKQILSN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1571 LKNNAPSKREIAQLKNQLEE--SEFTcaaavkarkAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ 1648
Cdd:PRK01156 317 IDAEINKYHAIIKKLSVLQKdyNDYI---------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1649 EDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM-----------------VDKS 1711
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgEEKS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1712 L---------VSRQEAKIRELEtrlefekTQVKRLENLASRLKETMEKLTEERDQRAAAENRekeQNKRLQRQLRDTKEE 1782
Cdd:PRK01156 468 NhiinhynekKSRLEEKIREIE-------IEVKDIDEKIVDLKKRKEYLESEEINKSINEYN---KIESARADLEDIKIK 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1783 MSELARKEAEASRKKHELE-MDLESLEA------------------ANQSLQADLKLAFKRIGDLQAAIEDEMESDE--N 1841
Cdd:PRK01156 538 INELKDKHDKYEEIKNRYKsLKLEDLDSkrtswlnalavislidieTNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyI 617
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1907082237 1842 EDLINSLQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKG 1888
Cdd:PRK01156 618 DKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS 664
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1472-1812 |
2.51e-12 |
|
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: 72.46 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1472 EMEMERMRQTH---SKEMESRD--EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTlsDQVNQRDFES 1546
Cdd:pfam17380 295 KMEQERLRQEKeekAREVERRRklEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKREL--ERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1547 EKRLRKDLKRtkalladaqIMLDHLKNNAPSKREI-AQLKNQLEESEFTcaaavKARKAMEVEMEDLHLQIDDiakaktA 1625
Cdd:pfam17380 373 EISRMRELER---------LQMERQQKNERVRQELeAARKVKILEEERQ-----RKIQQQKVEMEQIRAEQEE------A 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1626 LEEQLSRLQREKNEIQNRLEEDqedmnELMKKHkaavaqasrdmaQMNDLQAQIEESNKEKQELqEKLQALQSQVEFLEQ 1705
Cdd:pfam17380 433 RQREVRRLEEERAREMERVRLE-----EQERQQ------------QVERLRQQEEERKRKKLEL-EKEKRDRKRAEEQRR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1706 SMVDKSLVSRQEAKIRELETRLEFEKtqvkrlenlasRLKETMEKLTEERDQRAAAENREKEQN----KRLQRQLRDTKE 1781
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLEK-----------EMEERQKAIYEEERRREAEEERRKQQEmeerRRIQEQMRKATE 563
|
330 340 350
....*....|....*....|....*....|...
gi 1907082237 1782 EMSEL--ARKEAEASRKKHELEMDLESLEAANQ 1812
Cdd:pfam17380 564 ERSRLeaMEREREMMRQIVESEKARAEYEATTP 596
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1144-1724 |
1.01e-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: 70.92 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1144 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGEsasqlLDAETAERLRTEKE-M 1222
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD-----LKLQELQHLKNEGDhL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1223 KELQTQYDALKKQMEVMEMEVMEAR--LIRAAEINGEvDDDDAGGewrLKYERAVREVDFTKKRLQ-QELEDKMEVEQQS 1299
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRqqIENMTQLVGQ-HGRTAGA---MQVEKAQLEKEINDRRLElQEFKILKDKKDAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1300 RRQLERRLGDLQADS-------DESQRALQQLKKKCQRLTAELQDTKLHLEG---------QQVRN--HELEKKQRRFDS 1361
Cdd:pfam15921 620 IRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNksEEMETTTNKLKM 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1362 ELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLE---------------------AELQ 1420
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeamtnankekhflkeeknklsQELS 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1421 DISSQESKDEASLAKVKKQLRDLEAKVKDQEEELD-------EQAGSIQMLEQAKLRLEM-------EMERMRQTHSKEM 1486
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDkaslqfaECQDIIQRQEQESVRLKLqhtldvkELQGPGYTSNSSM 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1487 ESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALRE--KRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLAD 1563
Cdd:pfam15921 860 KPRlLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEdpTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALD 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1564 AQIMLDHLKNNAPSK---REIAQLKNQLEESEFTCAAAVKARKAMevEMEDLHLQIDDIAKAKTALEEQLSR---LQREK 1637
Cdd:pfam15921 940 DRVRDCIIESSLRSDichSSSNSLQTEGSKSSETCSREPVLLHAG--ELEDPSSCFTFPSTASPSVKNSASRsfhSSPKK 1017
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1638 NEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQmnDLQAQ-IEESNKEKQELQEKLQALQSQVEFLE---QSMvdKSLV 1713
Cdd:pfam15921 1018 SPVHSLLTSSAEGSIGSSSQYRSAKTIHSPDSVK--DSQSLpIETTGKTCRKLQNRLESLQTLVEDLQlknQAM--SSMI 1093
|
650
....*....|.
gi 1907082237 1714 SRQEAKIRELE 1724
Cdd:pfam15921 1094 RNQEKRIQKVK 1104
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1526-1789 |
1.19e-11 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 70.04 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1526 RELESKLSTLSDQVN--------QRDFESEKRlrkdlKRTKALLADAQIMLDHLKNNAPS-KREIAQLKNQLEEseftca 1596
Cdd:PHA02562 177 RELNQQIQTLDMKIDhiqqqiktYNKNIEEQR-----KKNGENIARKQNKYDELVEEAKTiKAEIEELTDELLN------ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1597 aavkarkaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQR-----EKNEIQNRLEEDQEDMNELMKKHKAavaqasrdmaQ 1671
Cdd:PHA02562 246 --------LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyEKGGVCPTCTQQISEGPDRITKIKD----------K 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1672 MNDLQAQIEESNKEKQELQEKLqalqsqVEFLEQSMvdkslvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKL 1751
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIM------DEFNEQSK-----------KLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907082237 1752 TEERDQRaaaenreKEQNKRLQRQLRDTKEEMSELARK 1789
Cdd:PHA02562 371 QAEFVDN-------AEELAKLQDELDKIVKTKSELVKE 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1607-1768 |
1.30e-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: 66.87 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1607 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ---EDMNELMKKHKAAVAQASRDMAQMNDLQAQIeESN 1683
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1684 KEkqelqekLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1763
Cdd:COG1579 89 KE-------YEALQKEIESLKR------RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*
gi 1907082237 1764 REKEQ 1768
Cdd:COG1579 156 AELEE 160
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1141-1787 |
1.40e-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: 70.25 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1141 PLIQVQLSeeqirNKDEEIQQLRSKLEKVEKERNELRLSSD-RLETRISELTSELTDERntgesasqlldaETAERLRTE 1219
Cdd:pfam12128 350 PSWQSELE-----NLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIR------------EARDRQLAV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1220 KEmKELQTQYDALKKQMEVMEMEVMEARL---IRAAEINGEVDDDDAGGEWRLKYERAVREVDftkkRLQQELEDKMEve 1296
Cdd:pfam12128 413 AE-DDLQALESELREQLEAGKLEFNEEEYrlkSRLGELKLRLNQATATPELLLQLENFDERIE----RAREEQEAANA-- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1297 QQSRRQLERRLgdLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdselSQAHEETQREKLQ 1376
Cdd:pfam12128 486 EVERLQSELRQ--ARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKE-------APDWEQSIGKVIS 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1377 REKLQREKDMLLAEAFSLKQQ-------MEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1449
Cdd:pfam12128 557 PELLHRTDLDPEVWDGSVGGElnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1450 QEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR--- 1526
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARtek 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1527 --ELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHL----KNNAPSKREIAQLKNQLEESEFTCAAAVK 1600
Cdd:pfam12128 717 qaYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIERIAVRRQEVLR 796
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1601 ARKAME----VEMEDLHLQIDDIAKAKTALEEQLSRLQ------REKNEIQNRLEEDQED-MNELMKKHKAAVAQASRDM 1669
Cdd:pfam12128 797 YFDWYQetwlQRRPRLATQLSNIERAISELQQQLARLIadtklrRAKLEMERKASEKQQVrLSENLRGLRCEMSKLATLK 876
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1670 AQMNDLQAQ--IEESNKEKQELQEKLQ----ALQSQVEFLEQSMVDKS---------LVSRQEAKIRELETRLEFEKTQV 1734
Cdd:pfam12128 877 EDANSEQAQgsIGERLAQLEDLKLKRDylseSVKKYVEHFKNVIADHSgsglaetweSLREEDHYQNDKGIRLLDYRKLV 956
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082237 1735 KRLENLASRLKETMEKLTEER------------DQRAAAENREKEQNKRLQRQLRDTK--EEMSELA 1787
Cdd:pfam12128 957 PYLEQWFDVRVPQSIMVLREQvsilgvdltefyDVLADFDRRIASFSRELQREVGEEAffEGVSESA 1023
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1150-1766 |
1.48e-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: 70.47 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1150 EQIRNKDEE-IQQLRSKLEKVEKERNELRLSSD--RLETRISELTSELTDERNTGESASQLLDaETAErlrTEKEmkelQ 1226
Cdd:TIGR01612 1135 EEIKKKSENyIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLN-EIAE---IEKD----K 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1227 TQYDALKKQMEVMEMEVMEARLiraaeinGEVDDDDAGGEWRLK-YERAVREVDFTKKRlQQELEDKMEVEQQSRRQLEr 1305
Cdd:TIGR01612 1207 TSLEEVKGINLSYGKNLGKLFL-------EKIDEEKKKSEHMIKaMEAYIEDLDEIKEK-SPEIENEMGIEMDIKAEME- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1306 rLGDLQADSDESQRALQQLKKKcqrltaELQDtklhlegqqVRNHELEKKQRRF-DSELSQAHEETQREKLQREKLQREK 1384
Cdd:TIGR01612 1278 -TFNISHDDDKDHHIISKKHDE------NISD---------IREKSLKIIEDFSeESDINDIKKELQKNLLDAQKHNSDI 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1385 DMLLAEAFSLKQQMEEKDL-----DIAGFTQKVvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdQEEELDEQ-- 1457
Cdd:TIGR01612 1342 NLYLNEIANIYNILKLNKIkkiidEVKEYTKEI---EENNKNIKDELDKSEKLIKKIKDDINLEECKSK-IESTLDDKdi 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1458 AGSIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEV-------EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELES 1530
Cdd:TIGR01612 1418 DECIKKIKELKNHILSE-ESNIDTYFKNADENNENVlllfkniEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1531 KLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDhLKNN-APSKREIAQLKNQLEE--SEFTCAAAVKARKAMEV 1607
Cdd:TIGR01612 1497 GCKDEADK-NAKAIEKNKELFEQYKKDVTELLNKYSALA-IKNKfAKTKKDSEIIIKEIKDahKKFILEAEKSEQKIKEI 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1608 EMEDLHLQiDDIAKA----KTALEEQLSrlqrekneIQNrLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESn 1683
Cdd:TIGR01612 1575 KKEKFRIE-DDAAKNdksnKAAIDIQLS--------LEN-FENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDT- 1643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1684 kekqELQEKLQALQSQVEFLEqSMVDkslvsrQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1763
Cdd:TIGR01612 1644 ----ELKENGDNLNSLQEFLE-SLKD------QKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIAN 1712
|
...
gi 1907082237 1764 REK 1766
Cdd:TIGR01612 1713 KEE 1715
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1150-1645 |
1.55e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1150 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntGESASQLLDAETAERLRTEKEMKELQTQy 1229
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL--AEAGLDDADAEAVEARREELEDRDEELR- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1230 DALKKQMevmemevmearlIRAAEINGEVddddaggewrlkyERAVREVDftkkrlqqELEDKMEVEQQSRRQLERRLGD 1309
Cdd:PRK02224 328 DRLEECR------------VAAQAHNEEA-------------ESLREDAD--------DLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1310 LQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEkkqrrfdSELSQAHEetqREKLQREKLQREKDMlLA 1389
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR-------EERDELRE---REAELEATLRTARER-VE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1390 EAFSLK---------QQMEEKDL--DIAGFTQKVVSLEAELQDISSQESKDEA------SLAKVKKQLRDLEAKVK---- 1448
Cdd:PRK02224 444 EAEALLeagkcpecgQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEERREdlee 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1449 ---DQEEELDEQAGSIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLE------------E 1513
Cdd:PRK02224 524 liaERRETIEEKRERAEELRERAAELEAEAEEKREA-AAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllaaiA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1514 EYEDKQKALREKRElesKLSTLSDQvnQRDFESEKRLRKDlkrtkalladaqimldhlknnapskreiaQLKNQLEESEF 1593
Cdd:PRK02224 603 DAEDEIERLREKRE---ALAELNDE--RRERLAEKRERKR-----------------------------ELEAEFDEARI 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1594 TCAAAVKARKA-----MEVEMEDLHLQIDDIAKAKTALE---EQLSRLQREKNEIQNRLE 1645
Cdd:PRK02224 649 EEAREDKERAEeyleqVEEKLDELREERDDLQAEIGAVEnelEELEELRERREALENRVE 708
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1157-1474 |
2.40e-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: 69.71 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1157 EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTD-ERNTGE---SASQLLDAETAERLRTEKEMKELQTQYDAL 1232
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDaSRKIGEiekEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1233 -----KKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRlKYERAVREVDFTKKRLQ----------QELEDKMEVEQ 1297
Cdd:TIGR02169 754 envksELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP-EIQAELSKLEEEVSRIEarlreieqklNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1298 QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQR 1377
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1378 EKLQREKDMLLAEAFSLKQQMEE-------------KDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE 1444
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEiedpkgedeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
330 340 350
....*....|....*....|....*....|
gi 1907082237 1445 AKVKDQEEELDEQAGSIQMLEQAKLRLEME 1474
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1293-1880 |
2.54e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.48 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1293 MEVEQQSRRQLERRLGDLQADsDESQRALQQLKKkcQRLTAELQDTKlHLEGQQVRNHELEKKQRRFDS------ELSQA 1366
Cdd:pfam12128 188 MHSKEGKFRDVKSMIVAILED-DGVVPPKSRLNR--QQVEHWIRDIQ-AIAGIMKIRPEFTKLQQEFNTlesaelRLSHL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1367 HEETQREKLQREKLQREKDMLLAEafslkqqmeekdldiagFTQKVVSLEAELQdissqESKDEASLakvkkQLRDLEAK 1446
Cdd:pfam12128 264 HFGYKSDETLIASRQEERQETSAE-----------------LNQLLRTLDDQWK-----EKRDELNG-----ELSAADAA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1447 VKDQEEEL---DEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEE-------YE 1516
Cdd:pfam12128 317 VAKDRSELealEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnnrdiagIK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1517 DKQKALREKRE------------LESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDhlknnapskreiaqL 1584
Cdd:pfam12128 397 DKLAKIREARDrqlavaeddlqaLESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE--------------L 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1585 KNQLEESEFTCAAAVKARKAMEVEMEDLHlqiDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQ 1664
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQ---SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1665 ASRDMAQMNDLQAQIEESNK-EKQELQEKLQALQSQVEF--------LEQSMVDKSLVSRQEAKIR--ELETRLEFEKTQ 1733
Cdd:pfam12128 540 LRKEAPDWEQSIGKVISPELlHRTDLDPEVWDGSVGGELnlygvkldLKRIDVPEWAASEEELRERldKAEEALQSAREK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1734 VKRLENLASRLKETMEKLT-EERDQRAAAENREKEQnKRL---QRQLRDTKEEMSELARKEAEASRKK--HELEMDLESL 1807
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASrEETFARTALKNARLDL-RRLfdeKQSEKDKKNKALAERKDSANERLNSleAQLKQLDKKH 698
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1808 EAANQSLQADLKLAfkRIGDLQAAIEDEMESDENEDLINslQDMVTKYQKKKNKLEG-DSDVDSELEDR-VDGVK 1880
Cdd:pfam12128 699 QAWLEEQKEQKREA--RTEKQAYWQVVEGALDAQLALLK--AAIAARRSGAKAELKAlETWYKRDLASLgVDPDV 769
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1297-1521 |
2.62e-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: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1297 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQ 1376
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1377 REKLQREKDMLLAEAFSLKQQMEEKDL-DIAGFTQKVVSLEAeLQDISSQeskDEASLAKVKKQLRDLEAKVKDQEEELD 1455
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLlSPEDFLDAVRRLQY-LKYLAPA---RREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 1456 EQAGSIQMLEQAKLRLEMEMERMRQT---HSKEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKA 1521
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAER 242
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1411-1817 |
3.58e-11 |
|
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: 68.61 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1411 KVVSLEAELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAgsiqmleQAKLRLEMEMERMRQTHSKEMESRD 1490
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH---KRARIELEKKASALKRQLDRES-------DRNQELQKRIRLLEKREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1491 EEVEEARQsCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFEsekrlrkdLKRTKALLADAQIMLDH 1570
Cdd:pfam05557 73 EQAELNRL-KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELE--------LQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1571 LKNNApskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhLQIDDIAKAKTALEEQLS--------RLQREKNEIQN 1642
Cdd:pfam05557 144 LKAKA---SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ---SQEQDSEIVKNSKSELARipelekelERLREHNKHLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1643 RLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ----------ALQSQVEFLEQSmvDKSL 1712
Cdd:pfam05557 218 ENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQdtglnlrspeDLSRRIEQLQQR--EIVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1713 VSRQ-----------------EAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERD-QRAAAENREKEQN-KRLQ 1773
Cdd:pfam05557 296 KEENssltssarqlekarrelEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgYRAILESYDKELTmSNYS 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1907082237 1774 RQLRDTKEEMSELARK-EAEASRKKHELEMDLESLEAANQSLQAD 1817
Cdd:pfam05557 376 PQLLERIEEAEDMTQKmQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1157-1374 |
3.80e-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: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1157 EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQm 1236
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1237 eVMEMEVMEARLIRAAEINGEVD--------DDDAGGEWRLKYERAVREVDFTK----KRLQQELEDKMEVEQQSRRQLE 1304
Cdd:COG4942 99 -LEAQKEELAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARREQaeelRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1305 RRLGDLQadsdESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAHEETQREK 1374
Cdd:COG4942 178 ALLAELE----EERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1146-1587 |
3.82e-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: 68.99 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1146 QLSEEQiRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETR-------ISELTSELTDERNTGESASQLLDAETAE-RLR 1217
Cdd:pfam15921 367 QFSQES-GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1218 TEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAeingeVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ 1297
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV-----VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEIT 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1298 QSRRQLERRLGDLQADSDESQRaLQQLKKKCQRLTAEL--QDTKLHLEGQQVRNHelekkqrrfdSELSQAHEET----Q 1371
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDH-LRNVQTECEALKLQMaeKDKVIEILRQQIENM----------TQLVGQHGRTagamQ 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1372 REKLQREKLQREKDMLLAEAFSLKqqmEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1451
Cdd:pfam15921 590 VEKAQLEKEINDRRLELQEFKILK---DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1452 EELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS-------------------------------C 1500
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkvamgmqkqitakrgqidaL 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1501 QKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTKALLADAQIMLDHLKNNAPSKRE 1580
Cdd:pfam15921 747 QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
....*..
gi 1907082237 1581 IAQLKNQ 1587
Cdd:pfam15921 826 IIQRQEQ 832
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1623-1831 |
4.84e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 67.16 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1623 KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL--QALQSQV 1700
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeRARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1701 EFLEQSMVDKSLVSRQeakIRELETRLEFektqvkrLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTK 1780
Cdd:COG3883 98 SGGSVSYLDVLLGSES---FSDFLDRLSA-------LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1781 EEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAA 1831
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1147-1695 |
5.59e-11 |
|
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: 67.84 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1147 LSEEQIRNKDEEIQQLRSKLEKVEKERNElrlsSDRLETRISELTSELTDErnTGESASQLLDAETAERlRTEKEMKELQ 1226
Cdd:pfam05557 66 EAEEALREQAELNRLKKKYLEALNKKLNE----KESQLADAREVISCLKNE--LSELRRQIQRAELELQ-STNSELEELQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1227 TQYDALKKqmevmemevmearliRAAEINGEVDDDDAGGEWRLKYERAVREVDFtkkRLQQELEDKMEVEQQSRRQLerR 1306
Cdd:pfam05557 139 ERLDLLKA---------------KASEAEQLRQNLEKQQSSLAEAEQRIKELEF---EIQSQEQDSEIVKNSKSELA--R 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1307 LGDLQadsdesqRALQQLKKKCQRLTaELQDTKLHLEGQQvrnHELEKKQRRfdselsqahEETQREKLQreKLQREKDM 1386
Cdd:pfam05557 199 IPELE-------KELERLREHNKHLN-ENIENKLLLKEEV---EDLKRKLER---------EEKYREEAA--TLELEKEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1387 LLAEAFSLKQQMEEKDLDIA---GFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK-------DQEEELDE 1456
Cdd:pfam05557 257 LEQELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAqylkkieDLNKKLKR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1457 QAGSIQMLEQAKLRLEMEMERMRQ------------THSKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqKALRE 1524
Cdd:pfam05557 337 HKALVRRLQRRVLLLTKERDGYRAilesydkeltmsNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLS-------VAEEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1525 KRELESKLSTLSDQVnqrdfesekrlrkDLKRTKALLADAqimldhlknnAPSKREIAQLKNQLEESEFTCAAAVKARKA 1604
Cdd:pfam05557 410 LGGYKQQAQTLEREL-------------QALRQQESLADP----------SYSKEEVDSLRRKLETLELERQRLREQKNE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1605 MEVEMED--------------LHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRdma 1670
Cdd:pfam05557 467 LEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFK--- 543
|
570 580
....*....|....*....|....*
gi 1907082237 1671 QMNDLQAQIEESNKEKQELQEKLQA 1695
Cdd:pfam05557 544 EVLDLRKELESAELKNQRLKEVFQA 568
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1342-1728 |
5.90e-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: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1342 LEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREkdmllaeafsLKQQMEEKDLDIAGFTQKVVSLEAELQD 1421
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE----------LESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1422 ISsqeskdeASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQScQ 1501
Cdd:pfam07888 106 LS-------ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-Q 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1502 KKLKQMEVQLeeeyedkqkalrekRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREI 1581
Cdd:pfam07888 178 AKLQQTEEEL--------------RSLSKEFQELRNSLAQRD-TQVLQLQDTITTLTQKLTTAH---RKEAENEALLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1582 AQLKNQLEESEFTCAA-------AVKARKAMEVEMEDLHLQIDD----IAKAKTALEEQLSRLQREKNEIQNRLEEDQED 1650
Cdd:pfam07888 240 RSLQERLNASERKVEGlgeelssMAAQRDRTQAELHQARLQAAQltlqLADASLALREGRARWAQERETLQQSAEADKDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1651 M----NELMKKHKAAVAQASR------DMAQMNDL-QAQIEESNKEKQELQEKLQALQSQVEFLeqsmvdksLVSRQE-- 1717
Cdd:pfam07888 320 IeklsAELQRLEERLQEERMEreklevELGREKDCnRVQLSESRRELQELKASLRVAQKEKEQL--------QAEKQEll 391
|
410
....*....|.
gi 1907082237 1718 AKIRELETRLE 1728
Cdd:pfam07888 392 EYIRQLEQRLE 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1131-1562 |
9.92e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1131 PWWKLFTTVRPLiQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgESASQLLDA 1210
Cdd:PRK03918 359 ERHELYEEAKAK-KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK---KAIEELKKA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1211 E----TAERLRTEKEMKELQTQYDA-LKKQMEVMEMEVMEARLIRAAEIngEVDDDDAGGEWRLKYERAVREVDFTKKRL 1285
Cdd:PRK03918 435 KgkcpVCGRELTEEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKELR--ELEKVLKKESELIKLKELAEQLKELEEKL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1286 QQELEDKMEVEQQSRRQLERRLGDLQADS---DESQRALQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSE 1362
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIkslKKELEKLEELKKKLAELEKKLDELEEELA-------ELLKELEELGFE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1363 LSQAHEETQREklqREKLQREkdmlLAEAFSLKQQMEEKDldiagftQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1442
Cdd:PRK03918 586 SVEELEERLKE---LEPFYNE----YLELKDAEKELEREE-------KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1443 LEAKVKDQEEEldeqagsiqMLEQAKLRLEMEMERMRqthskemeSRDEEVEEARQSCQKKLKqmevQLEEEYEDKQKAL 1522
Cdd:PRK03918 652 LEKKYSEEEYE---------ELREEYLELSRELAGLR--------AELEELEKRREEIKKTLE----KLKEELEEREKAK 710
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907082237 1523 REKRELESKLSTLsdqvnqrdfeseKRLRKDLKRTKALLA 1562
Cdd:PRK03918 711 KELEKLEKALERV------------EELREKVKKYKALLK 738
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1488-1855 |
1.65e-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: 66.74 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1488 SRDEEVEEARqscqkklkqmEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQrdfesekrLRKDLKRTKALLADAQIM 1567
Cdd:pfam01576 1 TRQEEEMQAK----------EEELQKVKERQQKAESELKELEKKHQQLCEEKNA--------LQEQLQAETELCAEAEEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1568 LDHLKNNAPSKREIAQ-LKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL-------------------- 1626
Cdd:pfam01576 63 RARLAARKQELEEILHeLESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvtteakikkleedill 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1627 -EEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQE--------------LQE 1691
Cdd:pfam01576 143 lEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQElekakrklegestdLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1692 KLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFEKTQ----VKRLENLASRLKETMEKLTEERDQRAAAEnreke 1767
Cdd:pfam01576 223 QIAELQAQIAELRAQL------AKKEEELQAALARLEEETAQknnaLKKIRELEAQISELQEDLESERAARNKAE----- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1768 qnkrlqRQLRDTKEEMSELarkeaeasrkKHELEMDLESlEAANQSLQADLKlafKRIGDLQAAIEDEMESDENEdlins 1847
Cdd:pfam01576 292 ------KQRRDLGEELEAL----------KTELEDTLDT-TAAQQELRSKRE---QEVTELKKALEEETRSHEAQ----- 346
|
....*...
gi 1907082237 1848 LQDMVTKY 1855
Cdd:pfam01576 347 LQEMRQKH 354
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1609-1863 |
1.65e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 64.55 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1609 MEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQE 1688
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1689 LQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFE-KTQVKRLEN---LASRLKETMEKLteerdQRAAAENR 1764
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRqQTEVLSPEEekeLVEKIKELEKEL-----EKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1765 EKEQNKRLQRQLRDTKEEMSELARKEAEASRK--KHELEMDlESLEAANQsLQADLKLAFKRIGDLQAAIEDEMES-DEN 1841
Cdd:COG1340 158 KNEKLKELRAELKELRKEAEEIHKKIKELAEEaqELHEEMI-ELYKEADE-LRKEADELHKEIVEAQEKADELHEEiIEL 235
|
250 260
....*....|....*....|..
gi 1907082237 1842 EDLINSLQDMVTKYQKKKNKLE 1863
Cdd:COG1340 236 QKELRELRKELKKLRKKQRALK 257
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1615-1881 |
1.88e-10 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 66.19 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1615 QIDDIAKAKT-ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdmaqmnDLQAQIEESNKEKQELQEKL 1693
Cdd:PHA02562 167 EMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA----------RKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1694 QALQSQVEFLEQSMVDkslVSRQEAKIRELETRLefeKTQVKRLENLASRLKE------TMEKLTEERDQRAAAENREKE 1767
Cdd:PHA02562 237 EELTDELLNLVMDIED---PSAALNKLNTAAAKI---KSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1768 QNKRLqRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDemESDENEDLINS 1847
Cdd:PHA02562 311 LQHSL-EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD--NAEELAKLQDE 387
|
250 260 270
....*....|....*....|....*....|....
gi 1907082237 1848 LQDMVTKYQKKKNKLEGDSDVDSELEDrvDGVKS 1881
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHRGIVTDLLKD--SGIKA 419
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1269-1863 |
2.10e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.61 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1269 LKYERAVREVDFTKKRLQQ---ELEDKME-VEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQdtklhLEG 1344
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKdnsELELKMEkVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR-----LLN 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1345 QQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISS 1424
Cdd:TIGR00606 340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1425 QESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKL 1504
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1505 KQMEVQLEEeyedkqkalrEKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMldhlKNNAPSKREIAQL 1584
Cdd:TIGR00606 500 KKEVKSLQN----------EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR----KIKSRHSDELTSL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1585 ------KNQLEEsefTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRL------EEDQEDMN 1652
Cdd:TIGR00606 566 lgyfpnKKQLED---WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1653 ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ-ALQSQVEFLEqsmvdksLVSRQEAKIRELETRLEFEK 1731
Cdd:TIGR00606 643 RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQrVFQTEAELQE-------FISDLQSKLRLAPDKLKSTE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1732 TQVKRLEnlasRLKETMEKLTEERDQRAAAENRE-KEQNKRLQRQLRDTKEEMSELARKEA--EASRKKHELEMDLESLE 1808
Cdd:TIGR00606 716 SELKKKE----KRRDEMLGLAPGRQSIIDLKEKEiPELRNKLQKVNRDIQRLKNDIEEQETllGTIMPEEESAKVCLTDV 791
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1809 AANQSLQADLKlafkrigDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLE 1863
Cdd:TIGR00606 792 TIMERFQMELK-------DVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD 839
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1464-1871 |
2.13e-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: 65.92 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1464 LEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELesklstlsdqvNQRD 1543
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIR-LLEKREAEAEEALREQAEL-----------NRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1544 FESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAK 1623
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1624 TALEEQLSRLQREKNEIQNrLE---EDQEDMNELMKKHKAAVAQasrdMAQMNDLQAQIEESNKEKQELQEKLQALQSQV 1700
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKE-LEfeiQSQEQDSEIVKNSKSELAR----IPELEKELERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1701 EFLEQSMvdkslvSRQE---AKIRELETRLEFEKTQVKRLENLASRLKETM---EKLTEERDQRAAAENREKEQNKRLQR 1774
Cdd:pfam05557 231 EDLKRKL------EREEkyrEEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQREIVLKEENSSLTS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1775 QLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE---DEME----SDENEDLINS 1847
Cdd:pfam05557 305 SARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILEsydKELTmsnySPQLLERIEE 384
|
410 420
....*....|....*....|....
gi 1907082237 1848 LQDMVTKYQKKKNKLEGDSDVDSE 1871
Cdd:pfam05557 385 AEDMTQKMQAHNEEMEAQLSVAEE 408
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1361-1749 |
2.95e-10 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 65.63 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1361 SELSQAHEETQREKLQREKLQRE--KDmLLAEAFS-------LKQQMEEKDLDIAGFTQKVVS---LEAE--LQDISSQE 1426
Cdd:PRK04778 129 QELLESEEKNREEVEQLKDLYRElrKS-LLANRFSfgpaldeLEKQLENLEEEFSQFVELTESgdyVEAReiLDQLEEEL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1427 SKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGSIQMLEQ----AKLRLEMEMERMRQTHSK---EMESRD-EEVEEARQ 1498
Cdd:PRK04778 208 AALEQIMEEIPELLKELQTELPDQLQEL--KAGYRELVEEgyhlDHLDIEKEIQDLKEQIDEnlaLLEELDlDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1499 SCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEkRLR-------KDLKRTKALLADAQIM---- 1567
Cdd:PRK04778 286 EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEID-RVKqsytlneSELESVRQLEKQLESLekqy 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1568 LDHLKNNAPSKREIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLE-- 1645
Cdd:PRK04778 365 DEITERIAEQEIAYSELQEELEEIL-------KQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEks 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1646 ------EDQEDMNELMKKH-KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM----------- 1707
Cdd:PRK04778 438 nlpglpEDYLEMFFEVSDEiEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQLIqyanryrsdne 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907082237 1708 -VDKSLVS--------RQEAKIRELETRLE-FEKTQVKRLENLASRLKETME 1749
Cdd:PRK04778 518 eVAEALNEaerlfreyDYKAALEIIATALEkVEPGVTKRIEDSYEKEKETIR 569
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1491-1716 |
4.02e-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: 64.40 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1491 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTKALLADAQIMLDH 1570
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1571 LKNNAPSKREIAQLKNQLEESEF-----TCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ---N 1642
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEallA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1643 RLEEDQEDMNELMKKHKAAVAQASRDMAQmndLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ 1716
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1144-1422 |
4.30e-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: 65.47 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1144 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAE-----TAERLRT 1218
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1219 EKEMKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQqELEDKMEVEQQ 1298
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRI---DLKEQIKSIEKEIENLNGKKE-ELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1299 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQrEKLQRE 1378
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLE 954
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1379 KLQREKDMLLAEAFSLK-------QQMEEKDLDIAGFTQKVVSLEAELQDI 1422
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1424-1863 |
5.31e-10 |
|
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: 64.99 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1424 SQESKDEASLAKVKKQLRDLEAKVKDQ--EEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEmeSRDEEVEEARQSCQ 1501
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLctPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL--TQKREAQEEQLKKQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1502 KKLKQMEVQLEE------EYEDKQKALREKRELEsKLSTLSDQVNQRDFESEkRLRKDLKRTKALLADAQIMLDHLKNNA 1575
Cdd:TIGR00618 260 QLLKQLRARIEElraqeaVLEETQERINRARKAA-PLAAHIKAVTQIEQQAQ-RIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1576 PSKREIAQLKNQL--EESEFTCAAAVKA--RKAMEVEMEDLHlQIDDIAKAKTALEEQ-------LSRLQREKNEIQNRL 1644
Cdd:TIGR00618 338 SSIEEQRRLLQTLhsQEIHIRDAHEVATsiREISCQQHTLTQ-HIHTLQQQKTTLTQKlqslckeLDILQREQATIDTRT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1645 EEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdKSLVSRQEAKIRELE 1724
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK---EQIHLQETRKKAVVL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1725 TRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQnKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDL 1804
Cdd:TIGR00618 494 ARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTY-AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 1805 ESLEAANQSLQADLKLAFKRIGDLQAAIedEMESDENEDLINSLQDMVTKYQKKKNKLE 1863
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNITVRLQDLT--EKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1610-1815 |
5.81e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 64.65 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1610 EDLHLQIDDIAKAKTALEEQLsrlqrekNEIQNRLEEDQEDMNELMKKHKAAVAQAsrdmaQMNDLQAQIEESNKEKQEL 1689
Cdd:COG3206 164 QNLELRREEARKALEFLEEQL-------PELRKELEEAEAALEEFRQKNGLVDLSE-----EAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1690 QEKLQALQSQVEFLEQSM----------VDKSLVSRQEAKIRELETRLEFEKTQV-----------KRLENLASRLKETM 1748
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpdalpelLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1749 EKLTEE-RDQRAAAENREKEqnkrLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQ 1815
Cdd:COG3206 312 QRILASlEAELEALQAREAS----LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1355-1907 |
7.61e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.54 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1355 KQRRFDSELSQAHEETQR---EKLQREKLQREKDMLLAEAFSLKQQMEekdlDIAGFTQKVVSLEAELQDISSQESKDEA 1431
Cdd:PRK01156 136 GQGEMDSLISGDPAQRKKildEILEINSLERNYDKLKDVIDMLRAEIS----NIDYLEEKLKSSNLELENIKKQIADDEK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1432 SLAKVKKQLRDLEAKVKDQEEE---LDEQAGSIQMLEQAKLRLEME---------MERMRQTHSKEMESRDEEVEEARQS 1499
Cdd:PRK01156 212 SHSITLKEIERLSIEYNNAMDDynnLKSALNELSSLEDMKNRYESEiktaesdlsMELEKNNYYKELEERHMKIINDPVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1500 CQKKLKQMEVQLEEEYEDKQKALRE-KRELES------KLSTLsdQVNQRDFESEKRLRKDLKRTKALLADaqimlDHLK 1572
Cdd:PRK01156 292 KNRNYINDYFKYKNDIENKKQILSNiDAEINKyhaiikKLSVL--QKDYNDYIKKKSRYDDLNNQILELEG-----YEMD 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1573 NNApSKREIAQLKNQLEE----SEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ 1648
Cdd:PRK01156 365 YNS-YLKSIESLKKKIEEysknIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELS 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1649 EDMNELMKKHKAAVAQASRDMAQMNDLqaqIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEA-KIRELET- 1725
Cdd:PRK01156 444 RNMEMLNGQSVCPVCGTTLGEEKSNHI---INHYNEKKSRLEEKIREIEIEVKDIDEKIVDlKKRKEYLESeEINKSINe 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1726 --RLEFEKTQVKRLENLASRLKETMEKLT-----------EERDQR----------------AAAENREKEQNKRLQRQL 1776
Cdd:PRK01156 521 ynKIESARADLEDIKIKINELKDKHDKYEeiknrykslklEDLDSKrtswlnalavislidiETNRSRSNEIKKQLNDLE 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1777 RDTKEEMSELARKEA--EASRKKHELEMD--------LESLEAANQSLQADLKLAFKRIGDLQAAIEDEME-----SDEN 1841
Cdd:PRK01156 601 SRLQEIEIGFPDDKSyiDKSIREIENEANnlnnkyneIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsriNDIE 680
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 1842 EDLINS---LQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDdgsLKSSRTALN 1907
Cdd:PRK01156 681 DNLKKSrkaLDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGD---LKRLREAFD 746
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1149-1691 |
1.12e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.15 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1149 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRIS-------ELTSELTDERNTGESASQLL---DAETAERLRT 1218
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINdpvyknrNYINDYFKYKNDIENKKQILsniDAEINKYHAI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1219 EKEMKELQTQYDA-LKKQMevmemevmearliRAAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ 1297
Cdd:PRK01156 328 IKKLSVLQKDYNDyIKKKS-------------RYDDLNNQILELE---GYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1298 QSRRQLERRLGD---LQADSDESQRALQQLKKKCQRLTA----------ELQDTKLHLEGQQV----RNHELEKKQRR-- 1358
Cdd:PRK01156 392 FISEILKIQEIDpdaIKKELNEINVKLQDISSKVSSLNQriralrenldELSRNMEMLNGQSVcpvcGTTLGEEKSNHii 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1359 --FDSELSQAHEETQREKLQREKLQREKDMLLaeafSLKQQMEEKDLD-IAGFTQKVVSLEAELQDissqeskDEASLAK 1435
Cdd:PRK01156 472 nhYNEKKSRLEEKIREIEIEVKDIDEKIVDLK----KRKEYLESEEINkSINEYNKIESARADLED-------IKIKINE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1436 VKKQlrdleakvKDQEEELDEQAGSIQmLEQAKLRLEMEMERMRQTHSKEME---SRDEEVEEARQSCQKKLKQMEVQLE 1512
Cdd:PRK01156 541 LKDK--------HDKYEEIKNRYKSLK-LEDLDSKRTSWLNALAVISLIDIEtnrSRSNEIKKQLNDLESRLQEIEIGFP 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1513 EEYEDKQKALrekRELESKLSTLSDQVNQrdFESEKRLRKDLKRTkalladaqimLDHLKNNAPSKREIAQLKNQLeese 1592
Cdd:PRK01156 612 DDKSYIDKSI---REIENEANNLNNKYNE--IQENKILIEKLRGK----------IDNYKKQIAEIDSIIPDLKEI---- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1593 ftcaaAVKARKaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMnELMKKHKAAVAQAS--RDMA 1670
Cdd:PRK01156 673 -----TSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETL-ESMKKIKKAIGDLKrlREAF 745
|
570 580
....*....|....*....|....*..
gi 1907082237 1671 QMNDLQAQIEES------NKEKQELQE 1691
Cdd:PRK01156 746 DKSGVPAMIRKSasqamtSLTRKYLFE 772
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1149-1594 |
1.44e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1149 EEQIRNKD-EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDE-----------RNTGESASQLLDAETAERL 1216
Cdd:COG4913 329 EAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefaalraeaAALLEALEEELEALEEALA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1217 RTEKEMKELQTQYDALKKQMEV---------MEMEVMEARLIRAAEING----------EVDDDDAggEWRL-------- 1269
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASlerrksnipARLLALRDALAEALGLDEaelpfvgeliEVRPEEE--RWRGaiervlgg 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1270 ---------KYERAVRE----------VDFTKKRLQQELEDKMEVEQQS----------------RRQLERRLGDLQADS 1314
Cdd:COG4913 487 faltllvppEHYAAALRwvnrlhlrgrLVYERVRTGLPDPERPRLDPDSlagkldfkphpfrawlEAELGRRFDYVCVDS 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1315 desqraLQQLKKKCQRLTAELQ----------DTKLHLEGQQV-------RNHELEKKQRRFDSELSQAHEETQREKLQR 1377
Cdd:COG4913 567 ------PEELRRHPRAITRAGQvkgngtrhekDDRRRIRSRYVlgfdnraKLAALEAELAELEEELAEAEERLEALEAEL 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1378 EKLQRekdmlLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDIssqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1457
Cdd:COG4913 641 DALQE-----RREALQRLAEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDEL 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1458 AGSIQMLEQAKLRLEMEMERMRQTHSkemESRDEEVEEARQSCQKKLKQmeVQLEEEYEDKQKALREKRE-LESKLSTLS 1536
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLELRALLEERFAA--ALGDAVERELRENLEERIDaLRARLNRAE 786
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082237 1537 DQVN------QRDFESEKRlrkDLKRTKALLADAQIMLDHLKNNA-PSKRE-IAQLKNQLEESEFT 1594
Cdd:COG4913 787 EELEramrafNREWPAETA---DLDADLESLPEYLALLDRLEEDGlPEYEErFKELLNENSIEFVA 849
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1273-1821 |
1.87e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.44 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1273 RAVREVDFTKKRLQQELEDKMEVEQQSRRQLERR--LGDLQADSDES----QRALQQLKKKCQRLTA------ELQDTKL 1340
Cdd:PRK04863 534 RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLesLSESVSEARERrmalRQQLEQLQARIQRLAArapawlAAQDALA 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1341 HLEGQQvrNHELEKKQRRfdSELSQAHEETQRE-KLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKV--VSLEA 1417
Cdd:PRK04863 614 RLREQS--GEEFEDSQDV--TEYMQQLLERERElTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFggVLLSE 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1418 ELQDISSQESKD-EASLAKVKKQL--RDLEAkVKDQEEELDEQAGSIQMLEQAKLRL--------EMEMERMRQTHSKEM 1486
Cdd:PRK04863 690 IYDDVSLEDAPYfSALYGPARHAIvvPDLSD-AAEQLAGLEDCPEDLYLIEGDPDSFddsvfsveELEKAVVVKIADRQW 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1487 E-SRDEEV----EEARQscqKKLKQMEVQLEEEYEDKQKALREKREL-----------------------ESKLSTLSDQ 1538
Cdd:PRK04863 769 RySRFPEVplfgRAARE---KRIEQLRAEREELAERYATLSFDVQKLqrlhqafsrfigshlavafeadpEAELRQLNRR 845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1539 VNQR-----DFES-EKRLRKDLKRTKALLADAQIMLDHLKNNAPSK--REIAQLKNQLEESEFtcAAAVKARKAMEVEme 1610
Cdd:PRK04863 846 RVELeralaDHESqEQQQRSQLEQAKEGLSALNRLLPRLNLLADETlaDRVEEIREQLDEAEE--AKRFVQQHGNALA-- 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1611 dlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE---DMNELM-KKHKAAVAQASRDMAQMNDLQAQIEESNKEK 1686
Cdd:PRK04863 922 ----QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafALTEVVqRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQA 997
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1687 QELQEKL--QALQSQVEFLEQSMVDKSLVSRQEAKireLETRLEFEKtqvkRLENLASRLKETME-KLTEERDQRAAAEN 1763
Cdd:PRK04863 998 EQERTRAreQLRQAQAQLAQYNQVLASLKSSYDAK---RQMLQELKQ----ELQDLGVPADSGAEeRARARRDELHARLS 1070
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1764 REKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEmdlESLEAANQSLQADLKLA 1821
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR---EQVVNAKAGWCAVLRLV 1125
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1149-1750 |
1.93e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.38 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1149 EEQIRNKDEEIQQLRSKLEKVEKernELRLSSDRLEtRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTq 1228
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEK---SHSITLKEIE-RLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAES- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1229 yDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYeravrevDFTKKRlqqELEDKMEVEQQSRRQLERRLG 1308
Cdd:PRK01156 264 -DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKN-------DIENKK---QILSNIDAEINKYHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1309 DLQADSDEsqraLQQLKKKCQRLTAELQDTKLHLEGQQ--VRNHELEKKQRRfdselsqahEETQREKLQREKLQREKDM 1386
Cdd:PRK01156 333 VLQKDYND----YIKKKSRYDDLNNQILELEGYEMDYNsyLKSIESLKKKIE---------EYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1387 LLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR------DL-EAKVKDQEEELDEQAG 1459
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLgEEKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1460 SiqmLEQAKLRLEMEMERM--RQTHSKEMESR--DEEVEEARQScQKKLKQMEVQLeEEYEDKQKALREKrelESKLSTL 1535
Cdd:PRK01156 480 R---LEEKIREIEIEVKDIdeKIVDLKKRKEYleSEEINKSINE-YNKIESARADL-EDIKIKINELKDK---HDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1536 SDQVNQRDFESekrlrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavKARKAMEVEMEDLHLQ 1615
Cdd:PRK01156 552 KNRYKSLKLED-----LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLE----------SRLQEIEIGFPDDKSY 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1616 IDDIAKaktALEEQLSRLQREKNEIQNrLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ- 1694
Cdd:PRK01156 617 IDKSIR---EIENEANNLNNKYNEIQE-NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDd 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082237 1695 ALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLaSRLKETMEK 1750
Cdd:PRK01156 693 AKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDL-KRLREAFDK 747
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1350-1708 |
2.13e-09 |
|
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: 62.56 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1350 HELEKKQRRFDSELSQ--AHEETQREKLQ--REKLQREKDMLLAEAFS-------LKQQMEEKDLDIAGFTQKVVS---L 1415
Cdd:pfam06160 96 DDIEEDIKQILEELDEllESEEKNREEVEelKDKYRELRKTLLANRFSygpaideLEKQLAEIEEEFSQFEELTESgdyL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1416 EAE--LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGSIQMLEQ----AKLRLEMEMERMRQTHSKEMES- 1488
Cdd:pfam06160 176 EARevLEKLEEETDALEELMEDIPPLYEELKTELPDQLEEL--KEGYREMEEEgyalEHLNVDKEIQQLEEQLEENLALl 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1489 ---RDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQ----------------------VNQRD 1543
Cdd:pfam06160 254 enlELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnkelkeelervqqsytlnenelERVRG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1544 FESE-KRLRKDLKRTKALLADAQI----MLDHLKnnapskreiaQLKNQLEEseftcaaavkarkaMEVEMEDLHLQIDD 1618
Cdd:pfam06160 334 LEKQlEELEKRYDEIVERLEEKEVayseLQEELE----------EILEQLEE--------------IEEEQEEFKESLQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1619 IAKAKTALEEQLSRLQREKNEIQNRLEEDQ-----EDMNELMKKHKAAVAQASRDMAQ----MNDLQAQIEESNKEKQEL 1689
Cdd:pfam06160 390 LRKDELEAREKLDEFKLELREIKRLVEKSNlpglpESYLDYFFDVSDEIEDLADELNEvplnMDEVNRLLDEAQDDVDTL 469
|
410
....*....|....*....
gi 1907082237 1690 QEKLQALQSQVEFLEQSMV 1708
Cdd:pfam06160 470 YEKTEELIDNATLAEQLIQ 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1073-1489 |
2.71e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1073 LARLEEQRDEQTSRHLTLFQAacRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRP-LIQVQLSEEQ 1151
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1152 IRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELT-SELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYD 1230
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1231 ALKKQMEVMEMEVMEARLIRAAEINGEV------DDDDAGGEWRLK---------------YERAVREVDFTKKRLQQEL 1289
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALlallglGGSLLSLILTIAgvlflvlgllallflLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1290 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE---LEKKQRRFDSELSQA 1366
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1367 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAgfTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-- 1444
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEed 468
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907082237 1445 -------AKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESR 1489
Cdd:COG4717 469 gelaellQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1277-1777 |
2.84e-09 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 62.45 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1277 EVDFTKKRLQQELEDKMEVEQQSRRQLerrlgdlqadsDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQ 1356
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRAR-----------IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1357 RrfdsELSQAHEETQREKLQREKLQREKDMLLAEA----FSLKQQMEEKDLDIAGFTQKVVSLEAELQDIS--------- 1423
Cdd:pfam05557 72 R----EQAELNRLKKKYLEALNKKLNEKESQLADAreviSCLKNELSELRRQIQRAELELQSTNSELEELQerldllkak 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1424 -SQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRL----EMEME----RMRQTHSKEMESRDEEVE 1494
Cdd:pfam05557 148 aSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELaripELEKElerlREHNKHLNENIENKLLLK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1495 EARQSCQKKLKQME------VQLEEEYEDKQKAL---------------------REKRELESKLSTLSDQV-------- 1539
Cdd:pfam05557 228 EEVEDLKRKLEREEkyreeaATLELEKEKLEQELqswvklaqdtglnlrspedlsRRIEQLQQREIVLKEENssltssar 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1540 ----NQRDFESEKR--------LRKDLKRTKALLADAQimldhlKNNAPSKREIAQLKNQLE--ESEFTCAAAVKARKAM 1605
Cdd:pfam05557 308 qlekARRELEQELAqylkkiedLNKKLKRHKALVRRLQ------RRVLLLTKERDGYRAILEsyDKELTMSNYSPQLLER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1606 EVEMEDLhlqIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelMKKHKAAVAQASRDMAQMNDLQAQIEESNKE 1685
Cdd:pfam05557 382 IEEAEDM---TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--ALRQQESLADPSYSKEEVDSLRRKLETLELE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1686 KQELQEKLQALQSQVEFLE----QSMVDKSLVSRQEAKIRELEtrlEFEKTQVKRLENLASRLKETMEKLTEERDQRAAA 1761
Cdd:pfam05557 457 RQRLREQKNELEMELERRClqgdYDPKKTKVLHLSMNPAAEAY---QQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRL 533
|
570
....*....|....*.
gi 1907082237 1762 ENREKEQNKRLQRQLR 1777
Cdd:pfam05557 534 PETTSTMNFKEVLDLR 549
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1510-1897 |
2.95e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.46 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1510 QLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQimldhlknnapskREIAQLKNQLE 1589
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------------EELEQLEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1590 ESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM 1669
Cdd:COG4372 70 QAR-------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1670 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETME 1749
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1750 KLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQ 1829
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1830 AAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDDG 1897
Cdd:COG4372 303 NLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1579-1760 |
3.69e-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: 59.55 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1579 REIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkh 1658
Cdd:COG1579 17 SELDRLEHRLKELP-------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1659 kaavaqasRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEKtqvKRLE 1738
Cdd:COG1579 86 --------RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE------LAELEAELAELEAELEEKK---AELD 148
|
170 180
....*....|....*....|..
gi 1907082237 1739 NLASRLKETMEKLTEERDQRAA 1760
Cdd:COG1579 149 EELAELEAELEELEAEREELAA 170
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1285-1699 |
6.41e-09 |
|
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: 61.20 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1285 LQQELEDKMEVEQQSrrqLERRLGDLQADSDESQRALQQLKkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELS 1364
Cdd:pfam05667 216 LAAAQEWEEEWNSQG---LASRLTPEEYRKRKRTKLLKRIA---EQLRSAALAGTEATSGASRSAQDLAELLSSFSGSST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1365 QAHEETQREKLQR-EKLQREKDMLLAEAFSLKQQMEEKDLDIAGfTQKVVSLEAELQDISSqeskdeaSLAKVKKQLRDL 1443
Cdd:pfam05667 290 TDTGLTKGSRFTHtEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLES-------SIQELEKEIKKL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1444 EAKVKDQEEELDEQagsiqmlEQAKLRLEMEMERMRQTHsKEMESRDEEVEEARQSCQKKLKQMeVQLEEEYEDKQKAL- 1522
Cdd:pfam05667 362 ESSIKQVEEELEEL-------KEQNEELEKQYKVKKKTL-DLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLi 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1523 REKRELESKLSTlsdqvnqRDFESEKRLR--KDLK-RTKALLADAQimldhlknnapSKRE-IAQLKNQLEE-------S 1591
Cdd:pfam05667 433 EEYRALKEAKSN-------KEDESQRKLEeiKELReKIKEVAEEAK-----------QKEElYKQLVAEYERlpkdvsrS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1592 EFTcaaavkaRKAMEVeMEDLHLQIDDIAKaktALEEQLSrLQREKNEIQNRLEEDQEDMNELM---KKHKAAVAQASRD 1668
Cdd:pfam05667 495 AYT-------RRILEI-VKNIKKQKEEITK---ILSDTKS-LQKEINSLTGKLDRTFTVTDELVfkdAKKDESVRKAYKY 562
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907082237 1669 MAQMNDLQAQ----IEESNK---EKQELQEKLQALQSQ 1699
Cdd:pfam05667 563 LAALHENCEQliqtVEETGTimrEIRDLEEQIETESGK 600
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1281-1700 |
7.76e-09 |
|
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: 61.08 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1281 TKKRLQQELEDKMEVEQQSRRQLerrlgdlqadSDESQR---ALQQLKKKCQRLT-AELQDTKLHLEGQQVRNhELEKKQ 1356
Cdd:pfam15964 301 TIERLTKERDDLMSALVSVRSSL----------AEAQQRessAYEQVKQAVQMTEeANFEKTKALIQCEQLKS-ELERQK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1357 RRFDSEL-SQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAK 1435
Cdd:pfam15964 370 ERLEKELaSQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1436 VKKQLRDLEAKVKDQEEELdeqagsiqmleqaklrlEMEMERMRQTHSKEMESRDEEVEEARQscqkKLKQMEVQLEEEY 1515
Cdd:pfam15964 450 VCGEMRYQLNQTKMKKDEA-----------------EKEHREYRTKTGRQLEIKDQEIEKLGL----ELSESKQRLEQAQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1516 EDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQLEESEFTC 1595
Cdd:pfam15964 509 QDAARAREECLKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELT------QKMQQMEAQHDKTVNEQ 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1596 AAAVKARKAMEVEMED----LHLQIDDIAKAKTALEEQLSR----LQREKNEIQNRLEEDQED------MNELMK----- 1656
Cdd:pfam15964 583 YSLLTSQNTFIAKLKEecctLAKKLEEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQcvqhgrMHERMKqrlrq 662
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907082237 1657 --KHKAAVAQasrdmaQMNDLQAQIEESNKEKQELQEKLQALQSQV 1700
Cdd:pfam15964 663 ldKHCQATAQ------QLVQLLSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1266-1705 |
8.53e-09 |
|
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: 61.12 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1266 EWRLKYERAV--REVDFTKKRLQQELEDKM-----EVEQQSRRQ--LERrlgDLQADSDESQRALQ--QLKKKCQRLTAE 1334
Cdd:COG3096 279 ERRELSERALelRRELFGARRQLAEEQYRLvemarELEELSAREsdLEQ---DYQAASDHLNLVQTalRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1335 LQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDML-------------LAEAfslKQQMEEK 1401
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqaLEKA---RALCGLP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1402 DLDIAGFTQKVVSLEAELQDISSQeskdeaslakvkkqLRDLEAKVKDQEEELDEQAGSIQMLEqaklRLEMEMERmrqt 1481
Cdd:COG3096 433 DLTPENAEDYLAAFRAKEQQATEE--------------VLELEQKLSVADAARRQFEKAYELVC----KIAGEVER---- 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1482 hSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSdqvnqrdfeseKRLRKDLkrtkall 1561
Cdd:COG3096 491 -SQAWQTARELLRRYRS--QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFC-----------QRIGQQL------- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1562 aDAQIMLDHLKnnapskreiAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID---DIAKAKTALEEQLSRLQREKN 1638
Cdd:COG3096 550 -DAAEELEELL---------AELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKelaARAPAWLAAQDALERLREQSG 619
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082237 1639 EiqnrleedqedmnelmkkhkaAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQ 1705
Cdd:COG3096 620 E---------------------ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1636-1874 |
8.53e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1636 EKNEIQNRLEEDQEDMNELMKKHKAAVaQASRdmaQMNDLQaQIEESNKEKQELQEKLQALQSQVEFLEqsmvdkslVSR 1715
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALE-DARE---QIELLE-PIRELAERYAAARERLAELEYLRAALR--------LWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1716 QEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERD----QRAAAENREKEQnkrLQRQLRDTKEEMSELARKEA 1791
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDeleaQIRGNGGDRLEQ---LEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1792 EASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMesDENEDLINSLQDMVTKYQKKKNKLE-GDSDVDS 1870
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL--AEAEAALRDLRRELRELEAEIASLErRKSNIPA 440
|
....
gi 1907082237 1871 ELED 1874
Cdd:COG4913 441 RLLA 444
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1525-1790 |
1.43e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 60.31 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1525 KRELESKLSTLSDQvnqRDFESEKrlrkdlkrtKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaAAVKARKA 1604
Cdd:PRK11281 38 EADVQAQLDALNKQ---KLLEAED---------KLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ------APAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1605 MEvEMEDlhLQIDDIAKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESN 1683
Cdd:PRK11281 100 QA-ELEA--LKDDNDEETRETLSTLsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1684 K---------------EKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELET----RLEfekTQVKRLENLAS-- 1742
Cdd:PRK11281 177 NllkggkvggkalrpsQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTariqRLE---HQLQLLQEAINsk 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1743 RLKETMEKLTEERDQRAAAEN-------REKEQNKRLQRQLRDTKEEMSELARKE 1790
Cdd:PRK11281 254 RLTLSEKTVQEAQSQDEAARIqanplvaQELEINLQLSQRLLKATEKLNTLTQQN 308
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1266-1607 |
1.54e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.14 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1266 EWRLKYE-RAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRlgdlqadsdeSQRALQQLKKKCQRltaELQDTKLHLEG 1344
Cdd:pfam17380 255 EYTVRYNgQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM----------EQERLRQEKEEKAR---EVERRRKLEEA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1345 QQVRNHELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMLLAEAFSLK-QQMEEKDLDIAGFTQKVVSLEAELQDI 1422
Cdd:pfam17380 322 EKARQAEMDRQAAIYAEQERMAMErERELERIRQEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1423 SSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQagsIQMLEQAKLRlemEMERMRQTHSKEMES----RDEEVEEARQ 1498
Cdd:pfam17380 402 RKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE---VRRLEEERAR---EMERVRLEEQERQQQverlRQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1499 SCQKKLKQMEVQLEEEY----------EDKQKALREKR-------ELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALL 1561
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQrrkilekeleERKQAMIEEERkrkllekEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907082237 1562 ADAQIMLDHLKNNAPSKREiAQLKNQLEESEftcaaavKARKAMEV 1607
Cdd:pfam17380 556 EQMRKATEERSRLEAMERE-REMMRQIVESE-------KARAEYEA 593
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1582-1846 |
1.61e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 58.78 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1582 AQLKNQLEESEFTCAAAVKARKAM-EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedmnELMKKHKA 1660
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED------ELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1661 AvaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFEKTQVK----R 1736
Cdd:pfam00038 102 E--------NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN---------HEEEVRELQAQVSDTQVNVEmdaaR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1737 LENLASRLKETMEKLTEE-RDQRAAAENREKEQNKRLQRQ-------LRDTKEEMSELarkeaeaSRKKHELEMDLESLE 1808
Cdd:pfam00038 165 KLDLTSALAEIRAQYEEIaAKNREEAEEWYQSKLEELQQAaarngdaLRSAKEEITEL-------RRTIQSLEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1809 AANQSLQA-----------DLKLAFKRIGDLQAA---IEDEMES--DENEDLIN 1846
Cdd:pfam00038 238 KQKASLERqlaeteeryelQLADYQELISELEAElqeTRQEMARqlREYQELLN 291
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1142-1545 |
2.36e-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: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1142 LIQVQLsEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgESASQLLDAETaerlRTEKE 1221
Cdd:pfam07888 31 LLQNRL-EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK---EELRQSREKHE----ELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1222 MKELQTQYDALKKQMevmemevmearliraaeingevdddDAGGEWRLKYERAVREVDFTKKRLQQ---ELEDKMEVEQQ 1298
Cdd:pfam07888 103 YKELSASSEELSEEK-------------------------DALLAQRAAHEARIRELEEDIKTLTQrvlERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1299 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETqreklqre 1378
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKE-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1379 klqrekdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQA 1458
Cdd:pfam07888 230 ----------AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1459 GSIQMlEQAKLRLEMEMERMR-QTHSKEMESRDEEVEEARQSCQKklkqMEVQLEEEYEDKQKALRE-KRELESKLSTLs 1536
Cdd:pfam07888 300 ARWAQ-ERETLQQSAEADKDRiEKLSAELQRLEERLQEERMEREK----LEVELGREKDCNRVQLSEsRRELQELKASL- 373
|
....*....
gi 1907082237 1537 dQVNQRDFE 1545
Cdd:pfam07888 374 -RVAQKEKE 381
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1156-1777 |
3.18e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 59.07 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1156 DEEIQQLRSKLEKVEKERNELRLSSDRLETRIS--ELTSELTDE-----------RNTGESASQLLDAETAERLRTEKEM 1222
Cdd:pfam10174 115 EENFRRLQSEHERQAKELFLLRKTLEEMELRIEtqKQTLGARDEsikkllemlqsKGLPKKSGEEDWERTRRIAEAEMQL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1223 KELQTQYD-------ALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgewrlKYERAVREVDFTKKRLQQELEDKMEV 1295
Cdd:pfam10174 195 GHLEVLLDqkekeniHLREELHRRNQLQPDPAKTKALQTVIEMKDTKIS-----SLERNIRDLEDEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1296 EQQSRRQLE----------RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEgqqVRNHELEKKQRRFD----- 1360
Cdd:pfam10174 270 REEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIE---VLKESLTAKEQRAAilqte 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1361 -SELSQAHEETQR------EKLQRekLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDissqesKDeasl 1433
Cdd:pfam10174 347 vDALRLRLEEKESflnkktKQLQD--LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD------KD---- 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1434 akvkKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQsCQKKLKQMEVQLEE 1513
Cdd:pfam10174 415 ----KQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKK-ENKDLKEKVSALQP 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1514 EYEDKQKALREKRELESKLST----LSDQVNQRDFESEKRlRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQL- 1588
Cdd:pfam10174 490 ELTEKESSLIDLKEHASSLASsglkKDSKLKSLEIAVEQK-KEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVa 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1589 ---EESEfTCAAAVKARKAM--EVEMEDlhlqiDDIAKAKTALEEQLSRLQREkneiQNRLEEDQEDMNELMKKHKAAVA 1663
Cdd:pfam10174 569 rykEESG-KAQAEVERLLGIlrEVENEK-----NDKDKKIAELESLTLRQMKE----QNKKVANIKHGQQEMKKKGAQLL 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1664 QASR---DMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKS--LVSRQEAKIRELETRLEF--------- 1729
Cdd:pfam10174 639 EEARrreDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghLTNLRAERRKQLEEILEMkqeallaai 718
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1730 -EK-TQVKRLENLASRLKETMEKLteerdqraAAENREKEqnkRLQRQLR 1777
Cdd:pfam10174 719 sEKdANIALLELSSSKKKKTQEEV--------MALKREKD---RLVHQLK 757
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1578-1794 |
4.05e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.87 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1578 KREIAQLKNQLEESEftcaAAVKARKAmEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedMNELMKK 1657
Cdd:COG3206 181 EEQLPELRKELEEAE----AALEEFRQ-KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1658 HKAAVAQASRDmAQMNDLQAQIEESNKEKQELQEKL-------QALQSQVEFLEQSmvdksLVSRQEAKIRELETRLEFE 1730
Cdd:COG3206 252 GPDALPELLQS-PVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-----LQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1731 KTQVKRLENLASRLKETMEKLTEERDQRAaaenrekeqnkRLQRQLRDTKEEMSELARKEAEAS 1794
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR-----------RLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1580-1877 |
5.44e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1580 EIAQLKNQLEESEFTCAAAVKARKAMEV---EMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMK 1656
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEvleEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1657 KHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL-QALQSQVEFLEQsmvdkslVSRQEAKIRELETRLEFEKTQVK 1735
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLeECRVAAQAHNEE-------AESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1736 RLEnlaSRLKETMEKLTEERDQRAAAENREKEQNKRLQR---QLRDTKEEMSELARKEAEASRKKHELEMDLESLE---A 1809
Cdd:PRK02224 367 ELE---SELEEAREAVEDRREEIEELEEEIEELRERFGDapvDLGNAEDFLEELREERDELREREAELEATLRTARervE 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082237 1810 ANQSLQADLKLA-----FKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELEDRVD 1877
Cdd:PRK02224 444 EAEALLEAGKCPecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEE 516
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1148-1821 |
6.32e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1148 SEEQIRNKDEEIQQLRSKLEKVEKERNEL----RLSSDRL------------ETRISELTSELTDERNTGESASQLLDAE 1211
Cdd:PRK04863 298 SRRQLAAEQYRLVEMARELAELNEAESDLeqdyQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1212 TAER----LRTEKEMKELQTQ-------YDALkkQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAvREVDF 1280
Cdd:PRK04863 378 QEENearaEAAEEEVDELKSQladyqqaLDVQ--QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQA-KEQEA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1281 TKKRLQqeLEDKMEVEQQSRRQLERRLGDLQ--ADSDESQRALQQLKKKCQRLTAE-LQDTKLhlegQQVRNHElekkqr 1357
Cdd:PRK04863 455 TEELLS--LEQKLSVAQAAHSQFEQAYQLVRkiAGEVSRSEAWDVARELLRRLREQrHLAEQL----QQLRMRL------ 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1358 rfdSELSQAHEETQR-EKLQREKLQREKDMLLAEAFsLKQQMEEkdldiagftqkvvsLEAELQDISSQeskdeaslakv 1436
Cdd:PRK04863 523 ---SELEQRLRQQQRaERLLAEFCKRLGKNLDDEDE-LEQLQEE--------------LEARLESLSES----------- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1437 KKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRdEEVEEARQSCQKKLKQMEVQlEEEYE 1516
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-QDVTEYMQQLLERERELTVE-RDELA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1517 dkqkalREKRELESKLSTLSdqvnQRDFESEKRLRKDLKRTKA-LLAD--AQIMLDhlknNAP----------------- 1576
Cdd:PRK04863 652 ------ARKQALDEEIERLS----QPGGSEDPRLNALAERFGGvLLSEiyDDVSLE----DAPyfsalygparhaivvpd 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1577 ---SKREIAQLKNQLEE------------------SEFTCAAAVK-----------------ARKAMEVEMEDLHLQIDD 1618
Cdd:PRK04863 718 lsdAAEQLAGLEDCPEDlyliegdpdsfddsvfsvEELEKAVVVKiadrqwrysrfpevplfGRAAREKRIEQLRAEREE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1619 IAkaktaleEQLSRLQREKNEIQnRLeedQEDMNELMKKHkAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQS 1698
Cdd:PRK04863 798 LA-------ERYATLSFDVQKLQ-RL---HQAFSRFIGSH-LAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRS 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1699 QVEFLEQSMV-------------DKSLVSRQEAkIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEnRE 1765
Cdd:PRK04863 866 QLEQAKEGLSalnrllprlnllaDETLADRVEE-IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLK-QD 943
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082237 1766 KEQNKRLQRQLRDTKEEMSEL-ARKEAEASrkkHELEMDLESLEAANQSLQADLKLA 1821
Cdd:PRK04863 944 YQQAQQTQRDAKQQAFALTEVvQRRAHFSY---EDAAEMLAKNSDLNEKLRQRLEQA 997
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1575-1770 |
8.66e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1575 APSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNEL 1654
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1655 ---MKKHKAAV-----------------------AQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV 1708
Cdd:COG3883 92 araLYRSGGSVsyldvllgsesfsdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082237 1709 D-KSLVSRQEAKIRELETRlefEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNK 1770
Cdd:COG3883 172 ElEAQQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1392-1776 |
1.05e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 57.15 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1392 FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ-------EEELDEQAGSIQML 1464
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANrfsfgpaLDELEKQLENLEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1465 -------------EQAK---LRLEMEMERMRQThskeMesrdEEVEEARQSCQKKLKQmevQLEEEYEDKQKALREKREL 1528
Cdd:PRK04778 181 fsqfveltesgdyVEAReilDQLEEELAALEQI----M----EEIPELLKELQTELPD---QLQELKAGYRELVEEGYHL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1529 ESKlstlsdqvnqrDFESE-KRLRKDLKRTKALLADAQimLDHLK-NNAPSKREIAQLKNQLEeseftcaAAVKARKAME 1606
Cdd:PRK04778 250 DHL-----------DIEKEiQDLKEQIDENLALLEELD--LDEAEeKNEEIQERIDQLYDILE-------REVKARKYVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1607 VEMEDLHLQIDDIAKAKTALEEQLSRLQ-----------------REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM 1669
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEEIDRVKqsytlneselesvrqleKQLESLEKQYDEITERIAEQEIAYSELQEELEEIL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1670 AQMNDLQAQIEESN-------KEKQELQEKLQALQSQVE----FLEQS---------MVDKSLVSRQeakIRELETRLE- 1728
Cdd:PRK04778 390 KQLEEIEKEQEKLSemlqglrKDELEAREKLERYRNKLHeikrYLEKSnlpglpedyLEMFFEVSDE---IEALAEELEe 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082237 1729 --FEKTQVKRLENLASRLKETMEKLTEE-RDQRAAAE------NREKEQNKRLQRQL 1776
Cdd:PRK04778 467 kpINMEAVNRLLEEATEDVETLEEETEElVENATLTEqliqyaNRYRSDNEEVAEAL 523
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1435-1783 |
1.61e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 56.40 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1435 KVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQaklrlememermrqthsKEMESRdEEVEEAR---QSCQKKLKQMEVQL 1511
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLE-----------------SEEKNR-EEVEELKdkyRELRKTLLANRFSY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1512 EEEYEDKQKALrekRELESKLSTLSDQVNQRDFESEK----RLRKDLKRTKALLADAQIMLDHLKNNAPskREIAQLKN- 1586
Cdd:pfam06160 145 GPAIDELEKQL---AEIEEEFSQFEELTESGDYLEARevleKLEEETDALEELMEDIPPLYEELKTELP--DQLEELKEg 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1587 --QLEESEFtcaaaVKARKAMEVEMEDLHlqiDDIAKAKTALEE-QLSRLQREKNEIQNRLEEDQEDM-------NELMK 1656
Cdd:pfam06160 220 yrEMEEEGY-----ALEHLNVDKEIQQLE---EQLEENLALLENlELDEAEEALEEIEERIDQLYDLLekevdakKYVEK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1657 KHKAAVAQASRDMAQMNDLQAQIEESNK----------EKQELQEKLQALQSQVEFLEQSMVDKSLV-SRQEAKIRELET 1725
Cdd:pfam06160 292 NLPEIEDYLEHAEEQNKELKEELERVQQsytlneneleRVRGLEKQLEELEKRYDEIVERLEEKEVAySELQEELEEILE 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 1726 RLE-FEKTQVKrlenlasrLKETMEKLTEErdqraaaENREKEQNKRLQRQLRDTKEEM 1783
Cdd:pfam06160 372 QLEeIEEEQEE--------FKESLQSLRKD-------ELEAREKLDEFKLELREIKRLV 415
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1519-1695 |
1.65e-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: 54.55 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1519 QKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESEFTCAAA 1598
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELE-DELAALEARLEAAKTELEDLEKEIKRLEL------EIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1599 VKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdmaqmnDLQ 1676
Cdd:COG1579 86 RNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA----------ELE 155
|
170
....*....|....*....
gi 1907082237 1677 AQIEESNKEKQELQEKLQA 1695
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1315-1529 |
1.66e-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: 54.28 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1315 DESQRALQQLKK----KCQRLTAELQDTKLHLEGQQVRNHELEKKqrrfdselSQAHEETQREKlqreklQREKDMLLAE 1390
Cdd:pfam15665 10 DEHEAEIQALKEaheeEIQQILAETREKILQYKSKIGEELDLKRR--------IQTLEESLEQH------ERMKRQALTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1391 AFSLKQQMEEKDL-DIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL-RDLEAKVKDQEEELDEQAGSIQMLEQAK 1468
Cdd:pfam15665 76 FEQYKRRVEERELkAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFeQEKRKALEELRAKHRQEIQELLTTQRAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1469 LRLEM-EMERMRQTHSKEMESRDEEVEEarqscqkkLKQMEVQLEEEYEDK---QKALREkRELE 1529
Cdd:pfam15665 156 SASSLaEQEKLEELHKAELESLRKEVED--------LRKEKKKLAEEYEQKlskAQAFYE-RELE 211
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1417-1600 |
2.61e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.79 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1417 AELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMER------MRQTH------SK 1484
Cdd:PHA02562 216 ARKQNKYDELVEEAKTI---KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQfqkvikMYEKGgvcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1485 EMESRDEEVEEARQS---CQKKLKQMEVQLEEEYE---DKQKALREKRELESKLSTLsDQVNQRDFESEKRLRKDLKRTK 1558
Cdd:PHA02562 293 QISEGPDRITKIKDKlkeLQHSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTN-KQSLITLVDKAKKVKAAIEELQ 371
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907082237 1559 ALLADaqimldhlknnapSKREIAQLKNQLEESEFTCAAAVK 1600
Cdd:PHA02562 372 AEFVD-------------NAEELAKLQDELDKIVKTKSELVK 400
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1440-1790 |
2.65e-07 |
|
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: 54.92 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1440 LRDLEAKV------KDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEE-VEEARQSCQKKLKQMEVQLE 1512
Cdd:pfam13868 8 LRELNSKLlaakcnKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEErKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1513 EEYEDKQKALREKRELesklstLSDQVNQRDFESEKRLRKDLKRTKAlladaqimldhlknnapsKREIAQLKNQLEese 1592
Cdd:pfam13868 88 KRQEEYEEKLQEREQM------DEIVERIQEEDQAEAEEKLEKQRQL------------------REEIDEFNEEQA--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1593 ftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQ----REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRD 1668
Cdd:pfam13868 141 -------EWKELEKEEEREEDERILEYLKEKAEREEEREAEReeieEEKEREIARLRAQQEKAQDEKAERDELRAKLYQE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1669 MAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV-----DKSLVSRQEAKIRELEtRLEFEKTQVKRLENLasR 1743
Cdd:pfam13868 214 EQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAeeaerEEEEFERMLRKQAEDE-EIEQEEAEKRRMKRL--E 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907082237 1744 LKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKE 1790
Cdd:pfam13868 291 HRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1150-1880 |
2.74e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 56.38 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1150 EQIRNKDEEIQQLRSKLEKVEKER------NELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAeRLRTEKEMK 1223
Cdd:PTZ00440 1190 EEIESYKKDIDQVKKNMSKERNDHlttfeyNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEI-KLQVFSYLQ 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1224 ELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEwrlKYER-AVREVDFTKkRLQQELEDKMEVEQQSRRQ 1302
Cdd:PTZ00440 1269 QVIKENNKMENALHEIKNMYEFLISIDSEKILKEILNSTKKAE---EFSNdAKKELEKTD-NLIKQVEAKIEQAKEHKNK 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1303 LERRLGDLQADSDesqraLQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAH------------EET 1370
Cdd:PTZ00440 1345 IYGSLEDKQIDDE-----IKKIEQIKEEISNKRKEINKYLS-------NIKSNKEKCDLHVRNASrgkdkidflnkhEAI 1412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1371 QREKLQREKLQREKDML------LAEAFSLKQQMEEKDLDIAGFTQKVVSLeaeLQD--ISSQESKDEaslaKVKKQLRD 1442
Cdd:PTZ00440 1413 EPSNSKEVNIIKITDNInkckqySNEAMETENKADENNDSIIKYEKEITNI---LNNssILGKKTKLE----KKKKEATN 1485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1443 LEAKVKDQEEELDEQAGSIQmleqaklrlememERMRQTHSKEMESRDEEV------EEARQSCQKKLKQMEVQLEEEYE 1516
Cdd:PTZ00440 1486 IMDDINGEHSIIKTKLTKSS-------------EKLNQLNEQPNIKREGDVlnndksTIAYETIQYNLGRVKHNLLNILN 1552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1517 DKQKA---LREKRELESKLSTLSDQVNQRDFES-EKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEES- 1591
Cdd:PTZ00440 1553 IKDEIetiLNKAQDLMRDISKISKIVENKNLENlNDKEADYVKYLDNILKEKQLMEAEYKKLNEIYSDVDNIEKELKKHk 1632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1592 --------EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL-------EEQLSRLQREKNEIQNRLEEDQEDMNELMK 1656
Cdd:PTZ00440 1633 knyeigllEKVIEINKNIKLYMDSTKESLNSLVNNFSSLFNNFylnkyniNENLEKYKKKLNEIYNEFMESYNIIQEKMK 1712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1657 KhkaavaqASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsMVDKSLVSRQEAKIRELETRLEFEKTQVKR 1736
Cdd:PTZ00440 1713 E-------VSNDDVDYNEAKTLREEAQKEEVNLNNKEEEAKKYLNDIKK-QESFRFILYMKEKLDELSKMCKQQYNIVDE 1784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1737 LENLASRLKETMEKLTEErDQRAAAENREKEQNKRLQRQLRDT-KEE-------------------MSELARKE--AEAS 1794
Cdd:PTZ00440 1785 GYNYIKKKIEYIKTLNDE-NNLSDSLNQAEDKNKEVANLTHYTnKNEaknllghvvksanfigikiMTGLQPTEltPDAS 1863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1795 RKK-------HELEMDLESLEAANQSLQAD---------------LKLAF---KRIGDLQAAIEDEMESDENEDLINSLQ 1849
Cdd:PTZ00440 1864 LETapeltfeSENNSDLELDHLSSNKNELDvykniqdayksslqiLKYSDdidKKQRDCNKLVEDGNEIYLKSTAINELK 1943
|
810 820 830
....*....|....*....|....*....|.
gi 1907082237 1850 DMVTKYQKKKNKLEGDSDVDSELEDRVDGVK 1880
Cdd:PTZ00440 1944 NMINSVKNKESAISNKIDNVSNKLSELNKIT 1974
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1430-1792 |
3.58e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1430 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQ----AKLRLEMEMERMRQThskemesrdeeveEARQSCQKKLK 1505
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQdyqaASDHLNLVQTALRQQ-------------EKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1506 QMEVQLEEEYEDKQKALREKRELESKLSTLSDQVnqrdfesekrlrkdlKRTKALLADAQIMLDHLKnnapsKREIA--Q 1583
Cdd:PRK04863 359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEV---------------DELKSQLADYQQALDVQQ-----TRAIQyqQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1584 LKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQreknEIQNRLEEdqedmneLMKKHKAAVA 1663
Cdd:PRK04863 419 AVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ----AAHSQFEQ-------AYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1664 QASRDMAQmNDLQAQIEESNKEKQELQeKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASR 1743
Cdd:PRK04863 488 EVSRSEAW-DVARELLRRLREQRHLAE-QLQQLRMRLSELEQ---RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907082237 1744 LKETMEKLTEErdQRAAAENREkeqnkRLQRQLRDTKEEMSELARKEAE 1792
Cdd:PRK04863 563 LEARLESLSES--VSEARERRM-----ALRQQLEQLQARIQRLAARAPA 604
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1501-1875 |
5.05e-07 |
|
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: 54.96 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1501 QKKLKQMEVQ-LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLR--KDLKRTKALLadaQIMLDHLKNNAPS 1577
Cdd:COG5185 165 FGKLTQELNQnLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGseSTLLEKAKEI---INIEEALKGFQDP 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1578 KREIAQLKNQLEESEFtcaaAVKARKamEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE-----DQEDMN 1652
Cdd:COG5185 242 ESELEDLAQTSDKLEK----LVEQNT--DLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSidikkATESLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1653 ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqSMVDKSLVSRQEAKIRELETRLEFEKT 1732
Cdd:COG5185 316 EQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIE----NIVGEVELSKSSEELDSFKDTIESTKE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1733 ----QVKRLENLASRLKETMEKLTEERDQraaaenrekeQNKRLQRQLRDTKEEMSELARK--EAEASRKKHELEMDLES 1806
Cdd:COG5185 392 sldeIPQNQRGYAQEILATLEDTLKAADR----------QIEELQRQIEQATSSNEEVSKLlnELISELNKVMREADEES 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1807 LE-------AANQSLQADLKLAFKRIGDLQAAI-----EDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELED 1874
Cdd:COG5185 462 QSrleeaydEINRSVRSKKEDLNEELTQIESRVstlkaTLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
.
gi 1907082237 1875 R 1875
Cdd:COG5185 542 E 542
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1149-1646 |
7.71e-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: 54.44 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1149 EEQIRNKDEEIQQLRSKLEKVEKERNE-------LRLSSDRLETRISELTSELTderntgesasqlldaetaerlRTEKE 1221
Cdd:pfam10174 246 ERNIRDLEDEVQMLKTNGLLHTEDREEeikqmevYKSHSKFMKNKIDQLKQELS---------------------KKESE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1222 MKELQTQYDALK------KQMEVMEMEVMEARLIRAAEINGEVDdddaggEWRLKYERAVREVDFTKKRLQQELEDK--- 1292
Cdd:pfam10174 305 LLALQTKLETLTnqnsdcKQHIEVLKESLTAKEQRAAILQTEVD------ALRLRLEEKESFLNKKTKQLQDLTEEKstl 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1293 ----------MEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHL--------EGQQV-----RN 1349
Cdd:pfam10174 379 ageirdlkdmLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALttleealsEKERIierlkEQ 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1350 HELEKKQRRFDSELSQAHEETQREK---LQREKLQREKDM--LLAEAFSLKQQMEEKD-----LDIAGFTQK--VVSLEA 1417
Cdd:pfam10174 459 REREDRERLEELESLKKENKDLKEKvsaLQPELTEKESSLidLKEHASSLASSGLKKDsklksLEIAVEQKKeeCSKLEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1418 ELQDISSQESKDEASlAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAkLRlEMEMERmrqtHSKEMESRDEEVEEAR 1497
Cdd:pfam10174 539 QLKKAHNAEEAVRTN-PEINDRIRLLEQEVARYKEESGKAQAEVERLLGI-LR-EVENEK----NDKDKKIAELESLTLR 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1498 QSCQKKLKQMEVQLEEEyEDKQKALREKRELESKLSTLSDQVNQRDFE----SEKRLRKDLKRTKALLADAQIMLD---- 1569
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQ-EMKKKGAQLLEEARRREDNLADNSQQLQLEelmgALEKTRQELDATKARLSSTQQSLAekdg 690
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082237 1570 HLKNNAPSKREiaQLKNQLEESEFTCAAAVKARKAMEVEMEdlhlqIDDIAKAKTAleEQLSRLQREKNEIQNRLEE 1646
Cdd:pfam10174 691 HLTNLRAERRK--QLEEILEMKQEALLAAISEKDANIALLE-----LSSSKKKKTQ--EEVMALKREKDRLVHQLKQ 758
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1486-1699 |
8.36e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1486 MESRDEEVEEARQSCQKKLKQMEVQLEEeyedKQKALREKRElESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQ 1565
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQ-KNGLVDLSEEAKLLL-QQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1566 IMLDHLKNNAPSKRE----------IAQLKNQLEESEFTCAAAVK-------ARKAMEVEMEDLHLQIDD-IAKAKTALE 1627
Cdd:COG3206 240 ARLAALRAQLGSGPDalpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQeAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082237 1628 EQLSRLQREKNEIQNRLEEdqedmnelmkkHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1699
Cdd:COG3206 320 AELEALQAREASLQAQLAQ-----------LEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1579-1863 |
8.64e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.36 E-value: 8.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1579 REIAQlKNQLEESEFTCAAAVKARKAMEVEMEDLHLQiddiakaktaLEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1658
Cdd:pfam17380 310 REVER-RRKLEEAEKARQAEMDRQAAIYAEQERMAME----------RERELERIRQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1659 KAAVAQASRdmaQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLE 1738
Cdd:pfam17380 379 ELERLQMER---QQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1739 NLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKE-EMSELARKEAEASRKKHELEMDLESLEAANQSLQAd 1817
Cdd:pfam17380 456 QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEkELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER- 534
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907082237 1818 lklafKRIGDLQAAIEDEMESDENedlinsLQDMVTKYQKKKNKLE 1863
Cdd:pfam17380 535 -----RREAEEERRKQQEMEERRR------IQEQMRKATEERSRLE 569
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1144-1837 |
1.09e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1144 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNEL------------RLSSDRLETRISELTSELTDERNTGESASQllDAE 1211
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqALEKARALCGLPDLTPENAEDYLAAFRAKE--QQA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1212 TAERLRTEKEM---KELQTQYDAlkkqmevmemevmEARLIRAaeINGEVDDDDAggewrlkYERAvREVdftkkrLQQE 1288
Cdd:COG3096 454 TEEVLELEQKLsvaDAARRQFEK-------------AYELVCK--IAGEVERSQA-------WQTA-REL------LRRY 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1289 LEDKMEVEQQSrrQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhlegqqvrNHELEKKQRRFDSELSQAHE 1368
Cdd:COG3096 505 RSQQALAQRLQ--QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-----------AEELEELLAELEAQLEELEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1369 ETQREKLQREKLQREKDMLLAEAFSLKQQmeekdldiAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK 1448
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAAR--------APAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREAT 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1449 DQEEEldeqagsiqmLEQAKLRLEMEMERMRQTHSkemesrdeeVEEARqscqkkLKQME-----VQLEEEYEDkqKALR 1523
Cdd:COG3096 644 VERDE----------LAARKQALESQIERLSQPGG---------AEDPR------LLALAerlggVLLSEIYDD--VTLE 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1524 EKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKRE-----IAQLKN-QLEESEFTcAA 1597
Cdd:COG3096 697 DAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEGDPDSFDDSVFDAEEledavVVKLSDrQWRYSRFP-EV 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1598 AVKARKAMEVEMEDLHLQIDDIAK--AKTAL----------------------------EEQLSRLQREKNEIQNRLEED 1647
Cdd:COG3096 776 PLFGRAAREKRLEELRAERDELAEqyAKASFdvqklqrlhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQH 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1648 QEDmnelMKKHKAAVAQASRDMAQMNDLQAQIEESNKEkqELQEKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRL 1727
Cdd:COG3096 856 RAQ----EQQLRQQLDQLKEQLQLLNKLLPQANLLADE--TLADRLEELREELDAAQE---AQAFIQQHGKALAQLEPLV 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1728 ----------EFEKTQVKRLENLASRLKETMEKLTEERDQRAA----------AENRekEQNKRLQRQLRDTKEEMSElA 1787
Cdd:COG3096 927 avlqsdpeqfEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyedavgllGENS--DLNEKLRARLEQAEEARRE-A 1003
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1788 RKEAEASRKKHE----LEMDLES-LEAANQSLQAdlklAFKRIGDLQAAIEDEME 1837
Cdd:COG3096 1004 REQLRQAQAQYSqynqVLASLKSsRDAKQQTLQE----LEQELEELGVQADAEAE 1054
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1469-1819 |
1.35e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 53.70 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1469 LRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQmevQLEEEYEDKQKALrekrELESKLSTLSDqvnqrdfESEK 1548
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKK---EIDLEYTEAVIAM----GLQERLENLRE-------EFSK 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1549 RLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavkarkamevemedlhlQIDDIAKAKTALEE 1628
Cdd:PLN03229 498 ANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLD-------------------------MLNEFSRAKALSEK 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1629 QlSRLQREKNEIQNRLEE--DQEDMNELMKKHKAAVAQ--ASRDMAQMNDLQAQIEESNKEKQ-ELQEKLQALQSQVEFL 1703
Cdd:PLN03229 553 K-SKAEKLKAEINKKFKEvmDRPEIKEKMEALKAEVASsgASSGDELDDDLKEKVEKMKKEIElELAGVLKSMGLEVIGV 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1704 EQsmvdKSLVSRQEAKIRELETRLEFEKTQV-KRLENL--ASRLKETMEKLTEERDQRAAAEN-REKEQNKRLQRQLRDT 1779
Cdd:PLN03229 632 TK----KNKDTAEQTPPPNLQEKIESLNEEInKKIERVirSSDLKSKIELLKLEVAKASKTPDvTEKEKIEALEQQIKQK 707
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907082237 1780 -KEEMSELARKEaeasrKKHELEMDLESLEAANQSLQADLK 1819
Cdd:PLN03229 708 iAEALNSSELKE-----KFEELEAELAAARETAAESNGSLK 743
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1351-1888 |
1.62e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.90 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1351 ELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMLLAEAFSLKQQME---EKDLD--IAGFTQKVVSLEAELQDISS 1424
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKIQNmETATVELHLSNIENKKNELLDIIVEIKKHIHgeiNKDLNkiLEDFKNKEKELSNKINDYAK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1425 ---QESKDEASLAKVKKQLRDLEA--KVKDQE-----EELDEQAGSIQMLEQAKLRLEMEMERMRQthskEMESRDEEVE 1494
Cdd:TIGR01612 777 ekdELNKYKSKISEIKNHYNDQINidNIKDEDakqnyDKSKEYIKTISIKEDEIFKIINEMKFMKD----DFLNKVDKFI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1495 EARQSCQKKLKQMEVQLEE-------EYEDKQKALREKRELESKlsTLSDQVNqRDFESEKRLRKDLKRTKALLADAqim 1567
Cdd:TIGR01612 853 NFENNCKEKIDSEHEQFAEltnkikaEISDDKLNDYEKKFNDSK--SLINEIN-KSIEEEYQNINTLKKVDEYIKIC--- 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1568 ldhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDlhlQIDD-IAKAKTALEEQLSRLQREKNEIQNrlee 1646
Cdd:TIGR01612 927 ----ENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKD---KFDNtLIDKINELDKAFKDASLNDYEAKN---- 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1647 dqedmNELMKKHKAAVAQASRDmaQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmVDKSLVSRQEAKIRELETR 1726
Cdd:TIGR01612 996 -----NELIKYFNDLKANLGKN--KENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIA-IHTSIYNIIDEIEKEIGKN 1067
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1727 LEFEKTQV-KRLENLASRLKETMEKLT---------EERDQRAAAENREKEQNKRLQRQLRDTKEEMSELarkeaeasRK 1796
Cdd:TIGR01612 1068 IELLNKEIlEEAEINITNFNEIKEKLKhynfddfgkEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI--------KK 1139
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1797 KHELEMDleslEAANQslqadlklafkrIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELEdRV 1876
Cdd:TIGR01612 1140 KSENYID----EIKAQ------------INDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIA-EI 1202
|
570
....*....|..
gi 1907082237 1877 DGVKSWLSKNKG 1888
Cdd:TIGR01612 1203 EKDKTSLEEVKG 1214
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1156-1457 |
2.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1156 DEEIQQLRSKLEKVEKERNELRLSSDRLEtrisELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQ 1235
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1236 MEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMeveqqsrRQLERRLGDLQADSD 1315
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAM-------RAFNREWPAETADLD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1316 ESQRALQQLKKKCQRLTAElqdtklHLEGQQVRNHELEKKQ-----RRFDSELSQAHEETqreklqREKLQREKDMLLAE 1390
Cdd:COG4913 809 ADLESLPEYLALLDRLEED------GLPEYEERFKELLNENsiefvADLLSKLRRAIREI------KERIDPLNDSLKRI 876
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082237 1391 AFS----LKQQMEE-KDLDIAGFTQkvvsleaELQDISSQESKDEASLAKVK-KQLRDLEAKVKDQEEELDEQ 1457
Cdd:COG4913 877 PFGpgryLRLEARPrPDPEVREFRQ-------ELRAVTSGASLFDEELSEARfAALKRLIERLRSEEEESDRR 942
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1150-1575 |
2.23e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1150 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESAsqlldaeTAERLRTEKEMKELQTQY 1229
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA-------PVDLGNAEDFLEELREER 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1230 DALKKQMEVMEMEVMEAR-LIRAAEingevddddaggewRLKYERAVREVDftkkrlqQELEDKMEVEQQSRRqlERRLG 1308
Cdd:PRK02224 422 DELREREAELEATLRTAReRVEEAE--------------ALLEAGKCPECG-------QPVEGSPHVETIEED--RERVE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1309 DLQADSDESQRALQQLKKKCQRLTaELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLL 1388
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIE-------RLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1389 AEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESkdeaSLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAK 1468
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE----SLERIRTLLAAIADAEDEIERLREKREALAELNDERR 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1469 LRLEMEMERMRQTHSKEMESRdeeVEEARQScqkklKQMEVQLEEEYEDKQKALREKR-ELESKLSTLsdqvnQRDFESE 1547
Cdd:PRK02224 627 ERLAEKRERKRELEAEFDEAR---IEEARED-----KERAEEYLEQVEEKLDELREERdDLQAEIGAV-----ENELEEL 693
|
410 420
....*....|....*....|....*...
gi 1907082237 1548 KRLRKDLKRtkalLADAQIMLDHLKNNA 1575
Cdd:PRK02224 694 EELRERREA----LENRVEALEALYDEA 717
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1290-1712 |
2.55e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1290 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKkkcqRLTAelqdTKLHLEGQQVRNHELEKKQRR---FDSELSQA 1366
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFS----RFIG----SHLAVAFEADPEAELRQLNRRrveLERALADH 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1367 HEETQREKLQREKLQREKDML--LAEAFSLkqqmeekdLDIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLrdle 1444
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALnrLLPRLNL--------LADETLADRVEEIREQLD----EAEEAKRFVQQHGNAL---- 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1445 akvkdqeEELDEQAGSIQMLEQaklrlemEMERMRQthskemesrdeEVEEARQScQKKLKQ--------MEVQLEEEYE 1516
Cdd:PRK04863 921 -------AQLEPIVSVLQSDPE-------QFEQLKQ-----------DYQQAQQT-QRDAKQqafaltevVQRRAHFSYE 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1517 DKQKALREKRELESKLSTLSDQVNQ-RDfesekRLRKDLKRTKALLADAQIMLDHLKNNAPSKREI-AQLKNQLEesEFT 1594
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQeRT-----RAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMlQELKQELQ--DLG 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1595 CAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA--QASRDMAQM 1672
Cdd:PRK04863 1048 VPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwCAVLRLVKD 1127
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907082237 1673 NDLqaqieesnkEKQELQEKLQALQSQVeflEQSMVDKSL 1712
Cdd:PRK04863 1128 NGV---------ERRLHRRELAYLSADE---LRSMSDKAL 1155
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1362-1552 |
2.90e-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: 50.69 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1362 ELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQlR 1441
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1442 DLEAKVKdqeeELDEQAGSIQMLEQAKLRLEMEMERMRqthskemesrdEEVEEARQSCQKKLKQMEvQLEEEYEDKQKA 1521
Cdd:COG1579 90 EYEALQK----EIESLKRRISDLEDEILELMERIEELE-----------EELAELEAELAELEAELE-EKKAELDEELAE 153
|
170 180 190
....*....|....*....|....*....|..
gi 1907082237 1522 LREKRE-LESKLSTLSDQVNQRDFESEKRLRK 1552
Cdd:COG1579 154 LEAELEeLEAEREELAAKIPPELLALYERIRK 185
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1288-1663 |
3.02e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1288 ELEDKMEVEQQSRRQLERRLGDLQADSDESQRA----LQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSEL 1363
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKalfeLDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1364 SQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEkdldiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDL 1443
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1444 EAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEearqscqKKLKQMEVQLEEEYEDKQKALR 1523
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE-------KLIESLPRELAEELLEAKDSLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1524 EKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARK 1603
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1604 AMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1663
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1301-1457 |
3.26e-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: 50.69 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1301 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLhlegqQVRNHELEKKQrrfdselSQAHEETQREKLQREKL 1380
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK-----EIKRLELEIEE-------VEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082237 1381 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1457
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1410-1695 |
4.02e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1410 QKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQmleqaKLRLEMemermrQTHSKEMESR 1489
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK-----ELREEA------QELREKRDEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1490 DEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQVNQ---------RDFESEKRLRKDLKRTKAL 1560
Cdd:COG1340 70 NEKVKELKEERDELNEKLN-ELREELDELRKELAELNKAGGSIDKLRKEIERlewrqqtevLSPEEEKELVEKIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1561 LADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEI 1640
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADEL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1641 QNRLEEDQEDMNELMKKHKAAvaqasRDMAQMNDLQAQIEESNKEKQELQEKLQA 1695
Cdd:COG1340 229 HEEIIELQKELRELRKELKKL-----RKKQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1371-1561 |
4.03e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1371 QREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQK--VVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK 1448
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1449 DQEEELDE---------QAGSIQMLEQAKLRLEMEMERMRQTHSKE---MESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1516
Cdd:COG3206 244 ALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082237 1517 DKQKALREKRELESKLSTLSDQVNQRDFESEkRLRKDLKRTKALL 1561
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELR-RLEREVEVARELY 367
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1427-1552 |
4.38e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.07 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1427 SKDEASLAKVkkqLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthskemESRDEEVEEARQSCQKKLKQ 1506
Cdd:COG1193 510 GEESIDVEKL---IEELERERRELEEEREEAERLREELEKLREELEEKLEELE-------EEKEEILEKAREEAEEILRE 579
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907082237 1507 MEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRK 1552
Cdd:COG1193 580 ARKEAEElirELREAQAEEEELKEARKKLEELKQELEEKLEKPKKKAKP 628
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1297-1630 |
4.48e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1297 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQ 1376
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1377 REKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR-----DLEAKVKDQE 1451
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1452 EELDEQAGSIQMLEQAKLRLEMEMERMRQTHS--KEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELE 1529
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1530 SKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEM 1609
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
|
330 340
....*....|....*....|.
gi 1907082237 1610 EDLHLQIDDIAKAKTALEEQL 1630
Cdd:COG4372 350 LLDNDVLELLSKGAEAGVADG 370
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1149-1818 |
5.87e-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: 51.88 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1149 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQ 1228
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1229 YDALKKQMEVMEMEVmeARLIRAAEINGE-VDDDDAGGEWRLKYERAVREVDFTKKRLQQEledKMEVEQQSRRQLerrl 1307
Cdd:COG3096 594 IKELAARAPAWLAAQ--DALERLREQSGEaLADSQEVTAAMQQLLEREREATVERDELAAR---KQALESQIERLS---- 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1308 gdlQADSDESQRaLQQLkkkCQRLTAEL-----QDTKLH-------LEGQQ-----VRNHELEKKQ-------------- 1356
Cdd:COG3096 665 ---QPGGAEDPR-LLAL---AERLGGVLlseiyDDVTLEdapyfsaLYGPArhaivVPDLSAVKEQlagledcpedlyli 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1357 ----RRFDSELSQAHEETQREKLQREKLQ----------------REK--DMLLAEAFSLKQQMEEKDLDIagftQKVVS 1414
Cdd:COG3096 738 egdpDSFDDSVFDAEELEDAVVVKLSDRQwrysrfpevplfgraaREKrlEELRAERDELAEQYAKASFDV----QKLQR 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1415 LEAELQDISSQ------ESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAgsiQMLEQAKLRLEMEMERMRQTHSKEMES 1488
Cdd:COG3096 814 LHQAFSQFVGGhlavafAPDPEAELAALRQRRSELERELAQHRAQEQQLR---QQLDQLKEQLQLLNKLLPQANLLADET 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1489 RDEEVEEARqscqkklkqmevqleEEYEDKQKALREKRELESKLSTLSDQVN--QRDFESEKRLRKDLKRTKALLADAQI 1566
Cdd:COG3096 891 LADRLEELR---------------EELDAAQEAQAFIQQHGKALAQLEPLVAvlQSDPEQFEQLQADYLQAKEQQRRLKQ 955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1567 MLDHLKNnapskreiaqlknqleeseftcaaaVKARKAmevemedlHLQIDDIAKaktaleeqlsrlqrekneiqnRLEE 1646
Cdd:COG3096 956 QIFALSE-------------------------VVQRRP--------HFSYEDAVG---------------------LLGE 981
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1647 DQeDMNELMKkHKAAVAQASRDMA--QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA 1718
Cdd:COG3096 982 NS-DLNEKLR-ARLEQAEEARREAreQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqADAEAEERARI 1059
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1719 KIRELETRL--------EFEKTQVKR---LENLASRLKETMEKLTEERDQRAAAenreKEQNKRLQRQLRDTKEE----M 1783
Cdd:COG3096 1060 RRDELHEELsqnrsrrsQLEKQLTRCeaeMDSLQKRLRKAERDYKQEREQVVQA----KAGWCAVLRLARDNDVErrlhR 1135
|
730 740 750
....*....|....*....|....*....|....*
gi 1907082237 1784 SELARKEAEASRkkhelEMDLESLEAANQSlQADL 1818
Cdd:COG3096 1136 RELAYLSADELR-----SMSDKALGALRLA-VADN 1164
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1435-1590 |
6.17e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1435 KVKKQLRDLEAKVKDQEEELDEQAGSIQmlEQAKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEE 1514
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKL----EKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1515 YEDKQKALREKRELESKLSTLSDQVNQRDFESEK---RLRKDLKRTKALLAD--AQIMLDHLKNNApsKREIAQLKNQLE 1589
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEElieEQLQELERISGLTAEeaKEILLEKVEEEA--RHEAAVLIKEIE 179
|
.
gi 1907082237 1590 E 1590
Cdd:PRK12704 180 E 180
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1430-1790 |
6.33e-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: 51.88 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1430 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQ----AKLRLEMEMERMRQThsKEMESRDEEVEEArqscQKKLK 1505
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQdyqaASDHLNLVQTALRQQ--EKIERYQEDLEEL----TERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1506 QMEVQLEEEYEDKQKAlREKRElesklstlsdqvnqrdfesekRLRKDLKRTKALLADAQIMLDHLKNNAPSKReiaQLK 1585
Cdd:COG3096 365 EQEEVVEEAAEQLAEA-EARLE---------------------AAEEEVDSLKSQLADYQQALDVQQTRAIQYQ---QAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1586 NQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEedqedmneLMKKHKAAV-AQ 1664
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE--------LVCKIAGEVeRS 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1665 ASRDMAQmndlqaQIEESNKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELEtrlEFEKTQVKRLENlASRL 1744
Cdd:COG3096 492 QAWQTAR------ELLRRYRSQQALAQRLQQLRAQLAELEQ------RLRQQQNAERLLE---EFCQRIGQQLDA-AEEL 555
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907082237 1745 KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKE 1790
Cdd:COG3096 556 EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1545-1844 |
7.69e-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: 50.58 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1545 ESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMevemedlhlqiddiAKAKT 1624
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSL--------------SASVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1625 ALEEQLSRLQREKNEIQNRLEED--QEDMN----ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQS 1698
Cdd:pfam15905 126 SLEKQLLELTRVNELLKAKFSEDgtQKKMSslsmELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1699 QVEFLEQSMVDkslvsrqeakireletrlefEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD 1778
Cdd:pfam15905 206 KLVSTEKEKIE--------------------EKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQS 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082237 1779 TKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKlafKRIGDLQAAIedEMESDENEDL 1844
Cdd:pfam15905 266 LEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN---AELEELKEKL--TLEEQEHQKL 326
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1210-1458 |
7.97e-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: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1210 AETAERLRTEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDDDDaggewrlkyeravREVDFTKKRLqQEL 1289
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK--------EEKALLKQLAALE-------------RRIAALARRI-RAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1290 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLtAELQDTKLHLEGQQVRnhELEKKQRRFDSELSQAHEE 1369
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1370 TQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1449
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
....*....
gi 1907082237 1450 QEEELDEQA 1458
Cdd:COG4942 232 LEAEAAAAA 240
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
442-577 |
9.56e-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: 51.28 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 442 LLEAFGNSPTIMNGSATRFSQILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEA------TFNVFYYLLACGD 510
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 511 A-----TLRTELHLNHL----------AENNVFGIVplSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYH 575
Cdd:cd14894 335 AfpfmrLLAKELHLDGIdcsaltylgrSDHKLAGFV--SKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLW 412
|
..
gi 1907082237 576 LG 577
Cdd:cd14894 413 LG 414
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1491-1799 |
1.24e-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: 50.34 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1491 EEVEEARQSCQKKLKQMEvQLEEEYED--------KQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRtkallA 1562
Cdd:COG5185 232 EEALKGFQDPESELEDLA-QTSDKLEKlveqntdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKS-----I 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1563 DAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaAAVKARKA-MEVEMEDLHLQIDDIAKAKTAL--EEQLSRLQREKNE 1639
Cdd:COG5185 306 DIKKATESLEEQLAAAEAEQELEESKRETE----TGIQNLTAeIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1640 IQNRLE----EDQEDMNELMKKHKAAVAQASRDMA----QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKS 1711
Cdd:COG5185 382 FKDTIEstkeSLDEIPQNQRGYAQEILATLEDTLKaadrQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEES 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1712 LVSRQEAK---IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELAR 1788
Cdd:COG5185 462 QSRLEEAYdeiNRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
330
....*....|.
gi 1907082237 1789 KEAEASRKKHE 1799
Cdd:COG5185 542 ENLIPASELIQ 552
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1491-1809 |
1.26e-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: 50.45 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1491 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDF----------ESEKRLRKDLKRTKAL 1560
Cdd:pfam15070 18 ENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAeeeqppagpsEEEQRLQEEAEQLQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1561 LADAQIML-DHLKNNAPSKREIAQLKNQLEESEFTC---AAAVKARKAMeveMEDLHLQIDDIAKAKT---ALEEQLSRL 1633
Cdd:pfam15070 98 LEALAGQLqAQVQDNEQLSRLNQEQEQRLLELERAAerwGEQAEDRKQI---LEDMQSDRATISRALSqnrELKEQLAEL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1634 Q-------REKNEIQNRLEEDQEDMNELMKKhkaaVAQASRDMAQMNDlqaQIEESNKEKQELQEK----LQALQSQVEF 1702
Cdd:pfam15070 175 QngfvkltNENMELTSALQSEQHVKKELAKK----LGQLQEELGELKE---TLELKSQEAQSLQEQrdqyLAHLQQYVAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1703 LEQSMVDKSLVSRQEAKIRELETRLEFEKTQVK-RLENLASRLKETMEKLTeerdqrAAAenrekEQNKRLQRQLRDTKE 1781
Cdd:pfam15070 248 YQQLASEKEELHKQYLLQTQLMDRLQHEEVQGKvAAEMARQELQETQERLE------ALT-----QQNQQLQAQLSLLAN 316
|
330 340 350
....*....|....*....|....*....|..
gi 1907082237 1782 EMS----ELARKEAEASRKKHELEMDLESLEA 1809
Cdd:pfam15070 317 PGEgdglESEEEEEEAPRPSLSIPEDFESREA 348
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1501-1872 |
1.33e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.82 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1501 QKKLKQMEVQLEEEYEDKQKALREKRelesklsTLSDQVNQrdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKRE 1580
Cdd:TIGR01612 458 KSKLKALEKRFFEIFEEEWGSYDIKK-------DIDENSKQ-----DNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNI 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1581 IAqlknqleeseFTCAAAVKARKAMEVEmedlhlqiddiAKAKTALEeQLSRLQREKNEIQNRLEEDQEDMNELMKkhka 1660
Cdd:TIGR01612 526 IG----------FDIDQNIKAKLYKEIE-----------AGLKESYE-LAKNWKKLIHEIKKELEEENEDSIHLEK---- 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1661 avaqasrdmaQMNDLQAQ----IEES---NKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQ 1733
Cdd:TIGR01612 580 ----------EIKDLFDKyleiDDEIiyiNKLKLELKEKIKNISDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQVPE 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1734 -VKRLENLASRLKETMEKLTEerDQRAAAENrekEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELE-MDLESLEAAN 1811
Cdd:TIGR01612 650 hLKNKDKIYSTIKSELSKIYE--DDIDALYN---ELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQnMETATVELHL 724
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1812 QSLQADLKLAFKRIGDLQAAIEDEMesdeNEDLINSLQDMVTKYQKKKNKLEGDSDVDSEL 1872
Cdd:TIGR01612 725 SNIENKKNELLDIIVEIKKHIHGEI----NKDLNKILEDFKNKEKELSNKINDYAKEKDEL 781
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1584-1818 |
1.37e-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: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1584 LKNQLEESEFTCAAAVKARKAMEVEMEDlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1663
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREK---EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1664 QASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKTQVKRLENLAS 1742
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERmKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1743 RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD----------TKEEMSELARKEAEASRKKHELEMDLESLEAANQ 1812
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTahrkeaeneaLLEELRSLQERLNASERKVEGLGEELSSMAAQRD 268
|
....*.
gi 1907082237 1813 SLQADL 1818
Cdd:pfam07888 269 RTQAEL 274
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1355-1762 |
1.40e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.67 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1355 KQRRFDSElsqaheETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLD-IAGFTQKVVSLEAELQDISSQesKDEASL 1433
Cdd:PLN02939 38 RRRGFSSQ------QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtVMELPQKSTSSDDDHNRASMQ--RDEAIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1434 AKVKKQLRdleaKVKDQEEELDEQAGS-IQMLEQAklrlEMEMERMRQTHSKEMESRDEEVEEaRQSCQKKLKQMEVQLE 1512
Cdd:PLN02939 110 AIDNEQQT----NSKDGEQLSDFQLEDlVGMIQNA----EKNILLLNQARLQALEDLEKILTE-KEALQGKINILEMRLS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1513 EEYEDKQKALREKRELEsklsTLSDQVNQRDFESEKRLRKDLKRTKALLADaqimLDHLK-NNAPSKREIAQLKNQL--- 1588
Cdd:PLN02939 181 ETDARIKLAAQEKIHVE----ILEEQLEKLRNELLIRGATEGLCVHSLSKE----LDVLKeENMLLKDDIQFLKAELiev 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1589 EESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEIqnrLEEDQEDMNELMKKHKAAVAQASRD 1668
Cdd:PLN02939 253 AETEERVFKLEKERSLLDASLRELESKF-------IVAQEDVSKLSPLQYDC---WWEKVENLQDLLDRATNQVEKAALV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1669 MAQMNDLQAQI---EESNKEKQELQEKLQalqsQVEFLEQSMvdKSLVSRQEAKIRELETrlefektQVKRLENLASRLK 1745
Cdd:PLN02939 323 LDQNQDLRDKVdklEASLKEANVSKFSSY----KVELLQQKL--KLLEERLQASDHEIHS-------YIQLYQESIKEFQ 389
|
410
....*....|....*..
gi 1907082237 1746 ETMEKLTEERDQRAAAE 1762
Cdd:PLN02939 390 DTLSKLKEESKKRSLEH 406
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1154-1479 |
1.61e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.15 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1154 NKDEEIQQLRSKL----EKVEkernELRLSSDRLETRISELTSELTDERN--------TGESASQLLDAETAERLRTEKE 1221
Cdd:pfam00038 1 NEKEQLQELNDRLasyiDKVR----FLEQQNKLLETKISELRQKKGAEPSrlyslyekEIEDLRRQLDTLTVERARLQLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1222 MKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDAGGEWRLKYERAVR----EVDFTKKRLQQELedkmeveq 1297
Cdd:pfam00038 77 LDNLRLAAEDFRQKYEDELNLRTSAE----NDLVGLRKDLDEATLARVDLEAKIEslkeELAFLKKNHEEEV-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1298 qsrRQLERRLGDlqadsdeSQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN-HELEKKQRRFDSELSQAhEETQREKLQ 1376
Cdd:pfam00038 145 ---RELQAQVSD-------TQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNrEEAEEWYQSKLEELQQA-AARNGDALR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1377 REKlqrekdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDIssqESKDEASLAKVKKQLRDLEAKVKDQEEELDE 1456
Cdd:pfam00038 214 SAK---------EEITELRRTIQSLEIELQSLKKQKASLERQLAET---EERYELQLADYQELISELEAELQETRQEMAR 281
|
330 340
....*....|....*....|...
gi 1907082237 1457 QAGSIQMLEQAKLRLEMEMERMR 1479
Cdd:pfam00038 282 QLREYQELLNVKLALDIEIATYR 304
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
28-210 |
1.83e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 28 VRKVVSKVLPGEEPGTAK--EPPgRGARSPEHPARGKkGEKAATSPKPPPPPPPPPAPpkpETKKEAAKDELSVGLRSlm 105
Cdd:PTZ00449 489 IKKSKKKLAPIEEEDSDKhdEPP-EGPEASGLPPKAP-GDKEGEEGEHEDSKESDEPK---EGGKPGETKEGEVGKKP-- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 106 srGRGKDHKSrgkqppgkgEKAP--SQEPASTGKSGSPDMVDSPKKAGSPAKPETPNKRCSPAPAQELADPNlagpklNP 183
Cdd:PTZ00449 562 --GPAKEHKP---------SKIPtlSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPK------SP 624
|
170 180
....*....|....*....|....*..
gi 1907082237 184 SGKQQAKSPASDVQQETGADPEVRLSP 210
Cdd:PTZ00449 625 KRPESPKSPKRPPPPQRPSSPERPEGP 651
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1383-1705 |
2.05e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1383 EKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEAS-------LAKVKKQLR-------------D 1442
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDyqaasdhLNLVQTALRqqekieryqadleE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1443 LEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMR-------------QTHSKEMESRDEEVEEARQSCQK---KLKQ 1506
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqaldvqQTRAIQYQQAVQALERAKQLCGLpdlTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1507 MEVQLEEeYEDKQKALREK-RELESKLSTLSDQVNQRD------------------FESEKRLRKDLKRTKALLADAQIM 1567
Cdd:PRK04863 440 AEDWLEE-FQAKEQEATEElLSLEQKLSVAQAAHSQFEqayqlvrkiagevsrseaWDVARELLRRLREQRHLAEQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1568 LDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE- 1646
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRl 598
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1647 ---------DQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQ 1705
Cdd:PRK04863 599 aarapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1330-1695 |
2.30e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1330 RLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFT 1409
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAAL---SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1410 QKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMErMRQTHSKEMESR 1489
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA-EREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1490 DEEVEEARQSCQKKLKQMEVQleEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLD 1569
Cdd:COG4372 159 LESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1570 HLKNNAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE 1649
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIE-ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1650 DM----NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQA 1695
Cdd:COG4372 316 ALlaalLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1300-1724 |
2.53e-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: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1300 RRQLERRLGDLQADSDESQRALQ-------QLKKKCQRLTAELQDTKLHLEGQQVrnhelEKKQRRFDSELSQ------- 1365
Cdd:pfam05701 37 RKLVELELEKVQEEIPEYKKQSEaaeaakaQVLEELESTKRLIEELKLNLERAQT-----EEAQAKQDSELAKlrveeme 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1366 ---AHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEkdldiagfTQKVVSLEAELQDISSQESKDEASLAK-VKKQLR 1441
Cdd:pfam05701 112 qgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELES--------LRKEYASLVSERDIAIKRAEEAVSASKeIEKTVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1442 DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKlKQMEVQLEEEYEdkqKA 1521
Cdd:pfam05701 184 ELTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQLLSA-KDLKSKLETASA---LL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1522 LREKREL----ESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIA-QLKNQLEEsEFTCA 1596
Cdd:pfam05701 260 LDLKAELaaymESKLKEEADG-EGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAaSLRSELEK-EKAEL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1597 AAVKARKAMEvemedlhlqiddiAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKhkaaVAQASRDMAQMNDLQ 1676
Cdd:pfam05701 338 ASLRQREGMA-------------SIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQ----LQQAAQEAEEAKSLA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907082237 1677 AQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvSRQEAKIRELE 1724
Cdd:pfam05701 401 QAAREELRKAKEEAEQAKAAASTVE------------SRLEAVLKEIE 436
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1489-1830 |
2.67e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1489 RDEEVEEArQSCQKKLKQMEVQLEEEyedkQKALREkreLESKLSTLSdqvnqrdfESEKRLRKDLKRTKALLADAQIML 1568
Cdd:PRK04863 281 RRVHLEEA-LELRRELYTSRRQLAAE----QYRLVE---MARELAELN--------EAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1569 DHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKA----KTALEEQLSRLQREKNEIQnRL 1644
Cdd:PRK04863 345 RQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladyQQALDVQQTRAIQYQQAVQ-AL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1645 EEDQEdMNELMKkhkAAVAQASRDMAQmndLQAQIEESNKEKQELQEKL---QALQSQVEF---LEQSMVDKslVSRQEA 1718
Cdd:PRK04863 424 ERAKQ-LCGLPD---LTADNAEDWLEE---FQAKEQEATEELLSLEQKLsvaQAAHSQFEQayqLVRKIAGE--VSRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1719 K--IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDqraaAENREKEQNKRLQRQLRDtkEEMSELARKEAEASRK 1796
Cdd:PRK04863 495 WdvARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQR----AERLLAEFCKRLGKNLDD--EDELEQLQEELEARLE 568
|
330 340 350
....*....|....*....|....*....|....
gi 1907082237 1797 khELEMDLESLEAANQSLQADLKLAFKRIGDLQA 1830
Cdd:PRK04863 569 --SLSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1290-1843 |
2.93e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1290 EDKMEVEQQSRRQLE----RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNH---------ELEKKQ 1356
Cdd:PRK10246 231 EEKQLLTAQQQQQQSlnwlTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHweriqeqsaALAHTR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1357 RRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDlDIAGFTQKVVSLEAELqdisSQESKDEASLAKV 1436
Cdd:PRK10246 311 QQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHD-RFRQWNNELAGWRAQF----SQQTSDREQLRQW 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1437 KKQLRDLEAKVKDQEE-----ELDEQAGSI-QMLEQAKLRlememERMRQTHSK--EMESRDEEVEEARQSCQKKLKQME 1508
Cdd:PRK10246 386 QQQLTHAEQKLNALPAitltlTADEVAAALaQHAEQRPLR-----QRLVALHGQivPQQKRLAQLQVAIQNVTQEQTQRN 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1509 VQLEEeyedKQKALREKRELESKLSTLSDQvnqrdfesEKRLrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKnqL 1588
Cdd:PRK10246 461 AALNE----MRQRYKEKTQQLADVKTICEQ--------EARI-KDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALE--P 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1589 EESEFTCAAAVKARKAMEVEMEDLHLQIDdiakaktALEEQLsrlQREKNEIQNRLEEDQEdmneLMKKHKAAVAQASRD 1668
Cdd:PRK10246 526 GVNQSRLDALEKEVKKLGEEGAALRGQLD-------ALTKQL---QRDESEAQSLRQEEQA----LTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1669 MAQMNDLQAQIEESNKEKQELQE--KLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFEKTQVK-RLENLASRLK 1745
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHERQLRLlsQRHELQGQIA-------------AHNQQIIQYQQQIEQRQQQLLtALAGYALTLP 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1746 ETMEKLT--EERDQRAAAENREKEQNKRLQRQ------LRDTKEEMSELARKEAEAS----RKKHElemDLESLEAANQS 1813
Cdd:PRK10246 659 QEDEEASwlATRQQEAQSWQQRQNELTALQNRiqqltpLLETLPQSDDLPHSEETVAldnwRQVHE---QCLSLHSQLQT 735
|
570 580 590
....*....|....*....|....*....|
gi 1907082237 1814 LQADLKLAFKRIGDLQAAIEDEMESDENED 1843
Cdd:PRK10246 736 LQQQDVLEAQRLQKAQAQFDTALQASVFDD 765
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1408-1475 |
3.30e-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: 46.85 E-value: 3.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1408 FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQML--EQAKLRLEMEM 1475
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLqdELVALQLQLNM 145
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1286-1785 |
3.76e-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: 49.13 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1286 QQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhleGQQVRNHELEKKQRrfDSELSQ 1365
Cdd:pfam15964 219 RLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAST----SSRVGGLCLKCAQH--EAVLAQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1366 AHEETQREKLQRekLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSleaelqdisSQESKDEASLAKVKK--QLRDL 1443
Cdd:pfam15964 293 THTNVHMQTIER--LTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQ---------AVQMTEEANFEKTKAliQCEQL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1444 EAKVKDQEEELDEQAGSiqmlEQAKLRLEMEMERmrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqKALR 1523
Cdd:pfam15964 362 KSELERQKERLEKELAS----QQEKRAQEKEALR------KEMKKEREELGATMLALSQNVAQLEAQVE-------KVTR 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1524 EKRELESKLSTLSDQVNQRDFESEK---RLRKDLKRTKALLADAQimLDHLKNNAPSKR-------EIAQLKNQLEESef 1593
Cdd:pfam15964 425 EKNSLVSQLEEAQKQLASQEMDVTKvcgEMRYQLNQTKMKKDEAE--KEHREYRTKTGRqleikdqEIEKLGLELSES-- 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1594 tcaaavkaRKAMEVEMEDLHLQIDDIAKaktaLEEQLSRLQREKNeiqnrleedqedmneLMKKHKAAVAQASRDMAQMN 1673
Cdd:pfam15964 501 --------KQRLEQAQQDAARAREECLK----LTELLGESEHQLH---------------LTRLEKESIQQSFSNEAKAQ 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1674 DLQAQIEEsnkekQELQEKLQALQSQvefleqsmvdkslvsrQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTE 1753
Cdd:pfam15964 554 ALQAQQRE-----QELTQKMQQMEAQ----------------HDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQ 612
|
490 500 510
....*....|....*....|....*....|..
gi 1907082237 1754 ERDQRAAAENREKEQNKRLQRQLRDTKEEMSE 1785
Cdd:pfam15964 613 KSRSEVEQLSQEKEYLQDRLEKLQKRNEELEE 644
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1393-1591 |
4.29e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1393 SLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLE 1472
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1473 M---------------EMERMRQTHSKEMesrdEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSD 1537
Cdd:COG3883 107 VllgsesfsdfldrlsALSKIADADADLL----EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1538 QVNQrdfesekrLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEES 1591
Cdd:COG3883 183 LLAQ--------LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1685-1842 |
5.42e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1685 EKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLteerdQRAAAEN 1763
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKElPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-----EARIKKY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 1764 REKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENE 1842
Cdd:COG1579 79 EEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
37-207 |
5.55e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.53 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 37 PGEEPGTAKEPPgrgaRSPEHpARGKKGEKAAT--SPKPPPPPPPPPAPPKPETKKEA-AKDELSVGLRSLMSRGRG-KD 112
Cdd:PTZ00449 510 PPEGPEASGLPP----KAPGD-KEGEEGEHEDSkeSDEPKEGGKPGETKEGEVGKKPGpAKEHKPSKIPTLSKKPEFpKD 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 113 HKS--RGKQPpgKGEKAP--SQEPASTGKSGSPDMVDSPKkagSPAKPETPNKRCSPAPAQELADPNlagpklNPSGKQQ 188
Cdd:PTZ00449 585 PKHpkDPEEP--KKPKRPrsAQRPTRPKSPKLPELLDIPK---SPKRPESPKSPKRPPPPQRPSSPE------RPEGPKI 653
|
170
....*....|....*....
gi 1907082237 189 AKSPASDVQQETGADPEVR 207
Cdd:PTZ00449 654 IKSPKPPKSPKPPFDPKFK 672
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1580-1849 |
6.16e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.75 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1580 EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK 1659
Cdd:pfam19220 91 RLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1660 AAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKT-QVKRL 1737
Cdd:pfam19220 171 LLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAeQAERERAEAQLEEAVEAHRAERAsLRMKL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1738 ENLASRLKETMEKLTEERDQ--RAAAENREKEQN--------KRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESL 1807
Cdd:pfam19220 251 EALTARAAATEQLLAEARNQlrDRDEAIRAAERRlkeasierDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1808 EAANQSLQADLKLAFKRIGDLQAAIE---DEMESDE------NEDLINSLQ 1849
Cdd:pfam19220 331 TKALAAKDAALERAEERIASLSDRIAeltKRFEVERaaleqaNRRLKEELQ 381
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1475-1821 |
6.46e-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: 48.21 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1475 MERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQ----LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFE----- 1545
Cdd:pfam07111 21 LERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEgsqaLSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRleaqa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1546 --------SEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEMEDLHLQID 1617
Cdd:pfam07111 101 meldalavAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLT-QAHEEALSSLTSKAEGLEKSLN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1618 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMN---ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ 1694
Cdd:pfam07111 180 SLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEaqvTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1695 ALQSQVEFLE---QSMVdKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEerdQRAAAENREKEQNKR 1771
Cdd:pfam07111 260 DLQATVELLQvrvQSLT-HMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---QLKAQDLEHRDSVKQ 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1772 LQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLA 1821
Cdd:pfam07111 336 LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRA 385
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1136-1511 |
6.47e-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: 48.36 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1136 FTTVRPLIQV-QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRlssdrletriSELTSELTDERNTGESASQLLDAETAE 1214
Cdd:pfam15964 349 FEKTKALIQCeQLKSELERQKERLEKELASQQEKRAQEKEALR----------KEMKKEREELGATMLALSQNVAQLEAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1215 RLRTEKEMKELQTQYDALKKQMEVMemevmearliraaeingEVDDDDAGGEWR-------LKYERAVREVDFTKKRLQQ 1287
Cdd:pfam15964 419 VEKVTREKNSLVSQLEEAQKQLASQ-----------------EMDVTKVCGEMRyqlnqtkMKKDEAEKEHREYRTKTGR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1288 ELEDKmeveQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDT--KLHLEGQqvrnhELEKKQRRFDSEL-S 1364
Cdd:pfam15964 482 QLEIK----DQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESehQLHLTRL-----EKESIQQSFSNEAkA 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1365 QAHEETQREK----------LQREKLQREKDMLLAEAFSLkqqmeekdldIAGFTQKVVSLEAELQDISSQESKDEASLA 1434
Cdd:pfam15964 553 QALQAQQREQeltqkmqqmeAQHDKTVNEQYSLLTSQNTF----------IAKLKEECCTLAKKLEEITQKSRSEVEQLS 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1435 KVKKQLRDLEAKVKDQEEELDEQAgsIQ---MLEQAKLRLEmEMERMRQTHSK---EMESRDEEVEEARQSCQKKLKQME 1508
Cdd:pfam15964 623 QEKEYLQDRLEKLQKRNEELEEQC--VQhgrMHERMKQRLR-QLDKHCQATAQqlvQLLSKQNQLFKERQNLTEEVQSLR 699
|
...
gi 1907082237 1509 VQL 1511
Cdd:pfam15964 700 SQV 702
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1641-1834 |
6.48e-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: 46.91 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1641 QNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvDKSLVSRQEAKI 1720
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAE-------AAPKEILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1721 RELETRLEFEKTQvkrLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQR------QLRDTKEEMSELARKEAEAS 1794
Cdd:pfam12795 81 EELEQRLLQTSAQ---LQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQirnrlnGPAPPGEPLSEAQRWALQAE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082237 1795 RKKHELEMDLESLEAANQSLQADL-----KLAFKRIGDLQAAIED 1834
Cdd:pfam12795 158 LAALKAQIDMLEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQA 202
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1315-1692 |
6.51e-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: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1315 DESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMllaeafs 1393
Cdd:pfam15905 24 EKSQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKElEKEIRALVQERGEQDKRL------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1394 lkQQMEEKdldiagftqkVVSLEAELQDISSQESKDEASLAKVKKQLRDLeAKVKDqeeeldeqagsiqmLEQAKLRLEM 1473
Cdd:pfam15905 97 --QALEEE----------LEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNE--------------LLKAKFSEDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1474 EMERMRQTHSKEMESRDEeVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRkd 1553
Cdd:pfam15905 150 TQKKMSSLSMELMKLRNK-LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLE-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1554 lkrtkalladaqimldhlknnapskrEIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1633
Cdd:pfam15905 227 --------------------------YITELSCVSEQVE-------KYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 1634 QREKNEIQNRLEEDQEDMNELMKKHKAavaQASRDMAQMNDLQAQIEESNKEKQELQEK 1692
Cdd:pfam15905 274 SKQIKDLNEKCKLLESEKEELLREYEE---KEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1545-1818 |
7.11e-05 |
|
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: 47.27 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1545 ESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREIAQLKNQL-EESEFTCAAAVKARKAMEVEMEDLHLQIDdiaKAK 1623
Cdd:pfam09311 16 EQEAETRDQVKKLQEMLRQAN---DQLEKTMKDKKELEDKMNQLsEETSNQVSTLAKRNQKSETLLDELQQAFS---QAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1624 TALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqaSRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFL 1703
Cdd:pfam09311 90 RNFQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHV---SLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADHM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1704 EQSMVDKSLVSRQEAKiRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLqRQLRDTKEEM 1783
Cdd:pfam09311 167 EEKLKAEILFLKEQIQ-AEQCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQLENGLTEKI-RQLEDLQTTK 244
|
250 260 270
....*....|....*....|....*....|....*
gi 1907082237 1784 SELARKEAEASRKKHELEMDLESLEAANQSLQADL 1818
Cdd:pfam09311 245 GSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTEL 279
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1272-1529 |
7.56e-05 |
|
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: 47.22 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1272 ERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRlgdlqadsdESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnHE 1351
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERKRYRQELEEQIEER---------EQKRQEEYEEKLQEREQMDEIVERIQEEDQAEA-EE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1352 LEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftqkvvsLEAELQDIssqeskdEA 1431
Cdd:pfam13868 121 KLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEE-------------REAEREEI-------EE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1432 SLAKVKKQLRDLEAKVKDQEEELDEQagsiqmleQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQK----KLKQM 1507
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDEL--------RAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEqielKERRL 252
|
250 260
....*....|....*....|..
gi 1907082237 1508 EVQLEEEYEDKQKALREKRELE 1529
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDE 274
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1501-1816 |
7.94e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.83 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1501 QKKLKQMEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS 1577
Cdd:pfam09731 124 QEKEKALEEVLKEaisKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1578 KREIAQLKNQLEESEFTCAAAVKARKAME--VEMEDLHLQIDDIAKAKTALEEQLSRLQREK--NEIQNRLEEDQEDMNE 1653
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEekVEKAQSLAKLVDQYKELVASERIVFQQELVSifPDIIPVLKEDNLLSND 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1654 lmkKHKAAVAQASRDMAQmndLQAQIEEsnKEKQELQEKLQALQSQVEFLEQSmvDKSLVSRQEAKIRELET--RLEFEK 1731
Cdd:pfam09731 284 ---DLNSLIAHAHREIDQ---LSKKLAE--LKKREEKHIERALEKQKEELDKL--AEELSARLEEVRAADEAqlRLEFER 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1732 TQVKRLENLASRLKETMEKLTEERDQRaaAENREKEQNKRLQRQ-LRDTKEEMSE----LARKEAEASRKKHELEMDLES 1806
Cdd:pfam09731 354 EREEIRESYEEKLRTELERQAEAHEEH--LKDVLVEQEIELQREfLQDIKEKVEEeragRLLKLNELLANLKGLEKATSS 431
|
330
....*....|.
gi 1907082237 1807 -LEAANQSLQA 1816
Cdd:pfam09731 432 hSEVEDENRKA 442
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
1454-1806 |
8.29e-05 |
|
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: 47.13 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1454 LDEQAGSIQMLEQAKLRLEMEMERMRqTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKREleskls 1533
Cdd:pfam09755 23 REQLQKRIESLQQENRVLKMELETYK-LRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKE------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1534 TLSDQVNQRdfesEKRLRKDLKRTkalladaqimLDHLKnnapskREIAQLKNQLEeseftcaaavkarKAMEVEMEDLH 1613
Cdd:pfam09755 96 TLAMNYEQE----EEFLTNDLSRK----------LTQLR------QEKVELEQTLE-------------QEQEYQVNKLM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1614 LQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM-NELMKKhkaavaqasrdmaqMNDLQAqieesnkEKQELQEK 1692
Cdd:pfam09755 143 RKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQEALvNRLWKR--------------MDKLEA-------EKRLLQEK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1693 LQALQSQVEFLEQSMVDKSLVSRQEAKIRELetrlefeKTQVKRLENlasRLKETMEKLTEERDQRAAAENREKEQNKRL 1772
Cdd:pfam09755 202 LDQPVSAPPSPRDSTSEGDTAQNLTAHIQYL-------RKEVERLRR---QLATAQQEHTEKMAQYAQEERHIREENLRL 271
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907082237 1773 QRQLRDTKEEMSELARK--EAEASrkkheLEMDLES 1806
Cdd:pfam09755 272 QRKLQLEMERREALCRHlsESESS-----LEMDEER 302
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1143-1462 |
9.09e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1143 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEM 1222
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1223 KELQTQYDALKKQMevmemevmearliraaeingevddddaggewrlkyeravrevdftkKRLQQELEDKmeveQQSRRQ 1302
Cdd:COG4372 104 ESLQEEAEELQEEL----------------------------------------------EELQKERQDL----EQQRKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1303 LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlegQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQR 1382
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALE-----QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1383 EKDMLLAEAfslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQ 1462
Cdd:COG4372 209 IESLPRELA---EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1548-1834 |
9.41e-05 |
|
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: 47.22 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1548 KRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE-----MEDLHLQIDDIAKA 1622
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEerkryRQELEEQIEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1623 KtalEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQE-KLQALQSQVE 1701
Cdd:pfam13868 89 R---QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRILEYLKEKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1702 FLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKR-----LQRQL 1776
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQelqqaREEQI 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1777 RDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRigDLQAAIED 1834
Cdd:pfam13868 246 ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR--ELEKQIEE 301
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1309-1804 |
9.45e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 47.38 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1309 DLQADSDESQralqQLKKKCQRL---TAELQDTKLHLegqQVRNHELEKKQRRFDSELSQA--------HEETQREKLQR 1377
Cdd:pfam05622 1 DLSEAQEEKD----ELAQRCHELdqqVSLLQEEKNSL---QQENKKLQERLDQLESGDDSGtpggkkylLLQKQLEQLQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1378 EKLQREKDmllAEAFSLKQQMEEKD-LDIAGFTQKVVSLEAElqdisSQESKDE-----ASLAKVKKqlrdLEAKV---K 1448
Cdd:pfam05622 74 ENFRLETA---RDDYRIKCEELEKEvLELQHRNEELTSLAEE-----AQALKDEmdilrESSDKVKK----LEATVetyK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1449 DQEEELDEQAGSIQMLEqaklrlEMEMERMRQTHSKEMESRDEEVEEAR-QSCQKKLKQMEVQLEEEYEDKQKALREKRE 1527
Cdd:pfam05622 142 KKLEDLGDLRRQVKLLE------ERNAEYMQRTLQLEEELKKANALRGQlETYKRQVQELHGKLSEESKKADKLEFEYKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1528 LESKLSTLsdqvnQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKN------------------QLE 1589
Cdd:pfam05622 216 LEEKLEAL-----QKEKERLIIERDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDnlaaeimpaeireklirlQHE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1590 ESEFTCaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLsRLQREK-NEIQNRLEEDQEDMNELMKKHKAAVAqasrd 1668
Cdd:pfam05622 291 NKMLRL----GQEGSYRERLTELQQLLEDANRRKNELETQN-RLANQRiLELQQQVEELQKALQEQGSKAEDSSL----- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1669 maqmndLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdkSLVSRQEAKIRELETRLefektQVKRLENLA--SRLKE 1746
Cdd:pfam05622 361 ------LKQKLEEHLEKLHEAQSELQKKKEQIEELEP-----KQDSNLAQKIDELQEAL-----RKKDEDMKAmeERYKK 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 1747 TMEKLTEE-RDQRAAAENREKEQNKRLQRQLRDtKEEMSELARKEAEASRKKHELEMDL 1804
Cdd:pfam05622 425 YVEKAKSViKTLDPKQNPASPPEIQALKNQLLE-KDKKIEHLERDFEKSKLQREQEEKL 482
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1282-1480 |
1.10e-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: 46.67 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1282 KKRLQQELEDKMEVEQ-QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhLEGQqvrnHELEKKQRRfd 1360
Cdd:pfam09787 23 KEKLIASLKEGSGVEGlDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE----LEAQ----QQEEAESSR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1361 SELSQAHEETQREKLQREKLQrekdmllAEAFSLKQQM----EEKDLDIAGFTQKVVSLEAELQDISSQ-ESKDEASLAK 1435
Cdd:pfam09787 93 EQLQELEEQLATERSARREAE-------AELERLQEELryleEELRRSKATLQSRIKDREAEIEKLRNQlTSKSQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082237 1436 vkkqlRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQ 1480
Cdd:pfam09787 166 -----SELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQ 205
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1400-1559 |
1.12e-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: 46.07 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1400 EKDLDIAGFTQKVVSLEAELQDIssqeskdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEmemERMR 1479
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAEL-------EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1480 QTHS-KEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKALRE-KRELESKLSTLSDQVNQRDfESEKRLRKDLKRT 1557
Cdd:COG1579 84 NVRNnKEYEALQKEIESLKRR-ISDLEDEILELMERIEELEEELAElEAELAELEAELEEKKAELD-EELAELEAELEEL 161
|
..
gi 1907082237 1558 KA 1559
Cdd:COG1579 162 EA 163
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1290-1499 |
1.18e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1290 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEE 1369
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1370 TQREKLQREKLqrekDMLL-AEAFS--------LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL 1440
Cdd:COG3883 95 LYRSGGSVSYL----DVLLgSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 1441 RDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS 1499
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1713-1830 |
1.21e-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: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1713 VSRQEAKIRELEtrlefekTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRDTKEEMSELARKEAE 1792
Cdd:COG2433 408 LTEEEEEIRRLE-------EQVERLEAEVEELEAELEEK--------------DERIERLERELSEARSEERREIRKDRE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907082237 1793 ASRKKHE---LEMDLESLEAANQSLQADLKLaFKRIGDLQA 1830
Cdd:COG2433 467 ISRLDREierLERELEEERERIEELKRKLER-LKELWKLEH 506
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1670-1850 |
1.25e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 45.79 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1670 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETrlEFEKTQvKRLENLASRLKEtME 1749
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAE------VAALNRRIQLLEE--ELERTE-ERLAEALEKLEE-AE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1750 KLTEERDQ-RAAAENREKEQNKR---LQRQLRDTKEEMSELARKEAEASRKKHELEMDLE-------SLEAANQSLQADL 1818
Cdd:pfam00261 71 KAADESERgRKVLENRALKDEEKmeiLEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraeeraeLAESKIVELEEEL 150
|
170 180 190
....*....|....*....|....*....|...
gi 1907082237 1819 KLAFKRIGDLQAAIEDEMES-DENEDLINSLQD 1850
Cdd:pfam00261 151 KVVGNNLKSLEASEEKASEReDKYEEQIRFLTE 183
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1146-1517 |
1.30e-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: 47.26 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1146 QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETrisELTSELTDERNTGESASQlldaETAERLRTEKEMKEL 1225
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENA---ESSKRLNENANNLIKQFE----NTKEKIAEYTKSIDI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1226 QTQYDALKKQmevmemevmearlIRAAEINGEvddddaggewrlkYERAVREVDFTKKRLQQELEdkmeveqQSRRQLER 1305
Cdd:COG5185 308 KKATESLEEQ-------------LAAAEAEQE-------------LEESKRETETGIQNLTAEIE-------QGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1306 RLGDLQADSDESQRALQQlkkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKL-QREKLQREK 1384
Cdd:COG5185 355 NLEAIKEEIENIVGEVEL-----SKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADrQIEELQRQI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1385 DmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAK--VKKQLRDLEAKVKDQEEELDEQAGSiq 1462
Cdd:COG5185 430 E-------QATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINrsVRSKKEDLNEELTQIESRVSTLKAT-- 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1463 mLEQAKLRLEMEMERMRQTHSKEMESRDEEvEEARQSCQKKLKQMEVQLEEEYED 1517
Cdd:COG5185 501 -LEKLRAKLERQLEGVRSKLDQVAESLKDF-MRARGYAHILALENLIPASELIQA 553
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1447-1781 |
1.37e-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: 46.60 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1447 VKDQEEELDEQAGSIQMLEQAKLRL---------EMEMER-----MRQTHSKEMESRDEEVEEARQSCQKKL--KQMEVQ 1510
Cdd:pfam15742 1 VSSGEKLKYQQQEEVQQLRQNLQRLqilctsaekELRYERgknldLKQHNSLLQEENIKIKAELKQAQQKLLdsTKMCSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1511 LEEEYEDKQKALREkRELESKLSTLSDQvnqrdfeSEKRLRKDLKRTKALLADAQimldhlknnapskREIAQLKNQLEE 1590
Cdd:pfam15742 81 LTAEWKHCQQKIRE-LELEVLKQAQSIK-------SQNSLQEKLAQEKSRVADAE-------------EKILELQQKLEH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1591 SEFTCAAAVKA--RKAMEVEMEDLhlqIDDIAKAKTAL-EEQLSR--LQREKNEIQNRLEEDQEDMNELMKKHKAAVAQA 1665
Cdd:pfam15742 140 AHKVCLTDTCIleKKQLEERIKEA---SENEAKLKQQYqEEQQKRklLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1666 SRDMAQMNDLQAQI---EESNKEKQELQEKLQALQSQVEFL--EQSMVDKSL----------VSRQEAKIRELETRLEFE 1730
Cdd:pfam15742 217 QQQEAQLKQLENEKrksDEHLKSNQELSEKLSSLQQEKEALqeELQQVLKQLdvhvrkynekHHHHKAKLRRAKDRLVHE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1731 KTQ----VKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKE 1781
Cdd:pfam15742 297 VEQrderIKQLENEIGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQEE 351
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1315-1458 |
1.56e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1315 DESQRALQQLKKKCQrLTA--ELQDTKLHLEGQ-QVRNHELEKKQRRFdselsQAHEETQREKLqrEKLQREKDMLLAEA 1391
Cdd:PRK12704 45 EEAKKEAEAIKKEAL-LEAkeEIHKLRNEFEKElRERRNELQKLEKRL-----LQKEENLDRKL--ELLEKREEELEKKE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1392 FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQeSKDEAS---LAKVKKQLR-DLEAKVKDQEEELDEQA 1458
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEEQLQELERISGL-TAEEAKeilLEKVEEEARhEAAVLIKEIEEEAKEEA 186
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1624-1809 |
1.65e-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: 46.29 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1624 TALEEQLSRLQREKN----EIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1699
Cdd:pfam09787 43 TALTLELEELRQERDllreEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1700 VEFLEQSMVdKSLVSRQEaKIRELETRLEFEKTQVK--------------RLENLASRL--KETM-EKLTEERDQRAAAE 1762
Cdd:pfam09787 123 LRYLEEELR-RSKATLQS-RIKDREAEIEKLRNQLTsksqssssqselenRLHQLTETLiqKQTMlEALSTEKNSLVLQL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907082237 1763 NREKEQNKRLQ-RQLRDTKEEMSELARKEAEASRKKHELEMDLESLEA 1809
Cdd:pfam09787 201 ERMEQQIKELQgEGSNGTSINMEGISDGEGTRLRNVPGLFSESDSDRA 248
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1720-1885 |
1.67e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1720 IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLqRQLRDTKEEMSELARKEAEASRKKHE 1799
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1800 LEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSdvdSELEDRVDGV 1879
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL---SRLEEEINGI 326
|
....*.
gi 1907082237 1880 KSWLSK 1885
Cdd:PRK03918 327 EERIKE 332
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1621-1993 |
1.75e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 46.96 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1621 KAKTALEEQLSRLQ--REKNEIQNRLEEDQedmnelmkkhkaavAQASRDMAQMNDLQAQIEESNKEKQELQEKLqaLQS 1698
Cdd:PTZ00108 1031 AKKKDLVKELKKLGyvRFKDIIKKKSEKIT--------------AEEEEGAEEDDEADDEDDEEELGAAVSYDYL--LSM 1094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1699 QVEFLEQSMVDKsLVSRQEAKIRELEtrlEFEKTQVKR--LENLAsRLKETMEKlTEERDQRAAAENREKEQNKRL-QRQ 1775
Cdd:PTZ00108 1095 PIWSLTKEKVEK-LNAELEKKEKELE---KLKNTTPKDmwLEDLD-KFEEALEE-QEEVEEKEIAKEQRLKSKTKGkASK 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1776 LRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKY 1855
Cdd:PTZ00108 1169 LRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKN 1248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1856 QKKKNKLEGDSDVDSELED-----RVDGVKSWLSKNKGPSKAPSDDGSLKSSRTalNSLPKEGKGPEERPSSVLSSLSYR 1930
Cdd:PTZ00108 1249 NSSKSSEDNDEFSSDDLSKegkpkNAPKRVSAVQYSPPPPSKRPDGESNGGSKP--SSPTKKKVKKRLEGSLAALKKKKK 1326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082237 1931 KRLTlkdsiggTGDQDSLLTTLSERATSPERPPRKARggPREEPDQaqgrrcEELDDCSSIFS 1993
Cdd:PTZ00108 1327 SEKK-------TARKKKSKTRVKQASASQSSRLLRRP--RKKKSDS------SSEDDDDSEVD 1374
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1143-1453 |
1.77e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1143 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEM 1222
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1223 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDK---MEVEQQS 1299
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1300 RRQLERRlgdlqadSDESQRALQQLKKKCQRLTAELQDTKLHLeGQQVRNHELEKKQRRFDSElsQAHEETQREKLQRE- 1378
Cdd:pfam05483 617 NKALKKK-------GSAENKQLNAYEIKVNKLELELASAKQKF-EEIIDNYQKEIEDKKISEE--KLLEEVEKAKAIADe 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1379 --KLQREKDML----LAEAFSLKQQ--------MEEKDLDIAGFTQK-------VVSLEAELQDIssqeskdEASLAKVK 1437
Cdd:pfam05483 687 avKLQKEIDKRcqhkIAEMVALMEKhkhqydkiIEERDSELGLYKNKeqeqssaKAALEIELSNI-------KAELLSLK 759
|
330
....*....|....*....
gi 1907082237 1438 KQL---RDLEAKVKDQEEE 1453
Cdd:pfam05483 760 KQLeieKEEKEKLKMEAKE 778
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1144-1513 |
2.00e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1144 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRIseltseLTDERNTGESASQLldaetaerlrtEKEMK 1223
Cdd:PRK04778 113 LLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL------LANRFSFGPALDEL-----------EKQLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1224 ELQTQYDalkkqmevmemevmearliRAAEINGEVDDDDAggewRLKYERAVREVDFTK----------KRLQQELEDKM 1293
Cdd:PRK04778 176 NLEEEFS-------------------QFVELTESGDYVEA----REILDQLEEELAALEqimeeipellKELQTELPDQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1294 EVEQQSRRQLER---RLGDLQADSDesqraLQQLKKKCQRLTAELQDtkLHLEGQQVRNHELEKK--------QRRFDSE 1362
Cdd:PRK04778 233 QELKAGYRELVEegyHLDHLDIEKE-----IQDLKEQIDENLALLEE--LDLDEAEEKNEEIQERidqlydilEREVKAR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1363 lSQAHEETQREKLQREKLQREKDMLLAEAFSLKQ--QMEEKDLDIA-GFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1439
Cdd:PRK04778 306 -KYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsyTLNESELESVrQLEKQLESLEKQYDEITERIAEQEIAYSELQEE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1440 LRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQ---THSKEMESRD-----EEVEEARQSCQKKLKQMEVQL 1511
Cdd:PRK04778 385 LEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklhEIKRYLEKSNlpglpEDYLEMFFEVSDEIEALAEEL 464
|
..
gi 1907082237 1512 EE 1513
Cdd:PRK04778 465 EE 466
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1634-1813 |
2.13e-04 |
|
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: 46.48 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1634 QREKNEIQNRLEEDQEDMNELMKKHkaaVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVE----FLEQSMVD 1709
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREE---LELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAqeraRQQQEEFR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1710 KSLVSRQEAKIRELETRLEFEKTQVKRLE-NLASRLKETMEKLTEERDQraaaenrekeqnkrLQRQlrdtKEEMSELAR 1788
Cdd:pfam15709 430 RKLQELQRKKQQEEAERAEAEKQRQKELEmQLAEEQKRLMEMAEEERLE--------------YQRQ----KQEAEEKAR 491
|
170 180
....*....|....*....|....*
gi 1907082237 1789 KEAEASRKKHELEMDLESLEAANQS 1813
Cdd:pfam15709 492 LEAEERRQKEEEAARLALEEAMKQA 516
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1144-1365 |
2.17e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1144 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNElRLSSDRLETRISELTSELTDERNT-GESASQLLDAETAERlRTEKEM 1222
Cdd:PRK11281 88 QLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLESRLAQTLDQLQNAQNDlAEYNSQLVSLQTQPE-RAQAAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1223 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQQELEDKMEVEQQsrrQ 1302
Cdd:PRK11281 166 YANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNA----QNDLQRKSLEGNTQLQDLLQKQRDYLTARIQ---R 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082237 1303 LERRLGDLQADSdeSQRALQQLKKKCQRltAELQDtklhlEGQQVRNHELEKKQRRFDSELSQ 1365
Cdd:PRK11281 239 LEHQLQLLQEAI--NSKRLTLSEKTVQE--AQSQD-----EAARIQANPLVAQELEINLQLSQ 292
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1578-1788 |
2.25e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.22 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1578 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEiQNRLEEDQEDMNELMKK 1657
Cdd:PRK11637 67 QQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQI-------DELNASIAKLEQQQAA-QERLLAAQLDAAFRQGE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1658 HKAAVAQASRDMAQ-------------------MNDLQAQIEESNKEKQELQEKlQALQSQVEFLEQSMVDKSLVSRQEA 1718
Cdd:PRK11637 139 HTGLQLILSGEESQrgerilayfgylnqarqetIAELKQTREELAAQKAELEEK-QSQQKTLLYEQQAQQQKLEQARNER 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082237 1719 K--IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD-------TKEEMSELAR 1788
Cdd:PRK11637 218 KktLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREAREAARVRDKQKQAKRkgstykpTESERSLMSR 296
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1156-1335 |
2.48e-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: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1156 DEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQT--QYDALK 1233
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1234 KQmevmemEVMEARLIRAAeingevddddaggewrlkyERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLGDLQAD 1313
Cdd:COG1579 96 KE------IESLKRRISDL-------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 1907082237 1314 SDESQRALQQLKKKCQRLTAEL 1335
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1437-1617 |
2.87e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.86 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1437 KKQLRDLEAKVKDQEEELDEQAgsiqMLEQAKLRLEMEMERMRqtHSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYE 1516
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEE----KLEAALLEAKELLLRER--NQQRQEARREREELQRE--EERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1517 DKQKALREKRELESKLSTLSDQVNQRdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEsEFTCA 1596
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEEL----EKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE-EADLE 173
|
170 180
....*....|....*....|.
gi 1907082237 1597 AAVKARKAMEVEMEDLHLQID 1617
Cdd:PRK12705 174 AERKAQNILAQAMQRIASETA 194
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1621-1872 |
2.99e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 46.09 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1621 KAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA----QASRDMAQMND------LQAQIEEsnKEKQELQ 1690
Cdd:pfam15818 21 EAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAvfkkQLQMKMCALEEekgkyqLATEIKE--KEIEGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1691 EKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEKTQVKRLEN----LASR---LKETMEKLtEERDQRAAAEN 1763
Cdd:pfam15818 99 ETLKALQVSKYSLQKK------VSEMEQKLQLHLLAKEDHHKQLNEIEKyyatITGQfglVKENHGKL-EQNVQEAIQLN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1764 -REKEQNKRLQRQLRDTKEEM----SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFkrigDLQAAIEDEME- 1837
Cdd:pfam15818 172 kRLSALNKKQESEICSLKKELkkvtSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMEL----ELNKKINEEITh 247
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907082237 1838 -SDENEDLINSLQDMVTKYQKkknKLEGDSDVDSEL 1872
Cdd:pfam15818 248 iQEEKQDIIISFQHMQQLLQQ---QTQANTEMEAEL 280
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1290-1694 |
3.72e-04 |
|
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: 45.77 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1290 EDKMEVEQQSRRQLERRLGDLQADSDESQ--------RALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQRrfdS 1361
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKhtqnvalnKKLSDIKTEYLYELNVLKEKS---------EAELTSKTK---K 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1362 ELSQAHEETQREKLQREKLQREKDMLLAEA-FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESkdEASLAKVKKQL 1440
Cdd:NF033838 122 ELDAAFEQFKKDTLEPGKKVAEATKKVEEAeKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--ELELVKEEAKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1441 RDLEAKVKDQEEELDEQAGSIQMLEQAKlrlememermrqthskemESRDEEVEEARQSCQKKLKQ-MEVQLEEEYEDKQ 1519
Cdd:NF033838 200 PRDEEKIKQAKAKVESKKAEATRLEKIK------------------TDREKAEEEAKRRADAKLKEaVEKNVATSEQDKP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1520 KAlREKRELESKLSTlsdqvnqrdfesekrlrKDLKRTKALLADAQIMLDHLKNnaPSKREiaqlKNQLEESEFTCAAAV 1599
Cdd:NF033838 262 KR-RAKRGVLGEPAT-----------------PDKKENDAKSSDSSVGEETLPS--PSLKP----EKKVAEAEKKVEEAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1600 KARKAMEVE---------MEDLHLQiddIAKAKTALEE-QLSRLQREKNEIQNrleedQEDMNELMKKHKAAVAQASRdM 1669
Cdd:NF033838 318 KKAKDQKEEdrrnyptntYKTLELE---IAESDVKVKEaELELVKEEAKEPRN-----EEKIKQAKAKVESKKAEATR-L 388
|
410 420
....*....|....*....|....*
gi 1907082237 1670 AQMNDLQAQIEESNKEKQELQEKLQ 1694
Cdd:NF033838 389 EKIKTDRKKAEEEAKRKAAEEDKVK 413
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1525-1699 |
3.99e-04 |
|
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: 45.01 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1525 KRELESKLSTLSdqvnqrdfESEKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQleeseftcaaavkarka 1604
Cdd:smart00787 146 KEGLDENLEGLK--------EDYKLLMKELELLNSIKPKLRDRKDALE------EELRQLKQL----------------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1605 mEVEMEDLHLQIDDIAKAKtaleeqLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEE--- 1681
Cdd:smart00787 195 -EDELEDCDPTELDRAKEK------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQcrg 267
|
170
....*....|....*....
gi 1907082237 1682 -SNKEKQELQEKLQALQSQ 1699
Cdd:smart00787 268 fTFKEIEKLKEQLKLLQSL 286
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1585-1759 |
4.15e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1585 KNQLEESEFTCAAAVK-ARKAMEVEMEDLHLQI-DDIAKAKTALEEQLsrlqREKNEIQNRLEEDQEDMNELMKKHKAAV 1662
Cdd:PRK12704 30 EAKIKEAEEEAKRILEeAKKEAEAIKKEALLEAkEEIHKLRNEFEKEL----RERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1663 AQASRDMAQMNDLQAQIEESNKEKQELQEKLQalQSQVEFLEQSMvdkSLvSRQEAK---IRELETRLEFEKtqvkrlen 1739
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELI--EEQLQELERIS---GL-TAEEAKeilLEKVEEEARHEA-------- 171
|
170 180
....*....|....*....|
gi 1907082237 1740 lASRLKETMEKLTEERDQRA 1759
Cdd:PRK12704 172 -AVLIKEIEEEAKEEADKKA 190
|
|
| secA |
PRK12903 |
preprotein translocase subunit SecA; Reviewed |
1667-1843 |
4.58e-04 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237258 [Multi-domain] Cd Length: 925 Bit Score: 45.43 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1667 RDMAQMNDLQAQIEESNKEKQELQEKLqALQSQVEFLEQSMVDKSLvsrqeaKIRELETRLEFEKTQVKRLENLASRL-K 1745
Cdd:PRK12903 741 VQYSQKNPYQVYTEEGTKKFNILLQEI-AYDVIVSLFNNPNAEKIL------IITEILSDGINNSDINDRPQELIDQIiE 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1746 ETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFK-R 1824
Cdd:PRK12903 814 SEEERLKALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEFKNDPKKLNKLIIAKdV 893
|
170
....*....|....*....
gi 1907082237 1825 IGDLQAAIEDEMESDENED 1843
Cdd:PRK12903 894 LIKLVISSDEIKQDEKTTK 912
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
1718-1843 |
5.48e-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: 42.00 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1718 AKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEnrekEQNKRLQRQLRDTKEEMSELARKEAEASRKK 1797
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELE----AEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907082237 1798 HELEMDLESLEAANQSLQADLKlafKRIGDLQAAIEDEMESDENED 1843
Cdd:pfam04871 77 DDLLLLLGDLEEKVEKYKARLK---ELGEEVLSDDEDDDEDDEEDD 119
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1597-1788 |
5.81e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.66 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1597 AAVKARKAMEVEMEDLHlqiDDIAKAKTALEEQLSRLQRekneIQNRLEEDQEDMNELMKKHKAAVAQASRDMA------ 1670
Cdd:COG1842 20 KAEDPEKMLDQAIRDME---EDLVEARQALAQVIANQKR----LERQLEELEAEAEKWEEKARLALEKGREDLArealer 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1671 ------QMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFEKTQVKRLENLAS-- 1742
Cdd:COG1842 93 kaeleaQAEALEAQLAQLEEQVEKLKEALRQLESKLE-------------ELKAKKDTLKARAKAAKAQEKVNEALSGid 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1743 -----RLKETMEKLTEERDQRAAAEnREKEQNKRLQRQLRDTKEEMS---ELAR 1788
Cdd:COG1842 160 sddatSALERMEEKIEEMEARAEAA-AELAAGDSLDDELAELEADSEvedELAA 212
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1373-1524 |
7.27e-04 |
|
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: 42.97 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1373 EKLQREKLQREKDMLLAEAFSLKQQMEEKdldIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLRDLEAKVKDQEE 1452
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEP---LQKAQEEVEELRKQLE----NYEKDKQSLKNLKARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082237 1453 ELDeqagsiqMLEQAKLRLEMEMErmrqthskEMESRDEE-VEEARQSCQKK---LKQMEVQLEEEYEDKQKALRE 1524
Cdd:pfam13851 107 EHE-------VLEQRFEKVERERD--------ELYDKFEAaIQDVQQKTGLKnllLEKKLQALGETLEKKEAQLNE 167
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1336-1857 |
7.44e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.21 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1336 QDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQreKLQREKLQREK-DMLLAEAFSLKQQMEEKDLDIagFTQKVVS 1414
Cdd:PTZ00440 617 EKNDLQEKVKYILNKFYKGDLQELLDELSHFLDDHK--YLYHEAKSKEDlQTLLNTSKNEYEKLEFMKSDN--IDNIIKN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1415 LEAELQDISSQesKDEAslakVKKQLRDLEAKVKDQEEELDEQAGSIQM-LEQAKlrlemEMERMRQTHSKEMESRDEEV 1493
Cdd:PTZ00440 693 LKKELQNLLSL--KENI----IKKQLNNIEQDISNSLNQYTIKYNDLKSsIEEYK-----EEEEKLEVYKHQIINRKNEF 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1494 EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQV--NQRDFESEKRLRKDLK--------RTKALL-- 1561
Cdd:PTZ00440 762 ILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKknNQDLLNSYNILIQKLEahtekndeELKQLLqk 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1562 ---ADAQIMLDHLKNNAPSKREIAQ-LKNQLEESEFTCAAAVKARKAMEVEMEDLHLqIDDIAKAKTALEEQLS------ 1631
Cdd:PTZ00440 842 fptEDENLNLKELEKEFNENNQIVDnIIKDIENMNKNINIIKTLNIAINRSNSNKQL-VEHLLNNKIDLKNKLEqhmkii 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1632 ----------------RLQREKNEIQNRLeeDQEDMNEL-MKKHKA-AVAQASRDMAQMND--LQAQIEESNKEKQELQE 1691
Cdd:PTZ00440 921 ntdniiqkneklnllnNLNKEKEKIEKQL--SDTKINNLkMQIEKTlEYYDKSKENINGNDgtHLEKLDKEKDEWEHFKS 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1692 KLQALQSQVEFLEQSMVDksLVSRQEAKIRELETRLEFEKTQ-----VKRLENLASRLKETMEKLTeerdqraAAENREK 1766
Cdd:PTZ00440 999 EIDKLNVNYNILNKKIDD--LIKKQHDDIIELIDKLIKEKGKeieekVDQYISLLEKMKTKLSSFH-------FNIDIKK 1069
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1767 EQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAF----KRIGDLQAAIE---DEMESD 1839
Cdd:PTZ00440 1070 YKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYnkkkKSLEKIYKQMEktlKELENM 1149
|
570
....*....|....*....
gi 1907082237 1840 ENEDL-INSLQDMVTKYQK 1857
Cdd:PTZ00440 1150 NLEDItLNEVNEIEIEYER 1168
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1621-1746 |
7.53e-04 |
|
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: 41.90 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1621 KAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQV 1700
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907082237 1701 EFLEQSMVDKslvsrqEAKIRELETRLEFEKTQVKRLENLASRLKE 1746
Cdd:pfam10473 83 ENLTKELQKK------QERVSELESLNSSLENLLEEKEQEKVQMKE 122
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1626-1815 |
7.53e-04 |
|
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: 44.67 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1626 LEEQLSRLQREKNEIQNRLEEDQEDMNELmkKHKAAVAQASRDM------AQMNDLQAQIEESNKEKQELQEKLQAlqsQ 1699
Cdd:pfam15070 34 LSEQVRTLREEKERSVSQVQELETSLAEL--KNQAAVPPAEEEQppagpsEEEQRLQEEAEQLQKELEALAGQLQA---Q 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1700 VEFLEQSmvdKSLVSRQEAKIRELETRLEFEKTQVKRLEnlasRLKETME--KLTeerDQRAAAENRE-KEQNKRLQRQ- 1775
Cdd:pfam15070 109 VQDNEQL---SRLNQEQEQRLLELERAAERWGEQAEDRK----QILEDMQsdRAT---ISRALSQNRElKEQLAELQNGf 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1776 LRDTKEEM-------------SELARKEAEASRKKHEL--EMDLESLEAanQSLQ 1815
Cdd:pfam15070 179 VKLTNENMeltsalqseqhvkKELAKKLGQLQEELGELkeTLELKSQEA--QSLQ 231
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1300-1517 |
7.98e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1300 RRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTK-----LHLEGQQvrnHELEKKQRRFDSELSQAHEETQREK 1374
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEA---KLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1375 LQREKLQREKDMLLAEAFSLKQqmeekDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ---- 1450
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaqri 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1451 ----EEELDEQAGSIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQ---SCQKKLKQMEVQLEEEYED 1517
Cdd:COG3206 315 laslEAELEALQAREASLQAQLAQLEARLAELPEL-EAELRRLEREVEVARElyeSLLQRLEEARLAEALTVGN 387
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1155-1460 |
8.01e-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: 44.56 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1155 KDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAE---TAERLRTEKEMKELQTQYDA 1231
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEaeqELEESKRETETGIQNLTAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1232 LKKQMEVMEmevmearliRAAEINGEVDDDDAGGEWRLKYER---AVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLG 1308
Cdd:COG5185 346 EQGQESLTE---------NLEAIKEEIENIVGEVELSKSSEEldsFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1309 DLQADSDESQRALQQLKKKcqrlTAELQDTKLHLEgqqvrnHELEKKQRRFDSELSQAHEETQREKLQR-----EKLQRE 1383
Cdd:COG5185 417 AADRQIEELQRQIEQATSS----NEEVSKLLNELI------SELNKVMREADEESQSRLEEAYDEINRSvrskkEDLNEE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1384 KDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLE---AELQDISSQESKDEASLAKVKKQlRDLEAKvKDQEEELDEQAGS 1460
Cdd:COG5185 487 LTQIESRVSTLKATLEKLRAKLERQLEGVRSKLdqvAESLKDFMRARGYAHILALENLI-PASELI-QASNAKTDGQAAN 564
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1651-1867 |
8.51e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.90 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1651 MNELMKKHKAAVAQASRDMAqMNDLQAQIEESNKEKQELQEKLQALQSQV-EFLEQSMVDKSlvsrqeaKIRELETRLEf 1729
Cdd:cd22656 96 ILELIDDLADATDDEELEEA-KKTIKALLDDLLKEAKKYQDKAAKVVDKLtDFENQTEKDQT-------ALETLEKALK- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1730 ektqvkrlenlasrlketmEKLTEErdqraaAENREKEQNKRLQRQLrdtKEEMSELARKEAEASRKKHELEMDLESLEA 1809
Cdd:cd22656 167 -------------------DLLTDE------GGAIARKEIKDLQKEL---EKLNEEYAAKLKAKIDELKALIADDEAKLA 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1810 ANQSLQADLKLAFKRIGDLQAAIEDEMESDENedLINSLQDMVTKYQKKKNKLEGDSD 1867
Cdd:cd22656 219 AALRLIADLTAADTDLDNLLALIGPAIPALEK--LQGAWQAIATDLDSLKDLLEDDIS 274
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1405-1636 |
8.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1405 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQaklrlememermrqthsk 1484
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1485 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESK-LSTLSDQVNQRDF--ESEKRLRKDLKRTKALL 1561
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsFSDFLDRLSALSKiaDADADLLEELKADKAEL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082237 1562 ADAQIMLDHLKNnapskrEIAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQRE 1636
Cdd:COG3883 146 EAKKAELEAKLA------ELEALKAELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1321-1538 |
8.78e-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: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1321 LQQLKKKCQRLTAELQdTKLHLEGQQV-RNHELEKKQRRFDSELSQAHEetqreklqrEKLQREKDMLLaeafSLKQQME 1399
Cdd:pfam07111 483 LEQLREERNRLDAELQ-LSAHLIQQEVgRAREQGEAERQQLSEVAQQLE---------QELQRAQESLA----SVGQQLE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1400 EKDLDIAGFTQKVVSLEAEL---QDISSQESKDEasLAKVKKQLRDLEAKVKDQ-EEELDEQAGSIQMLEQAKLRLEMEM 1475
Cdd:pfam07111 549 VARQGQQESTEEAASLRQELtqqQEIYGQALQEK--VAEVETRLREQLSDTKRRlNEARREQAKAVVSLRQIQHRATQEK 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082237 1476 ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQ 1538
Cdd:pfam07111 627 ERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDK 689
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1439-1753 |
9.07e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1439 QLRDLeaKVKDQEEELDEQAGSIQMLEQA--KLRLEMEMERMRQthSKEMESRDEEVEEARQSCQKKLKQmevqLEEEYE 1516
Cdd:PRK05771 32 HIEDL--KEELSNERLRKLRSLLTKLSEAldKLRSYLPKLNPLR--EEKKKVSVKSLEELIKDVEEELEK----IEKEIK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1517 DKQKALR----EKRELESKLSTLSdqvNQRDFESEKRLRKDLKRTKALLADAQimldhlKNNAPSKREIAQLKNQLEESE 1592
Cdd:PRK05771 104 ELEEEISelenEIKELEQEIERLE---PWGNFDLDLSLLLGFKYVSVFVGTVP------EDKLEELKLESDVENVEYIST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1593 F----TCAAAVKARKAMEV--EMEDLHLQIDDIAKAKTALEEqLSRLQREKNEIQNRLEEDQEDMNELMKKHKaavaqas 1666
Cdd:PRK05771 175 DkgyvYVVVVVLKELSDEVeeELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELAKKYL------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1667 rdmaqmNDLQAQIEESNKEKQELQEKLQALQS----QVE-FLEQSMVD--KSLVSRQEAK---IRELETRLEFEKTQVKr 1736
Cdd:PRK05771 247 ------EELLALYEYLEIELERAEALSKFLKTdktfAIEgWVPEDRVKklKELIDKATGGsayVEFVEPDEEEEEVPTK- 319
|
330
....*....|....*..
gi 1907082237 1737 LENlaSRLKETMEKLTE 1753
Cdd:PRK05771 320 LKN--PKFIKPFESLTE 334
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1208-1474 |
9.24e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.29 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1208 LDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVMEARliraaEINGEV-----------DDDDAGGEWRLKYERAVR 1276
Cdd:pfam05622 199 LSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLR-----ETNEELrcaqlqqaelsQADALLSPSSDPGDNLAA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1277 EV---DFTKKRLQQELEDKMEVEQQSrRQLERRLGDLQADSDESQRALQ----QLKKKCQR---LTAELQDTKLHLEGQQ 1346
Cdd:pfam05622 274 EImpaEIREKLIRLQHENKMLRLGQE-GSYRERLTELQQLLEDANRRKNeletQNRLANQRileLQQQVEELQKALQEQG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1347 VRNHELEKKQRRFDS---ELSQAHEETQREKLQREKLQREKDMLLAE-AFSLKQQMEEKDLDIAGFTQK----------- 1411
Cdd:pfam05622 353 SKAEDSSLLKQKLEEhleKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEERykkyvekaksv 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082237 1412 VVSLEAELQDISSQEskdeasLAKVKKQLRDLEAKVKDQEEEldeqagsiqmLEQAKLRLEME 1474
Cdd:pfam05622 433 IKTLDPKQNPASPPE------IQALKNQLLEKDKKIEHLERD----------FEKSKLQREQE 479
|
|
| DUF1633 |
pfam07794 |
Protein of unknown function (DUF1633); This family contains sequences derived from a group of ... |
1437-1628 |
9.51e-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: 44.49 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1437 KKQLRDLEAKVK-DQEEELDEQAgsiQMLEQAKLRLEMEMermrqTHSKEMESRDEEveearqscqkKLKQMEVQLEEEY 1515
Cdd:pfam07794 457 ERAIREEDPHLGaDQDREVRFGA---EGIVPGIERLKIEL-----STSKDLEKGYAE----------KIGFMEMEFGGLE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1516 EDKQKALREKRELESKLSTLSDQVnqRDFESEKR-LRKDLKRTKALLADAQI-MLDHLKNNAPSKREIAQLKNQLEESEF 1593
Cdd:pfam07794 519 ADKQMARNQIHRLEEKKDELSKKV--LDLTSIAQgAKKAVHDAKVELAAAYLkLLAGIKDKWVAKKEFTVLEGQAAEVES 596
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907082237 1594 TCA---AAVKARKAMEVEMEDLHLQIDDIaKAKTALEE 1628
Cdd:pfam07794 597 NLAlidQITKAAIDLTLEKPRFQAEIDDL-EARCKLKE 633
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1540-1811 |
9.59e-04 |
|
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: 43.06 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1540 NQRDFESEKRLRKDLKRTKALLADAQImldhlknnapSKREIAQLKNQLEEseftcaAAVKARKAMEvemEDLHLQIDDI 1619
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDA----------SKQRAAAYQKALDD------APAELRELRQ---ELAALQAKAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1620 AKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNELMKkhkaavaqasrdmaQMNDLQAQIEESNKEKQELQEKLQALQS 1698
Cdd:pfam12795 69 AAPKEILASLsLEELEQRLLQTSAQLQELQNQLAQLNS--------------QLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1699 QvefLEQSMVDKSLVSrqEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRaaaenreKEQNKRLQRQLRD 1778
Cdd:pfam12795 135 R---LNGPAPPGEPLS--EAQRWALQAELAALKAQIDMLEQELLSNNNRQDLLKARRDLL-------TLRIQRLEQQLQA 202
|
250 260 270
....*....|....*....|....*....|...
gi 1907082237 1779 TKEEMSELARKEAEASRKkhELEMDLESLEAAN 1811
Cdd:pfam12795 203 LQELLNEKRLQEAEQAVA--QTEQLAEEAAGDH 233
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1298-1541 |
9.97e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1298 QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLT-AELQdtklhlEGQQVrnhELEKKQRRfdseLSQAheetqrEKLq 1376
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELEaAALQ------PGEEE---ELEEERRR----LSNA------EKL- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1377 REKLQREKDML----------LAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESK-------DEASLAKVKK- 1438
Cdd:COG0497 225 REALQEALEALsggeggaldlLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRyldslefDPERLEEVEEr 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1439 --QLRDLEAKVKDQEEELdeqagsIQMLEQAKLRLEmemermrqthskEMESRDEEVEEarqscqkkLKQMEVQLEEEYE 1516
Cdd:COG0497 305 laLLRRLARKYGVTVEEL------LAYAEELRAELA------------ELENSDERLEE--------LEAELAEAEAELL 358
|
250 260
....*....|....*....|....*
gi 1907082237 1517 DKQKALREKRELESKlsTLSDQVNQ 1541
Cdd:COG0497 359 EAAEKLSAARKKAAK--KLEKAVTA 381
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1156-1336 |
1.00e-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: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1156 DEEIQQLRSKLEKVEKERNELRLSSDrletriseltseLTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQ 1235
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNG------------LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1236 MEVMEMEVMEAR--------LIRAAEINGEVDdddaggEWRLKY-------ERAVREVDFTKKRLQQELEDKMEVEQQSR 1300
Cdd:COG3206 249 LGSGPDALPELLqspviqqlRAQLAELEAELA------ELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907082237 1301 RQLERRLGDLQADSDESQRALQQLKKKCQRLtAELQ 1336
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAEL-RRLE 357
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1148-1234 |
1.02e-03 |
|
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: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1148 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldAETAERLRTEKEMKELQT 1227
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKDREISRLDR 472
|
....*..
gi 1907082237 1228 QYDALKK 1234
Cdd:COG2433 473 EIERLER 479
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1609-1700 |
1.06e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 43.90 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1609 MEDLHLQIDDIAKAKTALE--------EQLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRDMAQMNDLQA 1677
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAkrgfpldvDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKE 80
|
90 100
....*....|....*....|...
gi 1907082237 1678 QIEESNKEKQELQEKLQALQSQV 1700
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRI 103
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1738-1847 |
1.19e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1738 ENLASRLKETMEKLTEERDQRAaaenREKEQNKRLQRQLRDTKEEMSELArKEAEAsrKKHELEMDLESLEAANQSLQAD 1817
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQA----REKAQSQALAEAQQQELVALEGLA-AELEE--KQQELEAQLEQLQEKAAETSQE 213
|
90 100 110
....*....|....*....|....*....|
gi 1907082237 1818 LKLAFKRIGDlQAAIEDEMESDENEDLINS 1847
Cdd:PRK11448 214 RKQKRKEITD-QAAKRLELSEEETRILIDQ 242
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1345-1819 |
1.46e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1345 QQVRNHELEKKQRRFDSE--LSQAHEETQR----EKLQREKLQREkdmLLAEAFSLKQQMEEK------------DLDIA 1406
Cdd:NF041483 76 QLLRNAQIQADQLRADAEreLRDARAQTQRilqeHAEHQARLQAE---LHTEAVQRRQQLDQElaerrqtveshvNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1407 GFTQKVVSLEAE---LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEM-------- 1475
Cdd:NF041483 153 WAEQLRARTESQarrLLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAERLLnaastqaq 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1476 ------ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesEKR 1549
Cdd:NF041483 233 eatdhaEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESAN------EQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1550 LRKdlkrtkalladaqimldhlknnapSKREIAQLKNQ-LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE 1628
Cdd:NF041483 307 TRT------------------------AKEEIARLVGEaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1629 --QLSRLQREKNEIQNRLEEDQEDM-----NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQ--------ELQEKL 1693
Cdd:NF041483 363 aaQLAKAARTAEEVLTKASEDAKATtraaaEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTkeyraktvELQEEA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1694 QALQSQVEFLEQSMVDKSLVSRQEAKireletrlefeKTQVKRLENLASRLKETMEKLTEERDQ--RAAAENREKEQNKR 1771
Cdd:NF041483 443 RRLRGEAEQLRAEAVAEGERIRGEAR-----------REAVQQIEEAARTAEELLTKAKADADElrSTATAESERVRTEA 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1772 LQR--QLRDTKEEMSELARKEAEasRKKHELEMDLESLEAANQSLQADLK 1819
Cdd:NF041483 512 IERatTLRRQAEETLERTRAEAE--RLRAEAEEQAEEVRAAAERAARELR 559
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1770-1864 |
1.69e-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: 41.02 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1770 KRLQRQLRDTKEEM-SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEdLINSL 1848
Cdd:pfam03938 18 KAAQAQLEKKFKKRqAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQE-LLQPI 96
|
90
....*....|....*.
gi 1907082237 1849 QDMVTKYQKKKNKLEG 1864
Cdd:pfam03938 97 QDKINKAIKEVAKEKG 112
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1680-1798 |
1.70e-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: 40.29 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1680 EESNKEKQELQEKLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKL------TE 1753
Cdd:pfam20492 2 EEAEREKQELEERLKQYEEETKKAQEEL------EESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLeesaemEA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907082237 1754 ERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKH 1798
Cdd:pfam20492 76 EEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1414-1715 |
1.80e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1414 SLEAeLQDISSQESKDEASLAKVKKQLRDLeAKVKDQEEELDEqagsiqmLEQaklRLEMEMERMRQThSKEMES-RDEE 1492
Cdd:PRK11281 44 QLDA-LNKQKLLEAEDKLVQQDLEQTLALL-DKIDRQKEETEQ-------LKQ---QLAQAPAKLRQA-QAELEAlKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1493 VEEARQSCQK-KLKQMEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL---RKDLKRT----KALL 1561
Cdd:PRK11281 111 DEETRETLSTlSLRQLESRLAQtldQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLqqiRNLLKGGkvggKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1562 ADAQIMLdhlknNApskrEIAQLKNQLEESEFTCAAAVKarkameveMEDLHLQIDDIAKAKTA-LEEQLSRLQREKNei 1640
Cdd:PRK11281 191 PSQRVLL-----QA----EQALLNAQNDLQRKSLEGNTQ--------LQDLLQKQRDYLTARIQrLEHQLQLLQEAIN-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1641 QNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQI--------EESNK-EKQELQEKLQ---ALQSQVEFLEQSMV 1708
Cdd:PRK11281 252 SKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLsqrllkatEKLNTlTQQNLRVKNWldrLTQSERNIKEQISV 331
|
....*....
gi 1907082237 1709 DK-SLV-SR 1715
Cdd:PRK11281 332 LKgSLLlSR 340
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1656-1803 |
1.88e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1656 KKHKAAVAQASRDMAQMndlqaqIEESNKEKQELQeKLQALQSQVEFLE-QSMVDKSLVSRqEAKIRELETRLEFEKTQV 1734
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRI------LEEAKKEAEAIK-KEALLEAKEEIHKlRNEFEKELRER-RNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1735 KRLENLASRLKETMEKLTEERDQR--------AAAENREKEQNKRLQRQLRDTKEE-----MSELARK-EAEASRKKHEL 1800
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKqqelekkeEELEELIEEQLQELERISGLTAEEakeilLEKVEEEaRHEAAVLIKEI 178
|
...
gi 1907082237 1801 EMD 1803
Cdd:PRK12704 179 EEE 181
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1716-1824 |
1.91e-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: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1716 QEAKIRELETRLEFEKTQVKRLENLASRLKETMEklteERDQRAAaenREKEQNKRLQRQLRDTKEEMSELARKEAEASR 1795
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELE----EKDERIE---RLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|..
gi 1907082237 1796 KKHELE---MDLESLEAANQSLQADLKLAFKR 1824
Cdd:COG2433 477 LERELEeerERIEELKRKLERLKELWKLEHSG 508
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1645-1795 |
2.04e-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: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1645 EEDQEDMNELMKKHKAAVAQASRDMAQ-MNDLQAQIEESNKEKQELQEKLQalqsqvefleqsmvdkslvsRQEAKIREL 1723
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEeIRRLEEQVERLEAEVEELEAELE--------------------EKDERIERL 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082237 1724 ETRLEFEKTQVKRlenlasrlketmekltEERDQRaAAENREKEqNKRLQRQLRDTKEEMSELARKEAEASR 1795
Cdd:COG2433 447 ERELSEARSEERR----------------EIRKDR-EISRLDRE-IERLERELEEERERIEELKRKLERLKE 500
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1285-1422 |
2.09e-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: 42.66 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1285 LQQELEDKmEVEQQSRRQLERRLgdlqadsDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnheLEKKQRRFDSELS 1364
Cdd:pfam02841 178 LQEFLQSK-EAVEEAILQTDQAL-------TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQM---MEAQERSYQEHVK 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1365 QAHEETQREklqREKLQREKDMLLAeafslKQQMEEKDLDIAGFTQKVVSLEAELQDI 1422
Cdd:pfam02841 247 QLIEKMEAE---REQLLAEQERMLE-----HKLQEQEELLKEGFKTEAESLQKEIQDL 296
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1576-1873 |
2.15e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1576 PSKREIaqlKNQLEeseftcaaAVKARKAMEVE-------MEDLHLQIDDIAKAK---TALEEQLSRLQREKNEIQNRLE 1645
Cdd:PRK11281 36 PTEADV---QAQLD--------ALNKQKLLEAEdklvqqdLEQTLALLDKIDRQKeetEQLKQQLAQAPAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1646 EdqedmnelMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQvefleqsmvdksLVSRQEAKIReLET 1725
Cdd:PRK11281 105 A--------LKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQ------------LVSLQTQPER-AQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1726 RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELArkeaeasRKKHELemdle 1805
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLL-------QKQRDY----- 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1806 sLEAANQSLQadlklafKRIGDLQAAIedemesdeNEDLINSLQDMVTKYQ--KKKNKLEGDSDVDSELE 1873
Cdd:PRK11281 232 -LTARIQRLE-------HQLQLLQEAI--------NSKRLTLSEKTVQEAQsqDEAARIQANPLVAQELE 285
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1476-1801 |
2.24e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1476 ERMRQTHSKEMESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKalrekrelesklstLSDQVNQRDFESEKRLRKDL 1554
Cdd:pfam02029 18 ERRRQKEEEEPSGQvTESVEPNEHNSYEEDSELKPSGQGGLDEEEA--------------FLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1555 KRTKALLadaqimldhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhlqiddiakaktalEEQLSRlq 1634
Cdd:pfam02029 84 ERQKEFD----------PTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYK----------------EEETEI-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1635 REKNEIQNRLEEDQEDMNELMKKHKAAVAQASR-DMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS------M 1707
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEvPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKsqngeeE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1708 VDKSLVS--RQEAKIRELETRLEFEKTQV---KRLENLASRLKET----MEKLtEERDQRAAAE----NREKEQNKRL-- 1772
Cdd:pfam02029 216 VTKLKVTtkRRQGGLSQSQEREEEAEVFLeaeQKLEELRRRRQEKeseeFEKL-RQKQQEAELEleelKKKREERRKLle 294
|
330 340
....*....|....*....|....*....
gi 1907082237 1773 QRQLRDTKEEMSELARKEAEASRKKHELE 1801
Cdd:pfam02029 295 EEEQRRKQEEAERKLREEEEKRRMKEEIE 323
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1425-1789 |
2.64e-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: 43.13 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1425 QESKD-EASLAKVKKQLRDLEAKVKDQEEELdeqagsiqmlEQAKLRLEMEMERMRQTHSKEMESR-DEEVEEARQSCQK 1502
Cdd:pfam13166 89 EESIEiQEKIAKLKKEIKDHEEKLDAAEANL----------QKLDKEKEKLEADFLDECWKKIKRKkNSALSEALNGFKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1503 KLKQMEVQLEE--EYEDKQKALREKRELESKLSTLSDQ---------VNQRDFESEKRLRKDLKRTKALLADAQIMLDHL 1571
Cdd:pfam13166 159 EANFKSRLLREieKDNFNAGVLLSDEDRKAALATVFSDnkpeiapltFNVIDFDALEKAEILIQKVIGKSSAIEELIKNP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1572 KNNAPSKREIAQLKNQLEESEFtC--------AAAVKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQL----------S 1631
Cdd:pfam13166 239 DLADWVEQGLELHKAHLDTCPF-CgqplpaerKAALEAHfdDEFTEFQNRLQKLIEKVESAISSLLAQLpavsdlasllS 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1632 RLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASR---------DMAQMNDLQAQIEES----NKEKQELQEKLQALQS 1698
Cdd:pfam13166 318 AFELDVEDIESEAEVLNSQLDGLRRALEAKRKDPFKsieldsvdaKIESINDLVASINELiakhNEITDNFEEEKNKAKK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1699 QVEfleqsmvdKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRD 1778
Cdd:pfam13166 398 KLR--------LHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKL--------------REEIKELEAQLRD 455
|
410
....*....|....
gi 1907082237 1779 TK---EEMSELARK 1789
Cdd:pfam13166 456 HKpgaDEINKLLKA 469
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1285-1446 |
2.67e-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: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1285 LQQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRrfds 1361
Cdd:pfam13851 27 LIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELK---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1362 ELSQAHEEtqreKLQR-EKLQREKDMLLAE----AFSLKQQMEEKDLDIAgftQKVVSL-------EAELQDISSQESKD 1429
Cdd:pfam13851 103 DLKWEHEV----LEQRfEKVERERDELYDKfeaaIQDVQQKTGLKNLLLE---KKLQALgetlekkEAQLNEVLAAANLD 175
|
170
....*....|....*...
gi 1907082237 1430 EASLAKVKKQLRD-LEAK 1446
Cdd:pfam13851 176 PDALQAVTEKLEDvLESK 193
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1553-1809 |
2.70e-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: 42.97 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1553 DLKRTKALladaqIMLDHLKNNAPSKREiaQLKNQLE-ESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLS 1631
Cdd:pfam15964 348 NFEKTKAL-----IQCEQLKSELERQKE--RLEKELAsQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1632 RLQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDMA-QMNDLQAQIEESNKEKQELQEKlqaLQSQVEFLEQsmvdk 1710
Cdd:pfam15964 421 KVTREKNSLVSQLEEAQKQ----LASQEMDVTKVCGEMRyQLNQTKMKKDEAEKEHREYRTK---TGRQLEIKDQ----- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1711 slvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDqraaaenrEKEQNKRLQRQLRDTKEE-MSELARK 1789
Cdd:pfam15964 489 --------EIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG--------ESEHQLHLTRLEKESIQQsFSNEAKA 552
|
250 260
....*....|....*....|.
gi 1907082237 1790 EA-EASRKKHELEMDLESLEA 1809
Cdd:pfam15964 553 QAlQAQQREQELTQKMQQMEA 573
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1437-1524 |
2.78e-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: 40.25 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1437 KKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1516
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQ 97
|
....*....
gi 1907082237 1517 DK-QKALRE 1524
Cdd:pfam03938 98 DKiNKAIKE 106
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1579-1822 |
3.24e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1579 REIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1658
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1659 KAAVAQASRDMAQMNDLQAQI-------EESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEK 1731
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLkeakeiaEEADRKYEEVARKLVVVEGDLERAEER------AELAESKIVELEEELKVVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1732 TQVKRLENLAsrlketmekltEERDQRaaaENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAAN 1811
Cdd:pfam00261 155 NNLKSLEASE-----------EKASER---EDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKY 220
|
250
....*....|.
gi 1907082237 1812 QSLQADLKLAF 1822
Cdd:pfam00261 221 KAISEELDQTL 231
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1157-1651 |
3.24e-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: 42.74 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1157 EEIQQLRSKLEKVEKERnelrlssDRLETRISELTSELTDERNTGESASQLLDAETA----ERLRTEKEMKELQTQYDAL 1232
Cdd:pfam15070 29 QKMQQLSEQVRTLREEK-------ERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgpseEEQRLQEEAEQLQKELEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1233 kkqmevmemevmearlirAAEINGEVDDDDagGEWRLKYERAVREVDftkkrLQQELEDKMEVEQQSRRQLErrlgDLQA 1312
Cdd:pfam15070 102 ------------------AGQLQAQVQDNE--QLSRLNQEQEQRLLE-----LERAAERWGEQAEDRKQILE----DMQS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1313 DSDESQRALQQLKKKCQRLtAELQD-------------TKLHLEgQQVRNhELEKKQRRFDSELSQAHEETQREKLQREK 1379
Cdd:pfam15070 153 DRATISRALSQNRELKEQL-AELQNgfvkltnenmeltSALQSE-QHVKK-ELAKKLGQLQEELGELKETLELKSQEAQS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1380 LQREKDMLLAE----AFSLKQQMEEKDLdiagfTQKVVSLEAELQD-ISSQESKDEASLAKVKKQLRD----LEAKVKDQ 1450
Cdd:pfam15070 230 LQEQRDQYLAHlqqyVAAYQQLASEKEE-----LHKQYLLQTQLMDrLQHEEVQGKVAAEMARQELQEtqerLEALTQQN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1451 EEEldeQAGSIQMLEQAK---LRLEMEMERMRQTH---SKEMESRDEEVE---EARQSCQKKLKQMEVQLEEEYedkqka 1521
Cdd:pfam15070 305 QQL---QAQLSLLANPGEgdgLESEEEEEEAPRPSlsiPEDFESREAMVAffnSALAQAEEERAELRRQLKEQK------ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1522 lREKRELESKLSTLSDQvnQRDFESEKRLRKD---LKRTKALladaQIMLDHLKNNAPS-KREIAQLKNQLEESEFTCAa 1597
Cdd:pfam15070 376 -RRCRRLAQQAAPAQEE--PEHEAHAPGTGGDsvpVEVHQAL----QVAMEKLQSRFTElMQEKADLKERVEELEHRCI- 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082237 1598 avkarkamevemeDLHLQIDDIAKAKTALEEQ---LSRLQREKNEIQNRLEEDQEDM 1651
Cdd:pfam15070 448 -------------QLSGETDTIGEYIALYQSQraiLKQRHREKEEYISRLAQDKEEM 491
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1609-1776 |
3.64e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 41.26 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1609 MEDLHLQIDDIAKAKTALEEQ----LSRL----QRE----------KNEIQN----------RLEEDQEDMNELMKKHKA 1660
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQsqnlLSKLeiaqQKEskflenlaslKHENDNlssmlnrkerRLKDLEDQLSELKNSYEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1661 AVaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqSMVDKSLVSRQ--EAKIRELETRLE-FEKTQVKRL 1737
Cdd:pfam17078 85 LT-------ESNKQLKKRLENSSASETTLEAELERLQIQYD----ALVDSQNEYKDhyQQEINTLQESLEdLKLENEKQL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907082237 1738 ENLASRL----KETMEKLTEERDQRAAAENREKEQNKRLQRQL 1776
Cdd:pfam17078 154 ENYQQRIssndKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKL 196
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1585-1809 |
3.98e-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: 42.13 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1585 KNQLEESEFTCAAAVKARKAMEVEMEDLHLQ--IDDIAKAKTALEEQLS---RLQREKNEIQNRLEEDQEdmnelmkkhk 1659
Cdd:pfam15066 329 KQQMQIQDLQCSNLYLEKKVKELQMKITKQQvfVDIINKLKENVEELIEdkyNVILEKNDINKTLQNLQE---------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1660 aavaqasrdmaQMNDLQAQIEESNKEKQELQEKLQALQ-SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLE 1738
Cdd:pfam15066 399 -----------ILANTQKHLQESRKEKETLQLELKKIKvNYVHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQ 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082237 1739 nlasRLKETMEKLTEerdqrAAAENREKEQNKRLQRQLRDTKeemsELARKEAEASRKKHELEMDLESLEA 1809
Cdd:pfam15066 468 ----QLKGELEKATT-----SALDLLKREKETREQEFLSLQE----EFQKHEKENLEERQKLKSRLEKLVA 525
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
1670-1754 |
4.46e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 38.74 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1670 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS--------MVDKSLVSR-QEAKIRELETRLEFEKTQVKRLENL 1740
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLdedtkvykLIGDVLVKQdKEEVKEQLEERKETLEKEIKTLEKQ 81
|
90
....*....|....
gi 1907082237 1741 ASRLKETMEKLTEE 1754
Cdd:pfam01920 82 LEKLEKELEELKEE 95
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1203-1462 |
4.51e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1203 SASQLLDAETAERLRTEKEmkeLQTQYDALKKQMEVmemevmearliraaeingEVDDddaggewrlkyeravrevdftk 1282
Cdd:PRK11281 22 LSSAFARAASNGDLPTEAD---VQAQLDALNKQKLL------------------EAED---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1283 KRLQQELE------DKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAE-LQDTKL-HLEGQQV-RNHELE 1353
Cdd:PRK11281 59 KLVQQDLEqtlallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtLSTLSLrQLESRLAqTLDQLQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1354 KKQRRF---DSELSQAHeeTQREKLQRE---KLQR---------------------EKDMLLAEAFSLKQQMEEKDLDIA 1406
Cdd:PRK11281 139 NAQNDLaeyNSQLVSLQ--TQPERAQAAlyaNSQRlqqirnllkggkvggkalrpsQRVLLQAEQALLNAQNDLQRKSLE 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082237 1407 GFTQkvvsleaeLQDIsSQESKDEASL--AKVKKQLRDLE----AKVKDQEEELDEQAGSIQ 1462
Cdd:PRK11281 217 GNTQ--------LQDL-LQKQRDYLTAriQRLEHQLQLLQeainSKRLTLSEKTVQEAQSQD 269
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1474-1647 |
4.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1474 EMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQV-NQRDFES-EKRLr 1551
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEAlQKEI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1552 KDLKRTKALLADaqimldhlknnapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAktaLEEQLS 1631
Cdd:COG1579 99 ESLKRRISDLED----------------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELE 159
|
170
....*....|....*.
gi 1907082237 1632 RLQREKNEIQNRLEED 1647
Cdd:COG1579 160 ELEAEREELAAKIPPE 175
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
1638-1763 |
4.84e-03 |
|
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.
Pssm-ID: 464990 [Multi-domain] Cd Length: 181 Bit Score: 40.36 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1638 NEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEK-------QELQEK--LQALQSQVEF------ 1702
Cdd:pfam16043 10 DQLQALILDLQEELEKLSETTSELSERLQQRQKHLEALYQQIEKLEKVKadkevveEELDEKadKEALASKVSRdqfdet 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1703 ---LEQSMVDK-SLVSRQEAKIR---ELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1763
Cdd:pfam16043 90 leeLNQMLQELlDKLEGQEDAWKkalETLSEELDTKLDRLELDPLKELLERRIKALQKLLQEGSEELD 157
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1385-1862 |
4.88e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1385 DMLLAEAFSLKQQMEEKDLDIagfTQKVVSLEAELQDISSQESKDEASL-----------AKVKKQLRDLEAKVKDQEEE 1453
Cdd:PTZ00440 601 EELINEALFNKEKFINEKNDL---QEKVKYILNKFYKGDLQELLDELSHflddhkylyheAKSKEDLQTLLNTSKNEYEK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1454 LDEQAGSI--QMLEQAKLRLEmemermrqtHSKEMESR--DEEVEEARQSCQKKLKQMEvqleEEYEDKQKALREKRELE 1529
Cdd:PTZ00440 678 LEFMKSDNidNIIKNLKKELQ---------NLLSLKENiiKKQLNNIEQDISNSLNQYT----IKYNDLKSSIEEYKEEE 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1530 SKLSTLSDQVNQRdfesEKRLRKDLKRTKALLADAQIMLDHLKNNapsKREIAQLKNQLEESEFTCAAAVKARKAMEVEM 1609
Cdd:PTZ00440 745 EKLEVYKHQIINR----KNEFILHLYENDKDLPDGKNTYEEFLQY---KDTILNKENKISNDINILKENKKNNQDLLNSY 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1610 EDLHLQIDDIAKAKTALEEQLsrLQREKNEIQN-RLEEDQEDMNELMKKhkaavaqasrdmaqMNDLQAQIEESNKekqe 1688
Cdd:PTZ00440 818 NILIQKLEAHTEKNDEELKQL--LQKFPTEDENlNLKELEKEFNENNQI--------------VDNIIKDIENMNK---- 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1689 lqeKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEfektqvkrlenlaSRLKETMEKLTEERDQRAAAENREKEQ 1768
Cdd:PTZ00440 878 ---NINIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLE-------------QHMKIINTDNIIQKNEKLNLLNNLNKE 941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1769 NKRLQRQLRDTKeeMSELarkeaeasrkKHELEMDLESLEAANQSLQADLKLafkrigDLQAAIEDEMESDENEDLINSL 1848
Cdd:PTZ00440 942 KEKIEKQLSDTK--INNL----------KMQIEKTLEYYDKSKENINGNDGT------HLEKLDKEKDEWEHFKSEIDKL 1003
|
490
....*....|....
gi 1907082237 1849 QdmvTKYQKKKNKL 1862
Cdd:PTZ00440 1004 N---VNYNILNKKI 1014
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1601-1705 |
5.11e-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: 39.09 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1601 ARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIE 1680
Cdd:pfam13863 11 VQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIE 90
|
90 100
....*....|....*....|....*
gi 1907082237 1681 ESNKEKQELQEKLQALQSQVEFLEQ 1705
Cdd:pfam13863 91 ELKSEISKLEEKLEEYKPYEDFLEK 115
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1603-1789 |
5.77e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.60 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1603 KAMEVEMEDLHLQIDDIAKAktaLEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLqaQIEES 1682
Cdd:pfam04108 20 RSLLEELVVLLAKIAFLRRG---LSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNT--PVEPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1683 NKEKQELQEKLqalqsqvefleQSMVDKSLVSRQEAKIRELETRLefeKTQVKRLENLASRLKETMEKLTEERDQRAAAe 1762
Cdd:pfam04108 95 LPPGEEKQKTL-----------LDFIDEDSVEILRDALKELIDEL---QAAQESLDSDLKRFDDDLRDLQKELESLSSP- 159
|
170 180
....*....|....*....|....*..
gi 1907082237 1763 NREKEQNKRLQRQLRDTKEEMSELARK 1789
Cdd:pfam04108 160 SESISLIPTLLKELESLEEEMASLLES 186
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1285-1524 |
5.92e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.51 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1285 LQQELEDKMEVEQQSRRQLERRLGDLQADSDESQraLQQLKKKCQRLTAELQdtklhleGQQVRNHELEKKQRRFDSELS 1364
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLES--VEALLKKHEALEAELA-------AHEERVEALNELGEQLIEEGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1365 QAHEETQReklQREKLQREKDMLLAEAFSLKQQMEEKdLDIAGFTQKVVSLEAELQDISSQESKDE--ASLAKVKKQLRD 1442
Cdd:cd00176 72 PDAEEIQE---RLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1443 LeakvKDQEEELDEQAGSIQMLEQAKLRLEmemermrqthskemESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKAL 1522
Cdd:cd00176 148 H----KELEEELEAHEPRLKSLNELAEELL--------------EEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
|
..
gi 1907082237 1523 RE 1524
Cdd:cd00176 210 EE 211
|
|
| LXG |
pfam04740 |
LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of ... |
1637-1732 |
6.25e-03 |
|
LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of polymorphic toxin proteins in bacteria. It is predicted to use Type VII secretion pathway to mediate export of bacterial toxins.
Pssm-ID: 428100 [Multi-domain] Cd Length: 202 Bit Score: 40.31 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1637 KNEIQNRLEEDQEDMNELMKKHKAAVAQASR----DMAQMNDLQAQIEESNKEKQELQEKLQAL-QSQVEFLEQSmvdKS 1711
Cdd:pfam04740 101 EHELENGLKKAKEKTEELTDEINSILASVSDivslPKLSDSEVQDSLQKAKKKVKDTIEKLYDFdQEQTSELSEL---EA 177
|
90 100
....*....|....*....|.
gi 1907082237 1712 LVSRQEAKIRELETRLEFEKT 1732
Cdd:pfam04740 178 DLQALKTYVSELEEMTSNGKI 198
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
1610-1863 |
6.27e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 41.07 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1610 EDLHLQIDDIAKAKTALEEQLsrlqrekNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMA------QMNDLQAQIEESN 1683
Cdd:pfam13949 20 ERLEKSLDDLPKLKQRNREIL-------DEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELtatlraEIRKYREILEQAS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1684 KEKQELQEKLQALQSQVEFLEQSMVD--KSLVSRQEAKIREletrlefektqvkRLENLASRLKETMEKLTEERDQRAAA 1761
Cdd:pfam13949 93 ESDSQVRSKFREHEEDLELLSGPDEDleAFLPSSRRAKNSP-------------SVEEQVAKLRELLNKLNELKREREQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1762 EN--REKEQNKRLQRQLRDTKEEMSELARKEA---EASRKKHELEMDLESLEAANQSLQADLKLAFKRIgdLQAAIEDEM 1836
Cdd:pfam13949 160 LKdlKEKARNDDISPKLLLEKARLIAPNQEEQlfeEELEKYDPLQNRLEQNLHKQEELLKEITEANNEF--LQDKRVDSE 237
|
250 260
....*....|....*....|....*..
gi 1907082237 1837 ESDENEDLINSLQDMVTKYQKKKNKLE 1863
Cdd:pfam13949 238 KQRQREEALQKLENAYDKYKELVSNLQ 264
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1629-1818 |
6.89e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1629 QLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRdmaQMNDLQAQIEESNKEKQELQEKLQALQSQvefleQ 1705
Cdd:PRK11637 48 QLKSIQQDIAAKEKSVRQQQQQRASLlaqLKKQEEAISQASR---KLRETQNTLNQLNKQIDELNASIAKLEQQ-----Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1706 SMVDKSLVSRQEAKIRE-----LETRLEFEKTQVK-RLENLASRL----KETMEKLTEERDQrAAAENREKEQNKRLQRQ 1775
Cdd:PRK11637 120 AAQERLLAAQLDAAFRQgehtgLQLILSGEESQRGeRILAYFGYLnqarQETIAELKQTREE-LAAQKAELEEKQSQQKT 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907082237 1776 LRDTKEEmSELARKEAEASRKKhelemDLESLEAANQSLQADL 1818
Cdd:PRK11637 199 LLYEQQA-QQQKLEQARNERKK-----TLTGLESSLQKDQQQL 235
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1527-1797 |
8.02e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 40.83 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1527 ELESKLSTLSDQVNQRdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaavkarKAME 1606
Cdd:pfam04108 116 ILRDALKELIDELQAA----QESLDSDLKRFDDDLRDLQKELESLSSPSESISLIPTLLKELESLE----------EEMA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1607 VEMEDLHLQIDDIAKAKTALEEqlsrlqrEKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQmndLQAQIEESNKEK 1686
Cdd:pfam04108 182 SLLESLTNHYDQCVTAVKLTEG-------GRAEMLEVLENDARELDDVVPELQDRLDEMENNYER---LQKLLEQKNSLI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1687 QELQEKLQalqsqvefleqsmvdkslvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEE-RDQRAAAEN-- 1763
Cdd:pfam04108 252 DELLSALQ------------------------LIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSElEDLREFYEGfp 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907082237 1764 -----------REKEQNKRLQRQLRDTKEEMSELARKEAEAsRKK 1797
Cdd:pfam04108 308 saygsllleveRRREWAEKMKKILRKLAEELDRLQEEERKR-REK 351
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1148-1366 |
8.12e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1148 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDerntgesasqlldaetaerlrTEKEMKELQT 1227
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA---------------------LQAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1228 QYDALKKQmeVMEMEVMEARLIRAAEINGEVDDDDA---GGE------WRLKYERAVREVDFTKKRLQQELEDKMEVEQQ 1298
Cdd:COG3883 73 EIAEAEAE--IEERREELGERARALYRSGGSVSYLDvllGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082237 1299 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQA 1366
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1148-1371 |
8.50e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1148 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELtdeRNTGESASQLLDAETAERLRTekEMKELQT 1227
Cdd:COG3206 203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL---GSGPDALPELLQSPVIQQLRA--QLAELEA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1228 QYDALkkqmevmemevmearliraaeingevddddaggewRLKYERAVREVdftkKRLQQELEdkmEVEQQSRRQLERRL 1307
Cdd:COG3206 278 ELAEL-----------------------------------SARYTPNHPDV----IALRAQIA---ALRAQLQQEAQRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082237 1308 GDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSeLSQAHEETQ 1371
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES-LLQRLEEAR 378
|
|
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
1732-1807 |
9.23e-03 |
|
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.
Pssm-ID: 432481 [Multi-domain] Cd Length: 115 Bit Score: 38.30 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1732 TQVKRLENLASRLKETMEKLTEERDQrAAAE----NREKEQNKRLQRQLRDTKEEMSELARKEA-------EASRKKHEL 1800
Cdd:pfam12325 19 STIRRLEGELASLKEELARLEAQRDE-ARQEivklMKENEELKELKKELEELEKELKELEQRYEttlellgEKSEEVEEL 97
|
....*..
gi 1907082237 1801 EMDLESL 1807
Cdd:pfam12325 98 KADVEDL 104
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
1610-1703 |
9.35e-03 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 40.38 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1610 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKekqEL 1689
Cdd:pfam14932 70 EALEESLEEIREATEDLEAELQELQKTKQLKINRLNKLQAQASSLSQGLRALVAEEEEAAKQLEELQEELAALNA---KT 146
|
90
....*....|....
gi 1907082237 1690 QEKLQALQSQVEFL 1703
Cdd:pfam14932 147 NNVLQSLQSEVKEL 160
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1507-1928 |
9.56e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.86 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1507 MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrlrkDLKRTKALLADAQIMLDHLKNN-APSKREIAQLK 1585
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE----DLKRQNAVLQEAQVELDALQNQlALARAEMENIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1586 NQLEESEFTCAAAV-KARKAMEVEMEDLHLQIDDIAKA-----KTALEEQLSR-------LQREKNEIQNRLEEDQEDMN 1652
Cdd:pfam03528 82 AVATVSENTKQEAIdEVKSQWQEEVASLQAIMKETVREyevqfHRRLEQERAQwnqyresAEREIADLRRRLSEGQEEEN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1653 ---------ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKE-----KQELQEKLQALQSQVEFLEQSM----VDKSLVS 1714
Cdd:pfam03528 162 ledemkkaqEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKEleaskMKELNHYLEAEKSCRTDLEMYVavlnTQKSVLQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1715 RQEAKIR----ELETRLEFEKTQVKRL--------------ENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQL 1776
Cdd:pfam03528 242 EDAEKLRkelhEVCHLLEQERQQHNQLkhtwqkandqflesQRLLMRDMQRMESVLTSEQLRQVEEIKKKDQEEHKRART 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1777 RDTKEEMSE-----------LARKEAEASRKKHELEMDLESLEAANQSLQADLKL----AFKRIGDLqaaIEDEMESDEN 1841
Cdd:pfam03528 322 HKEKETLKSdrehtvsihavFSPAGVETSAPLSNVEEQINSAHGSVHSLDTDVVLgagdSFNKQEDP---FKEGLRRAQS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082237 1842 EDLINSLQDMVTKYQKKKNKLEGDSDVD-SELEDRV--DGV-KSWLSKNKGPSKAPSDDGSLKSSRTALNSLPKEgkgpE 1917
Cdd:pfam03528 399 TDSLGSSSSLQHKFLGHNQKAKSAGNLDeSDFGPLVgaDSVsENFDTSSLGSLKMPSGFMLTKDQEKAIKAMTPE----Q 474
|
490
....*....|.
gi 1907082237 1918 ERPSSVLSSLS 1928
Cdd:pfam03528 475 EETASLLSSVT 485
|
|
| |
