|
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 ... |
467-1213 |
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: 1128.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTSGtKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 626
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVG-GVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEE 706
Cdd:cd01386 160 LLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 707 QKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFRQGPEESGLG 783
Cdd:cd01386 240 QRAIWSILAAIYHLGAAGATKaasAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQESPARSSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 784 EGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGSARGASFEELCHNYAQDRLQR 863
Cdd:cd01386 320 GGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERLQL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 864 LFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASH--LVRSLAHADEARGLLWLLEEEALVPGATEDALLDRL 941
Cdd:cd01386 400 LFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqaLVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFLERL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 942 FSYYGPQEGDkKGQSPLLRSSKPRHFLLGHSHGTNWVEYNVAGWLNYTKQNPATQNAPRLLQDSQKKiisnlflgragsa 1021
Cdd:cd01386 480 FSHYGDKEGG-KGHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE------------- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1022 tvlsgsiagleggsqlalrratsmrktfttgMAAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGEPRsa 1101
Cdd:cd01386 546 -------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDERS-- 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1102 ssrrvsssseldlppGDPCEAGLLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYI 1181
Cdd:cd01386 593 ---------------TSSPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSE 657
|
730 740 750
....*....|....*....|....*....|..
gi 1907082213 1182 VVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd01386 658 VADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
468-1213 |
3.37e-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: 462.06 E-value: 3.37e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFS-----VEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 621
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSSsassiEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 622 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAEN---NVFGIVPLSKPEEKQKAAQQFSKLQAAMK 698
Cdd:cd00124 162 SIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYyylNDYLNSSGCDRIDGVDDAEEFQELLDALD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 699 VLAISPEEQKTCWLILASIYHLG-----AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTlqrstsf 773
Cdd:cd00124 242 VLGFSDEEQDSIFRILAAILHLGniefeEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGG------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 774 rqgpeESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSS--QHSLCSMMIVDTPGFQNPEWggsargASFEE 851
Cdd:cd00124 315 -----ETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTdaAESTSFIGILDIFGFENFEV------NSFEQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 852 LCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDLEPVAD------DSV-AAVDQASHLvrslahadeargllw 921
Cdd:cd00124 384 LCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSfidFPDNQDCLDliegkpLGIlSLLDEECLF--------------- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 922 lleeealvPGATEDALLDRLFSYYGPQEGDKKGqspllRSSKPRHFllGHSHGTNWVEYNVAGWLNYTKQNpatqnaprl 1001
Cdd:cd00124 449 --------PKGTDATFLEKLYSAHGSHPRFFSK-----KRKAKLEF--GIKHYAGDVTYDADGFLEKNKDT--------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1002 lqdsqkkiisnlflgragsatvLSGSIAGLeggsqlaLRRATSMRKtfttgmaavkkkslciqiklQVDALIDTIKRSKM 1081
Cdd:cd00124 505 ----------------------LPPDLVDL-------LRSGSQFRS--------------------QLDALMDTLNSTQP 535
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1082 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1161
Cdd:cd00124 536 HFVRCIKPNDEKKPG-----------------------------LFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1907082213 1162 RRRFDVLAPHLTKKHGRNYIVVDEKRAveellESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd00124 587 LKRYRILAPGATEKASDSKKAAVLALL-----LLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
448-1225 |
3.23e-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: 376.89 E-value: 3.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 448 NAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQ 527
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 528 TAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGtSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFS 605
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG-SNTEVGSVED-QILESnpILEAFGNAKTLRNNNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 606 QILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFgivpLSKPEEKQK 685
Cdd:smart00242 159 KFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRY----LNQGGCLTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 686 A----AQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG----AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAI 757
Cdd:smart00242 234 DgiddAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGniefEEGRNDNAASTVKDKEELSNAAELLGVDPEELEKAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 758 fkhqlkggtLQRSTSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQ- 836
Cdd:smart00242 314 ---------TKRKIKTGGEVITKPL---NVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEi 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 837 ---NpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVRS- 909
Cdd:smart00242 382 fevN----------SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDwtfIDFFDNQDCID-----------LIEKk 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 910 ----LAHADEArgllwlleeeALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEYNV 982
Cdd:smart00242 441 ppgiLSLLDEE----------CRFPKGTDQTFLEKLNQHH--------KKHPHFSKPKKKgrtEFIIKHYAGD--VTYDV 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 983 AGWLnytKQN--PATQNAPRLLQDSQKKIISNLFlgragsatvlsGSIAGleggsqlalrRATSMRKTFTTGMaavkkks 1060
Cdd:smart00242 501 TGFL---EKNkdTLSDDLIELLQSSKNPLIASLF-----------PSGVS----------NAGSKKRFQTVGS------- 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1061 lciQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSR 1140
Cdd:smart00242 550 ---QFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPG-----------------------------DFDSSLVLHQLRYLG 597
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1141 LLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFRAGTLARL 1220
Cdd:smart00242 598 VLENIRIRRAGFPYRLPFDEFLQRYRVLLPD-TWPPWGG----DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAEL 672
|
....*
gi 1907082213 1221 EEQRD 1225
Cdd:smart00242 673 EELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
429-1939 |
1.98e-110 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 388.67 E-value: 1.98e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 429 KLDHDGAILDVDEDDIEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMH 508
Cdd:COG5022 42 KEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 509 MFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKwQALST--L 586
Cdd:COG5022 122 SYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEK-QILATnpI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 587 LEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL--- 663
Cdd:COG5022 201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLqnp 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 664 ---NHLAENNVFGIVPLSKPEEkqkaaqqFSKLQAAMKVLAISPEEQKTCWLILASIYHLG--AAGATKAGRKQFARHEW 738
Cdd:COG5022 281 kdyIYLSQGGCDKIDGIDDAKE-------FKITLDALKTIGIDEEEQDQIFKILAAILHIGniEFKEDRNGAAIFSDNSV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 739 AQKAAYLLGCSLEELSSAIFKHQLKGG--TLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRA 816
Cdd:COG5022 354 LDKACYLLGIDPSLFVKWLVKRQIKTGgeWIVVPLNLEQ--------------ALAIRDSLAKALYSNLFDWIVDRINKS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 817 LKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVA 893
Cdd:COG5022 420 LDHSAAASNFIGVLDIYGFEIFEKN------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEwsfIDYFDNQPCI 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 894 DDSvaavdQASHLVRSLAHADEArgllwlleeeALVPGATEDALLDRLFSYYgPQEGDKKGQSPLLRSSKprhFLLGHSH 973
Cdd:COG5022 494 DLI-----EKKNPLGILSLLDEE----------CVMPHATDESFTSKLAQRL-NKNSNPKFKKSRFRDNK---FVVKHYA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 974 GTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvlsgsiaglEGGSQLALRRATSMrktfttgm 1053
Cdd:COG5022 555 GD--VEYDVEGFLDKNK-DPLNDDLLELLKASTNEFVSTLFDDEE-------------NIESKGRFPTLGSR-------- 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1054 aavkkkslciqIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLR 1133
Cdd:COG5022 611 -----------FKESLNSLMSTLNSTQPHYIRCIKPNEEKSPW-----------------------------TFDNQMVL 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1134 AQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNYIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:COG5022 651 SQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPS-KSWTGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFK 729
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1214 AGTLARLEEQRDEQTSRHLTLFQAACRGYLARQHF-KKRKIQDlAIRCVQKNIKKNKGVKDWPWWKLFTTVRPLIQVQLS 1292
Cdd:COG5022 730 AGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYlQALKRIK-KIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGS 808
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1293 EEQIRNKDEEIQQLRSKLEKV----EKERNELRLSSDRLETRISEltSELTDERNTGESASQLLDAETAERLRTEKEMKE 1368
Cdd:COG5022 809 RKEYRSYLACIIKLQKTIKREkklrETEEVEFSLKAEVLIQKFGR--SLKAKKRFSLLKKETIYLQSAQRVELAERQLQE 886
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1369 LQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDF----TKKRLQQELEDKMEVEQQSR 1444
Cdd:COG5022 887 LKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLeegpSIEYVKLPELNKLHEVESKL 966
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1445 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRrfdsELSQAHEETQREKLQREKL 1524
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPV----EVAELQSASKIISSESTEL 1042
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1525 QREKDMLLAEAFSLKQQME-EKDLdiagftqKVVSLEAELQDIssqESKDEASLAKVKKQLRDLEAK---VKDQEEELDE 1600
Cdd:COG5022 1043 SILKPLQKLKGLLLLENNQlQARY-------KALKLRRENSLL---DDKQLYQLESTENLLKTINVKdleVTNRNLVKPA 1112
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1601 QAGSIQMLEQAKLRLEMEMERM--RQTHSKEMESRDEEVEEARQSCQKKLKQMEvqlEEEYEDKQKALREKRELESKL-- 1676
Cdd:COG5022 1113 NVLQFIVAQMIKLNLLQEISKFlsQLVNTLEPVFQKLSVLQLELDGLFWEANLE---ALPSPPPFAALSEKRLYQSALyd 1189
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1677 --STLSDQVNQ---RDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLknqleESEFTCAAAVKarkamev 1751
Cdd:COG5022 1190 ekSKLSSSEVNdlkNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNL-----NKKFDTPASMS------- 1257
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1752 eMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLeeDQEDMNEL-MKKHKAAVAQASRDmaqmnDLQAQIEESNKEK 1830
Cdd:COG5022 1258 -NEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYI--NVGLFNALrTKASSLRWKSATEV-----NYNSEELDDWCRE 1329
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1831 QELQEklqaLQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKT-QVKRLENlasrlketmeklteeRDQRAAAENR- 1908
Cdd:COG5022 1330 FEISD----VDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPaEIQNLKS---------------RYDPADKENNl 1390
|
1530 1540 1550
....*....|....*....|....*....|.
gi 1907082213 1909 EKEQNKRLQRQLRDTKEEMSELARKEAEASR 1939
Cdd:COG5022 1391 PKEILKKIEALLIKQELQLSLEGKDETEVHL 1421
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
456-1213 |
3.33e-107 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 359.29 E-value: 3.33e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 456 EDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLM 535
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 536 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGT-SGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDF 612
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSgSAGNVGRLEE-QILQSnpILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 613 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL---------NHLAENNVFGIvplskpeek 683
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyhylSQSGCYTIDGI--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 684 qKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFA---RHEWAQKAAYLLGCSLEELSSAIFKH 760
Cdd:pfam00063 232 -DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAvpdDTENLQKAASLLGIDSTELEKALCKR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 761 QLKGGTLQRSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPE 839
Cdd:pfam00063 311 RIKTGRETVSKPQ------------NVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIgVLDIYGFEIFE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 840 WGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVRS-----LA 911
Cdd:pfam00063 379 KN------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEwtfIDFGDNQPCID-----------LIEKkplgiLS 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 912 HADEArgllwlleeeALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLNY 988
Cdd:pfam00063 442 LLDEE----------CLFPKATDQTFLDKLYSTF--------SKHPHFQKPRLQgetHFIIKHYAGD--VEYNVEGFLEK 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 989 TKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvLSGSIAGLEGGSQLALRRATSMRKtfTTGMaavkkkslciQIKLQ 1068
Cdd:pfam00063 502 NK-DPLNDDLVSLLKSSSDPLLAELFPDYE-----TAESAAANESGKSTPKRTKKKRFI--TVGS----------QFKES 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1069 VDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMY 1148
Cdd:pfam00063 564 LGELMKTLNSTNPHYIRCIKPNEKKRAG-----------------------------VFDNSLVLHQLRCNGVLEGIRIR 614
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1149 RQGYPDHMVFSEFRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
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, ... |
468-1213 |
1.05e-99 |
|
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: 1.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPyKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW-----QALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 619
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledQILQAnpILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 620 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFgIVPLSKPEEKQKAAQQFSKLQAAMKV 699
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFF-LSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 700 LAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRSTSFR 774
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAEldgTEEADKAAHLLGVNSSDLLKALLKPRIKVGRewVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 775 QgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQ----NpewggsargaSFE 850
Cdd:cd01377 320 Q--------------VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN----------SFE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 851 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF----DDLEPVADdsvaavdqashLVRS-----LAHADEargllw 921
Cdd:cd01377 376 QLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgLDLQPTID-----------LIEKpnmgiLSILDE------ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 922 lleeEALVPGATEDALLDRLFSYygpQEGDKKGQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLnyTK-QNPATQNAPR 1000
Cdd:cd01377 439 ----ECVFPKATDKTFVEKLYSN---HLGKSKNFKKPKPKKSEAHFILKHYAGD--VEYNIDGWL--EKnKDPLNENVVA 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1001 LLQDSQKKIISNLFlgragsatvlsgSIAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSK 1080
Cdd:cd01377 508 LLKKSSDPLVASLF------------KDYEESGGGGGKKKKKGGSFRT----VSQLHKEQL--------NKLMTTLRSTH 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1081 MHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSE 1160
Cdd:cd01377 564 PHFVRCIIPNEEKKPGK-----------------------------IDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAE 614
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 1161 FRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
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 ... |
467-1213 |
1.56e-89 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 307.71 E-value: 1.56e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIA-----GTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 619
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAsshkgRKDHNIPGELER-QLLQAnpILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 620 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF--GIVPLSkpeeKQKAAQQFSKLQAAM 697
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsnGYIPIP----GQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 698 KVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRSTs 772
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmpeNTVAQKLCHLLGMNVMEFTRAILTPRIKVGRdyVQKAQ- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 773 frqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEE 851
Cdd:cd14920 315 -------------TKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIgILDIAGFEIFELN------SFEQ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 852 LCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFD----DLEPVADdsvaAVDQASHLVRSLAHADEargllwlleeEA 927
Cdd:cd14920 376 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIdfglDLQPCID----LIERPANPPGVLALLDE----------EC 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 928 LVPGATEDALLDRLfsyygpqEGDKKGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQD 1004
Cdd:cd14920 442 WFPKATDKTFVEKL-------VQEQGSHSKFQKPRQLKdkaDFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVATLLHQ 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1005 SQKKIISNLFlgRAGSATVlsgSIAGLEGGSQLALRRATSMRKTFTTGMAAVKKKSLciqiklqvDALIDTIKRSKMHFV 1084
Cdd:cd14920 512 SSDRFVAELW--KDVDRIV---GLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESL--------TKLMATLRNTNPNFV 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1085 HCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1164
Cdd:cd14920 579 RCIIPNHEKRAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 629
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1907082213 1165 FDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14920 630 YEILTPNAIPK-----GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
467-1213 |
6.98e-84 |
|
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: 291.15 E-value: 6.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIA----GTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 620
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAsshkGKKDTSITGELEKQLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 621 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNV--FGIVPLSkpeeKQKAAQQFSKLQAAMK 698
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFlsNGFVPIP----AAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 699 VLAISPEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTSFRQ 775
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKernTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVG-----RDVVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 776 GPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEELCH 854
Cdd:cd14921 312 KAQ-------TKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEIFEVN------SFEQLCI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 855 NYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPGATE 934
Cdd:cd14921 379 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDE----------ECWFPKATD 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 935 DALLDRLFSyygPQEGDKKGQSPLLRSSKPRHFLLghsHGTNWVEYNVAGWLNyTKQNPATQNAPRLLQDSQKKIISNLF 1014
Cdd:cd14921 449 KSFVEKLCT---EQGNHPKFQKPKQLKDKTEFSII---HYAGKVDYNASAWLT-KNMDPLNDNVTSLLNASSDKFVADLW 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1015 LGragsatvlSGSIAGLEGGSQLALRRATSMRKTfTTGMAavkkKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGW 1094
Cdd:cd14921 522 KD--------VDRIVGLDQMAKMTESSLPSASKT-KKGMF----RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKR 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1095 PGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTK 1174
Cdd:cd14921 589 SG-----------------------------KLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIP 639
|
730 740 750
....*....|....*....|....*....|....*....
gi 1907082213 1175 KHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
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 ... |
467-1213 |
4.94e-83 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 288.80 E-value: 4.94e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIA-----GTSGTKVFSV-------EKWQAL---STLLEAFGNSPTIMNGSATRFSQILSLD 611
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpkGSGAVPHPAVnpavligELEQQLlqaNPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 612 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVF---GIVPLSKPEEkqkaAQ 688
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDD-VKSYAFlsnGSLPVPGVDD----YA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 689 QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGG 765
Cdd:cd14911 236 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQernNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 766 tlqrstsfRQGPEESGLGEGTKLSalecLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsa 844
Cdd:cd14911 316 --------RDFVTKAQTKEQVEFA----VEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIgILDMAGFEIFELN--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 845 rgaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFD----DLEPVADdsvaavdqashLVrslahaDEARGLL 920
Cdd:cd14911 381 ---SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIdfglDLQPTID-----------LI------DKPGGIM 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 921 WLLEEEALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLnYTKQNPATQN 997
Cdd:cd14911 441 ALLDEECWFPKATDKTFVDKLVSAH--------SMHPKFMKTDFRgvaDFAIVHYAGR--VDYSAAKWL-MKNMDPLNEN 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 998 APRLLQDSQKKIISNLFlgraGSATVLSGSIAGLeGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQVDALIDTIK 1077
Cdd:cd14911 510 IVSLLQGSQDPFVVNIW----KDAEIVGMAQQAL-TDTQFGARTRKGMFRTVSH------------LYKEQLAKLMDTLR 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1078 RSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMV 1157
Cdd:cd14911 573 NTNPNFVRCIIPNHEKRAG-----------------------------KIDAPLVLDQLRCNGVLEGIRICRQGFPNRIP 623
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1158 FSEFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
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 ... |
467-1213 |
2.29e-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: 284.23 E-value: 2.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTSGTK------VFS---VEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQA 615
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKkdqssiALShgeLEK-QLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 616 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQA 695
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDK--ELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTS 772
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKernSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVG-----RD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 773 FRQGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEE 851
Cdd:cd14932 313 YVQKAQ-------TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN------SFEQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 852 LCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPG 931
Cdd:cd14932 380 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDE----------ECWFPK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 932 ATEDALLDRLFSYYGpqeGDKKGQSPlLRSSKPRHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKIIS 1011
Cdd:cd14932 450 ATDKSFVEKVVQEQG---NNPKFQKP-KKLKDDADFCIIHYAGK--VDYKANEWL-MKNMDPLNENVATLLNQSTDKFVS 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1012 NLFlgRAGSATVLSGSIAGLEGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQVDALIDTIKRSKMHFVHCFLPVA 1091
Cdd:cd14932 523 ELW--KDVDRIVGLDKVAGMGESLHGAFKTRKGMFRTVGQ------------LYKEQLMNLMTTLRNTNPNFVRCIIPNH 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1092 EGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1171
Cdd:cd14932 589 EKKAG-----------------------------KLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1907082213 1172 LTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
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 ... |
467-1213 |
1.11e-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: 278.90 E-value: 1.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQAL---STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASI 623
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLlqaNPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 624 QTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQAAMKVLAIS 703
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK--DMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 704 PEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTSFRQGPEes 780
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKernTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG-----RDYVQKAQ-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 781 glgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEELCHNYAQD 859
Cdd:cd14919 312 -----TKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIgILDIAGFEIFDLN------SFEQLCINYTNE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 860 RLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPGATEDALLD 939
Cdd:cd14919 381 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDE----------ECWFPKATDKSFVE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 940 RLFSYYGPQegdKKGQSPLLRSSKPrHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKIISNLFlgRAG 1019
Cdd:cd14919 451 KVVQEQGTH---PKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWL-MKNMDPLNDNIATLLHQSSDKFVSELW--KDV 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1020 SATVLSGSIAGLeggSQLALRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDTIKRSKMHFVHCFLPVAEGWPGepr 1099
Cdd:cd14919 522 DRIIGLDQVAGM---SETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIPNHEKKAG--- 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1100 sassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHgrn 1179
Cdd:cd14919 588 --------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG--- 638
|
730 740 750
....*....|....*....|....*....|....
gi 1907082213 1180 yiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14919 639 --FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
467-1213 |
1.16e-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: 1.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTSGTKvfsvEKWQAL-------STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 619
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESK----KKLGALedqimqaNPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 620 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDATLRTELHLN------HLAENNVFGIvplskpeEKQKAAQQFSKL 693
Cdd:cd14929 157 SADIDIYLLEKSRVIFQQPGERNYHIFYQILS-GKKELRDLLLVSanpsdfHFCSCGAVAV-------ESLDDAEELLAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 694 QAAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARH---EWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQ 768
Cdd:cd14929 229 EQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEAdgtENADKAAFLMGINSSELVKGLIHPRIKVGNeyVT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 769 RSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaS 848
Cdd:cd14929 309 RSQNIEQVTYAVG--------------ALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYN------S 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 849 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELafddlepvaddsvAAVDQASHLVRSLAHADEARGLLWLLEEEAL 928
Cdd:cd14929 369 LEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDW-------------VSIDFGLDLQACIDLIEKPMGIFSILEEECM 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 929 VPGATEDALLDRLFSYYgpqegdkKGQSPLLRSSKPR------HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLL 1002
Cdd:cd14929 436 FPKATDLTFKTKLFDNH-------FGKSVHFQKPKPDkkkfeaHFELVHYAGV--VPYNISGWLEKNK-DLLNETVVAVF 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1003 QDSQKKIISNLFlgragSATVLSGSiaGLEGGSQlALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKMH 1082
Cdd:cd14929 506 QKSSNRLLASLF-----ENYISTDS--AIQFGEK-KRKKGASFQT-----VASLHKENL--------NKLMTNLKSTAPH 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1083 FVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1162
Cdd:cd14929 565 FVRCINPNVNKIPG-----------------------------VLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFK 615
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1163 RRFDVLAPHLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14929 616 QRYCILNPRTFPKSK----FVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
467-1213 |
1.27e-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: 266.93 E-value: 1.27e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELekqllqanpiLEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQAA 696
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDK--DLFTETMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 697 MKVLAISPEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRST 771
Cdd:cd15896 239 FRIMGIPEDEQIGMLKVVASVLQLGNMSFKKerhTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRdyVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 772 SFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFE 850
Cdd:cd15896 319 TQEQ--------------AEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN------SFE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 851 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVP 930
Cdd:cd15896 379 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDE----------ECWFP 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 931 GATEDALLDRLFSYYGPQEGDKKGQspllRSSKPRHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKII 1010
Cdd:cd15896 449 KATDKSFVEKVLQEQGTHPKFFKPK----KLKDEADFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVATLLNQSTDKFV 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1011 SNLFLGragsatvlSGSIAGLEGGSQLA-LRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDTIKRSKMHFVHCFLP 1089
Cdd:cd15896 522 SELWKD--------VDRIVGLDKVSGMSeMPGAFKTRKGMFRTVGQLYKE--------QLSKLMATLRNTNPNFVRCIIP 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1090 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1169
Cdd:cd15896 586 NHEKKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082213 1170 PHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd15896 637 PNAIPKG-----FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
467-1213 |
5.63e-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: 259.50 E-value: 5.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIA--GTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQ 614
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalGDGPGKKAQFLATKTGGTLedqiieanpaMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 615 AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLN------HLAENNVFGIVPLSKPEEkqkaaq 688
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmnpydyHFCSQGVTTVDNMDDGEE------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 689 qFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARH---EWAQKAAYLLGCSLEELSSAIFKHQLKGG 765
Cdd:cd14927 235 -LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAdgtESADKAAYLMGVSSADLLKGLLHPRVKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 766 tlQRSTSFRQGPEESGLGEGtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsar 845
Cdd:cd14927 314 --NEYVTKGQSVEQVVYAVG----------ALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFN---- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 846 gaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQASHLVRSLAHADEargllwllee 925
Cdd:cd14927 378 --SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDF---GLDLQACIDLIEKPLGILSILEE---------- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 926 EALVPGATEDALLDRLFSYYgpqegdkKGQSPLLRSSKP-------RHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNA 998
Cdd:cd14927 443 ECMFPKASDASFKAKLYDNH-------LGKSPNFQKPRPdkkrkyeAHFEVVHYAGV--VPYNIVGWLDKNK-DPLNETV 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 999 PRLLQDSQKKIISNLFLGRAGSATVlsgsiAGLEGGSQLALRRATSmrktFTTgMAAVKKKSLciqiklqvDALIDTIKR 1078
Cdd:cd14927 513 VAIFQKSQNKLLATLYENYVGSDST-----EDPKSGVKEKRKKAAS----FQT-VSQLHKENL--------NKLMTNLRA 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1079 SKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVF 1158
Cdd:cd14927 575 TQPHFVRCIIPNETKTPG-----------------------------VMDPFLVLHQLRCNGVLEGIRICRKGFPNRILY 625
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1159 SEFRRRFDVLAPHLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
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 ... |
467-1213 |
2.36e-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: 257.07 E-value: 2.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW----QALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 620
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGsledQVVQTnpVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 621 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlaeNNVFGIVPLSKPE---EKQKAAQQFSKLQAAM 697
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLS----DNIYDYYIVSQGKvtvPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 698 KVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARH---EWAQKAAYLLGCSLEELSSAIFKHQLKGGTlQRSTSFR 774
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQdgeEEGGRVSKLFGCDTAELYKNLLKPRIKVGN-EFVTQGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 775 QgpeesglgegtKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGsargasFEELCH 854
Cdd:cd14909 316 N-----------VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------FEQLCI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 855 NYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPGATE 934
Cdd:cd14909 379 NFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDF---GMDLLACIDLIEKPMGILSILEE----------ESMFPKATD 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 935 DALLDRLFSyygpqegDKKGQSPLLRSSKP-------RHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQK 1007
Cdd:cd14909 446 QTFSEKLTN-------THLGKSAPFQKPKPpkpgqqaAHFAIAHYAGC--VSYNITGWLEKNK-DPLNDTVVDQFKKSQN 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1008 KIISNLFLGRAGSatvlSGSIAGLEGGsqlalrratsmRKTFTTGMAAVKKkslciQIKLQVDALIDTIKRSKMHFVHCF 1087
Cdd:cd14909 516 KLLIEIFADHAGQ----SGGGEQAKGG-----------RGKKGGGFATVSS-----AYKEQLNSLMTTLRSTQPHFVRCI 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1088 LPvaegwpgeprsassrrvsssSELDLPpgdpceaGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1167
Cdd:cd14909 576 IP--------------------NEMKQP-------GV--VDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKI 626
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1907082213 1168 LAPHLTKKHgrnyivVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14909 627 LNPAGIQGE------EDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
467-1213 |
2.49e-70 |
|
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: 251.55 E-value: 2.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGT-SGTKVFSV-----EKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 620
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSpKGRKEPGVpgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 621 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQkaaQQFSKLQAAMKVL 700
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER---ELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 701 AISPEEQKTCWLILASIYHLGAAGATK---AGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTSFRQGP 777
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRernTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG-----RDYVQKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 778 EesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEELCHNY 856
Cdd:cd14930 313 Q-------TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFEIFQLN------SFEQLCINY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 857 AQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPGATEDA 936
Cdd:cd14930 380 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDE----------ECWFPKATDKS 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 937 LLDRLfsyygpqeGDKKGQSPllRSSKPRH------FLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKII 1010
Cdd:cd14930 450 FVEKV--------AQEQGGHP--KFQRPRHlrdqadFSVLHYAGK--VDYKANEWL-MKNMDPLNDNVAALLHQSTDRLT 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1011 SNLFLGRAGsatvlsgsIAGLEGGSQL--ALRRATSMRKTFTTgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFL 1088
Cdd:cd14930 517 AEIWKDVEG--------IVGLEQVSSLgdGPPGGRPRRGMFRT-VGQLYKESL--------SRLMATLSNTNPSFVRCIV 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1089 PVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1168
Cdd:cd14930 580 PNHEKRAG-----------------------------KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082213 1169 APHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14930 631 TPNAIPKG-----FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
468-1213 |
1.03e-69 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 249.58 E-value: 1.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLATIAGT------SGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 619
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdlakkKDSKMKGTLEDQIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 620 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA---A 696
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILS----NKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLAtdsA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 697 MKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGTlqrstsf 773
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKTAYLMGLNSSDLLKALCFPRVKVGN------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 774 rqgpEESGLGEgTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELC 853
Cdd:cd14913 311 ----EYVTKGQ-TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN------SLEQLC 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 854 HNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALVPGAT 933
Cdd:cd14913 380 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPMGIFSILEEECMFPKAT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 934 EDALLDRLFSYYGPQEGDKkgQSPLLRSSKPR-HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISN 1012
Cdd:cd14913 447 DTSFKNKLYDQHLGKSNNF--QKPKVVKGRAEaHFSLIHYAGT--VDYSVSGWLEKNK-DPLNETVVGLYQKSSNRLLAH 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1013 LFLGRAGS-ATVLSGSIAGLEGGSqlalrratsmrktFTTgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLPVA 1091
Cdd:cd14913 522 LYATFATAdADSGKKKVAKKKGSS-------------FQT-VSALFRENL--------NKLMSNLRTTHPHFVRCIIPNE 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1092 EGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1171
Cdd:cd14913 580 TKTPGA-----------------------------MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 630
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1907082213 1172 LTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14913 631 AIPE-GQ---FIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
468-1170 |
7.86e-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: 7.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLATIAGTSGtkvfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSS----GIEN-EILQTnpILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKpeekqkaAQQFSKLQAAMKV 699
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLksaseyKYLNQSNCLTIDGVDD-------AKKFHELKEALDT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 700 LAISPEEQKTCWLILASIYHLGAAGATKAGRKQF---ARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFrqg 776
Cdd:cd01383 228 VGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHvevVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKL--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 777 peesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQH-SLCSMMIVDTPGFQnpewggSARGASFEELCHN 855
Cdd:cd01383 305 ---------TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRrTGRSISILDIYGFE------SFQKNSFEQLCIN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 856 YAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEpvadDSVAAVDqashLVRS-----LAHADEargllwlleeEALVP 930
Cdd:cd01383 370 YANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFE----DNQECLD----LIEKkplglISLLDE----------ESNFP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 931 GATEDALLDRLFSYYGPQEGDKKGQSpllrsskpRHFLLGHSHGTnwVEYNVAGWLNytkqnpatQNAPRLLQDsqkkiI 1010
Cdd:cd01383 432 KATDLTFANKLKQHLKSNSCFKGERG--------GAFTIRHYAGE--VTYDTSGFLE--------KNRDLLHSD-----L 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1011 SNLFLGRAGSATVLSGSIAGLEGGSQLALRRATSMRKTfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPV 1090
Cdd:cd01383 489 IQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQ---------KQSVATKFKGQLFKLMQRLENTTPHFIRCIKPN 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1091 AEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1170
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 ... |
468-1213 |
8.05e-67 |
|
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: 240.78 E-value: 8.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLATIAG---------TSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQV 618
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 619 ASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA--- 695
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDML----LITNNPYDYAFISQGETTVASIDDAEELMAtdn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRS 770
Cdd:cd14917 237 AFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEpdgTEEADKSAYLMGLNSADLLKGLCHPRVKVGNeyVTKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 771 TSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFE 850
Cdd:cd14917 317 QNVQQVIYATG--------------ALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 851 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQAshlvrslahaDEARGLLWLLEEEALVP 930
Cdd:cd14917 377 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---GMDLQACIDLI----------EKPMGIMSILEEECMFP 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 931 GATEDALLDRLFSYYGPQEGDKkgQSPLLRSSKPR-HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKI 1009
Cdd:cd14917 444 KATDMTFKAKLFDNHLGKSNNF--QKPRNIKGKPEaHFSLIHYAGT--VDYNIIGWLQKNK-DPLNETVVGLYQKSSLKL 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1010 ISNLFLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLP 1089
Cdd:cd14917 519 LSNLFANYAGADAPIEKGKGKAKKGS------------SFQT-VSALHRENL--------NKLMTNLRSTHPHFVRCIIP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1090 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1169
Cdd:cd14917 578 NETKSPG-----------------------------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082213 1170 PHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
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 ... |
467-1213 |
2.15e-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: 239.54 E-value: 2.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTS-----GTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 621
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGkqssdGKGSLEDQIIQA-NPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 622 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKPEEKQKAaqqfsklQA 695
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvpnpkeYHWVSQGVTVVDNMDDGEELQIT-------DV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRS 770
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEvdtTEVADKVAHLMGLNSGELQKGITRPRVKVGNefVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 771 TSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFE 850
Cdd:cd14934 313 QNMEQCNNSIG--------------ALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN------SFE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 851 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQashlvrslahADEARGLLWLLEEEALVP 930
Cdd:cd14934 373 QLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDF---GLDLQACIDL----------LEKPMGIFSILEEQCVFP 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 931 GATE--------DALLDRLFSYYGPQEGDKKGQSPllrsskprHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLL 1002
Cdd:cd14934 440 KATDatfkaalyDNHLGKSSNFLKPKGGKGKGPEA--------HFELVHYAGT--VGYNITGWLEKNK-DPLNETVVGLF 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1003 QDSQkKIISNLFLGRAGSAtvlsgsiagleGGSQLALRRATSMrktfttgmaavkkkSLCIQIKLQVDALIDTIKRSKMH 1082
Cdd:cd14934 509 QKSS-LGLLALLFKEEEAP-----------AGSKKQKRGSSFM--------------TVSNFYREQLNKLMTTLHSTAPH 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1083 FVHCFLpvaegwpgeprsassrrvsssseldlpPGDPCEAGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1162
Cdd:cd14934 563 FVRCIV---------------------------PNEFKQSGV--VDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFK 613
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1163 RRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14934 614 QRYQVLNPNVIPQG-----FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
467-1213 |
1.09e-65 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 237.22 E-value: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGpSLLVlstrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 538
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTG-SILV-------AVnpykelpiYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 539 DQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTkvFSVEKwQAL--STLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd14883 73 NQSVIISGESGAGKTETTKLILQYLC--AVTNNH--SWVEQ-QILeaNTILEAFGNAKTVRNDNSSRFGKFIEVCFDASG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACG--DATLRTELHL---NHLAENNVFGIVPLSKPEEKQKaaqqFS 691
Cdd:cd14883 148 HIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLgepEDYHYLNQSGCIRIDNINDKKD----FD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 692 KLQAAMKVLAISPEEQKTCWLILASIYHLGAAgatkagrkQFARHEWAQkaayllgCSLEELSSAIFKH-----QLKGGT 766
Cdd:cd14883 224 HLRLAMNVLGIPEEMQEGIFSVLSAILHLGNL--------TFEDIDGET-------GALTVEDKEILKIvakllGVDPDK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 767 LQRSTSFRQgpeESGLGEGT----KLS-ALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWG 841
Cdd:cd14883 289 LKKALTIRQ---INVRGNVTeiplKVQeARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 842 gsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDLEPVADdsvaAVDQASHLVRSLAhADEARg 918
Cdd:cd14883 366 ------SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWShivFTDNQECLD----LIEKPPLGILKLL-DEECR- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 919 llwlleeealVPGATEDALLDRLFSYYGPQEGDKKgqsPLLRSSKPRhFLLGHSHGTnwVEYNVAGWLNytkQNPATQ-- 996
Cdd:cd14883 434 ----------FPKGTDLTYLEKLHAAHEKHPYYEK---PDRRRWKTE-FGVKHYAGE--VTYTVQGFLD---KNKDTQqd 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 997 NAPRLLQDSQKKIISNLFLGRAgsatvlsgsiagleggsQLALRRATSMRKTFTTGMAAVKKK-SLCIQIKLQVDALIDT 1075
Cdd:cd14883 495 DLFDLMSRSKNKFVKELFTYPD-----------------LLALTGLSISLGGDTTSRGTSKGKpTVGDTFKHQLQSLVDV 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1076 IKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDH 1155
Cdd:cd14883 558 LSATQPWYVRCIKPNSLKEPN-----------------------------VFDDELVLAQLRYAGMLEIIRIRKEGFPIH 608
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1156 MVFSEFRRRFDVLAPHLTKKHGRnyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14883 609 LTFKEFVDRYLCLDPRARSADHK-----ETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
468-1213 |
4.63e-65 |
|
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: 235.78 E-value: 4.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 617
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLedqiisanplLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 618 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 695
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQR 769
Cdd:cd14910 238 sAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAAYLQNLNSADLLKALCYPRVKVGNeyVTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 770 STSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSF 849
Cdd:cd14910 318 GQTVQQVYNAVG--------------ALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 850 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALV 929
Cdd:cd14910 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFSILEEECMF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 930 PGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKI 1009
Cdd:cd14910 445 PKATDTSFKNKLYEQHLGKSNNFQKPKPA-KGKVEAHFSLIHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSSMKT 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1010 ISNLFLGrAGSATVLSGsiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLP 1089
Cdd:cd14910 521 LALLFSG-AAAAEAEEG------GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTHPHFVRCIIP 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1090 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1169
Cdd:cd14910 581 NETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082213 1170 PHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14910 632 ASAIPE-GQ---FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
468-1213 |
4.77e-65 |
|
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: 235.73 E-value: 4.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLATIAgTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 617
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIA-VTGDKKKEQQPGKMQGTLedqiiqanplLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 618 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 695
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLL----LISTNPFDFPFVSQGEVTVASIDDSEELLAtd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELssaifkhqLKGGTLQRst 771
Cdd:cd14923 237 nAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAGYLMGLNSAEM--------LKGLCCPR-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 772 sFRQGPEESGLGEGTKlSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEE 851
Cdd:cd14923 307 -VKVGNEYVTKGQNVQ-QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 852 LCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALVPG 931
Cdd:cd14923 379 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFSILEEECMFPK 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 932 ATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIIS 1011
Cdd:cd14923 446 ATDTSFKNKLYDQHLGKSNNFQKPKPA-KGKAEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSSLKLLS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1012 NLFLGRAGSAtvlsgsiAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLPVA 1091
Cdd:cd14923 522 FLFSNYAGAE-------AGDSGGSKKGGKKKGSSFQT----VSAVFRENL--------NKLMTNLRSTHPHFVRCLIPNE 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1092 EGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1171
Cdd:cd14923 583 TKTPG-----------------------------VMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNAS 633
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1907082213 1172 LTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14923 634 AIPE-GQ---FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
468-1213 |
1.90e-64 |
|
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: 233.85 E-value: 1.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLATIA---------GTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAvtgekkkeeAASGKMQGTLED-QIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA- 695
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMAt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 --AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQ 768
Cdd:cd14915 237 dsAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAAYLTSLNSADLLKALCYPRVKVGNeyVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 769 RSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaS 848
Cdd:cd14915 317 KGQTVQQVYNSVG--------------ALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------S 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 849 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEAL 928
Cdd:cd14915 377 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFSILEEECM 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 929 VPGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKK 1008
Cdd:cd14915 444 FPKATDTSFKNKLYEQHLGKSNNFQKPKPA-KGKAEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSGMK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1009 IISNLFLGraGSATVLSGSiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFL 1088
Cdd:cd14915 520 TLAFLFSG--GQTAEAEGG-----GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTHPHFVRCLI 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1089 PVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1168
Cdd:cd14915 580 PNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082213 1169 APHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14915 631 NASAIPE-GQ---FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
469-1175 |
2.98e-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: 232.57 E-value: 2.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 469 VLHTLRQRYGASLLHTYAGPSLL-VLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIaVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQ-QVLESnpLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKPEEkqkaaqqFSKLQAAMKV 699
Cdd:cd01384 162 YLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 700 LAISPEEQKTCWLILASIYHLG------AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQlkggtlqrstsf 773
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGniefskGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRV------------ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 774 RQGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQnpewggSARGASFEELC 853
Cdd:cd01384 303 IVTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE------SFKTNSFEQFC 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 854 HNYAQDRLQRLFHERTFLQELERYKEDNIELAF----------DDLEPVADDSVAAVDQASHLVRSlahadeargllwll 923
Cdd:cd01384 377 INLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYiefvdnqdvlDLIEKKPGGIIALLDEACMFPRS-------------- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 924 eeealvpgaTEDALLDRLFSYYgpqeGDKKgqspllRSSKPR----HFLLGHSHGTnwVEYNVAGWLNYTKQN--PATQN 997
Cdd:cd01384 443 ---------THETFAQKLYQTL----KDHK------RFSKPKlsrtDFTIDHYAGD--VTYQTDLFLDKNKDYvvAEHQA 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 998 aprLLQDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKtFTtgmaavkkkSLCIQIKLQVDALIDTIK 1077
Cdd:cd01384 502 ---LLNASKCPFVAGLF--------------------PPLPREGTSSSSK-FS---------SIGSRFKQQLQELMETLN 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1078 RSKMHFVHCFLPVAEgwpgeprsassrrvsssseldLPPGDPCEAGLLQldvsllraQLRGSRLLDAMRMYRQGYPDHMV 1157
Cdd:cd01384 549 TTEPHYIRCIKPNNL---------------------LKPGIFENANVLQ--------QLRCGGVLEAVRISCAGYPTRKP 599
|
730
....*....|....*...
gi 1907082213 1158 FSEFRRRFDVLAPHLTKK 1175
Cdd:cd01384 600 FEEFLDRFGLLAPEVLKG 617
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
469-1213 |
4.05e-64 |
|
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: 233.09 E-value: 4.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 469 VLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSS 548
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 549 GSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQ--------ALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 620
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 621 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA---AM 697
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtdsAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 698 KVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGTlqrstsfr 774
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEpdgTEVADKAAYLQSLNSADLLKALCYPRVKVGN-------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 775 qgpEESGLGEgTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCH 854
Cdd:cd14918 311 ---EYVTKGQ-TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 855 NYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALVPGATE 934
Cdd:cd14918 381 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPLGIFSILEEECMFPKATD 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 935 DALLDRLFSYYGPQEGDKKgQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLF 1014
Cdd:cd14918 448 TSFKNKLYDQHLGKSANFQ-KPKVVKGKAEAHFSLIHYAGT--VDYNITGWLDKNK-DPLNDTVVGLYQKSAMKTLASLF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1015 LGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTGMAAVKKkslciqiklQVDALIDTIKRSKMHFVHCFLPVAEGW 1094
Cdd:cd14918 524 STYASAEADSGAKKGAKKKGS------------SFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCIIPNETKT 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1095 PGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTK 1174
Cdd:cd14918 583 PG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIP 633
|
730 740 750
....*....|....*....|....*....|....*....
gi 1907082213 1175 KhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
Cdd:cd14918 634 E-GQ---FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
468-1213 |
2.63e-63 |
|
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: 230.77 E-value: 2.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 617
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLedqiisanplLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 618 VASASIQTMLLEKLRVARRPASEATFNVFYYLlacgDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 695
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQI----TSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQR 769
Cdd:cd14912 238 sAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEpdgTEVADKAAYLQSLNSADLLKALCYPRVKVGNeyVTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 770 STSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSF 849
Cdd:cd14912 318 GQTVEQVTNAVG--------------ALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 850 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEEALV 929
Cdd:cd14912 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPMGIFSILEEECMF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 930 PGATEDALLDRLFSYYGPQEGDKKgQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKI 1009
Cdd:cd14912 445 PKATDTSFKNKLYEQHLGKSANFQ-KPKVVKGKAEAHFSLIHYAGV--VDYNITGWLDKNK-DPLNETVVGLYQKSAMKT 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1010 ISNLFLGragsATVLSGSIAGleGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLP 1089
Cdd:cd14912 521 LAYLFSG----AQTAEGASAG--GGAKKGGKKKGSSFQT----VSALFRENL--------NKLMTNLRSTHPHFVRCIIP 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1090 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1169
Cdd:cd14912 583 NETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 633
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082213 1170 PHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
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 ... |
468-1170 |
2.86e-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: 227.63 E-value: 2.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLATIA--GTSGTKVFSVEKWQAL-------STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQV 618
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAaiGDRSKKENPNANKGTLedqiiqaNPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 619 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA--- 695
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILS----NKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLAtds 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQLKGGT--LQRS 770
Cdd:cd14916 238 AFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEpdgTEDADKSAYLMGLNSADLLKGLCHPRVKVGNeyVTKG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 771 TSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFE 850
Cdd:cd14916 318 QSVQQ--------------VYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 851 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQAshlvrslahaDEARGLLWLLEEEALVP 930
Cdd:cd14916 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---GMDLQACIDLI----------EKPMGIMSILEEECMFP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 931 GATEDALLDRLF-SYYGPQEGDKKGQSplLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKI 1009
Cdd:cd14916 445 KASDMTFKAKLYdNHLGKSNNFQKPRN--VKGKQEAHFSLVHYAGT--VDYNILGWLEKNK-DPLNETVVGLYQKSSLKL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1010 ISNLFLGRAGSATvlsgsiaGLEGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHFVHCFLP 1089
Cdd:cd14916 520 MATLFSTYASADT-------GDSGKGKGGKKKGSSFQT-----VSALHRENL--------NKLMTNLKTTHPHFVRCIIP 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1090 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1169
Cdd:cd14916 580 NERKAPG-----------------------------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 630
|
.
gi 1907082213 1170 P 1170
Cdd:cd14916 631 P 631
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
467-1170 |
1.63e-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: 225.04 E-value: 1.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMS----RQDQS 541
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPyKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSgvldPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 542 IVLLGSSGSGKTTSFQHLVQYLATIagTSGTKVFSVEKWQALST------------------LLEAFGNSPTIMNGSATR 603
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARI--TSGFAQGASGEGEAASEaieqtlgsledrvlssnpLLESFGNAKTLRNDNSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 604 FSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLnhlaENNVFGIVPLSK--PE 681
Cdd:cd14890 159 FGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKL----QTPVEYFYLRGEcsSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 682 EKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG-----AAGATKAGRKQfARHEWAQKAAYLLGCSLEELSSA 756
Cdd:cd14890 235 PSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGnvdfeSENDTTVLEDA-TTLQSLKLAAELLGVNEDALEKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 757 IFKHQL--KGGTLQRstsfrqgPEESGLGEgTKLSALeclegmASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPG 834
Cdd:cd14890 314 LLTRQLfvGGKTIVQ-------PQNVEQAR-DKRDAL------AKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 835 FQNPEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADDSVAAVDQASHLVRSLa 911
Cdd:cd14890 380 FEKFEWNT------FEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDwqyITFNDNQACLELIEGKVNGKPGIFITL- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 912 haDEARGLLWLLEEEALVpgatedALLDRLF--SYYGPQEGDKKGQSPLLRSSK---PRHFLLGHSHGTnwVEYNVAGwl 986
Cdd:cd14890 453 --DDCWRFKGEEANKKFV------SQLHASFgrKSGSGGTRRGSSQHPHFVHPKfdaDKQFGIKHYAGD--VIYDASG-- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 987 nYTKQNPATqnaprlLQDSQKKIIsnlflgragsatvlsgsiagleggsqlalrrATSMRktfttgmaAVKKKSLCIQIK 1066
Cdd:cd14890 521 -FNEKNNET------LNAEMKELI-------------------------------KQSRR--------SIREVSVGAQFR 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1067 LQVDALIDTIKRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagLLQLDVSLlraQLRGSRLLDAMR 1146
Cdd:cd14890 555 TQLQELMAKISLTNPRYVRCIKPNETKAPGK--------------------------FDGLDCLR---QLKYSGMMEAIQ 605
|
730 740
....*....|....*....|....*..
gi 1907082213 1147 MYRQGYP---DHMVFseFrRRFDVLAP 1170
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, ... |
467-1089 |
7.63e-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: 7.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPslLVLST---RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIV 543
Cdd:cd01378 1 EAINENLKKRFENDEIYTYIGH--VLISVnpfKDLG-IYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 544 LLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVeKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 621
Cdd:cd01378 78 ISGESGAGKTEASKRIMQYIAAVSGGSESEVERV-KDMLLASnpLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 622 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKpeekqkaAQQFSKLQA 695
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLqrpeqyYYYSKSGCFDVDGIDD-------AADFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 AMKVLAISPEEQKTCWLILASIYHLGAAG--ATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRST-S 772
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQfaEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGRSVyE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 773 FRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGF----QNpewggsarga 847
Cdd:cd01378 310 VPLNVEQ----------AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIgVLDIYGFeifeKN---------- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 848 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA----FDDlEPVADdsvaavdqashLVRS-----LAHADEArg 918
Cdd:cd01378 370 SFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTpikyFNN-KIICD-----------LIEEkppgiFAILDDA-- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 919 llwlleeEALVPGATEDALLDRLFSYYGPQEGDKKGQSPllRSSKPRHFLLGHSHGTnwVEYNVAGwlnYTKQNPAT--Q 996
Cdd:cd01378 436 -------CLTAGDATDQTFLQKLNQLFSNHPHFECPSGH--FELRRGEFRIKHYAGD--VTYNVEG---FLDKNKDLlfK 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 997 NAPRLLQDSQKKIISNLFlgragsatvlsgsiagLEGGSQLALRRATsmrktfTTGMaavkkkslciQIKLQVDALIDTI 1076
Cdd:cd01378 502 DLKELMQSSSNPFLRSLF----------------PEGVDLDSKKRPP------TAGT----------KFKNSANALVETL 549
|
650
....*....|...
gi 1907082213 1077 KRSKMHFVHCFLP 1089
Cdd:cd01378 550 MKKQPSYIRCIKP 562
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
468-1173 |
2.30e-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: 215.43 E-value: 2.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGpSLL--VLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 545
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIG-SILasVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 546 GSSGSGKTTSFQHLVQYLATIAGTS-----GTKVFSVEKWQALST-LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 619
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelslKEKTSCVEQAILESSpIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 620 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhLAEN----NVFGIVPLSKPEEKqkaaQQFSKLQA 695
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENyhylNQSGCVEDKTISDQ----ESFREVIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRq 775
Cdd:cd14873 236 AMEVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPTQLTDAL---------TQRSMFLR- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 776 GPEESglgegTKLS---ALECLEGMASGLYSELFTLLISLVNRALKSSQHsLCSMMIVDTPGFQNPEWGgsargaSFEEL 852
Cdd:cd14873 306 GEEIL-----TPLNvqqAVDSRDSLAMALYARCFEWVIKKINSRIKGKED-FKSIGILDIFGFENFEVN------HFEQF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 853 CHNYAQDRLQRLFHERTF-LQELERYKEDnieLAFDDLEPVadDSVAAVDQASHLVRSLAHADEargllwlleeEALVPG 931
Cdd:cd14873 374 NINYANEKLQEYFNKHIFsLEQLEYSREG---LVWEDIDWI--DNGECLDLIEKKLGLLALINE----------ESHFPQ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 932 ATEDALLDRLFSyygpqeGDKKGQSPLlrssKPR--HFLLGHSHGTNWVEYNVAGWLnytKQNPAT--QNAPRLLQDSQK 1007
Cdd:cd14873 439 ATDSTLLEKLHS------QHANNHFYV----KPRvaVNNFGVKHYAGEVQYDVRGIL---EKNRDTfrDDLLNLLRESRF 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1008 KIISNLFlgragsatvlsgsiagleggsqlalRRATSMRKTFTTGMAAVKKK-SLCIQIKLQVDALIDTIKRSKMHFVHC 1086
Cdd:cd14873 506 DFIYDLF-------------------------EHVSSRNNQDTLKCGSKHRRpTVSSQFKDSLHSLMATLSSSNPFFVRC 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1087 FLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 1166
Cdd:cd14873 561 IKPNMQKMPD-----------------------------QFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYK 611
|
....*..
gi 1907082213 1167 VLAPHLT 1173
Cdd:cd14873 612 VLMRNLA 618
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
467-1170 |
4.83e-58 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 214.64 E-value: 4.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 545
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPyQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 546 GSSGSGKTTSFQHLVQYLATIAGtsGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAennVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 705
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANEC---AYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 706 EQKTCWLILASIYHLGAA----------GATKAGRKQFARHewaqkAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFRq 775
Cdd:cd14903 236 KQEVLFEVLAGILHLGQLqiqskpnddeKSAIAPGDQGAVY-----ATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 776 gpeesglgegtKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCHN 855
Cdd:cd14903 310 -----------KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHN------SFEQFCIN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 856 YAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDS-VAAVDQASHLVRSLAHADEARgllwlleeealvPGATE 934
Cdd:cd14903 373 YANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF---ADNQdVLAVIEDRLGIISLLNDEVMR------------PKGNE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 935 DALLDRLFSYYgpqeGDKKGQSPLLRSSKPRhFLLGHSHGTnwVEYNVAGWLNYTKQNpatqnaprLLQD-------SQK 1007
Cdd:cd14903 438 ESFVSKLSSIH----KDEQDVIEFPRTSRTQ-FTIKHYAGP--VTYESLGFLEKHKDA--------LLPDlsdlmrgSSK 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1008 KIISNLFLGRAGSATVLSGSIAGLEGgsqlalRRATSMRKTFTTGMaavkkkslciQIKLQVDALIDTIKRSKMHFVHCF 1087
Cdd:cd14903 503 PFLRMLFKEKVESPAAASTSLARGAR------RRRGGALTTTTVGT----------QFKDSLNELMTTIRSTNVHYVRCI 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1088 LPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1167
Cdd:cd14903 567 KPNSIKSPTE-----------------------------LDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
...
gi 1907082213 1168 LAP 1170
Cdd:cd14903 618 FLP 620
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
468-888 |
9.80e-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: 212.79 E-value: 9.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYG-ASLLHTYAGpslLVLStrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 538
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCG---IVLV-----AInpyedlpiYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 539 DQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd01380 74 NQSIIVSGESGAGKTVSAKYAMRYFATVGGSSSGET-QVEE-KVLASnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFGIVPLSKPEEKQKAAQQFSKLQAA 696
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGS-AEDFFYTNQGGSPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 697 MKVLAISPEEQKTCWLILASIYHLGAAGATKAGRK---QFARHEWAQKAAYLLGCSLEELSSAIFKHQLK--GGTLQRST 771
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDsasISPDDEHLQIACELLGIDESQLAKWLCKRKIVtrSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 772 SFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQ-HSLCSMM-IVDTPGFQNPEWGgsargaSF 849
Cdd:cd01380 311 TLQQ--------------AIVARDALAKHIYAQLFDWIVDRINKALASPVkEKQHSFIgVLDIYGFETFEVN------SF 370
|
410 420 430
....*....|....*....|....*....|....*....
gi 1907082213 850 EELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDD 888
Cdd:cd01380 371 EQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFID 409
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
467-1170 |
1.80e-57 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 212.50 E-value: 1.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGpSLLVlstrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 538
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTG-SILV-------AVnpyqilpiYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 539 DQSIVLLGSSGSGKTTSFQHLVQYLATIAGtsgtKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd01381 73 DQCVVISGESGAGKTESTKLILQYLAAISG----QHSWIEQ-QILEAnpILEAFGNAKTIRNDNSSRFGKYIDIHFNKNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNH------LAENNVFGIvplskpeEKQKAAQQF 690
Cdd:cd01381 148 VIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDasdyyyLTQGNCLTC-------EGRDDAAEF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 691 SKLQAAMKVLAISPEEQKTCWLILASIYHLG-----AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQL--K 763
Cdd:cd01381 221 ADIRSAMKVLMFTDEEIWDIFKLLAAILHLGnikfeATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIftR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 764 GGTLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRAL---KSSQHSLCSMMIVDTPGFQNPEW 840
Cdd:cd01381 301 GETVVSPLSAEQ--------------ALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENFEV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 841 GgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsVAAVDQAShlvrSLAHADEar 917
Cdd:cd01381 367 N------SFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINwqhIEFVDNQDVLD--LIALKPMN----IMSLIDE-- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 918 gllwlleeEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLLRSSKPRHFLlghshGTnwVEYNVAGWLNytKQNPA-TQ 996
Cdd:cd01381 433 --------ESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFA-----GV--VFYDTRGFLE--KNRDTfSA 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 997 NAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsQLALRRATSMRKtfttgmaavKKKSLCIQIKLQVDALIDTI 1076
Cdd:cd01381 496 DLLQLVQSSKNKFLKQLF---------------------NEDISMGSETRK---------KSPTLSSQFRKSLDQLMKTL 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1077 KRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHM 1156
Cdd:cd01381 546 SACQPFFVRCIKPNEYKKPML-----------------------------FDRELCVRQLRYSGMMETIRIRKAGYPIRH 596
|
730
....*....|....
gi 1907082213 1157 VFSEFRRRFDVLAP 1170
Cdd:cd01381 597 TFEEFVERYRVLVP 610
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
468-1015 |
1.68e-56 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 209.55 E-value: 1.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTSGTkvFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 626
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPSDDS--DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNH----------LAENNVFGIVplskpEEKQKAAQQFSKLQAA 696
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDpdchrilrddNRNRPVFNDS-----EELEYYRQMFHDLTNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 697 MKVLAISPEEQKTCWLILASIYHLG---------AAGATKAGRKQFarhewaQKAAYLLGCSLEELSSAIF--KHQLKGG 765
Cdd:cd14897 235 MKLIGFSEEDISVIFTILAAILHLTnivfipdedTDGVTVADEYPL------HAVAKLLGIDEVELTEALIsnVNTIRGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 766 TLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQ-----HSLCSMMIVDTPGFQNpew 840
Cdd:cd14897 309 RIQSWKSLRQ--------------ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKdfqimTRGPSIGILDMSGFEN--- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 841 ggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAfdDLEPVADDSV------------AAVDQASHLvr 908
Cdd:cd14897 372 ---FKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR--DIEYHDNDDVlelffkkplgilPLLDEESTF-- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 909 slahadeargllwlleeealvPGATEDALLDRLFSYYGPqegdkkgqSPLLRSSKPRHFLLGHSHGTNWVEYNVAGWLNY 988
Cdd:cd14897 445 ---------------------PQSTDSSLVQKLNKYCGE--------SPRYVASPGNRVAFGIRHYAEQVTYDADGFLEK 495
|
570 580
....*....|....*....|....*..
gi 1907082213 989 TKQNpATQNAPRLLQDSQKKIISNLFL 1015
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 ... |
468-894 |
7.36e-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: 207.51 E-value: 7.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLaTIAGTSGTKVFSvEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTML 627
Cdd:cd01379 82 SGAGKTESANLLVQQL-TVLGKANNRTLE-EKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 628 LEKLRVARRPASEATFNVFYYLLA-------CGDATLRTELHLNHLAEnnvFGIVPLSKpEEKQKAAQQFSKLQAAMKVL 700
Cdd:cd01379 160 LEKSRVVHQAIGERNFHIFYYIYAglaedkkLAKYKLPENKPPRYLQN---DGLTVQDI-VNNSGNREKFEEIEQCFKVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 701 AISPEEQKTCWLILASIYHLG-------AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQL--KGGTLQRST 771
Cdd:cd01379 236 GFTKEEVDSVYSILAAILHIGdieftevESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVvtRGETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 772 SFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHS---LCSMMIVDTPGFQNpewggsARGAS 848
Cdd:cd01379 316 TVEE--------------ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAsdePLSIGILDIFGFEN------FQKNS 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907082213 849 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL---AFDDLEPVAD 894
Cdd:cd01379 376 FEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVdliEYEDNRPLLD 424
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
464-892 |
3.13e-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: 202.78 E-value: 3.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 464 LNESSVLHTLRQRYGASLLHTYAGPS-LLVLSTRGAPAVYSEKVMHMFK-------GCRREDMAPHIYAVAQTAYRAMLM 535
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 536 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTS--GTKVfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFD 613
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSkkGTKL--SSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 614 QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF---GIVPL-SKPEEKQkaAQQ 689
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLpLGPGSDD--AEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 690 FSKLQAAMKVLAISPEEQKTCWLILASIYHLgaagatkaGRKQFA-----RHEWA--------QKAAYLLGCSLEELSSA 756
Cdd:cd14879 237 FQELKTALKTLGFKRKHVAQICQLLAAILHL--------GNLEFTydhegGEESAvvkntdvlDIVAAFLGVSPEDLETS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 757 I-FKHQLKGGtlQRSTSFrqgpeesgLG-EGTKLSALEclegMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTP 833
Cdd:cd14879 309 LtYKTKLVRK--ELCTVF--------LDpEGAAAQRDE----LARTLYSLLFAWVVETINQKLCAPEDDFATFIsLLDFP 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 834 GFQNPewgGSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA----FDDLEPV 892
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 ... |
467-1169 |
5.43e-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: 202.32 E-value: 5.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIagtsGTKVFSVEKWQALSTL--LEAFGNSPTIMNGSATRFSQILSLDFdQAGQVASASIQ 624
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVLpiLESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 625 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAEN----NVFGIVPLSKPEEkqkaAQQFSKLQAAMKVL 700
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETyyylNQGGACRLQGKED----AQDFEGLLKALQGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 701 AISPEEQKTCWLILASIYHLGAAGATKAGRKQF---ARHEWA--QKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFrq 775
Cdd:cd14896 231 GLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAeiHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPL-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 776 gPEEsglgegtklSALECLEGMASGLYSELFTLLISLVNRAL--KSSQHSLCSMMIVDTPGFQnpewggSARGASFEELC 853
Cdd:cd14896 309 -PVE---------GAIDARDALAKTLYSRLFTWLLKRINAWLapPGEAESDATIGVVDAYGFE------ALRVNGLEQLC 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 854 HNYAQDRLQRLFHERTFLQELERYKEDniELAFDDLEPVADDSVA--AVDQASHLVRSLahadeargllwllEEEALVPG 931
Cdd:cd14896 373 INLASERLQLFSSQTLLAQEEEECQRE--LLPWVPIPQPPRESCLdlLVDQPHSLLSIL-------------DDQTWLSQ 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 932 ATEDALLDRLFSYYGPQEGDKKGQSPLlrsskPRhFLLGHSHGTnwVEYNVAGWLNYTKQ--NPATQNaprLLQDSQKKI 1009
Cdd:cd14896 438 ATDHTFLQKCHYHHGDHPSYAKPQLPL-----PV-FTVRHYAGT--VTYQVHKFLNRNRDqlDPAVVE---MLAQSQLQL 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1010 ISNLFlgragsatvlsgsiagLEGGSQLALRRatsmrktfttgmaavKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLP 1089
Cdd:cd14896 507 VGSLF----------------QEAEPQYGLGQ---------------GKPTLASRFQQSLGDLTARLGRSHVYFIHCLNP 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1090 VAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1169
Cdd:cd14896 556 NPGKLPG-----------------------------LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG 606
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
467-1213 |
1.38e-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: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQaGQVASASIQTM 626
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLV--TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTE---------LHLNHLAENNVFGivplskpeekQKAAQQFSKLQAAM 697
Cdd:cd01387 158 LLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKyglqeaekyFYLNQGGNCEIAG----------KSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 698 KVLAISPEEQKTCWLILASIYHLGAAgatkagrkQFARHEW--AQKAAyLLGcSLEELSSAIFKHQLKGGTLQRSTSFR- 774
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNV--------YFHKRQLrhGQEGV-SVG-SDAEIQWVAHLLQISPEGLQKALTFKv 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 775 -QGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELC 853
Cdd:cd01387 298 tETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN------SFEQLC 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 854 HNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVAddsvaavdqasHLVrslahADEARGLLWLLEEEALVP 930
Cdd:cd01387 372 INYANENLQYYFNKHVFKLEQEEYIREQIDwteIAFADNQPVI-----------NLI-----SKKPVGILHILDDECNFP 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 931 GATEDALLDRLFSYYGPQEgdkkgqspllRSSKPR----HFLLGHSHGTNWveYNVAGWLNYTKqNPATQNAPRLLQDSQ 1006
Cdd:cd01387 436 QATDHSFLEKCHYHHALNE----------LYSKPRmplpEFTIKHYAGQVW--YQVHGFLDKNR-DQLRQDVLELLVSSR 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1007 KKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAAVKKKSLCIQIKLQ--VDALIDTIKRSKMHFV 1084
Cdd:cd01387 503 TRVVAHLF--------------------SSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQdsLLQLLEKMERCNPWFV 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1085 HCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1164
Cdd:cd01387 563 RC---------------------------LKPNHKKEPMLFDMDVVM--AQLRYSGMLETIRIRKEGYPVRLPFQVFIDR 613
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1907082213 1165 FDvlapHLTKKHGRNYIVVDEKRAVeELLESLDLEKSSCCLGLSRVFFR 1213
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 ... |
469-1168 |
7.14e-53 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 198.98 E-value: 7.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 469 VLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAML----MSRQDQSIVL 544
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 545 LGSSGSGKTTSFQHLVQYLATIAgtSGTKVFSVEKWQaLSTLLEAFGNSPTIMNGSATRFSQILSLDFdQAGQVASASIQ 624
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC--RGNSQLEQQILQ-VNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 625 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL----NHLAENNVFGivplsKPEEKQKAAQQFSKLQAAMKVL 700
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLldpgKYRYLNNGAG-----CKREVQYWKKKYDEVCNAMDMV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 701 AISPEEQKTCWLILASIYHLG----AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSsaifkhqlkgGTLQRSTSFRQG 776
Cdd:cd14889 234 GFTEQEEVDMFTILAGILSLGnitfEMDDDEALKVENDSNGWLKAAAGQFGVSEEDLL----------KTLTCTVTFTRG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 777 peESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHS---LCSMMIVDTPGFQNPEWGgsargaSFEELC 853
Cdd:cd14889 304 --EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSsveLREIGILDIFGFENFAVN------RFEQAC 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 854 HNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDLEPVAD-------DSVAAVDQASHLvrslahadeargllwll 923
Cdd:cd14889 376 INLANEQLQYFFNHHIFLMEQKEYKKEGIdwkEITYKDNKPILDlflnkpiGILSLLDEQSHF----------------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 924 eeealvPGATEDALLDRLFSYYGPQEGDKKGQspllrsSKPRHFLLGHSHGTnwVEYNVAGWLNYTKQN-PATQNAprLL 1002
Cdd:cd14889 439 ------PQATDESFVDKLNIHFKGNSYYGKSR------SKSPKFTVNHYAGK--VTYNASGFLEKNRDTiPASIRT--LF 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1003 QDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSQlalrratsmrktfttGMAAVKKKSLCIQIKLQVDALIDTIKRSKMH 1082
Cdd:cd14889 503 INSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD---------------NFNSTRKQSVGAQFKHSLGVLMEKMFAASPH 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1083 FVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1162
Cdd:cd14889 568 FVRCIKPNHVKVPG-----------------------------QLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFA 618
|
....*.
gi 1907082213 1163 RRFDVL 1168
Cdd:cd14889 619 ERYKIL 624
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
468-1170 |
1.18e-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: 1.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPyKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGtsGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 626
Cdd:cd14904 82 ESGAGKTETTKIVMNHLASVAG--GRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEE 706
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 707 QKTCWLILASIYHLGAAGATKAGRK--QFARHEWAQKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRQgpeESGLGE 784
Cdd:cd14904 240 QRTLFKILSGVLHLGEVMFDKSDENgsRISNGSQLSQVAKMLGLPTTRIEEAL---------CNRSVVTRN---ESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 785 GTKLSALECLEGMASGLYSELFTLLISLVNRALkSSQHSLCSMMI--VDTPGFQNPEWGGsargasFEELCHNYAQDRLQ 862
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAI-STDDDRIKGQIgvLDIFGFEDFAHNG------FEQFCINYANEKLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 863 RLFHERTFLQELERYKEDNieLAFDDLEPVADDSVAAVDQASHLVRSLAHaDEARGllwlleeealvPGATEDALLDRLF 942
Cdd:cd14904 381 QKFTTDVFKTVEEEYIREG--LQWDHIEYQDNQGIVEVIDGKMGIIALMN-DHLRQ-----------PRGTEEALVNKIR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 943 SYYGPQEGDKKGQSPllrSSKPRHFLLGHSHGTnwVEYNVAGWLNytKQNPATQN-APRLLQDSQKKIISNLFlgraGSA 1021
Cdd:cd14904 447 TNHQTKKDNESIDFP---KVKRTQFIINHYAGP--VTYETVGFME--KHRDTLQNdLLDLVLLSSLDLLTELF----GSS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1022 TVLSGSIAGLEGGSQLAlrratsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGEprsa 1101
Cdd:cd14904 516 EAPSETKEGKSGKGTKA-------------------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTE---- 572
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082213 1102 ssrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1170
Cdd:cd14904 573 -------------------------FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP 616
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
468-1213 |
3.38e-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: 196.92 E-value: 3.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVM--HMFKGCRRedMAPHIYAVAQTAYRAMLMSRQDQSIVLL 545
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMdqYMHKGPKE--MPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 546 GSSGSGKTTSFQHLVQYLATIAGTSGtkvfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASI 623
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTN----GVEQ-RVLLAnpILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 624 QTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlaenNVFGIVPLSKPEEKQKA--AQQFSKLQAAMKVLA 701
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSS-----AAYGYLSLSGCIEVEGVddVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 702 ISPEEQKTCWLILASIYHLG------AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QLKGgtlQRSTSF 773
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGniefasGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRlmEIKG---CDPTRI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 774 RQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSL-CSMMIVDTPGFQNPEWGgsargaSFEEL 852
Cdd:cd14872 307 PLTPAQ----------ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKtTFIGVLDIFGFEIFEKN------SFEQL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 853 CHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVrslahadEAR--GLLWLLEEEA 927
Cdd:cd14872 371 CINFTNEKLQQHFNQYTFKLEEALYQSEGVKfehIDFIDNQPVLD-----------LI-------EKKqpGLMLALDDQV 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 928 LVPGATEDALLDRLfsyyGPQEGDKKGQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQK 1007
Cdd:cd14872 433 KIPKGSDATFMIAA----NQTHAAKSTFVYAEVRTSRTEFIVKHYAGD--VTYDITGFLEKNK-DTLQKDLYVLLSSSKN 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1008 KIISNLFlgragsatvlsgsiagleggSQLALRRATSmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCf 1087
Cdd:cd14872 506 KLIAVLF--------------------PPSEGDQKTS-------------KVTLGGQFRKQLSALMTALNATEPHYIRC- 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1088 lpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1167
Cdd:cd14872 552 --------------------------VKPNQEKRARLFDGFMSL--EQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRF 603
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1907082213 1168 LAPHLTKKHGRnyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1213
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 ... |
468-1170 |
9.94e-52 |
|
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: 196.44 E-value: 9.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLaTIAGTSGTKVfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd01385 82 SGSGKTESTNFLLHHL-TALSQKGYGS-GVEQ-TILGAgpVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 705
Cdd:cd01385 159 YLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 706 EQKTCWLILASIYHLgaaGATKAGRKQFARHEWAQKA--------AYLLGCSLEELSSAIF--KHQLKGGTLQRSTSFrq 775
Cdd:cd01385 238 TQRQIFSVLSAVLHL---GNIEYKKKAYHRDESVTVGnpevldiiSELLRVKEETLLEALTtkKTVTVGETLILPYKL-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 776 gPEesglgegtklsALECLEGMASGLYSELFTLLISLVNRAL---KSSQHSLC-SMMIVDTPGFQNPEWGgsargaSFEE 851
Cdd:cd01385 313 -PE-----------AIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEAKGlSIGVLDIFGFEDFGNN------SFEQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 852 LCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLEPVadDSVAAVdqasHLVRSLAHadearGLLWLLEEEALVPG 931
Cdd:cd01385 375 FCINYANEHLQYYFNQHIFKLEQEEYKKEGIS--WHNIEYT--DNTGCL----QLISKKPT-----GLLCLLDEESNFPG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 932 ATEDALLDRLFS-------YYGPQEgdkkgqspllrssKPRHFLLGHSHGTnwVEYNVAGW----LNYTKQNPATqnapr 1000
Cdd:cd01385 442 ATNQTLLAKFKQqhkdnkyYEKPQV-------------MEPAFIIAHYAGK--VKYQIKDFreknLDLMRPDIVA----- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1001 LLQDSQKKIISNL-----------------FLGRAGSATVLSGSIAGLEGGSQLALRRATSMRktfttGMAAVKKKSLCI 1063
Cdd:cd01385 502 VLRSSSSAFVRELigidpvavfrwavlrafFRAMAAFREAGRRRAQRTAGHSLTLHDRTTKSL-----LHLHKKKKPPSV 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1064 QIKLQV--DALIDTIKRSKMHFVHCFLPVAEGWPgeprsassrrvsssseldlppgdpceaglLQLDVSLLRAQLRGSRL 1141
Cdd:cd01385 577 SAQFQTslSKLMETLGQAEPFFIRCIKSNAEKKP-----------------------------LRFDDELVLRQLRYTGM 627
|
730 740
....*....|....*....|....*....
gi 1907082213 1142 LDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1170
Cdd:cd01385 628 LETVRIRRSGYSVRYTFQEFITQFQVLLP 656
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
468-1175 |
1.25e-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: 196.65 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFK--------GCRREDMAPHIYAVAQTAYRAMLMS-R 537
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPlKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 538 QDQSIVLLGSSGSGKTTSFQHLVQYLATI-----AGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSL 610
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLTSVgrdqsSTEQEGSDAVEIGKRILQTnpILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 611 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAE---NNVFGIVPLSKPEEKQKAA 687
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKyelLNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 688 QQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG------AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQ 761
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGnvnftaENGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSRE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 762 LKGGtlQRSTSFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVN---------RALKSSQHSLCSMMIVDT 832
Cdd:cd14902 322 IKAG--VEVMVLKLTPEQ----------AKEICGSLAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGILDI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 833 PGFQNPEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVaddsVAAVDqashlvrs 909
Cdd:cd14902 390 FGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDwknISYPSNAAC----LALFD-------- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 910 lahaDEARGLLWLLEEEALVPGATEDALLDRLFSYYGPQEgdkkgqspllrsskprHFLLGHSHGTnwVEYNVAGWLNyT 989
Cdd:cd14902 452 ----DKSNGLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAGR--VCYNVEQFVE-K 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 990 KQNPATQNAPRLLQDSQKKIISNLFL-GRAGSATVLSGSiagleggsqlALRRATSMrktfttgmaaVKKKSLCIQIKLQ 1068
Cdd:cd14902 509 NTDALPADASDILSSSSNEVVVAIGAdENRDSPGADNGA----------AGRRRYSM----------LRAPSVSAQFKSQ 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1069 VDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMY 1148
Cdd:cd14902 569 LDRLIVQIGRTEAHYVRCLKPNEVKKPG-----------------------------IFDRERMVEQMRSVGVLEAVRIA 619
|
730 740
....*....|....*....|....*..
gi 1907082213 1149 RQGYPDHMVFSEFRRRFDVLAPHLTKK 1175
Cdd:cd14902 620 RHGYSVRLAHASFIELFSGFKCFLSTR 646
|
|
| PDZ_MYO18-like |
cd06747 |
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein ... |
220-308 |
1.33e-51 |
|
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MYO18 protein and related domains. MYO18 (also known as myosin XVIIIA, KIAA0216, MysPDZ), a member of the myosin superfamily, is involved in regulating cell protrusion and migration, and Golgi trafficking and morphology, and is required for myoblast adhesion and muscle integrity. The MYO18A/MRCK/LRAP35a complex regulates actomyosin retrograde flow in cell protrusion and migration; the PtdIns(4)P/GOLPH3/MYO18A/F-actin complex is a hub for signals that regulate Golgi trafficking function. The MYO18A PDZ domain binds p190Rho-guanine nucleotide exchange factor (p190RhoGEF), Golgin45, and leucine repeat adaptor protein 1 (Lurap1, also known as Lrap35a). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MYO18-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.
Pssm-ID: 467229 [Multi-domain] Cd Length: 90 Bit Score: 176.73 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPTGDFGFSLRRTTMLDRAPE-GQAYRRVVHFAEPGAGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQ 298
Cdd:cd06747 1 EITLKRQPTGDFGFSLRRGTIVERGPDdGQELKRTVHFAEPGAGTKNLATGLLPGDRLIEVNGVNVENASRDEIIEMIRK 80
|
90
....*....|
gi 1907082213 299 SGDSVRLKVQ 308
Cdd:cd06747 81 SGDTVTLKVQ 90
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
468-1170 |
4.11e-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: 4.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLL-VLSTRGAPAVYSEKVM--HMFKGcrrEDMAPHIYAVAQTAYRAMLMSRQDQSIVL 544
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIaVNPFKTIPGLYSDEMLlkFIQPS---ISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 545 LGSSGSGKTTSFQHLVQYLATiAGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQ-------- 614
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLAC-AGSEDIKKRSLVEAQVLESnpLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 615 -AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIV--PLSKPEEKQKAAQQFS 691
Cdd:cd14888 158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADakPISIDMSSFEPHLKFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 692 KLQ--------------------AAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARH------EWAQKAAYL 745
Cdd:cd14888 238 YLTksschelpdvddleefestlYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVvsasctDDLEKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 746 LGCSLEELSSAifkhqLKGGTLQRSTSFRQGPEESGLGEGTKlsaleclEGMASGLYSELFTLLISLVNRAL-KSSQHSL 824
Cdd:cd14888 318 LGVDAEDLLNA-----LCYRTIKTAHEFYTKPLRVDEAEDVR-------DALARALYSCLFDKVVERTNESIgYSKDNSL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 825 CSMMIVDTPGFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLE-PVADDSVAAVDQA 903
Cdd:cd14888 386 LFCGVLDIFGFE------CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIS--WNPLDfPDNQDCVDLLQEK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 904 SHLVrsLAHADEargllwlleeEALVPGATEDALLDRLFSYYGpqeGDKKGQSPllrSSKPRHFLLGHSHGTnwVEYNVA 983
Cdd:cd14888 458 PLGI--FCMLDE----------ECFVPGGKDQGLCNKLCQKHK---GHKRFDVV---KTDPNSFVIVHFAGP--VKYCSD 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 984 GWLNYTKqNPATQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsqlalrrATSMRKTFTTGMAAVKKKSLCI 1063
Cdd:cd14888 518 GFLEKNK-DQLSVDAQEVIKNSKNPFISNLF---------------------------SAYLRRGTDGNTKKKKFVTVSS 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1064 QIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPgeprsassrrvsssSELDlppgdpceagllQLDVSllrAQLRGSRLLD 1143
Cdd:cd14888 570 EFRNQLDVLMETIDKTEPHFIRCIKPNSQNVP--------------DLFD------------RISVN---EQLKYGGVLQ 620
|
730 740
....*....|....*....|....*..
gi 1907082213 1144 AMRMYRQGYPDHMVFSEFRRRFDVLAP 1170
Cdd:cd14888 621 AVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
470-1169 |
7.94e-51 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 193.05 E-value: 7.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 470 LHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSekVMHMFKGCRREDMA----PHIYAVAQTAYRAMLMSR----QDQ 540
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPyKSIPLLYD--VPGFDSQRKEEATAssppPHVFSIAERAYRAMKGVGkgqgTPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 541 SIVLLGSSGSGKTTSFQHLVQYLATI----AGTSGTKVF-----SVEKWQALS-TLLEAFGNSPTIMNGSATRFSQILSL 610
Cdd:cd14892 82 SIVVSGESGAGKTEASKYIMKYLATAsklaKGASTSKGAanaheSIEECVLLSnLILEAFGNAKTIRNDNSSRFGKYIQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 611 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAEnnvFGIVPLSKPEEKQKA--AQ 688
Cdd:cd14892 162 HYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAES---FLFLNQGNCVEVDGVddAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 689 QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGA----AGATKAGRK-QFARHEWAQKAAYLLGCSLEELSSAIFKHQLK 763
Cdd:cd14892 239 EFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNvrfeENADDEDVFaQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 764 GGtlqRSTSFRQ--GPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRAlkSSQHSLCSMMIVDTP-------- 833
Cdd:cd14892 319 TA---RGSVLEIklTARE----------AKNALDALCKYLYGELFDWLISRINAC--HKQQTSGVTGGAASPtfspfigi 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 834 ----GFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaaVDQASHL 906
Cdd:cd14892 384 ldifGFE------IMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDvsaIEFQDNQDCLD-----LIQKKPL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 907 vrslahadeargllwlleeeALVPGATEDALLDR-------LFSYYgpQEGDKKGQSpllrSSKPR----HFLLGHSHGT 975
Cdd:cd14892 453 --------------------GLLPLLEEQMLLKRkttdkqlLTIYH--QTHLDKHPH----YAKPRfecdEFVLRHYAGD 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 976 nwVEYNVAGWLnyTKQNPATQNAPRLLQDSQKKiisnlflgragsatvlsgsiagleggsqlalrratsmrktFTTgmaa 1055
Cdd:cd14892 507 --VTYDVHGFL--AKNNDNLHDDLRDLLRSSSK----------------------------------------FRT---- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1056 vkkkslciqiklQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvsssSELDLPPGDPCEagllqldvsLLRAQ 1135
Cdd:cd14892 539 ------------QLAELMEVLWSTTPSYIKCIKP--------------------NNLKFPGGFSCE---------LVRDQ 577
|
730 740 750
....*....|....*....|....*....|....
gi 1907082213 1136 LRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1169
Cdd:cd14892 578 LIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLA 611
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
468-1211 |
7.44e-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: 190.00 E-value: 7.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSE--KVMHMFKGCRRED----MAPHIYAVAQTAYRAMLMSR---- 537
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDetKEAYYEHGERRAAgerkLPPHVYAVADKAFRAMLFASrgqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 538 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW----QALST--LLEAFGNSPTIMNGSATRFSQILSLD 611
Cdd:cd14901 82 CDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATEREnvrdRVLESnpILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 612 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFS 691
Cdd:cd14901 162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 692 KLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRK----QFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTL 767
Cdd:cd14901 242 KTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEggtfSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 768 QRSTSFRqgPEESGLGEgtklsaleclEGMASGLYSELFTLLISLVNRALK--SSQHSLCSMMIVDTPGF----QNpewg 841
Cdd:cd14901 322 YITMPLS--VEQALLTR----------DVVAKTLYAQLFDWLVDRINESIAysESTGASRFIGIVDIFGFeifaTN---- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 842 gsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLePVADDSVAAVDQASHLVRSLahADEargllw 921
Cdd:cd14901 386 ------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-PNNDACVAMFEARPTGLFSL--LDE------ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 922 lleeEALVPGATEDALLDrlfSYYgpqegDKKGQSPLLRSSK----PRHFLLGHSHGTnwVEYNVAGWLNYTKQNPATqN 997
Cdd:cd14901 451 ----QCLLPRGNDEKLAN---KYY-----DLLAKHASFSVSKlqqgKRQFVIHHYAGA--VCYATDGFCDKNKDHVHS-E 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 998 APRLLQDSqkkiiSNLFLgragSATVLSgsiagleggsqlalrratsmrktfttgmaavkkkslciQIKLQVDALIDTIK 1077
Cdd:cd14901 516 ALALLRTS-----SNAFL----SSTVVA--------------------------------------KFKVQLSSLLEVLN 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1078 RSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDpcEAGLLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMV 1157
Cdd:cd14901 549 ATEPHFIRC---------------------------IKPND--VLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1158 FSEFRRRFDVLAPHLTKKHGRNYIVVDEKRAVEELLESLDLEKSSCCLGLSRVF 1211
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
467-1168 |
2.17e-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: 185.62 E-value: 2.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRRE--------DMAPHIYAVAQTAYRAMLMSR 537
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPyKQIDNLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 538 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAG----------------TSGTKVFSVEKwQALST--LLEAFGNSPTIMNG 599
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssirATSKSTKSIEQ-KILSCnpILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 600 SATRFSQILSLDFD-QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL-NHLAENNVFgivPL 677
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLkNQLSGDRYD---YL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 678 SKPE----EKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG-----AAGATKAGRKQFARHEWAQKAAYLLGC 748
Cdd:cd14907 237 KKSNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGnlqfdDSTLDDNSPCCVKNKETLQIIAKLLGI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 749 SLEELSSAIFKHQLKGGTlQRSTSfrqgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRAL-------- 817
Cdd:cd14907 317 DEEELKEALTTKIRKVGN-QVITS--------------PLSKKECinnRDSLSKELYDRLFNWLVERLNDTImpkdekdq 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 818 KSSQHSLCSMMIVDTPGFQNPEwggsarGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE-----LAFDDLEPV 892
Cdd:cd14907 382 QLFQNKYLSIGLLDIFGFEVFQ------NNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdylnqLSYTDNQDV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 893 AD--DS-----VAAVDQASHLvrslahadeargllwlleeealvPGATEDALLDRLFSYYGpqeGDKKGQSPllRSSKPR 965
Cdd:cd14907 456 IDllDKppigiFNLLDDSCKL-----------------------ATGTDEKLLNKIKKQHK---NNSKLIFP--NKINKD 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 966 HFLLGHSHGTnwVEYNVAGWL--NYTKQNPATQNaprLLQDSQKKIISNLFLGRAGSATVLSGSIAGleggsqlalrrat 1043
Cdd:cd14907 508 TFTIRHTAKE--VEYNIEGFRekNKDEISQSIIN---CIQNSKNRIISSIFSGEDGSQQQNQSKQKK------------- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1044 smrktfttgmAAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGwpgeprsassrrvsssseldlppgdpcEAG 1123
Cdd:cd14907 570 ----------SQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEK---------------------------KAD 612
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082213 1124 LLQLDVSLLraQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1168
Cdd:cd14907 613 LFIQGYVLN--QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
468-878 |
7.70e-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: 7.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFS--VEKwqalSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQ 624
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIEQriLEA----NPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 625 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENnvfgivplskpeekqkaAQQFSKLQAAMKVLAISP 704
Cdd:cd01382 158 HYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLDD-----------------VGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 705 EEQKTCWLILASIYHLG------AAGATKAGRKQFARHEWA-QKAAYLLGCSLEELSSAI---FKHQLKGGTlqRSTSFR 774
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGniefeeNGSDSGGGCNVKPKSEQSlEYAAELLGLDQDELRVSLttrVMQTTRGGA--KGTVIK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 775 QG--PEESGlgegtklSALECLegmASGLYSELFTLLISLVNRAL--KSSQHSLCsmmIVDTPGFQ----Npewggsarg 846
Cdd:cd01382 299 VPlkVEEAN-------NARDAL---AKAIYSKLFDHIVNRINQCIpfETSSYFIG---VLDIAGFEyfevN--------- 356
|
410 420 430
....*....|....*....|....*....|..
gi 1907082213 847 aSFEELCHNYAQDRLQRLFHERTFLQELERYK 878
Cdd:cd01382 357 -SFEQFCINYCNEKLQQFFNERILKEEQELYE 387
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1264-1958 |
3.57e-44 |
|
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: 176.90 E-value: 3.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1264 NIKKNKGVKDWPWWKLFTTVRPLIQVQLSEEQIRNKDE-EIQQLRSKLEKVEKERNELrlssdrlETRISELTSELtder 1342
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESERQRAEL-------AEKLSKLQSEL---- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1343 ntgESASQLLDAETAERLRTEKEMKELQTQ-YDALKKQMEVMEMEVMEARLIRA--AEINGEVDDDDAGGEWRLKYERAV 1419
Cdd:pfam01576 443 ---ESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQleDERNSLQEQLEEEEEAKRNVERQL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1420 REVDF----TKKRLQQELEdKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE 1495
Cdd:pfam01576 520 STLQAqlsdMKKKLEEDAG-TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1496 LEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSqeSKDEA 1575
Cdd:pfam01576 599 LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVS--SKDDV 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1576 --SLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEV 1653
Cdd:pfam01576 677 gkNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1654 QLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLrKDLKRTKALLADAQIMLDHLKNN-----APSKREIAQL 1728
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV-KQLKKLQAQMKDLQRELEEARASrdeilAQSKESEKKL 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1729 KN------QLEESeftCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1802
Cdd:pfam01576 836 KNleaellQLQED---LAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL 912
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1803 KAAVAQ---------ASRDMAQMND-LQAQIEESNKekqELQEKLQALQSQVEFLEqsmvdKSLVSRQEAKIRELETRLE 1872
Cdd:pfam01576 913 RKSTLQveqlttelaAERSTSQKSEsARQQLERQNK---ELKAKLQEMEGTVKSKF-----KSSIAALEAKIAQLEEQLE 984
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1873 FEKTQ----VKRLENLASRLKETMEKLTEER---DQRAAAENREKEQNKRLQRQLRDTKEEMSelarkEAEASRKKheLE 1945
Cdd:pfam01576 985 QESRErqaaNKLVRRTEKKLKEVLLQVEDERrhaDQYKDQAEKGNSRMKQLKRQLEEAEEEAS-----RANAARRK--LQ 1057
|
730
....*....|...
gi 1907082213 1946 MDLESLEAANQSL 1958
Cdd:pfam01576 1058 RELDDATESNESM 1070
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
468-1184 |
8.01e-44 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 171.26 E-value: 8.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF-------------KGcrREDMAPHIYAVAQTAYRAM 533
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfQKLPGLYSSDTMAKYllsfearssstrnKG--SDPMPPHIYQVAGEAYKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 534 LMSR----QDQSIVLLGSSGSGKTTSFQHLVQYLA---------TIAGTSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGS 600
Cdd:cd14900 80 MLGLngvmSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQT-NILLESFGNARTLRNDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 601 ATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDAtlrtelhlnhlaennvfgivplskp 680
Cdd:cd14900 159 SSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAI-GAS------------------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 681 eEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKqfarHEWAQKAAYLLGCSLEELSSAIFKH 760
Cdd:cd14900 213 -EAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENS----DRLGQLKSDLAPSSIWSRDAAATLL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 761 QLKGGTLQRSTS---FRQGPEESGLgegtKLSALEC---LEGMASGLYSELFTLLISLVNRALK-----SSQHSLCSMMI 829
Cdd:cd14900 288 SVDATKLEKALSvrrIRAGTDFVSM----KLSAAQAnnaRDALAKALYGRLFDWLVGKMNAFLKmddssKSHGGLHFIGI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 830 VDTPGF----QNpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEpvadDSVAAVDQ 902
Cdd:cd14900 364 LDIFGFevfpKN----------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDwkyVEFCDNQ----DCVNLISQ 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 903 ASHLVRSLahADEargllwlleeEALVPGATEDALLDRLFSyygpqegdKKGQSPLLRSSKPRH----FLLGHSHGTnwV 978
Cdd:cd14900 430 RPTGILSL--IDE----------ECVMPKGSDTTLASKLYR--------ACGSHPRFSASRIQRarglFTIVHYAGH--V 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 979 EYNVAGWLNytkqnpatQNAPRLLQDsqkkiISNLFLGragsatvlsgsiagleggsqlalrratsmrktfttgmaavkk 1058
Cdd:cd14900 488 EYSTDGFLE--------KNKDVLHQE-----AVDLFVY------------------------------------------ 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1059 kslCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRG 1138
Cdd:cd14900 513 ---GLQFKEQLTTLLETLQQTNPHYVRC---------------------------LKPNDLCKAGIYERERVL--NQLRC 560
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1139 SRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA----PHLTKKHGrnYIVVD 1184
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 ... |
468-1169 |
9.68e-44 |
|
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: 172.06 E-value: 9.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSekvMHMFkgcrREDM------APHIYAVAQTAYRAMLM----- 535
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPfKHIPGLYD---LHKY----REEMpgwtalPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 536 --SRQDQSIVLLGSSGSGKTTSFQHLVQYLA-----TIAGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQ 606
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskhTTATSSSKRRRAISGSELLSAnpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 607 ILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNvFGIVPLSKPE 681
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQE-FQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 682 EKQKAAQ---QFSKLQAAMKVLAISPEEQKTCWLILASIYHLG-----AAGATKAGRKQFARHEWAQKA----------- 742
Cdd:cd14895 234 QRNDGVRddkQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvASSEDEGEEDNGAASAPCRLAsaspssltvqq 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 743 -----AYLLGCSLEELSSAIFKHQLKGGtlqrstsfrqgpEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRAL 817
Cdd:cd14895 314 hldivSKLFAVDQDELVSALTTRKISVG------------GETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 818 KSSQHSLCS-----------MMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 886
Cdd:cd14895 382 PQRQFALNPnkaankdttpcIAVLDIFGFEEFEVN------QFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 887 DDLEpvaDDSVA--AVDQASHLVRSLAhaDEargllwlleeEALVPGATEDALLDRLFSYYGpqegDKKGQSPLLRSSKP 964
Cdd:cd14895 456 VDYE---DNSVCleMLEQRPSGIFSLL--DE----------ECVVPKGSDAGFARKLYQRLQ----EHSNFSASRTDQAD 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 965 RHFLLGHSHGTnwVEYNVAGWLNYTKQNPaTQNAPRLLQDSQKKIISNLFlgragsaTVLSGSIAGLEGGSQLALRRATS 1044
Cdd:cd14895 517 VAFQIHHYAGA--VRYQAEGFCEKNKDQP-NAELFSVLGKTSDAHLRELF-------EFFKASESAELSLGQPKLRRRSS 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1045 MRKTFTTGMaavkkkslciQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGl 1124
Cdd:cd14895 587 VLSSVGIGS----------QFKQQLASLLDVVQQTQTHYIRC---------------------------IKPNDESASD- 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082213 1125 lQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1169
Cdd:cd14895 629 -QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
507-883 |
3.67e-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: 3.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 507 MHMFKGCRREDMAPHIYAVAQTAYRAMLMSR---QDQSIVLLGSSGSGKTTSFQHLVQYLAT-----IAGTSGTKVFSVE 578
Cdd:cd14891 40 KSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQSIVISGESGAGKTETSKIILRFLTTravggKKASGQDIEQSSK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 579 KWQALST-----------LLEAFGNSPTIMNGSATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVF 646
Cdd:cd14891 120 KRKLSVTslderlmdtnpILESFGNAKTLRNHNSSRFGKFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 647 YYLLACGDATLRTELHlnhlaennvfgivpLSKPEEKQKAAQ-------------QFSKLQAAMKVLAISPEEQKTCWLI 713
Cdd:cd14891 200 YQLLAGASAELLKELL--------------LLSPEDFIYLNQsgcvsddniddaaNFDNVVSALDTVGIDEDLQLQIWRI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 714 LASIYHLG-------------AAGATKAGRKQFArhewaqKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRqgpees 780
Cdd:cd14891 266 LAGLLHLGniefdeedtsegeAEIASESDKEALA------TAAELLGVDEEALEKVI---------TQREIVTR------ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 781 GLGEGTKLSALECL---EGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEwggsaRGASFEELCHNYA 857
Cdd:cd14891 325 GETFTIKRNAREAVysrDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFE-----TKNDFEQLLINYA 399
|
410 420
....*....|....*....|....*.
gi 1907082213 858 QDRLQRLFHERTFLQELERYKEDNIE 883
Cdd:cd14891 400 NEALQATFNQQVFIAEQELYKSEGID 425
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
468-1181 |
1.76e-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: 162.46 E-value: 1.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 545
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 546 GSSGSGKTTSFQHLVQYLATiagTSGTKVF----------SVEKWQALST-LLEAFGNSPTIMNGSATRFSQILSLDFDQ 614
Cdd:cd14906 82 GESGSGKTEASKTILQYLIN---TSSSNQQqnnnnnnnnnSIEKDILTSNpILEAFGNSRTTKNHNSSRFGKFLKIEFRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 615 A-GQVASASIQTMLLEKLRVARRP-ASEATFNVFYYLLACGDATLRTELHLNH--------LAENNVFGIV------PLS 678
Cdd:cd14906 159 SdGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNdpskyrylDARDDVISSFksqssnKNS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 679 KPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG-------AAGATKAGRKQFARHEWAQkAAYLLGCSLE 751
Cdd:cd14906 239 NHNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGniefeedSDFSKYAYQKDKVTASLES-VSKLLGYIES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 752 ELSSAIFKHQLKGGTlqRSTSFRQgPEESGLGEGTKlsaleclEGMASGLYSELFTLLISLVNR-----------ALKSS 820
Cdd:cd14906 318 VFKQALLNRNLKAGG--RGSVYCR-PMEVAQSEQTR-------DALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 821 QHSLCSMMIVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDlepvADDSV 897
Cdd:cd14906 388 KKNNLFIGVLDIFGFEN------LSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSnsnFID----NKECI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 898 AAVDQASHLVRSLAHaDEArgllwlleeeaLVPGATEDALLDRLFSYYgpqegdKKGQSPLLRSSKPRHFLLGHSHGTnw 977
Cdd:cd14906 458 ELIEKKSDGILSLLD-DEC-----------IMPKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGD-- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 978 VEYNVAGWLNYTKQNPATqNAPRLLQDSQKKIISNLFLGRAGSATvlsgsiagleggsqlalrrATSMRKTFTTGMAAvk 1057
Cdd:cd14906 518 VTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT-------------------NTTKKQTQSNTVSG-- 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1058 kkslciQIKLQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvssssELDLPPGDpceagllqLDVSLLRAQLR 1137
Cdd:cd14906 576 ------QFLEQLNQLIQTINSTSVHYIRCIKP---------------------NQTMDCNN--------FNNVHVLSQLR 620
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082213 1138 GSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYI 1181
Cdd:cd14906 621 NVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPK 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
467-1169 |
1.01e-38 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 156.13 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMF---KGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIV 543
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 544 LLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSveKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDF-DQAGQVASAS 622
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDS--RFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 623 IQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVfgiVPLSKPEEKQKAA-----QQFSKLQAAM 697
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRY---LNQTMREDVSTAErslnrEKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 698 KVLAISPEEQKTCWLILASIYHLGAAG---ATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFK--HQLKGGTLQRSTS 772
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRftaLTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTdiQYFKGDMIIRRHT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 773 FRQGPEESGLgegtklsaleclegMASGLYSELFTLLISLVNRALKsSQHSLCSMM-----IVDTPGFQNpewggsARGA 847
Cdd:cd14878 316 IQIAEFYRDL--------------LAKSLYSRLFSFLVNTVNCCLQ-SQDEQKSMQtldigILDIFGFEE------FQKN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 848 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE-------------LAFDDLEPVADDSVaaVDQASHLVRSLAHAD 914
Cdd:cd14878 375 EFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTmetayspgnqtgvLDFFFQKPSGFLSL--LDEESQMIWSVEPNL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 915 EARgllwlleeealVPGATEDALLDRLFSYYGPQEGD--KKGQSPLlrsskprhFLLGHSHGTnwVEYNVAGWLNYTKqN 992
Cdd:cd14878 453 PKK-----------LQSLLESSNTNAVYSPMKDGNGNvaLKDQGTA--------FTVMHYAGR--VMYEIVGAIEKNK-D 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 993 PATQNAPRLLQDSQKKIISNLFLGRAgsATVlsgsiaglegGSQLalrratsmrktfttgmaavkKKSLC-IQIKLQvda 1071
Cdd:cd14878 511 SLSQNLLFVMKTSENVVINHLFQSKL--VTI----------ASQL--------------------RKSLAdIIGKLQ--- 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1072 lidtikRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQG 1151
Cdd:cd14878 556 ------KCTPHFIHCIKPNNSKLPD-----------------------------TFDNFYVSAQLQYIGVLEMVKIFRYG 600
|
730
....*....|....*...
gi 1907082213 1152 YPDHMVFSEFRRRFDVLA 1169
Cdd:cd14878 601 YPVRLSFSDFLSRYKPLA 618
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
468-1172 |
1.04e-37 |
|
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: 151.97 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGpsLLVLSTRGAPAVYSEKVMHMFKGCRREdMAPHIYAVAQTAYRAMLMSrQDQSIVLLGS 547
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSG--LVFLALNPYETIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 548 SGSGKTTSFQHLVQYLatIAGTSGTKvfSVEK-WQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDqaGQVASASIQTM 626
Cdd:cd14898 78 SGSGKTENAKLVIKYL--VERTASTT--SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSkpeekqkaaQQFSKLQAAMKVLAI-SPE 705
Cdd:cd14898 152 LLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFIDTSSTAGNKESIVQLS---------EKYKMTCSAMKSLGIaNFK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 706 EQKTCwliLASIYHLGAAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QLKGGTLQRSTSFRQgpeesglg 783
Cdd:cd14898 223 SIEDC---LLGILYLGSIQFVNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFsiQVKGETIEVFNTLKQ-------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 784 egtklsALECLEGMASGLYSELFTLLISLVNRALK-SSQHSLCsmmIVDTPGFQNPEWGGsargasFEELCHNYAQDRLQ 862
Cdd:cd14898 292 ------ARTIRNSMARLLYSNVFNYITASINNCLEgSGERSIS---VLDIFGFEIFESNG------LDQLCINWTNEKIQ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 863 RLFHERTFLQELERYKEDNIElaFDDLEPVADDSVaavdqashlvrsLAHADEARGLLWLLEEEALVPGATEDALLDRLF 942
Cdd:cd14898 357 NDFIKKMFRAKQGMYKEEGIE--WPDVEFFDNNQC------------IRDFEKPCGLMDLISEESFNAWGNVKNLLVKIK 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 943 SYYGPQEGDKKGQSPLLrsskprhfllghSHGTNWVEYNVAGWLNYTKQNpatqnaprllqdSQKKIISNLFLGRAGSat 1022
Cdd:cd14898 423 KYLNGFINTKARDKIKV------------SHYAGDVEYDLRDFLDKNREK------------GQLLIFKNLLINDEGS-- 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1023 vlsgsiagleggsqlalrratsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPgeprsas 1102
Cdd:cd14898 477 -----------------------------------KEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRP------- 514
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1103 srrvsssseldlppgdpceaglLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHL 1172
Cdd:cd14898 515 ----------------------WCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
470-1213 |
1.01e-36 |
|
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: 150.95 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 470 LHTLRQRYGA--------SLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQS 541
Cdd:cd14887 4 LENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 542 IVLLGSSGSGKTTSFQHLVQYLATI------AGTSGTKvfsvEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQA 615
Cdd:cd14887 84 ILISGESGAGKTETSKHVLTYLAAVsdrrhgADSQGLE----ARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 616 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLlaCGDATLRTELHlnhlaennvfgivplSKPEEKQKAAQQFSKLQA 695
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYAL--CNAAVAAATQK---------------SSAGEGDPESTDLRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFARH-----------EWAQKAAYLLgcSLEELSSAIFKHQLKG 764
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKrkltsvsvgceETAADRSHSS--EVKCLSSGLKVTEASR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 765 GTLQRSTSFRQGPEESGLGEGTKLS-----------------ALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSM 827
Cdd:cd14887 301 KHLKTVARLLGLPPGVEGEEMLRLAlvsrsvretrsffdldgAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSESD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 828 MIVDTP--------------GFQNPEWGGSARgasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL-----AFDD 888
Cdd:cd14887 381 SDEDTPsttgtqtigildlfGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQnqdcsAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 889 LEPVADDSVAAVDQASHLvrSLAHADEARGLLWLLEEEALVPGATEDALLdrlfsyygpqegdkkgQSPLLRSSKPRHFL 968
Cdd:cd14887 458 SFPLASTLTSSPSSTSPF--SPTPSFRSSSAFATSPSLPSSLSSLSSSLS----------------SSPPVWEGRDNSDL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 969 LGHShgtnwVEYNVAGWLNYTKQNPAtqnaprlLQDSQKKIISNLFLGRA---------GSATVLSGSIAGLEGGSQLAL 1039
Cdd:cd14887 520 FYEK-----LNKNIINSAKYKNITPA-------LSRENLEFTVSHFACDVtydardfcrANREATSDELERLFLACSTYT 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1040 RRATSMRKTFTTGMAAvKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGwpgeprsassrrvsssseldlppgdp 1119
Cdd:cd14887 588 RLVGSKKNSGVRAISS-RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQ-------------------------- 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1120 cEAGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHgrnyivVDEKRAVEELLESLDLE 1199
Cdd:cd14887 641 -EAGI--FEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREA------LTPKMFCKIVLMFLEIN 711
|
810
....*....|....
gi 1907082213 1200 KSSCCLGLSRVFFR 1213
Cdd:cd14887 712 SNSYTFGKTKIFFR 725
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
468-886 |
2.36e-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: 149.29 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFK--GCRRE-------DMAPHIYAVAQTAYRAMLM-SR 537
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiespqALGPHVFAIADRSYRQMMSeIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 538 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL---------LEAFGNSPTIMNGSATRFSQIL 608
Cdd:cd14908 82 ASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSIMdrvlqsnpiLEAFGNARTLRNDNSSRFGKFI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 609 SLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNvfgivpLSKPEEKQKAAQ 688
Cdd:cd14908 162 ELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGG------LQLPNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 689 -------------QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGA---AGATKAGRKQFAR---HEWAQKAAYLLGCS 749
Cdd:cd14908 236 ggapdlreftdedGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQlefESKEEDGAAEIAEegnEKCLARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 750 LEELSSAIFKHQLKGGTLQRSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALK--SSQHSLCSM 827
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKL------------TPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRSSV 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082213 828 MIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 886
Cdd:cd14908 384 GVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAF 436
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
467-886 |
1.38e-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: 146.53 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQ--DQSI 542
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPfKPVPQLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 543 VLLGSSGSGKTTSFQHLVQYLATIAG--TSGTKVFSVEKWQAL----STLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAspTSWESHKIAERIEQRilnsNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLnhlAENNVFGIVPLSkpeEKQKAAQQFSKLQAA 696
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHL---PEGAAFSWLPNP---ERNLEEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 697 MKVLAISPEEQKTCWLILASIYHLGAAGATKAGRKQFA------RHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRS 770
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpmddTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 771 tsFRQgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQN-PEwggsar 845
Cdd:cd14880 315 --FKK-----------PCSRAECdtrRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIgLLDVYGFESfPE------ 375
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1907082213 846 gASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 886
Cdd:cd14880 376 -NSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSF 415
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
402-1269 |
1.51e-35 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 147.87 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 402 LVHRDgfSLASQLKSEELSLPEGKarvkldhdgaILDVDEDDIEKANAP-SCDRLEDLASLVYLNESSVLHTLRQRYGAS 480
Cdd:PTZ00014 56 LVLPG--STGEKLTLKQIDPPTNS----------TFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 481 LLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHL 559
Cdd:PTZ00014 124 QIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 560 VQYLAtiAGTSGTKVFSVEK--WQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRP 637
Cdd:PTZ00014 204 MRYFA--SSKSGNMDLKIQNaiMAA-NPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 638 ASEATFNVFYYLLACGDATLRTELHLNHLAENNVfgIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASI 717
Cdd:PTZ00014 281 DDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKY--INPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 718 YHLG--------AAGATKAGRKQFARHEWAQKAAYLLGCSLEELS-SAIFKHQLKGGTLQRStsfRQGPEESglgEGTKL 788
Cdd:PTZ00014 359 LLLGnveiegkeEGGLTDAAAISDESLEVFNEACELLFLDYESLKkELTVKVTYAGNQKIEG---PWSKDES---EMLKD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 789 SaleclegMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQ----NpewggsargaSFEELCHNYAQDRLQRL 864
Cdd:PTZ00014 433 S-------LSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEvfknN----------SLEQLFINITNEMLQKN 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 865 FHERTFLQELERYKEDNI---ELAFDDLEPVAD------DSVAAV--DQashlvrSLAhadeargllwlleeealvPGAT 933
Cdd:PTZ00014 496 FVDIVFERESKLYKDEGIsteELEYTSNESVIDllcgkgKSVLSIleDQ------CLA------------------PGGT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 934 EDALLDRLFSYYGPQEGDKKGqspllRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNL 1013
Cdd:PTZ00014 552 DEKFVSSCNTNLKNNPKYKPA-----KVDSNKNFVIKHTIGD--IQYCASGFLFKNK-DVLRPELVEVVKASPNPLVRDL 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1014 FLGragsATVLSGSIA-GLEGGSQLalrratsMRktfttgmaavkkkslciqiklQVDALIDTIKRSKMHFVHCFLPvae 1092
Cdd:PTZ00014 624 FEG----VEVEKGKLAkGQLIGSQF-------LN---------------------QLDSLMSLINSTEPHFIRCIKP--- 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1093 gwpgeprsassrrvssssELDLPPGDPCEAGLLqldvsllrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHL 1172
Cdd:PTZ00014 669 ------------------NENKKPLDWNSSKVL--------IQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAV 722
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1173 TKKHGrnyivVDEKRAVEELLESLDLEKSSCCLGLSRVFFR---AGTLARLEEQRDEQTSRHLTLFQAACRGYLARQHFK 1249
Cdd:PTZ00014 723 SNDSS-----LDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVR 797
|
890 900
....*....|....*....|
gi 1907082213 1250 KRkIQDLAIrcVQKNIKKNK 1269
Cdd:PTZ00014 798 KN-IKSLVR--IQAHLRRHL 814
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
467-1165 |
5.44e-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: 145.24 E-value: 5.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF----------KGCRREDMAPHIYAVAQTAYRAMLM 535
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPfQDLPQLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 536 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW-------------QALST--LLEAFGNSPTIMNGS 600
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESIsppaspsrttieeQVLQSnpILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 601 ATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLA----CGDATLRTELHLNHLAEN-NVFGI 674
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSadnnCVSKEQKQVLALSGGPQSfRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 675 VPLSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGA---------------AGATKAGRKQFARHEWA 739
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNvdfeqiphkgddtvfADEARVMSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 740 QKAAYLLGCSLEELSSAIFKHQLKGGtlqrSTSFRQGPEESGLGEGTKLSALEClegmasglYSELFTLLISLVNRALK- 818
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHAS----NETLVVGVDVAHARNTRNALTMEC--------YRLLFEWLVARVNNKLQr 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 819 --------------SSQHSLCSMMIVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL 884
Cdd:cd14899 389 qasapwgadesdvdDEEDATDFIGLLDIFGFED------MAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 885 AFDDLEpvadDSVAAVDQASHlvrslahadEARGLLWLLEEEALVPGATEDALLDRlfsYYgpQEGDKKGQSPLLRSS-- 962
Cdd:cd14899 463 SFVDFP----NNRACLELFEH---------RPIGIFSLTDQECVFPQGTDRALVAK---YY--LEFEKKNSHPHFRSApl 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 963 --KPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLflgRAGSATVLSGSIAGLEGGSQLALR 1040
Cdd:cd14899 525 iqRTTQFVVAHYAGC--VTYTIDGFLAKNK-DSFCESAAQLLAGSSNPLIQAL---AAGSNDEDANGDSELDGFGGRTRR 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1041 RATSmrktfttgmaAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPC 1120
Cdd:cd14899 599 RAKS----------AIAAVSVGTQFKIQLNELLSTVRATTPRYVRC---------------------------IKPNDSH 641
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082213 1121 EAGLLQldVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRF 1165
Cdd:cd14899 642 VGSLFQ--STRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1303-2021 |
1.31e-32 |
|
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: 139.43 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1303 IQQLRSKLEKVEKERNELRLSSDRLETRISELTSE---LTDERNTGESASQLL----DAETAERLR----TEKEMKELQT 1371
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerLRREREKAERYQALLkekrEYEGYELLKekeaLERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1372 QYDALKKQMEVMEMEVM------EARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTK-KRLQQELEDKMEVEQQSR 1444
Cdd:TIGR02169 245 QLASLEEELEKLTEEISelekrlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1445 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKL 1524
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1525 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDE-------ASLAKVKKQLRDLEAKVKDQEEE 1597
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1598 LDEQAGSIQMLEqAKLRLEMEMERMRQTHSKEMESRDEEV---------------------------------EEARQSC 1644
Cdd:TIGR02169 485 LSKLQRELAEAE-AQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgeryataievaagnrlnnvvvedDAVAKEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1645 QKKLKQME----------------------------------VQLEEEYEDKQK----------ALREKREL--ESKLST 1678
Cdd:TIGR02169 564 IELLKRRKagratflplnkmrderrdlsilsedgvigfavdlVEFDPKYEPAFKyvfgdtlvveDIEAARRLmgKYRMVT 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1679 L-------------------SDQVNQR-DFESEKRLRKDLKRTKALLADAQIMLDHLKNNA--------PSKREIAQLKN 1730
Cdd:TIGR02169 644 LegelfeksgamtggsraprGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIENRLdelsqelsDASRKIGEIEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1731 QLEESEFTcAAAVKAR--------KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEI-----QNRLEEDQEDMNE 1797
Cdd:TIGR02169 724 EIEQLEQE-EEKLKERleeleedlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1798 LMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLE----F 1873
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------IENLNGKKEELEEELEeleaA 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1874 EKTQVKRLENLAS---RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHElEMDLES 1950
Cdd:TIGR02169 877 LRDLESRLGDLKKerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLED 955
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1951 LEAANQSLQADLklafKRIGDLQAAIEDEMEsdENEDLINSLQDmvtkyqkKKNKLEGDSDvdsELEDRVD 2021
Cdd:TIGR02169 956 VQAELQRVEEEI----RALEPVNMLAIQEYE--EVLKRLDELKE-------KRAKLEEERK---AILERIE 1010
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1301-2008 |
6.47e-32 |
|
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: 136.84 E-value: 6.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1301 EEI-QQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDErntgESASQLLDAEtaeRLRTEKEMKELQTQYDALKKQ 1379
Cdd:pfam01576 74 EEIlHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE----EAARQKLQLE---KVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1380 MEVMEMEVMEARLiRAAEINGEVDDDDAG----GEWRLKYERAVREVDftkKRLQQELEDKMEVEQqSRRQLERRLGDLQ 1455
Cdd:pfam01576 147 NSKLSKERKLLEE-RISEFTSNLAEEEEKakslSKLKNKHEAMISDLE---ERLKKEEKGRQELEK-AKRKLEGESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1456 ADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEA 1535
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1536 FSLKQQMEEkdldiagfTQKVVSLEAELQdissqeSKDEASLAKVKK-----------QLRDLEAKVKDQEEELDEQags 1604
Cdd:pfam01576 302 EALKTELED--------TLDTTAAQQELR------SKREQEVTELKKaleeetrsheaQLQEMRQKHTQALEELTEQ--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1605 iqmLEQAKlRLEMEMERMRQTHSKEMESRDEEV---EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLS- 1680
Cdd:pfam01576 365 ---LEQAK-RNKANLEKAKQALESENAELQAELrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQs 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1681 --DQVNQRDFESEK---RLRKDLKRTKALLADAQIML-------------------------DHLKNNAPSKREI----- 1725
Cdd:pfam01576 441 elESVSSLLNEAEGkniKLSKDVSSLESQLQDTQELLqeetrqklnlstrlrqledernslqEQLEEEEEAKRNVerqls 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1726 ------AQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQRE----------KNEIQNRLE 1789
Cdd:pfam01576 521 tlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElddllvdldhQRQLVSNLE 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1790 EDQEDMNELMKKHKAAVAQAS--RDMAQMN---------DLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM--VDKSL 1856
Cdd:pfam01576 601 KKQKKFDQMLAEEKAISARYAeeRDRAEAEareketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKddVGKNV 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1857 VSRQEAKiRELETRLEFEKTQVKRL-------ENLASRLKETME--KLTEERDQRAAAENREkEQNKRLQRQLRDTKEEM 1927
Cdd:pfam01576 681 HELERSK-RALEQQVEEMKTQLEELedelqatEDAKLRLEVNMQalKAQFERDLQARDEQGE-EKRRQLVKQVRELEAEL 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1928 SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMEsdENEDLINSLQDMVTKYQKKKNKLE 2007
Cdd:pfam01576 759 EDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQR--ELEEARASRDEILAQSKESEKKLK 836
|
.
gi 1907082213 2008 G 2008
Cdd:pfam01576 837 N 837
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
468-902 |
8.31e-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: 134.48 E-value: 8.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKvMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQE-FHAKYRCKsRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLATIA-GTSGTkvfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd14882 81 ESYSGKTTNARLLIKHLCYLGdGNRGA----TGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRteLHLNHLAENNVFGIVPLSKPEEKQKA----------AQQFSKLQA 695
Cdd:cd14882 157 YQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNR--LKEYNLKAGRNYRYLRIPPEVPPSKLkyrrddpegnVERYKEFEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATKA-GRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQL-KGGTLQRStsf 773
Cdd:cd14882 235 ILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNgGYAELENTEIASRVAELLRLDEKKFMWALTNYCLiKGGSAERR--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 774 RQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVN------RALKSSQHSLcsmMIVDTPGFQNPEWGGsarga 847
Cdd:cd14882 312 KHTTEE----------ARDARDVLASTLYSRLVDWIINRINmkmsfpRAVFGDKYSI---SIHDMFGFECFHRNR----- 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082213 848 sFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIelafddlePVAD----DSVAAVDQ 902
Cdd:cd14882 374 -LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDI--------PTINlrfyDNKTAVDQ 423
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
467-1171 |
1.42e-31 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 134.71 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRRE----------DMAPHIYAVAQTAYRAMLMS 536
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 537 RQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALS----------TLLEAFGNSPTIMNGSATRFSQ 606
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHpigqqilhafTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 607 ILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAC--GDATLRTELHLNHLAENnvFGIVPLSKPEEKQ 684
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKCVNE--FVMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 685 KA--AQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG---------AAGATKAGRKQFARHEWA----QKAAYLLGCS 749
Cdd:cd14893 239 FAldARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGnvdfvpdpeGGKSVGGANSTTVSDAQScalkDPAQILLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 750 LEELSSAIFKHQLKggtLQRSTSFRQGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVN--------RALKS-- 819
Cdd:cd14893 319 LLEVEPVVLDNYFR---TRQFFSKDGNKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNgilggifdRYEKSni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 820 ---SQhslcSMMIVDTPGFQNPEwggsARGASFEELCHNYAQDRLQRLFHERTfLQELERYKEDNIELAFDDLepvADDS 896
Cdd:cd14893 396 vinSQ----GVHVLDMVGFENLT----PSQNSFDQLCFNYWSEKVHHFYVQNT-LAINFSFLEDESQQVENRL---TVNS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 897 VAAVDQASHLVRSLAHaDEARGLLWLLEEEALVPGATEDALLDRLFS-------YYGPQEGDKKGQSPLLRSSKPR-HFL 968
Cdd:cd14893 464 NVDITSEQEKCLQLFE-DKPFGIFDLLTENCKVRLPNDEDFVNKLFSgneavggLSRPNMGADTTNEYLAPSKDWRlLFI 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 969 LGHSHGTnwVEYNVAGwlnYTKQNPATQNA--PRLLQDSQkkiisNLFLGRAGSATVLSGSIAglEGGSQLALRRATS-- 1044
Cdd:cd14893 543 VQHHCGK--VTYNGKG---LSSKNMLSISStcAAIMQSSK-----NAVLHAVGAAQMAAASSE--KAAKQTEERGSTSsk 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1045 MRKTFTTGMAAVK-KKSLCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAG 1123
Cdd:cd14893 611 FRKSASSARESKNiTDSAATDVYNQADALLHALNHTGKNFLVC---------------------------IKPNETLEEG 663
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1907082213 1124 LlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1171
Cdd:cd14893 664 V--FDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH 709
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1287-2009 |
4.23e-31 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 134.41 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1287 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldaetAERLRTEKEM 1366
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--------------LEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1367 KELQTQYDALKkqmevmemevmearliraAEINgevddddaggewrlkyeRAVREVDFTKKRLQQeLEDKMEVEQQSRRQ 1446
Cdd:TIGR02168 284 EELQKELYALA------------------NEIS-----------------RLEQQKQILRERLAN-LERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1447 LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQR 1526
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1527 EKDMLLAEAFSLKQQMEEKDLDIAgftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQ 1606
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLE---------EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1607 M----LEQAKLRLEMeMERMRQTHSKEMESRDEEVEEARQ------------SCQKKLKQ-MEVQLEE-----EYEDKQK 1664
Cdd:TIGR02168 479 AaereLAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAaIEAALGGrlqavVVENLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1665 ALRE----KRELESKLSTLS-DQVNQRDFESEKRLRKDLKRTKALLAD--------AQIMLDHLKNN---APSKREIAQL 1728
Cdd:TIGR02168 558 AKKAiaflKQNELGRVTFLPlDSIKGTEIQGNDREILKNIEGFLGVAKdlvkfdpkLRKALSYLLGGvlvVDDLDNALEL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1729 KNQLEESE----------FTCAAAVKARK-------AMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEED 1791
Cdd:TIGR02168 638 AKKLRPGYrivtldgdlvRPGGVITGGSAktnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1792 QEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV-DKSLVSRQEAKIRELETR 1870
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAeAEAEIEELEAQIEQLKEE 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1871 LEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLES 1950
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1951 LEAANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINSLQDMVTKYQKKKNKLEGD 2009
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRElESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1427-2007 |
5.63e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 133.91 E-value: 5.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1427 KRLQQELED-KMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1505
Cdd:COG1196 216 RELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1506 ELSQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR 1585
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLE-------ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1586 DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMEsRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKA 1665
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1666 LREKRELESKLSTLSDQVnqrdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESeftcAAAVKA 1745
Cdd:COG1196 448 AEEEAELEEEEEALLELL--------AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG----VKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1746 RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQReknEIQNRLEEDQEDMNELMKKHKAAVA-------QASRDMAQMND 1818
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ---NIVVEDDEVAAAAIEYLKAAKAGRAtflpldkIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1819 LQAQIEESNKEKQELQEKLQALQSQveFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEE 1898
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYV--LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1899 RDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED 1978
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
570 580 590
....*....|....*....|....*....|
gi 1907082213 1979 EMESDENEDL-INSLQDMVTKYQKKKNKLE 2007
Cdd:COG1196 751 EALEELPEPPdLEELERELERLEREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1312-1994 |
6.13e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.44 E-value: 6.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1312 KVEKERNELRLSS--DRLEtRISELTSELtdERNTGESASQlldAETAERLRtekemkELQTQYDALKKQMEVMEMEVME 1389
Cdd:COG1196 171 KERKEEAERKLEAteENLE-RLEDILGEL--ERQLEPLERQ---AEKAERYR------ELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1390 ARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQ-QELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQL 1468
Cdd:COG1196 239 AELEELEAELEELEAELE----ELEAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1469 KKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLD 1548
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1549 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSK 1628
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1629 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLrkdlkrtkALLADA 1708
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL--------EAALAA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1709 QIMLDHLKNNAPSKREIAQLK-NQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR 1787
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1788 LEEDQEDM-NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvSRQEAKIRE 1866
Cdd:COG1196 627 LVAARLEAaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA------------ERLAEEELE 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1867 LETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEM 1946
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1947 DLESLEAANqslqadlklafkrigdlQAAIE--DEME------SDENEDLINSLQD 1994
Cdd:COG1196 775 EIEALGPVN-----------------LLAIEeyEELEerydflSEQREDLEEARET 813
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1287-2018 |
7.30e-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: 7.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1287 IQVQLSE--EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldaetAERLRTEK 1364
Cdd:pfam01576 227 LQAQIAElrAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESER--------------AARNKAEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1365 EMKELQTQYDALKkqmevmemevmearliraAEINGEVDDDDAGGEWRLKYERAVREVdftKKRLQQELEDKMEVEQQSR 1444
Cdd:pfam01576 293 QRRDLGEELEALK------------------TELEDTLDTTAAQQELRSKREQEVTEL---KKALEEETRSHEAQLQEMR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1445 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKL 1524
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1525 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGS 1604
Cdd:pfam01576 432 AEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1605 IQMLEQAKLRLEMEMERMRQtHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLS-DQV 1683
Cdd:pfam01576 512 KRNVERQLSTLQAQLSDMKK-KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvDLD 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1684 NQRDFES--EKRLRK---DLKRTKALLADAQIMLDHLKNNAPSKREIA-QLKNQLEESEFTCAAAVKARKAMEVEMEDLH 1757
Cdd:pfam01576 591 HQRQLVSnlEKKQKKfdqMLAEEKAISARYAEERDRAEAEAREKETRAlSLARALEEALEAKEELERTNKQLRAEMEDLV 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1758 LQIDDIAK-------AKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDmaqmndLQAQiEESNKEK 1830
Cdd:pfam01576 671 SSKDDVGKnvhelerSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERD------LQAR-DEQGEEK 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1831 QelqeklQALQSQVefleqsmvdkslvsrqeakiRELETRLEFEKTQvkRLENLASRLKETMEKLTEERDQRAAAENREK 1910
Cdd:pfam01576 744 R------RQLVKQV--------------------RELEAELEDERKQ--RAQAVAAKKKLELDLKELEAQIDAANKGREE 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1911 --EQNKRLQRQLRDTKEEMSE--LARKEAEASRKkhELEMDLESLEAANQSLQADLKLAFKrigdlqAAIEDEMESDENE 1986
Cdd:pfam01576 796 avKQLKKLQAQMKDLQRELEEarASRDEILAQSK--ESEKKLKNLEAELLQLQEDLAASER------ARRQAQQERDELA 867
|
730 740 750
....*....|....*....|....*....|...
gi 1907082213 1987 DLINSLQDMVTKYQKKKNKLEGD-SDVDSELED 2018
Cdd:pfam01576 868 DEIASGASGKSALQDEKRRLEARiAQLEEELEE 900
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
520-1175 |
2.88e-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: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 520 PHIYAVAQTAYRAMLM-SRQDQSIVLLGSSGSGKTTSFQHLVQYLA---------TIAGTSGTKVFSVEKWQalSTLLEA 589
Cdd:cd14875 56 PHIWQVAHKAFNAIFVqGLGNQSVVISGESGSGKTENAKMLIAYLGqlsymhssnTSQRSIADKIDENLKWS--NPVMES 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 590 FGNSPTIMNGSATRFSQILSLDFDQA-GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDAT-------LRTEL 661
Cdd:cd14875 134 FGNARTVRNDNSSRFGKYIKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEekkelggLKTAQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 662 HLNHLAENNVF---GI--VPLSKPEEkqkaaqqFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKagrKQFARH 736
Cdd:cd14875 214 DYKCLNGGNTFvrrGVdgKTLDDAHE-------FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES---DQNDKA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 737 EWAQKAAYLLGCSLEELSSAifkhQLKGGTLQRS-----TSFRQGPEESGLgegtklsalecLEGMASGLYSELFTLLIS 811
Cdd:cd14875 284 QIADETPFLTACRLLQLDPA----KLRECFLVKSktslvTILANKTEAEGF-----------RNAFCKAIYVGLFDRLVE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 812 LVNRALKSSQH-SLCSMM-IVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAF 886
Cdd:cd14875 349 FVNASITPQGDcSGCKYIgLLDIFGFEN------FTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQipkIEF 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 887 DDlepvADDSVAAVDQASHLVRSLahADEargllwlleeEALVPGATEDALLDRLFSYYGpqegdkkGQSPLL---RSSK 963
Cdd:cd14875 423 PD----NSECVNMFDQKRTGIFSM--LDE----------ECNFKGGTTERFTTNLWDQWA-------NKSPYFvlpKSTI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 964 PRHFllGHSHGTNWVEYNVAGWLNytKQNPA-TQNAPRLLQDSQKKIISNLFLGRAGSAtvlsgsiagleggsqlalRRa 1042
Cdd:cd14875 480 PNQF--GVNHYAAFVNYNTDEWLE--KNTDAlKEDMYECVSNSTDEFIRTLLSTEKGLA------------------RR- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1043 tsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpcea 1122
Cdd:cd14875 537 ---------------KQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPS-------------------------- 575
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 1123 gllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKK 1175
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 ... |
469-883 |
4.56e-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: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 469 VLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRRE-----DMAPHIYAVAQTAYRAMLMSRQDQSI 542
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfKQIRNLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 543 VLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVekwqALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 620
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSL----ILGSnpLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 621 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF-GIVPLSKPE-EKQKaaqQFSKLQAAMK 698
Cdd:cd14886 159 GKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLnASKCYDAPGiDDQK---EFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 699 VLaISPEEQKTCWLILASIYHLG--------AAGATKAGRkqFARHEWAQKAAYLLGCSLEELSSAIfkhqlkggtLQRS 770
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGniefseegDMGVINAAK--ISNDEDFGKMCELLGIESSKAAQAI---------ITKV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 771 TSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFE 850
Cdd:cd14886 304 VVINNETIISPV---TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN------TYE 374
|
410 420 430
....*....|....*....|....*....|...
gi 1907082213 851 ELCHNYAQDRLQRLFHERTFLQELERYKEDNIE 883
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 ... |
468-902 |
2.07e-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: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF-------KGCRREDMAPHIYAVAQTAYRAMLMSRQD 539
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPyKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 540 QSIVLLGSSGSGKTTSFQHLVQYLATIAGTSgTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQ----- 614
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTDS-QMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 615 ----AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLL-ACGDATLRT-----ELHLNHLAENNVFGIVPLSK----- 679
Cdd:cd14884 161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLrGLSDEDLARrnlvrNCGVYGLLNPDESHQKRSVKgtlrl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 680 --------PEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGaagatkagrkqfarhEWAQKAAyllgCSLE 751
Cdd:cd14884 241 gsdsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLG---------------NRAYKAA----AECL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 752 ELSSAIFKHQLKGGTLQ-RSTSFRQgpeesglgEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSM--- 827
Cdd:cd14884 302 QIEEEDLENVIKYKNIRvSHEVIRT--------ERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDned 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 828 ---------MIVDTPGFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIeLAFDDLEPVADDSVA 898
Cdd:cd14884 374 iysineaiiSILDIYGFE------ELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCSDVAPSYSDTLI 446
|
....
gi 1907082213 899 AVDQ 902
Cdd:cd14884 447 FIAK 450
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
469-1089 |
1.92e-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: 120.86 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 469 VLHTLRQRYGASLLHTYAGPSLLVLST---------------RGAPAVysekvmhmfkgcrrEDMAPHIYAVAQTAYRAM 533
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirkyRDAPDL--------------TKLPPHVFYTARRALENL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 534 LMSRQDQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTKVFSVEKW-QALSTLLEAFGNSPTIMNGSATRFSQILSLDF 612
Cdd:cd14876 69 HGVNKSQTIIVSGESGAGKTEATKQIMRYFA--SAKSGNMDLRIQTAiMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 613 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENN--------VFGIVPLskpeekq 684
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKflnpkcldVPGIDDV------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 685 kaaQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLG---AAGATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQ 761
Cdd:cd14876 220 ---ADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGnvkITGKTEQGVDDAAAISNESLEVFKEACSLLFLDPEALKRE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 762 L------KGGtlQRSTSFRQGPEesglGEGTKLSaleclegMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGF 835
Cdd:cd14876 297 LtvkvtkAGG--QEIEGRWTKDD----AEMLKLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 836 ---QNpewggsargASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDLEPVAD------DSVAAV--D 901
Cdd:cd14876 364 evfKN---------NSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIptaELEYTSNAEVIDvlcgkgKSVLSIleD 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 902 QAshlvrsLAhadeargllwlleeealvPGATEDALLDRLFSyygpQEGDKKGQSPLLRSSKpRHFLLGHSHGTnwVEYN 981
Cdd:cd14876 435 QC------LA------------------PGGSDEKFVSACVS----KLKSNGKFKPAKVDSN-INFIVVHTIGD--IQYN 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 982 VAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGragsATVLSGSIA-GLEGGSQLalrratsMRktfttgmaavkkks 1060
Cdd:cd14876 484 AEGFLFKNK-DVLRAELVEVVQASTNPVVKALFEG----VVVEKGKIAkGSLIGSQF-------LK-------------- 537
|
650 660
....*....|....*....|....*....
gi 1907082213 1061 lciqiklQVDALIDTIKRSKMHFVHCFLP 1089
Cdd:cd14876 538 -------QLESLMGLINSTEPHFIRCIKP 559
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1293-1955 |
4.92e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 121.32 E-value: 4.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1293 EEQIRNKDEEIQQLRSKLEKVEKERNELR-----LSSD--RLETRISELTSELTDERNTGESASQLLDAETAERLRTEKE 1365
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQkelyaLANEisRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1366 MKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQeLEDKMEVEQQSRR 1445
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-LEARLERLEDRRE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1446 QLERRLGDLQADSDESQRALQQLKkkCQRLTAELQDTKLHLEGQQVR----NHELEKKQRRFDSELSQAHEETQR----E 1517
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEAleelREELEEAEQALDAAERELAQLQARldslE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1518 KLQR--EKLQREKDMLLAEAF-------SLKQQME-----EKDLDIA--GFTQKVV--SLEAELQDISSQESKDE---AS 1576
Cdd:TIGR02168 496 RLQEnlEGFSEGVKALLKNQSglsgilgVLSELISvdegyEAAIEAAlgGRLQAVVveNLNAAKKAIAFLKQNELgrvTF 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1577 LAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERM--------------RQTHSKEMESR--------- 1633
Cdd:TIGR02168 576 LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddldnalELAKKLRPGYRivtldgdlv 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1634 ---------DEEVEEARQSCQKKLKQMEVQ---LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL---RKDL 1698
Cdd:TIGR02168 656 rpggvitggSAKTNSSILERRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1699 KRTKALLADAQIMLDHL-KNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1777
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLsKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1778 QREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSL 1856
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALlRSE 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1857 VSRQEAKIRELETRlefektqVKRLENLasrLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARK--- 1933
Cdd:TIGR02168 896 LEELSEELRELESK-------RSELRRE---LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKied 965
|
730 740
....*....|....*....|...
gi 1907082213 1934 -EAEASRKKHELEMDLESLEAAN 1955
Cdd:TIGR02168 966 dEEEARRRLKRLENKIKELGPVN 988
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1291-1995 |
6.02e-27 |
|
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: 120.94 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1291 LSEEqiRNKDEEIQQLRSKLEKVE-----KERNELRLSSDRLETRISELTSELT------DERN-TGESASQLLDAETAE 1358
Cdd:TIGR02169 203 LRRE--REKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEklteeiSELEkRLEEIEQLLEELNKK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1359 -RLRTEKEMKELQTQYDALKKQMEVMEMEVMEA--RLIRAAE--INGEVDDDDAGGEWRlKYERAVREVDFTKKRLQQEL 1433
Cdd:TIGR02169 281 iKDLGEEEQLRVKEKIGELEAEIASLERSIAEKerELEDAEErlAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1434 EDKmeveQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhLEGQQVRnheLEKKQRRFDSELSQAHEE 1513
Cdd:TIGR02169 360 AEL----KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE----LKRELDR---LQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1514 TQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKV-- 1591
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVrg 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1592 -KDQEEELD------------------------EQAGS-----------------IQMLEQAKL-RLE-MEMERMRQTHS 1627
Cdd:TIGR02169 509 gRAVEEVLKasiqgvhgtvaqlgsvgeryataiEVAAGnrlnnvvveddavakeaIELLKRRKAgRATfLPLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1628 -KEMESRD------------------------------EEVEEAR----------------------------------- 1641
Cdd:TIGR02169 589 dLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvvEDIEAARrlmgkyrmvtlegelfeksgamtggsraprggilf 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1642 --------QSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEkRLRKDLKRTKALLADAQIMLD 1713
Cdd:TIGR02169 669 srsepaelQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLS 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1714 HLKNN-APSKREIAQLKNQLEESEftcAAAVKARKAME-VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEED 1791
Cdd:TIGR02169 748 SLEQEiENVKSELKELEARIEELE---EDLHKLEEALNdLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1792 QEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETR 1870
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlKKERDELEAQLRELERK 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1871 LEFEKTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRDTKEEMSELARKEAEASRKKhELEMDLES 1950
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEAL--------------EEELSEIEDPKGEDEEIPEEELSLEDVQAELQ-RVEEEIRA 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1907082213 1951 LEAANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINSLQDM 1995
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKlEEERKAILERIEEYEKK 1015
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1430-2006 |
2.46e-26 |
|
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: 117.81 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1430 QQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQR--RFDSEL 1507
Cdd:TIGR04523 35 EKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN---------DKLKKNKDKinKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1508 SQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKdeaslakVKKQLRDL 1587
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELN-------KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1588 EAKVKDQEEELDEQAGSIQMLEQAKLRLEMEM---ERMRQTHsKEMESRDEEVEEARQSCQKKLKQmevqLEEEYEDKQK 1664
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKN-KSLESQISELKKQNNQLKDNIEK----KQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1665 ALREKrelESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESeftCAAAVK 1744
Cdd:TIGR04523 247 EISNT---QTQLNQLKDE-QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS------EISDLNNQKEQD---WNKELK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1745 AR-KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKN-------EIQNRLEEDQEDMnELMKKHKAAVAQASRDM-AQ 1815
Cdd:TIGR04523 314 SElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTnsesensEKQRELEEKQNEI-EKLKKENQSYKQEIKNLeSQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1816 MNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQ--------------EAKIRELETRLEFEKTQVKR 1880
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlKETIIKNnseikdltnqdsvkELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1881 LENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQA 1960
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1961 DLKLAF--KRIGDLQAAIEdEMEsDENEDLINS---LQDMVTKYQKKKNKL 2006
Cdd:TIGR04523 553 ELKKENleKEIDEKNKEIE-ELK-QTQKSLKKKqeeKQELIDQKEKEKKDL 601
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
467-1170 |
2.52e-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: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVmhmFKGCrredmapHIYAVAQTAYRAML-MSRQDQSIVLL 545
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLV---IKKC-------HISGVAENALDRIKsMSSNAESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 546 GSSGSGKTTSFQHLVQYLATIAGTSGTKVFSvekwQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHS----SAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLaeNNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 705
Cdd:cd14874 147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 706 EQKTCWLILASIYHLGAAgATKAGRKQFARHE-----------WaqkAAYLLGCSLEELSSAIFKHQLKGGTLQRStsfr 774
Cdd:cd14874 225 HCISIYKIISTILHIGNI-YFRTKRNPNVEQDvveignmsevkW---VAFLLEVDFDQLVNFLLPKSEDGTTIDLN---- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 775 qgpeesglgegtklSALECLEGMASGLYSELFTLLISLVNRALKSSQHSlCSMMIVDTPGFQNPEWGGsargasFEELCH 854
Cdd:cd14874 297 --------------AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHT-GVISILDHYGFEKYNNNG------VEEFLI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 855 NYAQDRLQRLFHERTFLQELERYKEDNIELafddlepvaDDSVAAVDQASHLVRSLAHADEarGLLWLLEEEALVPGATE 934
Cdd:cd14874 356 NSVNERIENLFVKHSFHDQLVDYAKDGISV---------DYKVPNSIENGKTVELLFKKPY--GLLPLLTDECKFPKGSH 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 935 DALLDRL------FSYYGPQegdkkgqspllRSSKPRHFLLGHSHGTNWveYNVAGWLNYTKQNpATQNAPRLLQDSQKK 1008
Cdd:cd14874 425 ESYLEHCnlnhtdRSSYGKA-----------RNKERLEFGVRHCIGTTW--YNVTDFFSRNKRI-ISLSAVQLLRSSKNP 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1009 IISNLFLGRAGSATVLSGSIAgleggsQLALRRATSmrktfttgmaavkkkslciqiklqvdaLIDTIKRSKMHFVHCFL 1088
Cdd:cd14874 491 IIGLLFESYSSNTSDMIVSQA------QFILRGAQE---------------------------IADKINGSHAHFVRCIK 537
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1089 PVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1168
Cdd:cd14874 538 SNNERQPK-----------------------------KFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
..
gi 1907082213 1169 AP 1170
Cdd:cd14874 589 LP 590
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1291-1986 |
6.09e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 117.93 E-value: 6.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1291 LSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRL--ETRISELTSELTDERNTgESASQLLDAETAERLRTEKEMKE 1368
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaeDARKAEEARKAEDAKRV-EIARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1369 LQTQYDALKKQMEVMEMEVMEARLIRAAEingevddddaggewRLKYERAVREVdftkkrlqQELEDKMEVEQqSRRQLE 1448
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAAR--------------KAEEERKAEEA--------RKAEDAKKAEA-VKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1449 RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK--QRRFDSELSQAHEETQREKLQREKLQR 1526
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1527 EKdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-AKVKDQEEELDEQAGSI 1605
Cdd:PTZ00121 1315 KK----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1606 QMLEQAKLRLEMEMERMRQTHSKEMESRdeEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQ 1685
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1686 RDFESEKRLRKDLKR----TKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCA-AAVKARKAMEVEMEDLHLQI 1760
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKkadeAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkKAEEAKKADEAKKAEEKKKA 1548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1761 DDIAKA---KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL 1837
Cdd:PTZ00121 1549 DELKKAeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1838 QALQSQVEFLEQSMVDKslvSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQ 1917
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1918 R-------------QLRDTKEE----MSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEM 1980
Cdd:PTZ00121 1706 ElkkkeaeekkkaeELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
....*.
gi 1907082213 1981 ESDENE 1986
Cdd:PTZ00121 1786 DEEDEK 1791
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1288-1930 |
7.68e-25 |
|
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: 113.19 E-value: 7.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1288 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMK 1367
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1368 ELQTQYDALKKQMEVMEMEVMEARLIRAaEINgevddddaggewrlKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQL 1447
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKSLES-QIS--------------ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1448 E----------RRLGDLQADSDESQRALQQLKKKCQRLTAELQDtkLHLEGQQVRNHEL-------EKKQRRFDSELSQA 1510
Cdd:TIGR04523 256 NqlkdeqnkikKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELkselknqEKKLEEIQNQISQN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1511 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAK 1590
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEK--------------QNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1591 VKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHS------KEMESRD-------EEVEEARQSCQKKLKQMEVQ--- 1654
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseiKDLTNQDsvkeliiKNLDNTRESLETQLKVLSRSink 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1655 LEEEYEDKQKALREKrelESKLSTLSDQVNQrdfeSEKRLrKDLKRTKALLADAQIMLDHLKNNapSKREIAQLKNQLEE 1734
Cdd:TIGR04523 480 IKQNLEQKQKELKSK---EKELKKLNEEKKE----LEEKV-KDLTKKISSLKEKIEKLESEKKE--KESKISDLEDELNK 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1735 SEFTcaaavkarkamevemedlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMA 1814
Cdd:TIGR04523 550 DDFE-------------------LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1815 QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA--KIRELETRL-EFEKTQVKRLENLA 1885
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVkqiketIKEIRNKWPEIikKIKESKTKIdDIIELMKDWLKELS 690
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1907082213 1886 SRLKETMEKLTEERDqraaaENREKEQNKRLQRQLRDTKEEMSEL 1930
Cdd:TIGR04523 691 LHYKKYITRMIRIKD-----LPKLEEKYKEIEKELKKLDEFSKEL 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1288-1933 |
1.20e-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: 113.23 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1288 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLD----AETAERL-RT 1362
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelKELQAELeEL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1363 EKEMKELQTQYDALKKQMEVMEMEVMEARLIR------AAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRL---QQEL 1433
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALdaaereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgiLGVL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1434 EDKMEVEQQSRRQLERRLG-DLQA----DSDESQRALQQLKK--------------KCQRLTAELQDTKLHLEGQQVRNH 1494
Cdd:TIGR02168 526 SELISVDEGYEAAIEAALGgRLQAvvveNLNAAKKAIAFLKQnelgrvtflpldsiKGTEIQGNDREILKNIEGFLGVAK 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1495 ELEKKQRRFDSELS------------QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAE 1562
Cdd:TIGR02168 606 DLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEK 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1563 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERmrqtHSKEMESRDEEVEEArq 1642
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTEL-- 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1643 scQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSK 1722
Cdd:TIGR02168 760 --EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1723 -REIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1801
Cdd:TIGR02168 837 eRRLEDLEEQIEELS-------EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1802 HKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQsQVEFleqsMVDKSLVSRQEAKIRELETRLEFEKTQVKRL 1881
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY-SLTL----EEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1882 E--NLASrlketMEKLTEERdQRAAAENREKEQNKRLQRQLRDTKEEMSELARK 1933
Cdd:TIGR02168 985 GpvNLAA-----IEEYEELK-ERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1213-2002 |
7.94e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 111.00 E-value: 7.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1213 RAGTLARLEEQRDEQTSRHLTLF---QAACRGYLARQHFKKRKIQDlAIRCVQ----KNIKKNKGVKDWPWWKLFTTVRP 1285
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIArkaEDARKAEEARKAEDAKKAEA-ARKAEEvrkaEELRKAEDARKAEAARKAEEERK 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1286 LIQVQLSEEQIR----NKDEEIQQLRSKLEKVEKERNE---LRLSSDRLETRISELTSELTDERNTGESASQLLDAETAE 1358
Cdd:PTZ00121 1214 AEEARKAEDAKKaeavKKAEEAKKDAEEAKKAEEERNNeeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1359 RLRTEKEMKELqtqyDALKKQMEVMEMEVMEARliRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKME 1438
Cdd:PTZ00121 1294 EAKKAEEKKKA----DEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1439 VEQQSRRQLERRLGDLQADSDESQRAlQQLKKKCQrltaelQDTKlhlEGQQVRNHELEKKQRrfdSELSQAHEETQREK 1518
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAE------EDKK---KADELKKAAAAKKKA---DEAKKKAEEKKKAD 1434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1519 LQREKLQREKdmllaEAFSLKQQMEEKDldiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEEL 1598
Cdd:PTZ00121 1435 EAKKKAEEAK-----KADEAKKKAEEAK-------------KAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEA 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1599 DEQAGSIQMLEQAKLRLEmEMERMRQTHSKEMESRDEE---VEEARQSCQKKlKQMEVQLEEEY---EDKQKALREKREL 1672
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEakkADEAKKAEEKK-KADELKKAEELkkaEEKKKAEEAKKAE 1573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1673 ESKLSTL-----SDQVNQRDFESEKRLRKDLKRTKALLA----DAQIMLDHLKNNAPSKREIAQLKNQLEES-------- 1735
Cdd:PTZ00121 1574 EDKNMALrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaeelk 1653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1736 ----EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTalEEQLSRLQREK---NEIQNRLEEDQEDMNELMKKHKAAVAQ 1808
Cdd:PTZ00121 1654 kaeeENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--AEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1809 ASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLAS-- 1886
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANii 1811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1887 --------RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSL 1958
Cdd:PTZ00121 1812 eggkegnlVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1907082213 1959 QADLKlafkrigDLQAAIEDEMESDENEDLINSLQDmVTKYQKK 2002
Cdd:PTZ00121 1892 KIDKD-------DIEREIPNNNMAGKNNDIIDDKLD-KDEYIKR 1927
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1409-1977 |
8.11e-24 |
|
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: 110.65 E-value: 8.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1409 GEWRLKYERAVREVDFTKKRLQQELE-----DKMEVEQQSRRQ-LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDT 1482
Cdd:pfam01576 29 KELEKKHQQLCEEKNALQEQLQAETElcaeaEEMRARLAARKQeLEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1483 KLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMllaeafslkqqmeekdldiagftqkvvsLEAE 1562
Cdd:pfam01576 109 EEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL----------------------------LEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1563 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSkEMESRDEEVEEARQ 1642
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA-ELQAQIAELRAQLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1643 SCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLsdqvnQRDFESEKRLRKDLKRTK-----ALLADAQIMLDHLKN 1717
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISEL-----QEDLESERAARNKAEKQRrdlgeELEALKTELEDTLDT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1718 NAP-----SKR--EIAQLKNQLEESEFTCAAAVKA-RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLE 1789
Cdd:pfam01576 315 TAAqqelrSKReqEVTELKKALEEETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1790 EDQEDMNELMKKHKAAvaqasrdMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLeqsmvdKSLVSRQEAKIRELEt 1869
Cdd:pfam01576 395 TLQQAKQDSEHKRKKL-------EGQLQELQARLSESERQRAELAEKLSKLQSELESV------SSLLNEAEGKNIKLS- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1870 rlefektqvKRLENLASRLKETMEKLTEERDQRAAAENR----EKEQNKrLQRQLRDTKE-------EMSELARKEAEAS 1938
Cdd:pfam01576 461 ---------KDVSSLESQLQDTQELLQEETRQKLNLSTRlrqlEDERNS-LQEQLEEEEEakrnverQLSTLQAQLSDMK 530
|
570 580 590
....*....|....*....|....*....|....*....
gi 1907082213 1939 RKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1977
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1217-1902 |
3.00e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1217 LARLEEQRdEQTSRHLTLfQAACRGYLARQHFKKRKIQDLAIRCVQKNIKKNKgvkdwpwwklfttvrplIQVQLSEEQI 1296
Cdd:COG1196 202 LEPLERQA-EKAERYREL-KEELKELEAELLLLKLRELEAELEELEAELEELE-----------------AELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1297 RNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDAL 1376
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1377 KKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREvdftkkrlQQELEDKMEVEQQSRRQLERRLGDLQA 1456
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE--------LLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1457 DSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAF 1536
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1537 SLKQQMEEKDLDIAGftqkvvSLEAELQDISSQESKDEASLAKVKKQLRD-----LEAKVKDQEEELDEQAGS-IQMLEQ 1610
Cdd:COG1196 495 LLLEAEADYEGFLEG------VKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaaLAAALQNIVVEDDEVAAAaIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1611 AKL-RLE-MEMERMRQTHSKEMESRDEEVEEARqscqkklkqmevqLEEEYEDKQKALREKRELESKLSTLSDQvnqrdf 1688
Cdd:COG1196 569 AKAgRATfLPLDKIRARAALAAALARGAIGAAV-------------DLVASDLREADARYYVLGDTLLGRTLVA------ 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1689 eseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaaVKARKAMEVEMEDLHLQIDDIAKAKT 1768
Cdd:COG1196 630 ---ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL------LEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1769 ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLE 1848
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1849 QsmVDksLVSRQEAKirELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQR 1902
Cdd:COG1196 781 P--VN--LLAIEEYE--ELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
467-882 |
3.49e-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: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 467 SSVLHTLRQRYGASLLHTYAGPSLLVLStrgaPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISIN----PYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLatIAGTSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 626
Cdd:cd14937 77 ESGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDS-NFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISpEE 706
Cdd:cd14937 154 LLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIR--SENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMH-DM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 707 QKTCWLILASIYHLGAA---GATKAGRKQFAR-----HEWAQKAAYLLGCSLEELSSAIfkhqlkggTLQRSTSFRQGPE 778
Cdd:cd14937 231 KDDLFLTLSGLLLLGNVeyqEIEKGGKTNCSEldknnLELVNEISNLLGINYENLKDCL--------VFTEKTIANQKIE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 779 esglgegTKLSALECL---EGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQnpewggSARGASFEELCHN 855
Cdd:cd14937 303 -------IPLSVEESVsicKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFE------IFSKNSLEQLLIN 369
|
410 420
....*....|....*....|....*..
gi 1907082213 856 YAQDRLQRLFHERTFLQELERYKEDNI 882
Cdd:cd14937 370 IANEEIHSIYLYIVYEKETELYKAEDI 396
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1393-2007 |
4.82e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 107.84 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1393 IRAAEINGEVDDDDA---------GGEwrlKYERA-------VREVDFTKKRLQQELEDKMEVEQQSRRQlERRLGDLQA 1456
Cdd:PRK03918 132 IRQGEIDAILESDESrekvvrqilGLD---DYENAyknlgevIKEIKRRIERLEKFIKRTENIEELIKEK-EKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1457 DSDESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRRFDSELSQAhEETQREKLQREKLQREKDMLLA 1533
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIREL-EERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1534 EAfslkQQMEEKDLDIAGFTQKVVSleaELQDISSQESKDEASLAKVKKQLRDLE---AKVKDQEEELDEQAGSIQMLEQ 1610
Cdd:PRK03918 287 EL----KEKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1611 AKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQrdFES 1690
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKL----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE--LKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1691 EKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQidDIAKAKTAL 1770
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR---KELRELEKVLKKESELIKLK--ELAEQLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1771 EEQLSRLQREKNEiqnRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS 1850
Cdd:PRK03918 509 EEKLKKYNLEELE---KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1851 MVDKSlvsrqEAKIRELET---RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEM 1927
Cdd:PRK03918 586 SVEEL-----EERLKELEPfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1928 SElarkeaEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED----EMESDENEDLINSLQDMVTKYQKKK 2003
Cdd:PRK03918 661 YE------ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEErekaKKELEKLEKALERVEELREKVKKYK 734
|
....
gi 1907082213 2004 NKLE 2007
Cdd:PRK03918 735 ALLK 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1414-1936 |
8.60e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 107.07 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1414 KYERAVREVDFTKKRLQqELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN 1493
Cdd:PRK03918 225 KLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1494 HELEKKQR--RFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFtQKVVSLEAELQDISSQES 1571
Cdd:PRK03918 304 EYLDELREieKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1572 kdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSK----EMESRDEEVEEARQSCQKK 1647
Cdd:PRK03918 383 --GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1648 LKQMEVQLEEEYEDKQKALREKRELESKLstlsdqvnqrdfESEKRLRKDLKrtkalladaqiMLDHLKN--NAPSKREI 1725
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVL------------KKESELIKLKE-----------LAEQLKEleEKLKKYNL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1726 AQLKNQLEESEFTCAAAVKARKAMEVEMEDLHlQIDDIAKAKTALEEQLSRLQREKNEIQNRL--------EEDQEDMNE 1797
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1798 LMKKH------KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLvSRQEAKIRELETRL 1871
Cdd:PRK03918 597 LEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY-EELREEYLELSREL 675
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1872 EFEKTQVKRLENLASRLKETMEKLTEERDQRAAAE------NREKEQNKRLQRQLRDTKEEMSELARKEAE 1936
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKkeleklEKALERVEELREKVKKYKALLKERALSKVG 746
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1294-1952 |
1.18e-22 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 106.26 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1294 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESasqlLDAET---AERLRTEKEMK-EL 1369
Cdd:TIGR04523 47 NELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK----LNSDLskiNSEIKNDKEQKnKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1370 QTQYDALKKQMEVMEMEVmearliraAEINGEV-DDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ------Q 1442
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNI--------DKFLTEIkKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKnidkikN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1443 SRRQLERRLGDLQAdsdesqralqqLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFdSELSQAHEETQrEKLQRE 1522
Cdd:TIGR04523 195 KLLKLELLLSNLKK-----------KIQKNKSLESQISELK---KQNNQLKDNIEKKQQEI-NEKTTEISNTQ-TQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1523 KLQREKDmllaeafslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKVKDQEEE 1597
Cdd:TIGR04523 259 KDEQNKI---------KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1598 LDEQAGSIQMLEQAKLRLEMEmermRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLS 1677
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1678 TLSDQVNQRD-----FESEKR-LRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESEFTcaaavkarkamev 1751
Cdd:TIGR04523 402 NQEKLNQQKDeqikkLQQEKElLEKEIERLKETIIKNNSEIKDLTN------QDSVKELIIKNLDNT------------- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1752 emedlhlqiddiakaKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASrdmaqmnDLQAQIEESNKEKQ 1831
Cdd:TIGR04523 463 ---------------RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK-------ELEEKVKDLTKKIS 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1832 ELQEKLQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFE--KTQVKRLENLASRLKETMEKLTEERDQ-RAAAENR 1908
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDL------EDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEkQELIDQK 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082213 1909 EKEQNK-------------RLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLE 1952
Cdd:TIGR04523 595 EKEKKDlikeieekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1560-2018 |
5.70e-22 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 104.49 E-value: 5.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1560 EAELQDISSQESKDEASLAKVKKQLRDLEAKVkdqeEELDEQAGSIQMLEQAKLRLEMEMERMRQTHS----------KE 1629
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKH----QQLCEEKNALQEQLQAETELCAEAEEMRARLAarkqeleeilHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1630 MESRDEEVEEARQSCQ---KKLKQ----MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTK 1702
Cdd:pfam01576 80 LESRLEEEEERSQQLQnekKKMQQhiqdLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLE-DQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1703 ALLADAQI----------MLDHLKNNAPSKreIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE 1772
Cdd:pfam01576 159 ERISEFTSnlaeeeekakSLSKLKNKHEAM--ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1773 QLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVE-FLEQSM 1851
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1852 VDKSLVSRQEAKIRELETRLEFE-KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSEL 1930
Cdd:pfam01576 317 AQQELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1931 ARKEAEASRKKHELEMDLESLEA-ANQSLQADLKLAfKRIGDLQAAIEdemesdenedlinSLQDMVTKYQKKKNKLEGD 2009
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQArLSESERQRAELA-EKLSKLQSELE-------------SVSSLLNEAEGKNIKLSKD 462
|
490
....*....|
gi 1907082213 2010 -SDVDSELED 2018
Cdd:pfam01576 463 vSSLESQLQD 472
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1292-1998 |
1.63e-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: 102.41 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1292 SEEQIRNKDEEIQQLRSKL----EKVEKERNELRLSSDRLETR---ISELTSELTDERNTGESASQLLDAETAERLRTEK 1364
Cdd:TIGR04523 73 SNNKIKILEQQIKDLNDKLkknkDKINKLNSDLSKINSEIKNDkeqKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1365 EMKELQTQYDALKKQmevmemevmearliraaeingevddddaggewrlkyeraVREVDFTKKRLQQELEDKMEVEQQSR 1444
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQ---------------------------------------KEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1445 RQLERrlgdlqadsdeSQRALQQLKKKCQRLTaELQDTKLHLEGQQ-VRNHELEKKQRRFdSELSQAHEETQrEKLQREK 1523
Cdd:TIGR04523 194 NKLLK-----------LELLLSNLKKKIQKNK-SLESQISELKKQNnQLKDNIEKKQQEI-NEKTTEISNTQ-TQLNQLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1524 LQREKDmllaeafslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKVKDQEEEL 1598
Cdd:TIGR04523 260 DEQNKI---------KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQNQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1599 DEQAGSIQMLEQAKLRLEMEmermRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLST 1678
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1679 LSDQVNQRD-----FESEKR-LRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESEFTcaaavkarkameve 1752
Cdd:TIGR04523 403 QEKLNQQKDeqikkLQQEKElLEKEIERLKETIIKNNSEIKDLTN------QDSVKELIIKNLDNT-------------- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1753 medlhlqiddiakaKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKKHKaavaqasrdmaqmndlqaQIEESNKEKQE 1832
Cdd:TIGR04523 463 --------------RESLETQLKVLSRSINKIKQNLEQKQK---ELKSKEK------------------ELKKLNEEKKE 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1833 LQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKTQVKRlenlaSRLKETMEKLTEERDQRAAAENREKE 1911
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKlESEKKEKESKISDLEDELNKDDFELKK-----ENLEKEIDEKNKEIEELKQTQKSLKK 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1912 QNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQ---SLQADLKLAFKRIGDLQAAIEDEMESDENE-- 1986
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEklsSIIKNIKSKKNKLKQEVKQIKETIKEIRNKwp 662
|
730
....*....|..
gi 1907082213 1987 DLINSLQDMVTK 1998
Cdd:TIGR04523 663 EIIKKIKESKTK 674
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1286-1926 |
1.98e-21 |
|
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: 102.74 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1286 LIQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLE-----TRISELTSELTDERNTGESASQLLDAETAERl 1360
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1361 rtekeMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgeWRLKYERAVREVDFTKKrLQQELEDKMEVE 1440
Cdd:TIGR00618 324 -----AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS--IREISCQQHTLTQHIHT-LQQQKTTLTQKL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1441 QQSRRQLE--RRLGDLQADSDESQRALQQlkkkcqrltaelqdTKLHLEGQQVRNHELEKKQRRFDSElsQAHEETQREK 1518
Cdd:TIGR00618 396 QSLCKELDilQREQATIDTRTSAFRDLQG--------------QLAHAKKQQELQQRYAELCAAAITC--TAQCEKLEKI 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1519 LQREKLQ--REKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISS---QESKDEASLAKVKKQLRDLEAKVKD 1593
Cdd:TIGR00618 460 HLQESAQslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnPARQDIDNPGPLTRRMQRGEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1594 QEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRD---EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR 1670
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNrskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1671 ELESKLSTLSDQVNQRDFESEKRLRK-DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAM 1749
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1750 EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKE 1829
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1830 KQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQvKRLENLASRLKETMEKLTEERDQRAAAENRE 1909
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-QEEEQFLSRLEEKSATLGEITHQLLKYEECS 858
|
650
....*....|....*..
gi 1907082213 1910 KEQNKRLQRQLRDTKEE 1926
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 ... |
1284-2040 |
2.28e-21 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 102.74 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1284 RPLIQVQLSEEQIRNKDEEIQqlRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTE 1363
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELK--LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1364 KEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQS 1443
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1444 RRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREK 1523
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1524 LQREKDMLLAEAFSL--KQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1601
Cdd:pfam02463 414 ARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1602 AG-SIQMLEQ------AKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELES 1674
Cdd:pfam02463 494 KLeERSQKESkarsglKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1675 KLStlSDQVNQRDFESEKRLRKDLK------RTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaavKARKA 1748
Cdd:pfam02463 574 PLG--ARKLRLLIPKLKLPLKSIAVleidpiLNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKE-------SAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1749 MEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNK 1828
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1829 EKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENR 1908
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1909 E--KEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENE 1986
Cdd:pfam02463 805 AleEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKL 884
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 1987 DLINS---------LQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDD 2040
Cdd:pfam02463 885 KDELEskeekekeeKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADE 947
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1293-2003 |
7.51e-21 |
|
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: 100.57 E-value: 7.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1293 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSE---LTDERNTGESASQLLD---AETAERL-RTEKE 1365
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdLIKENNATRHLCNLLKetcARSAEKTkKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1366 MKELQTQYDALKKQMEvmemevmeaRLIRAAEiNGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKmevEQQSRR 1445
Cdd:pfam05483 178 REETRQVYMDLNNNIE---------KMILAFE-ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK---EKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1446 QL------ERRLGDLQADSDESQRALQQLKKKcqrltAELQDTKLHlegqqvrnhELEKKQRRFDSELSQAHEETQREKL 1519
Cdd:pfam05483 245 LLiqitekENKMKDLTFLLEESRDKANQLEEK-----TKLQDENLK---------ELIEKKDHLTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1520 QREKLQREKDMLLAEAFSLKQ----QMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1595
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEekeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1596 EELDEQAG-----SIQMLEQAKLRLEME--MERMRQTH--SKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKAL 1666
Cdd:pfam05483 391 SELEEMTKfknnkEVELEELKKILAEDEklLDEKKQFEkiAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1667 REKRELESKLstlsdqvnqrdfESEKrlrkdLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaaVKAR 1746
Cdd:pfam05483 471 KEVEDLKTEL------------EKEK-----LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED--------IINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1747 KAMEvemEDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQ 1822
Cdd:pfam05483 526 KKQE---ERMLKQIENLEEKEMNLRDELESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1823 IEESNKEKQELQEKLQALQsqveflEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKE----TMEKLTEE 1898
Cdd:pfam05483 603 IENKNKNIEELHQENKALK------KKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEdkkiSEEKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1899 RDQRAA----AENREKEQNKRLQRQLRD---------------TKEEMSELA---RKEAEASRKKHELEMDLESLEAANQ 1956
Cdd:pfam05483 677 VEKAKAiadeAVKLQKEIDKRCQHKIAEmvalmekhkhqydkiIEERDSELGlykNKEQEQSSAKAALEIELSNIKAELL 756
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1907082213 1957 SLQADLklafkrigdlqaaiedEMESDENEDLINSLQDMVTKYQKKK 2003
Cdd:pfam05483 757 SLKKQL----------------EIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
468-909 |
1.19e-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: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPlRYLPFLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 547 SSGSGKTTSFQHLVQYLAT--IAGTSGTKVFSVEKwqalSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQ 624
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTtdLSRSKYLRDYILES----GIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 625 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL---NHLAENNVFGIVPLSKPEEKqkaaQQFSKLQAAMKVLA 701
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLgdiNSYHYLNQGGSISVESIDDN----RVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 702 ISPEEQKTCWLILASIYHLGAAG-ATKAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKhqlkggtlQRSTSFRQgpees 780
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTfFQKNGKTEVKDRTLIESLSHNITFDSTKLENILIS--------DRSMPVNE----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 781 glgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLcSMMIVDTPGFQNPEWGGsargasFEELCHNYAQDR 860
Cdd:cd14905 299 ---------AVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNG------YEQFSINFLEER 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 861 LQRLFHERTFLQELERYKEDNI----ELAFDDLE---PVADDSVAAVDQASHLVRS 909
Cdd:cd14905 363 LQQIYLQTVLKQEQREYQTERIpwmtPISFKDNEesvEMMEKIINLLDQESKNINS 418
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1293-2020 |
2.49e-20 |
|
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: 99.04 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1293 EEQIRNKDEEIQQLRSKL----EKVEKERNELRLSSDRLETRISELTSE---LTDERNTgESASQ----------LLDAE 1355
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLnesnELHEKQKFYLRQSVIDLQTKLQEMQMErdaMADIRRR-ESQSQedlrnqlqntVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1356 TAERLRtEKEMKELQTQYDALKKQMEVMEMEVMEARLIRaaeingeVDDDDAGGEWRLKYERA----VREVDFTKKRLQQ 1431
Cdd:pfam15921 156 AAKCLK-EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL-------VDFEEASGKKIYEHDSMstmhFRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1432 ELEDKMEVEQQSRRQLERRLGDLQADS-DESQRALQQLKKKCQRLTAE--LQDTKLHLEGQQVRNhELEKKQRRFDSELS 1508
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSESqNKIELLLQQHQDRIEQLISEheVEITGLTEKASSARS-QANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1509 QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE 1588
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1589 AKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVeearQSCQKKLKQMEVQLEEEYEDKQKALRE 1668
Cdd:pfam15921 384 ADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLR----RELDDRNMEV----QRLEALLKAMKSECQGQMERQMAAIQG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1669 KRELESKLSTLSDQVnqrdfESEKRLrkdLKRTKALLADAQIMLDHlknnapSKREIAQLKNQLEESE----FTCAAAVK 1744
Cdd:pfam15921 456 KNESLEKVSSLTAQL-----ESTKEM---LRKVVEELTAKKMTLES------SERTVSDLTASLQEKEraieATNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1745 ARKAMEVEMEDL-HLQIDDIAKAKTALEEQLSRLQ-REKNEIQNRLEEDQEDMNELmkkhkaaVAQASRDMAQMNDLQAQ 1822
Cdd:pfam15921 522 LRSRVDLKLQELqHLKNEGDHLRNVQTECEALKLQmAEKDKVIEILRQQIENMTQL-------VGQHGRTAGAMQVEKAQ 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1823 IE-ESNKEKQELQEKlqalqsqvefleqsmvdKSLVSRQEAKIRELETR---LEFEKTqvkRLENLASRLKETMEKLTEE 1898
Cdd:pfam15921 595 LEkEINDRRLELQEF-----------------KILKDKKDAKIRELEARvsdLELEKV---KLVNAGSERLRAVKDIKQE 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1899 RDQ-------RAAAENREKEQNKRLQRQLRDTKEEMSELARK-EAEASRKKHELEM---DLESLEAAN-------QSLQA 1960
Cdd:pfam15921 655 RDQllnevktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQtrnTLKSMEGSDghamkvaMGMQK 734
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1961 DLKLAFKRIGDLQAAI---EDEMESDENEDLI-----NSLQDMVTKYQKKKNKLEGDSDVDSELEDRV 2020
Cdd:pfam15921 735 QITAKRGQIDALQSKIqflEEAMTNANKEKHFlkeekNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1548-1938 |
9.25e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.45 E-value: 9.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1548 DIAG---FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEELDEQAGSIQMLEQAKLRLEMEmermrq 1624
Cdd:TIGR02169 161 EIAGvaeFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR-REREKAERYQALLKEKREYEGYELLKEKE------ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1625 thskEMESRDEEVEEARQSCQKKLKQMEVQLEEeyedkqkalREKR--ELESKLSTLSDQVNQRDFESEKRLRKDLKRTK 1702
Cdd:TIGR02169 234 ----ALERQKEAIERQLASLEEELEKLTEEISE---------LEKRleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1703 ALLADAQimldhlknnapskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKN 1782
Cdd:TIGR02169 301 AEIASLE-------------RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1783 EIQNRLEEDQEDMNELMKKHKAAVaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKslvsrqEA 1862
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYR-------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI------EA 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1863 KIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRaaaenreKEQNKRLQRQLRDTKeemSELARKEAEAS 1938
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQ---RELAEAEAQAR 500
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
498-616 |
1.34e-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: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 498 APAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTK---- 573
Cdd:cd01363 11 LPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgete 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907082213 574 ---------VFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd01363 91 gwvylteitVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1358-2007 |
2.27e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 96.19 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1358 ERLRTEKEM---KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERA---VREVDFTKKRLQQ 1431
Cdd:pfam02463 154 RRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEkleLEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1432 ELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAH 1511
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1512 EETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLaKVKKQLRDLEAKV 1591
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1592 KDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRE 1671
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEK---KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1672 LESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAM-- 1749
Cdd:pfam02463 470 SEDLLKETQLVKLQEQ-LELLLSRQKLEERSQKESKARSGLK--VLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAis 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1750 ---EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM----NELMKKHKAAVAQASRDMAQMNDLQAQ 1822
Cdd:pfam02463 547 tavIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleiDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1823 IEESNKEKQELQEKLQALQSQVefLEQSMVDKSLVSRQEAKIRELETRLEfekTQVKRLENLASRLKETMEKLTEERDQR 1902
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGL--RKGVSLEEGLAEKSEVKASLSELTKE---LLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1903 AAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRigdLQAAIEDEMES 1982
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS---ELSLKEKELAE 778
|
650 660
....*....|....*....|....*
gi 1907082213 1983 DENEDLINSLQDMVTKYQKKKNKLE 2007
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEEL 803
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1418-1999 |
2.74e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.49 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1418 AVREVDFTKKRLQQELEDkmEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELE 1497
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKA--QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1498 kkqrrfdsELSQAHEETQREKLQREklqREKDMLLAEAFSLKQQMEEkdldiagftqkvvsLEAELQDISSQESKDEASL 1577
Cdd:PRK02224 255 --------TLEAEIEDLRETIAETE---REREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1578 AKVKKQLRDLEAKVKDQEEELDEQAGSIQML-EQAK------LRLEMEMERMRqTHSKEMESRDEEVEEARQSCQKKLKQ 1650
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHnEEAEslredaDDLEERAEELR-EEAAELESELEEAREAVEDRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1651 MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqRDFESEKRLRKDLKRTKALLADAQIMLDHLKnnAPskrEIAQlkn 1730
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERD-ELREREAELEATLRTARERVEEAEALLEAGK--CP---ECGQ--- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1731 QLEESEFTCAAAVK--ARKAMEVEMEDLHLQIDDIAKAKTALEEqLSRLQREKNeiqnRLEEDQEDMNELMKKHKAAVaq 1808
Cdd:PRK02224 460 PVEGSPHVETIEEDreRVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIE----RLEERREDLEELIAERRETI-- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1809 asrdmaqmNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKslvsRQEAKirELETRLEFEKTQVKRLENLASRL 1888
Cdd:PRK02224 533 --------EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA----REEVA--ELNSKLAELKERIESLERIRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1889 ------KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHE-----LEMDLESLEAANQS 1957
Cdd:PRK02224 599 aaiadaEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEeyleqVEEKLDELREERDD 678
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907082213 1958 LQadlklafKRIGDLQAAIEdEMES--DENEDLINSLQDMVTKY 1999
Cdd:PRK02224 679 LQ-------AEIGAVENELE-ELEElrERREALENRVEALEALY 714
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1425-2007 |
2.54e-18 |
|
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: 92.34 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1425 TKKRLQQELEDKMEVEQQSRRQLeRRLGDLQADSDESQRALQQLKKKCQRLTA-----ELQDTKLHLEGQQVRNHELEKK 1499
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAqeavlEETQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1500 QRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQ--MEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1577
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1578 AKVKKQLRDLEAKVK---DQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVEEARQSCQKKLkQMEVQ 1654
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQslcKELDILQREQATIDTRTSAFRDLQGQLAHAK----KQQELQQRYAELCAAAITCTA-QCEKL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1655 LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL-------RKDLKRTKALLADAQIMLDHLKNNAPSKR---E 1724
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeqT 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1725 IAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKKHKA 1804
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE---AEDMLACE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1805 AVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ---------EAKIRELETRLEFEK 1875
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkellasrQLALQKMQSEKEQLT 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1876 TQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEA--------SRKKHELEMD 1947
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkarteahFNNNEEVTAA 773
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1948 L------ESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQdMVTKYQKKKNKLE 2007
Cdd:TIGR00618 774 LqtgaelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCET-LVQEEEQFLSRLE 838
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1560-1985 |
3.32e-18 |
|
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: 92.04 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1560 EAELQDISSQESKD--EASLAKVKKQLRDLEAKVKDQEE--ELDEQagsiqmLEQAKLRLememermrqtHSKEMESRDE 1635
Cdd:TIGR02168 176 ETERKLERTRENLDrlEDILNELERQLKSLERQAEKAERykELKAE------LRELELAL----------LVLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1636 EVEEARQScqkkLKQMEVQLEEeyedkqkALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHL 1715
Cdd:TIGR02168 240 ELEELQEE----LKEAEEELEE-------LTAELQELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1716 KNnapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM 1795
Cdd:TIGR02168 308 RE------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1796 NELmkkhKAAVAQASRdmaQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMvdkslvsrQEAKIRELETRLEfek 1875
Cdd:TIGR02168 382 ETL----RSKVAQLEL---QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--------EEAELKELQAELE--- 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1876 tqvkrlenlasRLKETMEKLTEERDQRAAAEnrekeqnKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAAN 1955
Cdd:TIGR02168 444 -----------ELEEELEELQEELERLEEAL-------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS 505
|
410 420 430
....*....|....*....|....*....|
gi 1907082213 1956 QSLQAdLKLAFKRIGDLQAAIEDEMESDEN 1985
Cdd:TIGR02168 506 EGVKA-LLKNQSGLSGILGVLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1398-1797 |
5.33e-18 |
|
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: 91.66 E-value: 5.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1398 INGEVDDDDAGgewRLKYERAVREVDFTKKRLQQ---ELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQR 1474
Cdd:TIGR02168 661 ITGGSAKTNSS---ILERRREIEELEEKIEELEEkiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1475 LTAELQdtklhlegqqvrnhELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQ 1554
Cdd:TIGR02168 738 LEAEVE--------------QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1555 KVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRD 1634
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1635 eEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesekRLRKDLKRTK-ALLADAQIMLD 1713
Cdd:TIGR02168 884 -SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE--------GLEVRIDNLQeRLSEEYSLTLE 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1714 HLKNN--------APSKREIAQLKNQLEE---------SEFtcaAAVKARKamevemEDLHLQIDDIAKAKTALEEQLSR 1776
Cdd:TIGR02168 955 EAEALenkieddeEEARRRLKRLENKIKElgpvnlaaiEEY---EELKERY------DFLTAQKEDLTEAKETLEEAIEE 1025
|
410 420
....*....|....*....|.
gi 1907082213 1777 LQReknEIQNRLEEDQEDMNE 1797
Cdd:TIGR02168 1026 IDR---EARERFKDTFDQVNE 1043
|
|
| PDZ_canonical |
cd00136 |
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ... |
220-308 |
1.39e-17 |
|
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467153 [Multi-domain] Cd Length: 81 Bit Score: 79.51 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPTGDFGFSLRRTTMLDRAPegqayrrVVHFAEPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:cd00136 1 TVTLEKDPGGGLGFSIRGGKDGGGGI-------FVSRVEPG-GPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSA 72
|
....*....
gi 1907082213 300 GDSVRLKVQ 308
Cdd:cd00136 73 GGEVTLTVR 81
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1249-1838 |
1.47e-17 |
|
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: 89.69 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1249 KKRKIQDLAIRCVQKNIKKNKgvkdwpwwKLFTTVRPLIQVQLS-EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRL 1327
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNK--------SLESQISELKKQNNQlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1328 ETRISELTSELtderntgESASQLLDaetaerlRTEKEMKELQTQYDALKKQmevmemevmearliRAAEINGEVDDDDA 1407
Cdd:TIGR04523 266 KKQLSEKQKEL-------EQNNKKIK-------ELEKQLNQLKSEISDLNNQ--------------KEQDWNKELKSELK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1408 GGEWRL--------KYERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKkcqrLTAEL 1479
Cdd:TIGR04523 318 NQEKKLeeiqnqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN----LESQI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1480 QDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSL 1559
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-------DLTNQDSVKELIIKNLDNTRESL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1560 EAELQDISSQESKDEASLAKVKKQLrdleakvKDQEEELDeqagsiqMLEQAKLRLEMEMermrqthsKEMESRdeevee 1639
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKEL-------KSKEKELK-------KLNEEKKELEEKV--------KDLTKK------ 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1640 arqscQKKLKQMEVQLEeeyedkqkalREKRELESKLSTLSDQVNQRDFESEKRLRKD-----------LKRTKALLADA 1708
Cdd:TIGR04523 519 -----ISSLKEKIEKLE----------SEKKEKESKISDLEDELNKDDFELKKENLEKeideknkeieeLKQTQKSLKKK 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1709 QIMLDHLKNNapSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR- 1787
Cdd:TIGR04523 584 QEEKQELIDQ--KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKw 661
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1788 ---------LEEDQEDMNELMKKHK----AAVAQASRDMAQMNDLQaQIEESNKEKQELQEKLQ 1838
Cdd:TIGR04523 662 peiikkikeSKTKIDDIIELMKDWLkelsLHYKKYITRMIRIKDLP-KLEEKYKEIEKELKKLD 724
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1284-2013 |
2.74e-17 |
|
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: 89.34 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1284 RPLIQVQLSEEQIRNKDEEIQ--QLRSKLEKVEKE-------RNELRLSSDRLETR---ISELTSELTDERNTGESASQL 1351
Cdd:TIGR00606 351 RLQLQADRHQEHIRARDSLIQslATRLELDGFERGpfserqiKNFHTLVIERQEDEaktAAQLCADLQSKERLKQEQADE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1352 LDAETAERLRT--------EKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVR--- 1420
Cdd:TIGR00606 431 IRDEKKGLGRTielkkeilEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQnek 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1421 -EVDFTKKRLQQELE-----------------DKMEVEQQSRRQLERRLGDLQA------DSDESQRALQQLKKKCQRLT 1476
Cdd:TIGR00606 511 aDLDRKLRKLDQEMEqlnhhtttrtqmemltkDKMDKDEQIRKIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTR 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1477 AELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-----------ETQREKLQR--EKLQREKDMLLAEAFSLKQQME 1543
Cdd:TIGR00606 591 DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcgsqdeESDLERLKEeiEKSSKQRAMLAGATAVYSQFIT 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1544 EKDLDIAG---FTQKVVSLEAELQDISsqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME 1620
Cdd:TIGR00606 671 QLTDENQSccpVCQRVFQTEAELQEFI---SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1621 RMRQTHSK------EMESRDEEVEEARQSCQKKLKQMEV---------QLEEEYEDKQKALREK-RELESKLSTLS-DQV 1683
Cdd:TIGR00606 748 ELRNKLQKvnrdiqRLKNDIEEQETLLGTIMPEEESAKVcltdvtimeRFQMELKDVERKIAQQaAKLQGSDLDRTvQQV 827
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1684 NQRDFESEKRLRK---DLKRTKALLADAQIMLDHLKNNApskreiaqlkNQLEESEFTCAAAVKARKAME-------VEM 1753
Cdd:TIGR00606 828 NQEKQEKQHELDTvvsKIELNRKLIQDQQEQIQHLKSKT----------NELKSEKLQIGTNLQRRQQFEeqlvelsTEV 897
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1754 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEED----QEDMNELMKKHKAAVA---------------QASRDMA 1814
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSnkkaQDKVNDIKEKVKNIHGymkdienkiqdgkddYLKQKET 977
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1815 QMNDLQAQIEESNKEKQELQEKLQALQSQVE---FLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLasRLKET 1891
Cdd:TIGR00606 978 ELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVL--QMKQE 1055
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1892 MEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAsrKKHELEMDLESLEAANQSL--------QADLK 1963
Cdd:TIGR00606 1056 HQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE--KYREMMIVMRTTELVNKDLdiyyktldQAIMK 1133
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1964 LAFKRIGDLQAAIED--------------EMESDENEDLinSLQDMVTKYQKKKNKLEGDSDVD 2013
Cdd:TIGR00606 1134 FHSMKMEEINKIIRDlwrstyrgqdieyiEIRSDADENV--SASDKRRNYNYRVVMLKGDTALD 1195
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1294-1781 |
1.14e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 86.36 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1294 EQIRNKDEEIQQLRSKLEKVEKERNELrlssDRLETRISELTSELTDERNTGESASQLLDAET--AERLRTEKEMKELQT 1371
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1372 QYDALKKQMEVMEmevmearliraaeingevddddaggEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRL 1451
Cdd:COG4717 147 RLEELEERLEELR-------------------------ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1452 GDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQvrnhelekkqrrfdselsqaheetqreklQREKLQREKDML 1531
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-----------------------------LEERLKEARLLL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1532 LAEA-----FSLKQQMEEKDLDIAGFTQKVVSLeaeLQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQ 1606
Cdd:COG4717 253 LIAAallalLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1607 MLEQAKL-RLEMEMERMRQTHSKEMESRDEE----VEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSD 1681
Cdd:COG4717 330 LPPDLSPeELLELLDRIEELQELLREAEELEeelqLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1682 QVNQR--------DFESEKRLRKDLKRTKALLADAQIMLDHLknnapsKREIAQLKNQLE--ESEFTCAAAVKARKAMEV 1751
Cdd:COG4717 410 QLEELlgeleellEALDEEELEEELEELEEELEELEEELEEL------REELAELEAELEqlEEDGELAELLQELEELKA 483
|
490 500 510
....*....|....*....|....*....|
gi 1907082213 1752 EMEDLHLQIDDIAKAKTALEEQLSRLQREK 1781
Cdd:COG4717 484 ELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1293-1774 |
1.33e-16 |
|
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: 86.77 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1293 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISEL---TSELTDERNTGESAsqlldaetaeRLRTEKEMKEL 1369
Cdd:pfam01576 656 ERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMktqLEELEDELQATEDA----------KLRLEVNMQAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1370 QTQYDAlkkqmevmemevmearliraaEINGEvddDDAGGEWRLKYERAVREvdftkkrLQQELEDKMEVEQQ---SRRQ 1446
Cdd:pfam01576 726 KAQFER---------------------DLQAR---DEQGEEKRRQLVKQVRE-------LEAELEDERKQRAQavaAKKK 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1447 LERRLGDLQADSDESQR----ALQQLKK---KCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKL 1519
Cdd:pfam01576 775 LELDLKELEAQIDAANKgreeAVKQLKKlqaQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1520 QREKLQREKDmllaeafslkqqmeekdldiagftqkvvsleaELQDISSQESKDEASLAKVKkqlRDLEAKVKDQEEELD 1599
Cdd:pfam01576 855 ARRQAQQERD--------------------------------ELADEIASGASGKSALQDEK---RRLEARIAQLEEELE 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1600 EQAGSIQMLEQAKLRLEMEMERMRQTHSKEmESRDEEVEEARQSCQKKLKQMEVQL-EEEYEDKQKALREKRELESKLST 1678
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLQVEQLTTELAAE-RSTSQKSESARQQLERQNKELKAKLqEMEGTVKSKFKSSIAALEAKIAQ 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1679 LSDQVNQrdfESEKRLR--KDLKRTKALLADAQIMLDHLKNNAPSKREIA--------QLKNQLEESEFTCAAAVKARKA 1748
Cdd:pfam01576 979 LEEQLEQ---ESRERQAanKLVRRTEKKLKEVLLQVEDERRHADQYKDQAekgnsrmkQLKRQLEEAEEEASRANAARRK 1055
|
490 500
....*....|....*....|....*.
gi 1907082213 1749 MEVEMEDLHLQIDDIAKAKTALEEQL 1774
Cdd:pfam01576 1056 LQRELDDATESNESMNREVSTLKSKL 1081
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1475-1975 |
1.57e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 85.97 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1475 LTAELQDTKLHLEGQQVRNHELEKKQRRfdsELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQ 1554
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELK---ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1555 KVvsleaELQDISSQESKDEASLAKVKKQLRDLEAkvkdQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRD 1634
Cdd:COG4717 124 LL-----QLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1635 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQvnqrdfesekrlrKDLKRTKALLADAQIMLdh 1714
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-------------ERLKEARLLLLIAAALL-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1715 lknnapskrEIAQLKNQLEESEFTCAAAVKARKAMevemedLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQED 1794
Cdd:COG4717 260 ---------ALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1795 MNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKlQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFE 1874
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED------EEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1875 KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQnkRLQRQLRDTKEEMSELARKEAEASRKKHELEMD--LESLE 1952
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELE--ELEEELEELEEELEELREELAELEAELEQLEEDgeLAELL 475
|
490 500
....*....|....*....|...
gi 1907082213 1953 AANQSLQADLKLAFKRIGDLQAA 1975
Cdd:COG4717 476 QELEELKAELRELAEEWAALKLA 498
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
468-650 |
1.81e-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: 86.04 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKgCRR--EDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 545
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYK-CIDciEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 546 GSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQAL---------------------STLLEAFGNSPTIMNGSATRF 604
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDnihneentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907082213 605 SQILSLDFDQAgQVASASIQTMLLEKLRVARRPASEATFNVFYYLL 650
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYII 205
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1287-1803 |
2.10e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.89 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1287 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLET---------RISELTSELTDERNTGE-------SASQ 1350
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEkrlsrleEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1351 LLDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEvddddaggewRLKYERAVREVDFTKKRLQ 1430
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE----------RLKKRLTGLTPEKLEKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1431 QELEDKMEVEQQsRRQLERRLGDLQADSDESQRALQQLKK---KCQRLTAELQDtklhlegqqvrnHELEKKQRRFDSEL 1507
Cdd:PRK03918 395 ELEKAKEEIEEE-ISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTE------------EHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1508 SQAHEETQREKLQREKLQREKDMLlaEAFSLKQQMEEKDLDIAgftQKVVSLEAELQDISSQE-SKDEASLAKVKKQLRD 1586
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELA---EQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1587 LEAKVKDQEEELDEQagsiqmleqaklrlememermrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEE----YEDK 1662
Cdd:PRK03918 537 LKGEIKSLKKELEKL--------------------------EELKKKLAELEKKLDELEEELAELLKELEELgfesVEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1663 QKALREKRELESKLSTLSDQVnqRDFESEKRLRKDLKRTkalLADAQIMLDHLKNNAPSKR-EIAQLKNQLEESEFTCAA 1741
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAE--KELEREEKELKKLEEE---LDKAFEELAETEKRLEELRkELEELEKKYSEEEYEELR 665
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082213 1742 AVKARKAMEV-----EMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNrLEEDQEDMNELMKKHK 1803
Cdd:PRK03918 666 EEYLELSRELaglraELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVK 731
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1566-2018 |
3.05e-16 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 85.46 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1566 ISSQESKD---EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEmemERMRQTHSKEMESRD-------- 1634
Cdd:TIGR04523 28 ANKQDTEEkqlEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILE---QQIKDLNDKLKKNKDkinklnsd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1635 -----EEVEEARQSCQKK---LKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesekrlrkDLKRTKALLA 1706
Cdd:TIGR04523 105 lskinSEIKNDKEQKNKLeveLNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN------------DLKKQKEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1707 DAQIMLDHLKNNApsKREIAQLKNQLEESEFTCAAAVKARKamevEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQN 1786
Cdd:TIGR04523 173 NELNLLEKEKLNI--QKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1787 RLEEDQEDMNELMKKHKaavaqasRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD------KSLVSRQ 1860
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQN-------KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelKSELKNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1861 EAKIRELETRLEFEKTQVKRLENLASRLKETMEKLT---EERDQRAAAENRE----KEQNKRLQRQLRDTKEEMSELARK 1933
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEieklKKENQSYKQEIKNLESQINDLESK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1934 EAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESD-ENEDLINSLQDMVTKYQKKKNKLEGD-SD 2011
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDsVKELIIKNLDNTRESLETQLKVLSRSiNK 479
|
....*..
gi 1907082213 2012 VDSELED 2018
Cdd:TIGR04523 480 IKQNLEQ 486
|
|
| PDZ_NHERF-like |
cd06768 |
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ... |
222-307 |
3.80e-16 |
|
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467249 [Multi-domain] Cd Length: 80 Bit Score: 75.17 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 222 ELQRRPTGdFGFSLRRttmlDRAPEGQaYRRVVhfaEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGD 301
Cdd:cd06768 4 HLVKGPEG-YGFNLHA----EKGRPGH-FIREV---DPG-SPAERA-GLKDGDRLVEVNGENVEGESHEQVVEKIKASGN 72
|
....*.
gi 1907082213 302 SVRLKV 307
Cdd:cd06768 73 QVTLLV 78
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1667-2023 |
1.02e-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: 83.96 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1667 REKRELESKLSTLS--DQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcaAAVK 1744
Cdd:TIGR02169 153 VERRKIIDEIAGVAefDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGY--ELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1745 ARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM-AQMNDLQAQI 1823
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELeAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1824 EESNKEKQELQEKLQ-------ALQSQVEFLEQSMVDKSL--------VSRQEAKIRELETRLEFEKTQVKRLENLASRL 1888
Cdd:TIGR02169 311 AEKERELEDAEERLAkleaeidKLLAEIEELEREIEEERKrrdklteeYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1889 KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1968
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1969 IGDLQA---AIEDEMESDENEdlinsLQDMVTKYQKKKNKLEGDSDVDSELEDRVDGV 2023
Cdd:TIGR02169 471 LYDLKEeydRVEKELSKLQRE-----LAEAEAQARASEERVRGGRAVEEVLKASIQGV 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1287-1633 |
1.11e-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: 83.95 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1287 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLET-------RISELTSELTDERNTGESASQLLDAETAER 1359
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAeveqleeRIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1360 LRTEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDD-DDAGGEWRLKYERAVREVDFTKKRLqQELEDKME 1438
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALRE--------ALDELRAELTLlNEEAANLRERLESLERRIAATERRL-EDLEEQIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1439 VEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREK 1518
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1519 LQREKLQREKDMLLaEAFSLKQQMeekdldiagftqkvvsleaELQDISSQESKDEASLAKVKKQLRDLEAKVK------ 1592
Cdd:TIGR02168 929 LRLEGLEVRIDNLQ-ERLSEEYSL-------------------TLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvn 988
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907082213 1593 --------DQEEELDEQAGSIQMLEQAKLRLEMEMERMrqthSKEMESR 1633
Cdd:TIGR02168 989 laaieeyeELKERYDFLTAQKEDLTEAKETLEEAIEEI----DREARER 1033
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1290-1941 |
2.12e-15 |
|
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: 83.10 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1290 QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDaetaERLRTEKEMKEL 1369
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ----GKLTEEKEELEK 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1370 QTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELE--DKMEVEQQSRRQL 1447
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggRIISAHGRLGDLG 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1448 ERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEETQREKLQREKLQRE 1527
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK---LPLKSIAVLEIDPILNLAQLDKAT 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1528 KDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQE------SKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1601
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaekSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1602 AGSIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSD 1681
Cdd:pfam02463 693 EILRRQLEIKKKEQREK-EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1682 QVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID 1761
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1762 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqasrdMAQMNDLQAQIEESNKEKQELQEKLQALQ 1841
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEK------EEKKELEEESQKLNLLEEKENEIEERIKE 925
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1842 SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLEN---LASRLKETMEKLTEERDQRAAAENREKEQN----K 1914
Cdd:pfam02463 926 EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLakeELGKVNLMAIEEFEEKEERYNKDELEKERLeeekK 1005
|
650 660
....*....|....*....|....*..
gi 1907082213 1915 RLQRQLRDTKEEMSELARKEAEASRKK 1941
Cdd:pfam02463 1006 KLIRAIIEETCQRLKEFLELFVSINKG 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1685-2018 |
2.33e-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: 82.80 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1685 QRDFESEKRLRK---DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaavkarkamevemedlhLQID 1761
Cdd:TIGR02168 172 ERRKETERKLERtreNLDRLEDILNELERQLKSLERQAEKAERYKELKAELRE-----------------------LELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1762 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkhkaavaqasrdmaqmndlQAQIEESNKEKQELQEKLQALQ 1841
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQEL---------------------EEKLEELRLEVSELEEEIEELQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1842 SqvEFLEQSmvdkslvsrqeAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLR 1921
Cdd:TIGR02168 288 K--ELYALA-----------NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1922 DTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQK 2001
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
330
....*....|....*..
gi 1907082213 2002 KKNKLEGDSDVDSELED 2018
Cdd:TIGR02168 435 LKELQAELEELEEELEE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1428-1933 |
2.81e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.66 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1428 RLQQELEDKMEVEQQSRRQLERR--LGDLQADSDESQRALQQLKkkcqrlTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1505
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIelLEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1506 ELSQAHEETQREKLQREKLQREKDMLLAEAFS--------LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1577
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1578 AKVKKQLR------------------DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKE---------- 1629
Cdd:COG4913 383 AALRAEAAallealeeelealeealaEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlgldeaelpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1630 ----MESRDEE-------------------VEEARQSC------QKKLKQmEVQLEEEYEDKQKALREK-------RELE 1673
Cdd:COG4913 463 vgelIEVRPEEerwrgaiervlggfaltllVPPEHYAAalrwvnRLHLRG-RLVYERVRTGLPDPERPRldpdslaGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1674 SKLSTLSDQVNQ---RDF-----ESEKRLRKDlkrTKALLADAQImldhlKNNApSKREIaQLKNQLEESEFTCAAAVKA 1745
Cdd:COG4913 542 FKPHPFRAWLEAelgRRFdyvcvDSPEELRRH---PRAITRAGQV-----KGNG-TRHEK-DDRRRIRSRYVLGFDNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1746 RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelmkkhkaaVAQASRDMAQMNDLQAQIEE 1825
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID---------VASAEREIAELEAELERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1826 SNKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFEKTQVK----RLENLASRLKETMEKLTEERDQ 1901
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEE------ELDELKGEIGRLEKELEQAEEELDelqdRLEAAEDLARLELRALLEERFA 756
|
570 580 590
....*....|....*....|....*....|..
gi 1907082213 1902 RAAAENREKEQNKRLQRQLRDTKEEMSELARK 1933
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
468-1186 |
3.15e-15 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 81.70 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 468 SVLHTLRQRYGASLLHTYAGPSLLVLST---RGAPAVYSEKvmhmfkgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVL 544
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPyrdVGNPLTLTST--------RSSPLAPQLLKVVQEAVRQQSETGYPQAIIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 545 LGSSGSGKTTSFQHLVQYLATIAGtSGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQaGQVASASIQ 624
Cdd:cd14881 74 SGTSGSGKTYASMLLLRQLFDVAG-GGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 625 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLN--------HLAENNVFgivplskpEEKQKAAQQFSKLQAA 696
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgyspanlrYLSHGDTR--------QNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 697 MKVLAISpeeqktcWL----ILASIYHLGAAG-ATKAGRKQFARHEWAQKA-AYLLGCSleelSSAIFKhqlkgGTLQRS 770
Cdd:cd14881 224 LGILGIP-------FLdvvrVLAAVLLLGNVQfIDGGGLEVDVKGETELKSvAALLGVS----GAALFR-----GLTTRT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 771 TSFRQGPEESGLGEGTKLSALECLegmASGLYSELFTLLISLVNrALKSSQHSLC------SMMIVDTPGFQNPewggsa 844
Cdd:cd14881 288 HNARGQLVKSVCDANMSNMTRDAL---AKALYCRTVATIVRRAN-SLKRLGSTLGthatdgFIGILDMFGFEDP------ 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 845 RGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELafdDLEPVADDSVAAVDqashLVRSLahadeARGLLWLLE 924
Cdd:cd14881 358 KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQC---EVEVDYVDNVPCID----LISSL-----RTGLLSMLD 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 925 EEALVPGATEdalldrlfSYYGPQEGDKKGQSPLLRSSK--PRHFLLGHSHGTnwVEYNVAGWLnytkqnpatqnaprll 1002
Cdd:cd14881 426 VECSPRGTAE--------SYVAKIKVQHRQNPRLFEAKPqdDRMFGIRHFAGR--VVYDASDFL---------------- 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1003 qDSQKKIISNlflgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAavkkkslciQIKLQVDALIDTIKRSKMH 1082
Cdd:cd14881 480 -DTNRDVVPD----------------------DLVAVFYKQNCNFGFATHTQ---------DFHTRLDNLLRTLVHARPH 527
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1083 FVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1162
Cdd:cd14881 528 FVRCIRSNTTETPN-----------------------------HFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFN 578
|
730 740
....*....|....*....|....
gi 1907082213 1163 RRFDVLAPHLTKKHGRNYIVVDEK 1186
Cdd:cd14881 579 ARYRLLAPFRLLRRVEEKALEDCA 602
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1297-1902 |
6.41e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1297 RNKDEEIQQLRSKLEkvEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDaETAERLrteKEMKELQTQYDAL 1376
Cdd:PRK02224 183 SDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRD-EADEVL---EEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1377 KkqmevmemevmearliraAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELED---KMEVEQQSRRQLERRLGD 1453
Cdd:PRK02224 257 E------------------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDllaEAGLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1454 LQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDmlla 1533
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE---- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1534 eafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD-------QEEELDEQAGSIQ 1606
Cdd:PRK02224 395 ---ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1607 MLEQAKLRLEMEMERMRQTHskemESRDEEVEEArqscqKKLKQMEVQLEEeyedkqkaLREKRELESKLSTlsdqvNQR 1686
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEV----EEVEERLERA-----EDLVEAEDRIER--------LEERREDLEELIA-----ERR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1687 DFESEKRLRKDLKRTKAlladaqimlDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE----MEDLHLQIDD 1762
Cdd:PRK02224 530 ETIEEKRERAEELRERA---------AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKEriesLERIRTLLAA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1763 IAKAKTALE---EQLSRLQREKNEIQNRLEEDQEDMNELMKKH-KAAVAQASRDMAQMNDLQAQIEEsnkEKQELQEKLQ 1838
Cdd:PRK02224 601 IADAEDEIErlrEKREALAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEE---KLDELREERD 677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082213 1839 ALQSQVefleqSMVDKSLvsrqeAKIRELETRLEFEKTQVKRLENL---ASRLKETMEKLTEERDQR 1902
Cdd:PRK02224 678 DLQAEI-----GAVENEL-----EELEELRERREALENRVEALEALydeAEELESMYGDLRAELRQR 734
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1722-1938 |
2.34e-14 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 77.50 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1722 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1801
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1802 -------HKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdkslvsRQEAKIRELETRLEFE 1874
Cdd:COG4942 113 lyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA---------ELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1875 KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAS 1938
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1606-2007 |
2.59e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.04 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1606 QMLEQaklRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQVNQ 1685
Cdd:COG4717 45 AMLLE---RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1686 -RDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS----KREIAQLKNQLEESEFTCAAAVK-ARKAMEVEMEDLHLQ 1759
Cdd:COG4717 121 lEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1760 IDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK-----------AAVA--------------------- 1807
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaAALLallglggsllsliltiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1808 ---------------QASRDMAQMNDLQAQIEESNKEKQELQEKLQALQ----SQVEFLEQSMVDKSLVSRQEAKIRELE 1868
Cdd:COG4717 281 lvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGlppdLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1869 TRLEFEKTQvKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAsrkkhELEMDL 1948
Cdd:COG4717 361 EELQLEELE-QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEEL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082213 1949 ESLEAANQSLQADLKLAFKRIGDLQAAIEdEMESDEnedlinSLQDMVTKYQKKKNKLE 2007
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELE-QLEEDG------ELAELLQELEELKAELR 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1294-1930 |
3.13e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1294 EQIRNKDEEIQQLRSKLEKVEKERNELRLssDRLETRISELTSELTDERntgesasQLLDAETAERLRTEKEMKELQTQY 1373
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAELEELR-------AELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1374 DALKKQMevmemevmearliraaeingevddDDAGGEwRLkyERAVREVdftkKRLQQELEDKmeveQQSRRQLERRLGD 1453
Cdd:COG4913 326 DELEAQI------------------------RGNGGD-RL--EQLEREI----ERLERELEER----ERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1454 LQADSDESQRALQQLKKKCQRLTAELQDtklHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQR----EKLQREKD 1529
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEE---ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1530 MLlAEAFSLKqqmeEKDLDIAGftqkvvsleaELQDISSQESK------------------DEASLAKVKKQL--RDLEA 1589
Cdd:COG4913 448 AL-AEALGLD----EAELPFVG----------ELIEVRPEEERwrgaiervlggfaltllvPPEHYAAALRWVnrLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1590 KVKDQEEELDEQAGSIQMLEQAKL--RLEMEMERMRQTHSKEMESRD-----EEVEEARQ-------SCQKKL------K 1649
Cdd:COG4913 513 RLVYERVRTGLPDPERPRLDPDSLagKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRhpraitrAGQVKGngtrheK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1650 QMEVQLEEEY------EDKQKALREKR-ELESKLSTLSDQVNQRdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSK 1722
Cdd:COG4913 593 DDRRRIRSRYvlgfdnRAKLAALEAELaELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1723 REIAQLKNQ---LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE----DQEDM 1795
Cdd:COG4913 668 REIAELEAElerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlARLEL 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1796 NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQveFLEQSMVDKSLVSRQEAKIRELETRLEfek 1875
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA--FNREWPAETADLDADLESLPEYLALLD--- 822
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1876 tqvkRLENlaSRLKETMEKLteeRDQRAAAENREKEQ-NKRLQRQLRDTKEEMSEL 1930
Cdd:COG4913 823 ----RLEE--DGLPEYEERF---KELLNENSIEFVADlLSKLRRAIREIKERIDPL 869
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1405-2017 |
5.14e-14 |
|
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: 78.94 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1405 DDAGGEWRLKYERAVREVDFTKKRLQQeledkmeveqqsrrQLERRLGDLQADSDESQRALQQLKKKCQRLTaELQDTKL 1484
Cdd:TIGR01612 1099 DDFGKEENIKYADEINKIKDDIKNLDQ--------------KIDHHIKALEEIKKKSENYIDEIKAQINDLE-DVADKAI 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1485 HLEGQQvrnhELEKKQRRFDSELSQA---HEETQreKLQREKLQREKDmllaeafslKQQMEE-KDLDIAgFTQKVVSLE 1560
Cdd:TIGR01612 1164 SNDDPE----EIEKKIENIVTKIDKKkniYDEIK--KLLNEIAEIEKD---------KTSLEEvKGINLS-YGKNLGKLF 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1561 aeLQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEELDEQAGsIQMLEQAklrlemEMERMRQTHSKEM------ESRD 1634
Cdd:TIGR01612 1228 --LEKIDEEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMG-IEMDIKA------EMETFNISHDDDKdhhiisKKHD 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1635 EEVEEARQscqKKLKQMEVQLEE-EYEDKQKAL--------REKRELESKLSTLSDQVNQRDFESEKRLRKDLKR-TKAL 1704
Cdd:TIGR01612 1298 ENISDIRE---KSLKIIEDFSEEsDINDIKKELqknlldaqKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKEyTKEI 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1705 LADAQIMLDHLKNnapSKREIAQLKNQLeeSEFTCAAAVKArkamEVEMEDLHLQIDDIAKAKTALEEQLSRLQ------ 1778
Cdd:TIGR01612 1375 EENNKNIKDELDK---SEKLIKKIKDDI--NLEECKSKIES----TLDDKDIDECIKKIKELKNHILSEESNIDtyfkna 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1779 REKNE----IQNRLEEDQEDMNELMKKHKAavaQASRDMA-QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvd 1853
Cdd:TIGR01612 1446 DENNEnvllLFKNIEMADNKSQHILKIKKD---NATNDHDfNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQY--- 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1854 KSLVSRQEAKIRELETRLEFEKTQvKRLENLASRLKETMEKLTEErdqraaAENREKEQNKRLQRQLRDTKEemselARK 1933
Cdd:TIGR01612 1520 KKDVTELLNKYSALAIKNKFAKTK-KDSEIIIKEIKDAHKKFILE------AEKSEQKIKEIKKEKFRIEDD-----AAK 1587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1934 EAEASRKKHELEMDLESLEaaNQSLQ-ADLKlafKRIGDLQAAIED-------------EMESDENEDLINSLQDMVTKY 1999
Cdd:TIGR01612 1588 NDKSNKAAIDIQLSLENFE--NKFLKiSDIK---KKINDCLKETESiekkissfsidsqDTELKENGDNLNSLQEFLESL 1662
|
650 660
....*....|....*....|..
gi 1907082213 2000 QKKKNKLEGDS----DVDSELE 2017
Cdd:TIGR01612 1663 KDQKKNIEDKKkeldELDSEIE 1684
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1466-1999 |
5.73e-14 |
|
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: 78.09 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1466 QQLKKKCQRLTAELQDTKLHLEGQQVRNHElekKQRRFDSELSQAHEETQREKLQREKLQREkDMLLAEAFSLKQQMEEK 1545
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHE---RKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1546 DLDIAGFT--QKVVSLEAELQDISSQESK---DEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME 1620
Cdd:TIGR00618 266 RARIEELRaqEAVLEETQERINRARKAAPlaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1621 RMRQTHSKEMESRDE-EVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFE--SEKRLRKD 1697
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAhEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRtsAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1698 LKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcaaAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1777
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ---SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1778 QREKNE-----------------IQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQAL 1840
Cdd:TIGR00618 503 PCPLCGscihpnparqdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1841 QSQVEFLEQSMVD------------KSLVSRQEAKIRELETRLE------FEKTQVKRLENLASRLKETMEKLTEERDQR 1902
Cdd:TIGR00618 583 KEDIPNLQNITVRlqdlteklseaeDMLACEQHALLRKLQPEQDlqdvrlHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1903 AAAENREKEQNKRLQRQLRDTKEE-------------------MSELARKEAEASRKKHELEMDLESLEaanQSLQADLK 1963
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQsekeqltywkemlaqcqtlLRELETHIEEYDREFNEIENASSSLG---SDLAARED 739
|
570 580 590
....*....|....*....|....*....|....*.
gi 1907082213 1964 LAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKY 1999
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1443-2008 |
7.34e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.03 E-value: 7.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1443 SRRQLERRLGDLQADSDESQRALQqlkkkcQRLTAelqdtKLHLEGQQ--------------------VRNHELEKKQ-- 1500
Cdd:COG4913 156 DIRALKARLKKQGVEFFDSFSAYL------ARLRR-----RLGIGSEKalrllhktqsfkpigdlddfVREYMLEEPDtf 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1501 RRFDS------ELSQAHEETQREKLQREKLQREKDmlLAEAF-SLKQQMEEKDLDIAGFTQKVVSLEAELQdissqeskd 1573
Cdd:COG4913 225 EAADAlvehfdDLERAHEALEDAREQIELLEPIRE--LAERYaAARERLAELEYLRAALRLWFAQRRLELL--------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1574 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKL--------RLEMEMERMRQTHskemesrdEEVEEARQSCQ 1645
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLEREL--------EERERRRARLE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1646 KKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQImLDHLKNNAPskREI 1725
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS-LERRKSNIP--ARL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1726 AQLKNQLEEseftcAAAVKARKA------MEVEMED--------------------------------------LHLQID 1761
Cdd:COG4913 443 LALRDALAE-----ALGLDEAELpfvgelIEVRPEEerwrgaiervlggfaltllvppehyaaalrwvnrlhlrGRLVYE 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1762 DI------AKAKTALEEQLSR-LQREKNEIQNRLE------------EDQEDmnelMKKHKAAVAQA-----SRDMAQMN 1817
Cdd:COG4913 518 RVrtglpdPERPRLDPDSLAGkLDFKPHPFRAWLEaelgrrfdyvcvDSPEE----LRRHPRAITRAgqvkgNGTRHEKD 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1818 DL-------------QAQIEESNKEKQELQEKLQALQSQVEFLEQSMvdKSLVSRQEAKIRELETRleFEKTQVKRLENL 1884
Cdd:COG4913 594 DRrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAEL--DALQERREALQRLAEYS--WDEIDVASAERE 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1885 ASRLKETMEKLTEERDQRAAAENREKEQNKR---LQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEA-ANQSLQA 1960
Cdd:COG4913 670 IAELEAELERLDASSDDLAALEEQLEELEAEleeLEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlARLELRA 749
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1907082213 1961 DLKLAFkrigdlQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEG 2008
Cdd:COG4913 750 LLEERF------AAALGDAVERELRENLEERIDALRARLNRAEEELER 791
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1623-2052 |
8.02e-14 |
|
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: 77.37 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1623 RQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTK 1702
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK-LNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1703 AlladaQIMLD-HLKNNapSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREK 1781
Cdd:TIGR04523 110 S-----EIKNDkEQKNK--LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1782 NEIQN----------RLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSm 1851
Cdd:TIGR04523 183 LNIQKnidkiknkllKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1852 vDKSLVSRQEAKIRELETrlefEKTQVKRLENLASRLKETMEKLteerdqraaaeNREKEQN--KRLQRQLRDTKEEMSE 1929
Cdd:TIGR04523 262 -QNKIKKQLSEKQKELEQ----NNKKIKELEKQLNQLKSEISDL-----------NNQKEQDwnKELKSELKNQEKKLEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1930 LarkeaeasrkkhelemdlesleaanqslqadlklafkrigdlqaaiedEMESDENEDLINSLQDMVTKYQKKKNKLEGD 2009
Cdd:TIGR04523 326 I------------------------------------------------QNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907082213 2010 -SDVDSELEDRVDGVKSWLSKNKGPSKAPSddgSLKSSRTALNS 2052
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 ... |
1413-1965 |
1.98e-13 |
|
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: 76.40 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1413 LKYERAVREVDFTKKRLqqeLEDKMEVEQQSRRQLERRLGDLQaDSDESQRALQQL----KKKCQRLTAELQDTKLHLEG 1488
Cdd:pfam10174 41 LKKERALRKEEAARISV---LKEQYRVTQEENQHLQLTIQALQ-DELRAQRDLNQLlqqdFTTSPVDGEDKFSTPELTEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1489 QQVRNHELEKKQRRFDSELSQAHEE------TQREKL--QREKLQREKDMLLAEAFSLKQQMEEKDLD--IAGFTQKVVS 1558
Cdd:pfam10174 117 NFRRLQSEHERQAKELFLLRKTLEEmelrieTQKQTLgaRDESIKKLLEMLQSKGLPKKSGEEDWERTrrIAEAEMQLGH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1559 LEAELQDISSQESKDEASLaKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVE 1638
Cdd:pfam10174 197 LEVLLDQKEKENIHLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1639 --EARQSCQKKLKQMEVQLEEEYEDKQKalrEKRELESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLK 1716
Cdd:pfam10174 276 qmEVYKSHSKFMKNKIDQLKQELSKKES---ELLALQTKLETLTNQ-NSDCKQHIEVLKESLTAKEQRAAILQTEVDALR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1717 NNAPSKREIAQLKNQ----LEESEFTCAAA---------VKARKAMEVE--MEDLHLQIDDIAKAKTALEEQLSRLQREK 1781
Cdd:pfam10174 352 LRLEEKESFLNKKTKqlqdLTEEKSTLAGEirdlkdmldVKERKINVLQkkIENLQEQLRDKDKQLAGLKERVKSLQTDS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1782 NEIQNRL---EE---DQEDMNELMKKHKAAVAQASRDmaqmndlqaQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-- 1853
Cdd:pfam10174 432 SNTDTALttlEEalsEKERIIERLKEQREREDRERLE---------ELESLKKENKDLKEKVSALQPELTEKESSLIDlk 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1854 ---KSLVSR---QEAKIRELETRLEFEKTQVKRLENlasRLKETMEKlteERDQRAAAENREKEQNkrLQRqlrdtkeem 1927
Cdd:pfam10174 503 ehaSSLASSglkKDSKLKSLEIAVEQKKEECSKLEN---QLKKAHNA---EEAVRTNPEINDRIRL--LEQ--------- 565
|
570 580 590
....*....|....*....|....*....|....*....
gi 1907082213 1928 sELARKEAEASRKKHELEMDLESL-EAANQSLQADLKLA 1965
Cdd:pfam10174 566 -EVARYKEESGKAQAEVERLLGILrEVENEKNDKDKKIA 603
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1507-1709 |
2.35e-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: 74.42 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1507 LSQAHEETQREKlQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1586
Cdd:COG4942 16 AAQADAAAEAEA-ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1587 LEAKVKDQEEELDEQAGSIQML-EQAKLRLEM------EMERMRQTHSKEMESRDEEVEEARQScQKKLKQMEVQLEEEY 1659
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgRQPPLALLLspedflDAVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1660 EDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQ 1709
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1764-1968 |
2.67e-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: 74.03 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1764 AKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1843
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1844 VEFLEQSMVD--------------KSLVSRQEAK-----IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAA 1904
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqpplALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1905 AENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1968
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1416-1954 |
4.67e-13 |
|
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: 75.26 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1416 ERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRL----GDLQADSDESQRALQQLKkkcQRLTAELQDTKLHLEGQQV 1491
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHG---AFLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1492 RNHELEKKQRRFDSeLSQAHEETQREKLQREKL--QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQ 1569
Cdd:pfam12128 352 WQSELENLEERLKA-LTGKHQDVTAKYNRRRSKikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1570 eSKDEASLAKVKKQLRDLEAKVK-----DQEEELDEQAGSIQMLEQAKLRLEM---EMERMrQTHSKEMESRDEEVEEAR 1641
Cdd:pfam12128 431 -GKLEFNEEEYRLKSRLGELKLRlnqatATPELLLQLENFDERIERAREEQEAanaEVERL-QSELRQARKRRDQASEAL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1642 QSCQKKLKQMEVQLEE-------------EYEDKQKALREK---RELESKLSTLSDQVNQRDFESEKR------LRKDLK 1699
Cdd:pfam12128 509 RQASRRLEERQSALDElelqlfpqagtllHFLRKEAPDWEQsigKVISPELLHRTDLDPEVWDGSVGGelnlygVKLDLK 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1700 RTkallaDAQIMLDHlknNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDiakAKTALEEQLSRLQR 1779
Cdd:pfam12128 589 RI-----DVPEWAAS---EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETF---ARTALKNARLDLRR 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1780 EKNEIQNrleeDQEDMNELMKKHKAAVAQASRDMAQ-----MNDLQAQIEESNKEKQELQ-EKLQALQSQVEFLEQSM-- 1851
Cdd:pfam12128 658 LFDEKQS----EKDKKNKALAERKDSANERLNSLEAqlkqlDKKHQAWLEEQKEQKREARtEKQAYWQVVEGALDAQLal 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1852 VDKSLVSRQEAKIRELETRLEFEKTQVKRL---ENLASRLKETMEKLTE-----ERDQRAAAENRE------KEQNKRLQ 1917
Cdd:pfam12128 734 LKAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIRTLERkieriAVRRQEVLRYFDwyqetwLQRRPRLA 813
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1907082213 1918 RQLRDTKEEMSE----LARKEAEASRKKHELEMDLESLEAA 1954
Cdd:pfam12128 814 TQLSNIERAISElqqqLARLIADTKLRRAKLEMERKASEKQ 854
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1616-1956 |
5.46e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 74.77 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1616 EMEMERMRQTH---SKEMESRD--EEVEEARQScqkklkQMEVQLEEEYEDKQKALREKRELE----SKLSTLSDQVNQR 1686
Cdd:pfam17380 295 KMEQERLRQEKeekAREVERRRklEEAEKARQA------EMDRQAAIYAEQERMAMERERELErirqEERKRELERIRQE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1687 DFESEKRLRKDLKRtkalladaqIMLDHLKNNAPSKREI-AQLKNQLEESEFTcaaavKARKAMEVEMEDLHLQIDDiak 1765
Cdd:pfam17380 369 EIAMEISRMRELER---------LQMERQQKNERVRQELeAARKVKILEEERQ-----RKIQQQKVEMEQIRAEQEE--- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1766 aktALEEQLSRLQREKNEIQNRLEEDqedmnELMKKHkaavaqasrdmaQMNDLQAQIEESNKEKQELqEKLQALQSQVE 1845
Cdd:pfam17380 432 ---ARQREVRRLEEERAREMERVRLE-----EQERQQ------------QVERLRQQEEERKRKKLEL-EKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1846 FLEQSMVDKSLVSRQEAKIRELETRLEFEKtqvkrlenlasRLKETMEKLTEERDQRAAAENREKEQN----KRLQRQLR 1921
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEK-----------EMEERQKAIYEEERRREAEEERRKQQEmeerRRIQEQMR 559
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907082213 1922 DTKEEMSEL--ARKEAEASRKKHELEMDLESLEAANQ 1956
Cdd:pfam17380 560 KATEERSRLeaMEREREMMRQIVESEKARAEYEATTP 596
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1558-2032 |
1.16e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 73.78 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1558 SLEAELQDISSQESKDEAS---LAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMermrqthsKEMESRD 1634
Cdd:PRK01156 177 MLRAEISNIDYLEEKLKSSnleLENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL--------NELSSLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1635 EEVeearqscqkklKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRkDLKRTKALLADAQIMLDH 1714
Cdd:PRK01156 249 DMK-----------NRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIN-DYFKYKNDIENKKQILSN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1715 LKNNAPSKREIAQLKNQLEE--SEFTcaaavkarkAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ 1792
Cdd:PRK01156 317 IDAEINKYHAIIKKLSVLQKdyNDYI---------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1793 EDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM-----------------VDKS 1855
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgEEKS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1856 L---------VSRQEAKIRELEtrlefekTQVKRLENLASRLKETMEKLTEERDQRAAAENRekeQNKRLQRQLRDTKEE 1926
Cdd:PRK01156 468 NhiinhynekKSRLEEKIREIE-------IEVKDIDEKIVDLKKRKEYLESEEINKSINEYN---KIESARADLEDIKIK 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1927 MSELARKEAEASRKKHELE-MDLESLEA------------------ANQSLQADLKLAFKRIGDLQAAIEDEMESDE--N 1985
Cdd:PRK01156 538 INELKDKHDKYEEIKNRYKsLKLEDLDSkrtswlnalavislidieTNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyI 617
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1907082213 1986 EDLINSLQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKG 2032
Cdd:PRK01156 618 DKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS 664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1288-1868 |
2.44e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 72.84 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1288 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGEsasqlLDAETAERLRTEKE-M 1366
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD-----LKLQELQHLKNEGDhL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1367 KELQTQYDALKKQMEVMEMEVMEAR--LIRAAEINGEvDDDDAGGewrLKYERAVREVDFTKKRLQ-QELEDKMEVEQQS 1443
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRqqIENMTQLVGQ-HGRTAGA---MQVEKAQLEKEINDRRLElQEFKILKDKKDAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1444 RRQLERRLGDLQADS-------DESQRALQQLKKKCQRLTAELQDTKLHLEG---------QQVRN--HELEKKQRRFDS 1505
Cdd:pfam15921 620 IRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNksEEMETTTNKLKM 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1506 ELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLE---------------------AELQ 1564
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeamtnankekhflkeeknklsQELS 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1565 DISSQESKDEASLAKVKKQLRDLEAKVKDQEEELD-------EQAGSIQMLEQAKLRLEM-------EMERMRQTHSKEM 1630
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDkaslqfaECQDIIQRQEQESVRLKLqhtldvkELQGPGYTSNSSM 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1631 ESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALRE--KRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLAD 1707
Cdd:pfam15921 860 KPRlLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEdpTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALD 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1708 AQIMLDHLKNNAPSK---REIAQLKNQLEESEFTCAAAVKARKAMevEMEDLHLQIDDIAKAKTALEEQLSR---LQREK 1781
Cdd:pfam15921 940 DRVRDCIIESSLRSDichSSSNSLQTEGSKSSETCSREPVLLHAG--ELEDPSSCFTFPSTASPSVKNSASRsfhSSPKK 1017
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1782 NEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQmnDLQAQ-IEESNKEKQELQEKLQALQSQVEFLE---QSMvdKSLV 1857
Cdd:pfam15921 1018 SPVHSLLTSSAEGSIGSSSQYRSAKTIHSPDSVK--DSQSLpIETTGKTCRKLQNRLESLQTLVEDLQlknQAM--SSMI 1093
|
650
....*....|.
gi 1907082213 1858 SRQEAKIRELE 1868
Cdd:pfam15921 1094 RNQEKRIQKVK 1104
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1751-1912 |
3.38e-12 |
|
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: 68.41 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1751 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ---EDMNELMKKHKAAVAQASRDMAQMNDLQAQIeESN 1827
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1828 KEkqelqekLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1907
Cdd:COG1579 89 KE-------YEALQKEIESLKR------RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*
gi 1907082213 1908 REKEQ 1912
Cdd:COG1579 156 AELEE 160
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1294-1789 |
4.54e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1294 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntGESASQLLDAETAERLRTEKEMKELQTQy 1373
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL--AEAGLDDADAEAVEARREELEDRDEELR- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1374 DALKKQMevmemevmearlIRAAEINGEVddddaggewrlkyERAVREVDftkkrlqqELEDKMEVEQQSRRQLERRLGD 1453
Cdd:PRK02224 328 DRLEECR------------VAAQAHNEEA-------------ESLREDAD--------DLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1454 LQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEkkqrrfdSELSQAHEetqREKLQREKLQREKDMlLA 1533
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR-------EERDELRE---REAELEATLRTARER-VE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1534 EAFSLK---------QQMEEKDL--DIAGFTQKVVSLEAELQDISSQESKDEA------SLAKVKKQLRDLEAKVK---- 1592
Cdd:PRK02224 444 EAEALLeagkcpecgQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEERREdlee 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1593 ---DQEEELDEQAGSIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLE------------E 1657
Cdd:PRK02224 524 liaERRETIEEKRERAEELRERAAELEAEAEEKREA-AAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllaaiA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1658 EYEDKQKALREKRElesKLSTLSDQvnQRDFESEKRLRKDlkrtkalladaqimldhlknnapskreiaQLKNQLEESEF 1737
Cdd:PRK02224 603 DAEDEIERLREKRE---ALAELNDE--RRERLAEKRERKR-----------------------------ELEAEFDEARI 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1738 TCAAAVKARKA-----MEVEMEDLHLQIDDIAKAKTALE---EQLSRLQREKNEIQNRLE 1789
Cdd:PRK02224 649 EEAREDKERAEeyleqVEEKLDELREERDDLQAEIGAVEnelEELEELRERREALENRVE 708
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1285-1931 |
5.17e-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: 71.79 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1285 PLIQVQLSeeqirNKDEEIQQLRSKLEKVEKERNELRLSSD-RLETRISELTSELTDERntgesasqlldaETAERLRTE 1363
Cdd:pfam12128 350 PSWQSELE-----NLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIR------------EARDRQLAV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1364 KEmKELQTQYDALKKQMEVMEMEVMEARL---IRAAEINGEVDDDDAGGEWRLKYERAVREVDftkkRLQQELEDKMEve 1440
Cdd:pfam12128 413 AE-DDLQALESELREQLEAGKLEFNEEEYrlkSRLGELKLRLNQATATPELLLQLENFDERIE----RAREEQEAANA-- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1441 QQSRRQLERRLgdLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdselSQAHEETQREKLQ 1520
Cdd:pfam12128 486 EVERLQSELRQ--ARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKE-------APDWEQSIGKVIS 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1521 REKLQREKDMLLAEAFSLKQQ-------MEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1593
Cdd:pfam12128 557 PELLHRTDLDPEVWDGSVGGElnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1594 QEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR-EL 1672
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARtEK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1673 ESKL----STLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHL----KNNAPSKREIAQLKNQLEESEFTCAAAVK 1744
Cdd:pfam12128 717 QAYWqvveGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIERIAVRRQEVLR 796
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1745 ARKAME----VEMEDLHLQIDDIAKAKTALEEQLSRLQ------REKNEIQNRLEEDQED-MNELMKKHKAAVAQASRDM 1813
Cdd:pfam12128 797 YFDWYQetwlQRRPRLATQLSNIERAISELQQQLARLIadtklrRAKLEMERKASEKQQVrLSENLRGLRCEMSKLATLK 876
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1814 AQMNDLQAQ--IEESNKEKQELQEKLQ----ALQSQVEFLEQSMVDKS---------LVSRQEAKIRELETRLEFEKTQV 1878
Cdd:pfam12128 877 EDANSEQAQgsIGERLAQLEDLKLKRDylseSVKKYVEHFKNVIADHSgsglaetweSLREEDHYQNDKGIRLLDYRKLV 956
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082213 1879 KRLENLASRLKETMEKLTEER------------DQRAAAENREKEQNKRLQRQLRDTK--EEMSELA 1931
Cdd:pfam12128 957 PYLEQWFDVRVPQSIMVLREQvsilgvdltefyDVLADFDRRIASFSRELQREVGEEAffEGVSESA 1023
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1767-1975 |
5.60e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 70.24 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1767 KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL--QALQSQV 1844
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeRARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1845 EFLEQSMVDKSLVSRQeakIRELETRLEFektqvkrLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTK 1924
Cdd:COG3883 98 SGGSVSYLDVLLGSES---FSDFLDRLSA-------LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1925 EEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAA 1975
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1294-1910 |
6.47e-12 |
|
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: 72.01 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1294 EQIRNKDEE-IQQLRSKLEKVEKERNELRLSSD--RLETRISELTSELTDERNTGESASQLLDaETAErlrTEKEmkelQ 1370
Cdd:TIGR01612 1135 EEIKKKSENyIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLN-EIAE---IEKD----K 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1371 TQYDALKKQMEVMEMEVMEARLiraaeinGEVDDDDAGGEWRLK-YERAVREVDFTKKRlQQELEDKMEVEQQSRRQLEr 1449
Cdd:TIGR01612 1207 TSLEEVKGINLSYGKNLGKLFL-------EKIDEEKKKSEHMIKaMEAYIEDLDEIKEK-SPEIENEMGIEMDIKAEME- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1450 rLGDLQADSDESQRALQQLKKKcqrltaELQDtklhlegqqVRNHELEKKQRRF-DSELSQAHEETQREKLQREKLQREK 1528
Cdd:TIGR01612 1278 -TFNISHDDDKDHHIISKKHDE------NISD---------IREKSLKIIEDFSeESDINDIKKELQKNLLDAQKHNSDI 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1529 DMLLAEAFSLKQQMEEKDL-----DIAGFTQKVvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdQEEELDEQ-- 1601
Cdd:TIGR01612 1342 NLYLNEIANIYNILKLNKIkkiidEVKEYTKEI---EENNKNIKDELDKSEKLIKKIKDDINLEECKSK-IESTLDDKdi 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1602 AGSIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEV-------EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELES 1674
Cdd:TIGR01612 1418 DECIKKIKELKNHILSE-ESNIDTYFKNADENNENVlllfkniEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1675 KLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDhLKNN-APSKREIAQLKNQLEE--SEFTCAAAVKARKAMEV 1751
Cdd:TIGR01612 1497 GCKDEADK-NAKAIEKNKELFEQYKKDVTELLNKYSALA-IKNKfAKTKKDSEIIIKEIKDahKKFILEAEKSEQKIKEI 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1752 EMEDLHLQiDDIAKA----KTALEEQLSrlqrekneIQNrLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESn 1827
Cdd:TIGR01612 1575 KKEKFRIE-DDAAKNdksnKAAIDIQLS--------LEN-FENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDT- 1643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1828 kekqELQEKLQALQSQVEFLEqSMVDkslvsrQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1907
Cdd:TIGR01612 1644 ----ELKENGDNLNSLQEFLE-SLKD------QKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIAN 1712
|
...
gi 1907082213 1908 REK 1910
Cdd:TIGR01612 1713 KEE 1715
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1441-1665 |
8.26e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1441 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAheETQREKLQ 1520
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--EKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1521 REKLQREKDM--LLAEAFSLKQQMEEKDL-DIAGFTQKVVSLEAeLQDISSQeskDEASLAKVKKQLRDLEAKVKDQEEE 1597
Cdd:COG4942 97 AELEAQKEELaeLLRALYRLGRQPPLALLlSPEDFLDAVRRLQY-LKYLAPA---RREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1598 LDEQAGSIQMLEQAKLRLEMEMERMRQT---HSKEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKA 1665
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1437-2024 |
8.50e-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: 71.02 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1437 MEVEQQSRRQLERRLGDLQADsDESQRALQQLKKkcQRLTAELQDTKlHLEGQQVRNHELEKKQRRFDS------ELSQA 1510
Cdd:pfam12128 188 MHSKEGKFRDVKSMIVAILED-DGVVPPKSRLNR--QQVEHWIRDIQ-AIAGIMKIRPEFTKLQQEFNTlesaelRLSHL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1511 HEETQREKLQREKLQREKDMLLAEafslkqqmeekdldiagFTQKVVSLEAELQdissqESKDEASLakvkkQLRDLEAK 1590
Cdd:pfam12128 264 HFGYKSDETLIASRQEERQETSAE-----------------LNQLLRTLDDQWK-----EKRDELNG-----ELSAADAA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1591 VKDQEEEL---DEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEE-------YE 1660
Cdd:pfam12128 317 VAKDRSELealEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnnrdiagIK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1661 DKQKALREKRE------------LESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDhlknnapskreiaqL 1728
Cdd:pfam12128 397 DKLAKIREARDrqlavaeddlqaLESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE--------------L 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1729 KNQLEESEFTCAAAVKARKAMEVEMEDLHlqiDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQ 1808
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQ---SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1809 ASRDMAQMNDLQAQIEESNK-EKQELQEKLQALQSQVEF--------LEQSMVDKSLVSRQEAKIR--ELETRLEFEKTQ 1877
Cdd:pfam12128 540 LRKEAPDWEQSIGKVISPELlHRTDLDPEVWDGSVGGELnlygvkldLKRIDVPEWAASEEELRERldKAEEALQSAREK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1878 VKRLENLASRLKETMEKLT-EERDQRAAAENREKEQnKRL---QRQLRDTKEEMSELARKEAEASRKK--HELEMDLESL 1951
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASrEETFARTALKNARLDL-RRLfdeKQSEKDKKNKALAERKDSANERLNSleAQLKQLDKKH 698
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1952 EAANQSLQADLKLAfkRIGDLQAAIEDEMESDENEDLINslQDMVTKYQKKKNKLEG-DSDVDSELEDR-VDGVK 2024
Cdd:pfam12128 699 QAWLEEQKEQKREA--RTEKQAYWQVVEGALDAQLALLK--AAIAARRSGAKAELKAlETWYKRDLASLgVDPDV 769
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1301-1618 |
8.86e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.25 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1301 EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTD-ERNTGESASQLLDAEtaERLRTEKE-MKELQTQYDAL-- 1376
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDaSRKIGEIEKEIEQLE--QEEEKLKErLEELEEDLSSLeq 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1377 KKQMEVMEMEVMEARL---------IRAAEinGEVDDDDAGGEWRlKYERAVREVDFTKKRLQ----------QELEDKM 1437
Cdd:TIGR02169 752 EIENVKSELKELEARIeeleedlhkLEEAL--NDLEARLSHSRIP-EIQAELSKLEEEVSRIEarlreieqklNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1438 EVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQRE 1517
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1518 KLQREKLQREKDMLLAEAFSLKQQMEE-------------KDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL 1584
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEiedpkgedeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL 988
|
330 340 350
....*....|....*....|....*....|....
gi 1907082213 1585 RDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEME 1618
Cdd:TIGR02169 989 DELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1670-1933 |
9.53e-12 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 70.43 E-value: 9.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1670 RELESKLSTLSDQVN--------QRDFESEKRlrkdlKRTKALLADAQIMLDHLKNNAPS-KREIAQLKNQLEEseftca 1740
Cdd:PHA02562 177 RELNQQIQTLDMKIDhiqqqiktYNKNIEEQR-----KKNGENIARKQNKYDELVEEAKTiKAEIEELTDELLN------ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1741 aavkarkaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQR-----EKNEIQNRLEEDQEDMNELMKKHKAavaqasrdmaQ 1815
Cdd:PHA02562 246 --------LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyEKGGVCPTCTQQISEGPDRITKIKD----------K 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1816 MNDLQAQIEESNKEKQELQEKLqalqsqVEFLEQSMvdkslvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKL 1895
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIM------DEFNEQSK-----------KLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907082213 1896 TEERDQRaaaenreKEQNKRLQRQLRDTKEEMSELARK 1933
Cdd:PHA02562 371 QAEFVDN-------AEELAKLQDELDKIVKTKSELVKE 401
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1486-1872 |
9.97e-12 |
|
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: 69.92 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1486 LEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREkdmllaeafsLKQQMEEKDLDIAGFTQKVVSLEAELQD 1565
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE----------LESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1566 ISsqeskdeASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQScQ 1645
Cdd:pfam07888 106 LS-------ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-Q 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1646 KKLKQMEVQLeeeyedkqkalrekRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREI 1725
Cdd:pfam07888 178 AKLQQTEEEL--------------RSLSKEFQELRNSLAQRD-TQVLQLQDTITTLTQKLTTAH---RKEAENEALLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1726 AQLKNQLEESEFTCAA-------AVKARKAMEVEMEDLHLQIDD----IAKAKTALEEQLSRLQREKNEIQNRLEEDQED 1794
Cdd:pfam07888 240 RSLQERLNASERKVEGlgeelssMAAQRDRTQAELHQARLQAAQltlqLADASLALREGRARWAQERETLQQSAEADKDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1795 M----NELMKKHKAAVAQASR------DMAQMNDL-QAQIEESNKEKQELQEKLQALQSQVEFLeqsmvdksLVSRQE-- 1861
Cdd:pfam07888 320 IeklsAELQRLEERLQEERMEreklevELGREKDCnRVQLSESRRELQELKASLRVAQKEKEQL--------QAEKQEll 391
|
410
....*....|.
gi 1907082213 1862 AKIRELETRLE 1872
Cdd:pfam07888 392 EYIRQLEQRLE 402
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1291-1839 |
1.01e-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: 70.54 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1291 LSEEQIRNKDEEIQQLRSKLEKVEKERNElrlsSDRLETRISELTSELTDErnTGESASQLLDAETAERlRTEKEMKELQ 1370
Cdd:pfam05557 66 EAEEALREQAELNRLKKKYLEALNKKLNE----KESQLADAREVISCLKNE--LSELRRQIQRAELELQ-STNSELEELQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1371 TQYDALKKqmevmemevmearliRAAEINGEVDDDDAGGEWRLKYERAVREVDFtkkRLQQELEDKMEVEQQSRRQLerR 1450
Cdd:pfam05557 139 ERLDLLKA---------------KASEAEQLRQNLEKQQSSLAEAEQRIKELEF---EIQSQEQDSEIVKNSKSELA--R 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1451 LGDLQadsdesqRALQQLKKKCQRLTaELQDTKLHLEGQQvrnHELEKKQRRfdselsqahEETQREKLQreKLQREKDM 1530
Cdd:pfam05557 199 IPELE-------KELERLREHNKHLN-ENIENKLLLKEEV---EDLKRKLER---------EEKYREEAA--TLELEKEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1531 LLAEAFSLKQQMEEKDLDIA---GFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK-------DQEEELDE 1600
Cdd:pfam05557 257 LEQELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAqylkkieDLNKKLKR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1601 QAGSIQMLEQAKLRLEMEMERMRQ------------THSKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqKALRE 1668
Cdd:pfam05557 337 HKALVRRLQRRVLLLTKERDGYRAilesydkeltmsNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLS-------VAEEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1669 KRELESKLSTLSDQVnqrdfesekrlrkDLKRTKALLADAqimldhlknnAPSKREIAQLKNQLEESEFTCAAAVKARKA 1748
Cdd:pfam05557 410 LGGYKQQAQTLEREL-------------QALRQQESLADP----------SYSKEEVDSLRRKLETLELERQRLREQKNE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1749 MEVEMED--------------LHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRdma 1814
Cdd:pfam05557 467 LEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFK--- 543
|
570 580
....*....|....*....|....*
gi 1907082213 1815 QMNDLQAQIEESNKEKQELQEKLQA 1839
Cdd:pfam05557 544 EVLDLRKELESAELKNQRLKEVFQA 568
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1555-1961 |
1.05e-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: 70.54 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1555 KVVSLEAELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAgsiqmleQAKLRLEMEMERMRQTHSKEMESRD 1634
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH---KRARIELEKKASALKRQLDRES-------DRNQELQKRIRLLEKREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1635 EEVEEARQsCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFEsekrlrkdLKRTKALLADAQIMLDH 1714
Cdd:pfam05557 73 EQAELNRL-KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELE--------LQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1715 LKNNApskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhLQIDDIAKAKTALEEQLS--------RLQREKNEIQN 1786
Cdd:pfam05557 144 LKAKA---SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ---SQEQDSEIVKNSKSELARipelekelERLREHNKHLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1787 RLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ----------ALQSQVEFLEQSmvDKSL 1856
Cdd:pfam05557 218 ENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQdtglnlrspeDLSRRIEQLQQR--EIVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1857 VSRQ-----------------EAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERD-QRAAAENREKEQN-KRLQ 1917
Cdd:pfam05557 296 KEENssltssarqlekarrelEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgYRAILESYDKELTmSNYS 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1907082213 1918 RQLRDTKEEMSELARK-EAEASRKKHELEMDLESLEAANQSLQAD 1961
Cdd:pfam05557 376 PQLLERIEEAEDMTQKmQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1301-1518 |
1.34e-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: 69.02 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1301 EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQm 1380
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1381 eVMEMEVMEARLIRAAEINGEVD--------DDDAGGEWRLKYERAVREVDFTK----KRLQQELEDKMEVEQQSRRQLE 1448
Cdd:COG4942 99 -LEAQKEELAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARREQaeelRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1449 RRLGDLQadsdESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAHEETQREK 1518
Cdd:COG4942 178 ALLAELE----EERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1290-1731 |
1.44e-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: 70.53 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1290 QLSEEQiRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETR-------ISELTSELTDERNTGESASQLLDAETAE-RLR 1361
Cdd:pfam15921 367 QFSQES-GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1362 TEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAeingeVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ 1441
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV-----VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEIT 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1442 QSRRQLERRLGDLQADSDESQRaLQQLKKKCQRLTAEL--QDTKLHLEGQQVRNHelekkqrrfdSELSQAHEET----Q 1515
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDH-LRNVQTECEALKLQMaeKDKVIEILRQQIENM----------TQLVGQHGRTagamQ 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1516 REKLQREKLQREKDMLLAEAFSLKqqmEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1595
Cdd:pfam15921 590 VEKAQLEKEINDRRLELQEFKILK---DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1596 EELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS-------------------------------C 1644
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkvamgmqkqitakrgqidaL 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1645 QKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTKALLADAQIMLDHLKNNAPSKRE 1724
Cdd:pfam15921 747 QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
....*..
gi 1907082213 1725 IAQLKNQ 1731
Cdd:pfam15921 826 IIQRQEQ 832
|
|
| PDZ_SHANK1_3-like |
cd06746 |
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ... |
223-307 |
1.47e-11 |
|
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.
Pssm-ID: 467228 [Multi-domain] Cd Length: 101 Bit Score: 63.00 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 223 LQRRPTGdFGFSLRRT---------TMLDRAPEGQAYRRVvhfaEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIV 293
Cdd:cd06746 11 LQKGDKG-FGFVLRGAkavgpilefTPTPAFPALQYLESV----DPG-GVADKA-GLKKGDFLLEINGEDVVKASHEQVV 83
|
90
....*....|....
gi 1907082213 294 EMIRQSGDSVRLKV 307
Cdd:cd06746 84 NLIRQSGNTLVLKV 97
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1632-1999 |
1.71e-11 |
|
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: 70.20 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1632 SRDEEVEEARqscqkklkqmEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQrdfesekrLRKDLKRTKALLADAQIM 1711
Cdd:pfam01576 1 TRQEEEMQAK----------EEELQKVKERQQKAESELKELEKKHQQLCEEKNA--------LQEQLQAETELCAEAEEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1712 LDHLKNNAPSKREIAQ-LKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL-------------------- 1770
Cdd:pfam01576 63 RARLAARKQELEEILHeLESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvtteakikkleedill 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1771 -EEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQE--------------LQE 1835
Cdd:pfam01576 143 lEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQElekakrklegestdLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1836 KLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFEKTQ----VKRLENLASRLKETMEKLTEERDQRAAAEnreke 1911
Cdd:pfam01576 223 QIAELQAQIAELRAQL------AKKEEELQAALARLEEETAQknnaLKKIRELEAQISELQEDLESERAARNKAE----- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1912 qnkrlqRQLRDTKEEMSELarkeaeasrkKHELEMDLESlEAANQSLQADLKlafKRIGDLQAAIEDEMESDENEdlins 1991
Cdd:pfam01576 292 ------KQRRDLGEELEAL----------KTELEDTLDT-TAAQQELRSKRE---QEVTELKKALEEETRSHEAQ----- 346
|
....*...
gi 1907082213 1992 LQDMVTKY 1999
Cdd:pfam01576 347 LQEMRQKH 354
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1275-1706 |
1.92e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1275 PWWKLFTTVRPLiQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgESASQLLDA 1354
Cdd:PRK03918 359 ERHELYEEAKAK-KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK---KAIEELKKA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1355 E----TAERLRTEKEMKELQTQYDA-LKKQMEVMEMEVMEARLIRAAEIngEVDDDDAGGEWRLKYERAVREVDFTKKRL 1429
Cdd:PRK03918 435 KgkcpVCGRELTEEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKELR--ELEKVLKKESELIKLKELAEQLKELEEKL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1430 QQELEDKMEVEQQSRRQLERRLGDLQADS---DESQRALQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSE 1506
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIkslKKELEKLEELKKKLAELEKKLDELEEELA-------ELLKELEELGFE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1507 LSQAHEETQREklqREKLQREkdmlLAEAFSLKQQMEEKDldiagftQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1586
Cdd:PRK03918 586 SVEELEERLKE---LEPFYNE----YLELKDAEKELEREE-------KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1587 LEAKVKDQEEEldeqagsiqMLEQAKLRLEMEMERMRqthskemeSRDEEVEEARQSCQKKLKqmevQLEEEYEDKQKAL 1666
Cdd:PRK03918 652 LEKKYSEEEYE---------ELREEYLELSRELAGLR--------AELEELEKRREEIKKTLE----KLKEELEEREKAK 710
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907082213 1667 REKRELESKLSTLsdqvnqrdfeseKRLRKDLKRTKALLA 1706
Cdd:PRK03918 711 KELEKLEKALERV------------EELREKVKKYKALLK 738
|
|
| PDZ |
smart00228 |
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
220-309 |
2.24e-11 |
|
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.
Pssm-ID: 214570 [Multi-domain] Cd Length: 85 Bit Score: 62.01 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPTGdFGFSLRRttmlDRAPEGQAYrrVVHFAEPGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:smart00228 4 LVELEKGGGG-LGFSLVG----GKDEGGGVV--VSSVVPGSPAAKA---GLRVGDVILEVNGTSVEGLTHLEAVDLLKKA 73
|
90
....*....|
gi 1907082213 300 GDSVRLKVQP 309
Cdd:smart00228 74 GGKVTLTVLR 83
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1753-2007 |
2.61e-11 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 67.24 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1753 MEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQE 1832
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1833 LQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFE-KTQVKRLEN---LASRLKETMEKLteerdQRAAAENR 1908
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRqQTEVLSPEEekeLVEKIKELEKEL-----EKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1909 EKEQNKRLQRQLRDTKEEMSELARKEAEASRK--KHELEMDlESLEAANQsLQADLKLAFKRIGDLQAAIEDEMES-DEN 1985
Cdd:COG1340 158 KNEKLKELRAELKELRKEAEEIHKKIKELAEEaqELHEEMI-ELYKEADE-LRKEADELHKEIVEAQEKADELHEEiIEL 235
|
250 260
....*....|....*....|..
gi 1907082213 1986 EDLINSLQDMVTKYQKKKNKLE 2007
Cdd:COG1340 236 QKELRELRKELKKLRKKQRALK 257
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1413-2007 |
5.32e-11 |
|
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: 68.53 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1413 LKYERAVREVDFTKKRLQQ---ELEDKME-VEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQdtklhLEG 1488
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKdnsELELKMEkVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR-----LLN 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1489 QQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISS 1568
Cdd:TIGR00606 340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1569 QESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKL 1648
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1649 KQMEVQLEEeyedkqkalrEKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMldhlKNNAPSKREIAQL 1728
Cdd:TIGR00606 500 KKEVKSLQN----------EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR----KIKSRHSDELTSL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1729 ------KNQLEEsefTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRL------EEDQEDMN 1796
Cdd:TIGR00606 566 lgyfpnKKQLED---WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1797 ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ-ALQSQVEFLEqsmvdksLVSRQEAKIRELETRLEFEK 1875
Cdd:TIGR00606 643 RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQrVFQTEAELQE-------FISDLQSKLRLAPDKLKSTE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1876 TQVKRLEnlasRLKETMEKLTEERDQRAAAENRE-KEQNKRLQRQLRDTKEEMSELARKEA--EASRKKHELEMDLESLE 1952
Cdd:TIGR00606 716 SELKKKE----KRRDEMLGLAPGRQSIIDLKEKEiPELRNKLQKVNRDIQRLKNDIEEQETllGTIMPEEESAKVCLTDV 791
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1953 AANQSLQADLKlafkrigDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLE 2007
Cdd:TIGR00606 792 TIMERFQMELK-------DVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD 839
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1608-2015 |
6.51e-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: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1608 LEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELesklstlsdqvNQRD 1687
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIR-LLEKREAEAEEALREQAEL-----------NRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1688 FESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAK 1767
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1768 TALEEQLSRLQREKNEIQNrLE---EDQEDMNELMKKHKAAVAQasrdMAQMNDLQAQIEESNKEKQELQEKLQALQSQV 1844
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKE-LEfeiQSQEQDSEIVKNSKSELAR----IPELEKELERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1845 EFLEQSMvdkslvSRQE---AKIRELETRLEFEKTQVKRLENLASRLKETM---EKLTEERDQRAAAENREKEQNKRLQR 1918
Cdd:pfam05557 231 EDLKRKL------EREEkyrEEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQREIVLKEENSSLTS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1919 QLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE---DEME----SDENEDLINS 1991
Cdd:pfam05557 305 SARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILEsydKELTmsnySPQLLERIEE 384
|
410 420
....*....|....*....|....
gi 1907082213 1992 LQDMVTKYQKKKNKLEGDSDVDSE 2015
Cdd:pfam05557 385 AEDMTQKMQAHNEEMEAQLSVAEE 408
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1538-2007 |
9.09e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 67.69 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1538 LKQQMEEKDLDIAGFTqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ--EEELDEQAGSIQMLEQAKLRL 1615
Cdd:TIGR00618 158 LKAKSKEKKELLMNLF------PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1616 EMEMERMRQTHSKEmeSRDEEVEEARQSCQKKLKQMEVQLEE------EYEDKQKALREKRELEsKLSTLSDQVNQRDFE 1689
Cdd:TIGR00618 232 REALQQTQQSHAYL--TQKREAQEEQLKKQQLLKQLRARIEElraqeaVLEETQERINRARKAA-PLAAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1690 SEkRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQL--EESEFTCAAAVKA--RKAMEVEMEDLHlQIDDIAK 1765
Cdd:TIGR00618 309 AQ-RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhsQEIHIRDAHEVATsiREISCQQHTLTQ-HIHTLQQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1766 AKTALEEQ-------LSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ 1838
Cdd:TIGR00618 387 QKTTLTQKlqslckeLDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1839 ALQSqvefLEQSMVDKSLVSRQEAKIRELE-TRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQnKRLQ 1917
Cdd:TIGR00618 467 SLKE----REQQLQTKEQIHLQETRKKAVVlARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTY-AQLE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1918 RQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIedEMESDENEDLINSLQDMVT 1997
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT--EKLSEAEDMLACEQHALLR 619
|
490
....*....|
gi 1907082213 1998 KYQKKKNKLE 2007
Cdd:TIGR00618 620 KLQPEQDLQD 629
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1505-1893 |
1.02e-10 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 67.17 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1505 SELSQAHEETQREKLQREKLQRE--KDmLLAEAFS-------LKQQMEEKDLDIAGFTQKVVS---LEAE--LQDISSQE 1570
Cdd:PRK04778 129 QELLESEEKNREEVEQLKDLYRElrKS-LLANRFSfgpaldeLEKQLENLEEEFSQFVELTESgdyVEAReiLDQLEEEL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1571 SKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGSIQMLEQ----AKLRLEMEMERMRQTHSK---EMESRD-EEVEEARQ 1642
Cdd:PRK04778 208 AALEQIMEEIPELLKELQTELPDQLQEL--KAGYRELVEEgyhlDHLDIEKEIQDLKEQIDEnlaLLEELDlDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1643 SCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEkRLR-------KDLKRTKALLADAQIM---- 1711
Cdd:PRK04778 286 EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEID-RVKqsytlneSELESVRQLEKQLESLekqy 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1712 LDHLKNNAPSKREIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLE-- 1789
Cdd:PRK04778 365 DEITERIAEQEIAYSELQEELEEIL-------KQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEks 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1790 ------EDQEDMNELMKKH-KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM----------- 1851
Cdd:PRK04778 438 nlpglpEDYLEMFFEVSDEiEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQLIqyanryrsdne 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907082213 1852 -VDKSLVS--------RQEAKIRELETRLE-FEKTQVKRLENLASRLKETME 1893
Cdd:PRK04778 518 eVAEALNEaerlfreyDYKAALEIIATALEkVEPGVTKRIEDSYEKEKETIR 569
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1635-1860 |
1.33e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.94 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1635 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTKALLADAQIMLDH 1714
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1715 LKNN-APSKREIAQLKNQ------LEESEFtcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ-- 1785
Cdd:COG4942 102 QKEElAELLRALYRLGRQpplallLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEal 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1786 -NRLEEDQEDMNELMKKHKAAVAQASRDMAQmndLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ 1860
Cdd:COG4942 180 lAELEEERAALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1759-2025 |
1.69e-10 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 66.19 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1759 QIDDIAKAKT-ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdmaqmnDLQAQIEESNKEKQELQEKL 1837
Cdd:PHA02562 167 EMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA----------RKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1838 QALQSQVEFLEQSMVDkslVSRQEAKIRELETRLefeKTQVKRLENLASRLKE------TMEKLTEERDQRAAAENREKE 1911
Cdd:PHA02562 237 EELTDELLNLVMDIED---PSAALNKLNTAAAKI---KSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1912 QNKRLqRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDemESDENEDLINS 1991
Cdd:PHA02562 311 LQHSL-EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD--NAEELAKLQDE 387
|
250 260 270
....*....|....*....|....*....|....
gi 1907082213 1992 LQDMVTKYQKKKNKLEGDSDVDSELEDrvDGVKS 2025
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHRGIVTDLLKD--SGIKA 419
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1288-1566 |
1.80e-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: 67.02 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1288 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAE-----TAERLRT 1362
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1363 EKEMKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQqELEDKMEVEQQ 1442
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRI---DLKEQIKSIEKEIENLNGKKE-ELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1443 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQrEKLQRE 1522
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLE 954
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1523 KLQREKDMLLAEAFSLK-------QQMEEKDLDIAGFTQKVVSLEAELQDI 1566
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1654-2041 |
2.47e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.92 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1654 QLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQimldhlknnapskREIAQLKNQLE 1733
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------------EELEQLEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1734 ESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM 1813
Cdd:COG4372 70 QAR-------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1814 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETME 1893
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1894 KLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQ 1973
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1974 AAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDDG 2041
Cdd:COG4372 303 NLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1499-2051 |
3.77e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 65.69 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1499 KQRRFDSELSQAHEETQR---EKLQREKLQREKDMLLAEAFSLKQQMEekdlDIAGFTQKVVSLEAELQDISSQESKDEA 1575
Cdd:PRK01156 136 GQGEMDSLISGDPAQRKKildEILEINSLERNYDKLKDVIDMLRAEIS----NIDYLEEKLKSSNLELENIKKQIADDEK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1576 SLAKVKKQLRDLEAKVKDQEEE---LDEQAGSIQMLEQAKLRLEME---------MERMRQTHSKEMESRDEEVEEARQS 1643
Cdd:PRK01156 212 SHSITLKEIERLSIEYNNAMDDynnLKSALNELSSLEDMKNRYESEiktaesdlsMELEKNNYYKELEERHMKIINDPVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1644 CQKKLKQMEVQLEEEYEDKQKALRE-KRELES------KLSTLsdQVNQRDFESEKRLRKDLKRTKALLADaqimlDHLK 1716
Cdd:PRK01156 292 KNRNYINDYFKYKNDIENKKQILSNiDAEINKyhaiikKLSVL--QKDYNDYIKKKSRYDDLNNQILELEG-----YEMD 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1717 NNApSKREIAQLKNQLEE----SEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ 1792
Cdd:PRK01156 365 YNS-YLKSIESLKKKIEEysknIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELS 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1793 EDMNELMKKHKAAVAQASRDMAQMNDLqaqIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEA-KIRELET- 1869
Cdd:PRK01156 444 RNMEMLNGQSVCPVCGTTLGEEKSNHI---INHYNEKKSRLEEKIREIEIEVKDIDEKIVDlKKRKEYLESeEINKSINe 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1870 --RLEFEKTQVKRLENLASRLKETMEKLT-----------EERDQR----------------AAAENREKEQNKRLQRQL 1920
Cdd:PRK01156 521 ynKIESARADLEDIKIKINELKDKHDKYEeiknrykslklEDLDSKrtswlnalavislidiETNRSRSNEIKKQLNDLE 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1921 RDTKEEMSELARKEA--EASRKKHELEMD--------LESLEAANQSLQADLKLAFKRIGDLQAAIEDEME-----SDEN 1985
Cdd:PRK01156 601 SRLQEIEIGFPDDKSyiDKSIREIENEANnlnnkyneIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsriNDIE 680
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082213 1986 EDLINS---LQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDdgsLKSSRTALN 2051
Cdd:PRK01156 681 DNLKKSrkaLDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGD---LKRLREAFD 746
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1754-1959 |
3.79e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 65.42 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1754 EDLHLQIDDIAKAKTALEEQLsrlqrekNEIQNRLEEDQEDMNELMKKHKAAVAQAsrdmaQMNDLQAQIEESNKEKQEL 1833
Cdd:COG3206 164 QNLELRREEARKALEFLEEQL-------PELRKELEEAEAALEEFRQKNGLVDLSE-----EAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1834 QEKLQALQSQVEFLEQSM----------VDKSLVSRQEAKIRELETRLEFEKTQV-----------KRLENLASRLKETM 1892
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpdalpelLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1893 EKLTEE-RDQRAAAENREKEqnkrLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQ 1959
Cdd:COG3206 312 QRILASlEAELEALQAREAS----LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1421-1921 |
5.87e-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: 64.76 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1421 EVDFTKKRLQQELEDKMEVEQQSRRQLerrlgdlqadsDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQ 1500
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRAR-----------IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1501 RrfdsELSQAHEETQREKLQREKLQREKDMLLAEA----FSLKQQMEEKDLDIAGFTQKVVSLEAELQDIS--------- 1567
Cdd:pfam05557 72 R----EQAELNRLKKKYLEALNKKLNEKESQLADAreviSCLKNELSELRRQIQRAELELQSTNSELEELQerldllkak 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1568 -SQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRL----EMEME----RMRQTHSKEMESRDEEVE 1638
Cdd:pfam05557 148 aSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELaripELEKElerlREHNKHLNENIENKLLLK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1639 EARQSCQKKLKQME------VQLEEEYEDKQKAL---------------------REKRELESKLSTLSDQV-------- 1683
Cdd:pfam05557 228 EEVEDLKRKLEREEkyreeaATLELEKEKLEQELqswvklaqdtglnlrspedlsRRIEQLQQREIVLKEENssltssar 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1684 ----NQRDFESEKR--------LRKDLKRTKALLADAQimldhlKNNAPSKREIAQLKNQLE--ESEFTCAAAVKARKAM 1749
Cdd:pfam05557 308 qlekARRELEQELAqylkkiedLNKKLKRHKALVRRLQ------RRVLLLTKERDGYRAILEsyDKELTMSNYSPQLLER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1750 EVEMEDLhlqIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelMKKHKAAVAQASRDMAQMNDLQAQIEESNKE 1829
Cdd:pfam05557 382 IEEAEDM---TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--ALRQQESLADPSYSKEEVDSLRRKLETLELE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1830 KQELQEKLQALQSQVEFLE-QSMVDKS------LVSRQEAKIRELEtrlefeKTQVKRLENLASRLKETMEKLTEERDQR 1902
Cdd:pfam05557 457 RQRLREQKNELEMELERRClQGDYDPKktkvlhLSMNPAAEAYQQR------KNQLEKLQAEIERLKRLLKKLEDDLEQV 530
|
570
....*....|....*....
gi 1907082213 1903 AAAENREKEQNKRLQRQLR 1921
Cdd:pfam05557 531 LRLPETTSTMNFKEVLDLR 549
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1293-1835 |
6.64e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.92 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1293 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRIS-------ELTSELTDERNTGESASQLL---DAETAERLRT 1362
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINdpvyknrNYINDYFKYKNDIENKKQILsniDAEINKYHAI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1363 EKEMKELQTQYDA-LKKQMevmemevmearliRAAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ 1441
Cdd:PRK01156 328 IKKLSVLQKDYNDyIKKKS-------------RYDDLNNQILELE---GYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1442 QSRRQLERRLGD---LQADSDESQRALQQLKKKCQRLTA----------ELQDTKLHLEGQQV----RNHELEKKQRR-- 1502
Cdd:PRK01156 392 FISEILKIQEIDpdaIKKELNEINVKLQDISSKVSSLNQriralrenldELSRNMEMLNGQSVcpvcGTTLGEEKSNHii 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1503 --FDSELSQAHEETQREKLQREKLQREKDMLLaeafSLKQQMEEKDLD-IAGFTQKVVSLEAELQDissqeskDEASLAK 1579
Cdd:PRK01156 472 nhYNEKKSRLEEKIREIEIEVKDIDEKIVDLK----KRKEYLESEEINkSINEYNKIESARADLED-------IKIKINE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1580 VKKQlrdleakvKDQEEELDEQAGSIQmLEQAKLRLEMEMERMRQTHSKEME---SRDEEVEEARQSCQKKLKQMEVQLE 1656
Cdd:PRK01156 541 LKDK--------HDKYEEIKNRYKSLK-LEDLDSKRTSWLNALAVISLIDIEtnrSRSNEIKKQLNDLESRLQEIEIGFP 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1657 EEYEDKQKALrekRELESKLSTLSDQVNQrdFESEKRLRKDLKRTkalladaqimLDHLKNNAPSKREIAQLKNQLeese 1736
Cdd:PRK01156 612 DDKSYIDKSI---REIENEANNLNNKYNE--IQENKILIEKLRGK----------IDNYKKQIAEIDSIIPDLKEI---- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1737 ftcaaAVKARKaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMnELMKKHKAAVAQAS--RDMA 1814
Cdd:PRK01156 673 -----TSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETL-ESMKKIKKAIGDLKrlREAF 745
|
570 580
....*....|....*....|....*..
gi 1907082213 1815 QMNDLQAQIEES------NKEKQELQE 1835
Cdd:PRK01156 746 DKSGVPAMIRKSasqamtSLTRKYLFE 772
|
|
| PDZ7_MUPP1-PD6_PATJ-like |
cd06671 |
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ... |
221-310 |
7.07e-10 |
|
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of MUPP1 and PDZ domain 6 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467159 [Multi-domain] Cd Length: 96 Bit Score: 58.10 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 221 LELQRRPTGDFGFSL---RrtTMLDRAPEGQAYRRVV--HFAE-PGAGTKDLalgLVPGDRLVEINGQNVENKSRDEIVE 294
Cdd:cd06671 5 VELWREPGKSLGISIvggR--VMGSRLSNGEEIRGIFikHVLEdSPAGRNGT---LKTGDRILEVNGVDLRNATHEEAVE 79
|
90
....*....|....*.
gi 1907082213 295 MIRQSGDSVRLKVQPI 310
Cdd:cd06671 80 AIRNAGNPVVFLVQSL 95
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1417-1965 |
7.60e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.98 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1417 RAVREVDFTKKRLQQELEDKMEVEQQSRRQLERR--LGDLQADSDES----QRALQQLKKKCQRLTA------ELQDTKL 1484
Cdd:PRK04863 534 RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLesLSESVSEARERrmalRQQLEQLQARIQRLAArapawlAAQDALA 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1485 HLEGQQvrNHELEKKQRRfdSELSQAHEETQRE-KLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKV--VSLeA 1561
Cdd:PRK04863 614 RLREQS--GEEFEDSQDV--TEYMQQLLERERElTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFggVLL-S 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1562 EL-QDISSQESKD-EASLAKVKKQL--RDLEAkVKDQEEELDEQAGSIQMLEQAKLRL--------EMEMERMRQTHSKE 1629
Cdd:PRK04863 689 EIyDDVSLEDAPYfSALYGPARHAIvvPDLSD-AAEQLAGLEDCPEDLYLIEGDPDSFddsvfsveELEKAVVVKIADRQ 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1630 ME-SRDEEV----EEARQscqKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQR-------DFESE-KRLRK 1696
Cdd:PRK04863 768 WRySRFPEVplfgRAARE---KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHlavafeaDPEAElRQLNR 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1697 DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESeftcaAAVKARKAMEVEMEDLHLQIDDIAKAK--------- 1767
Cdd:PRK04863 845 RRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPR-----LNLLADETLADRVEEIREQLDEAEEAKrfvqqhgna 919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1768 -TALEEQLSRLQREKNEI---QNRLEEDQEDMNELMKKHKA-----------AVAQASRDMAQMNDLQAQIEESNKEKQE 1832
Cdd:PRK04863 920 lAQLEPIVSVLQSDPEQFeqlKQDYQQAQQTQRDAKQQAFAltevvqrrahfSYEDAAEMLAKNSDLNEKLRQRLEQAEQ 999
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1833 LQEKL--QALQSQVEFLEQSMVDKSLVSRQEAKireLETRLEFEKtqvkRLENLASRLKETME-KLTEERDQRAAAENRE 1909
Cdd:PRK04863 1000 ERTRAreQLRQAQAQLAQYNQVLASLKSSYDAK---RQMLQELKQ----ELQDLGVPADSGAEeRARARRDELHARLSAN 1072
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1910 KEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEmdlESLEAANQSLQADLKLA 1965
Cdd:PRK04863 1073 RSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR---EQVVNAKAGWCAVLRLV 1125
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1293-1738 |
8.09e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1293 EEQIRNKD-EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDE-----------RNTGESASQLLDAETAERL 1360
Cdd:COG4913 329 EAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefaalraeaAALLEALEEELEALEEALA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1361 RTEKEMKELQTQYDALKKQMEV---------MEMEVMEARLIRAAEING----------EVDDDDAggEWRL-------- 1413
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASlerrksnipARLLALRDALAEALGLDEaelpfvgeliEVRPEEE--RWRGaiervlgg 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1414 ---------KYERAVRE----------VDFTKKRLQQELEDKMEVEQQS----------------RRQLERRLGDLQADS 1458
Cdd:COG4913 487 faltllvppEHYAAALRwvnrlhlrgrLVYERVRTGLPDPERPRLDPDSlagkldfkphpfrawlEAELGRRFDYVCVDS 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1459 desqraLQQLKKKCQRLTAELQ----------DTKLHLEGQQV-------RNHELEKKQRRFDSELSQAHEETQREKLQR 1521
Cdd:COG4913 567 ------PEELRRHPRAITRAGQvkgngtrhekDDRRRIRSRYVlgfdnraKLAALEAELAELEEELAEAEERLEALEAEL 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1522 EKLQRekdmlLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDIssqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1601
Cdd:COG4913 641 DALQE-----RREALQRLAEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDEL 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1602 AGSIQMLEQAKLRLEMEMERMRQTHSkemESRDEEVEEARQSCQKKLKQmeVQLEEEYEDKQKALREKRE-LESKLSTLS 1680
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLELRALLEERFAA--ALGDAVERELRENLEERIDaLRARLNRAE 786
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1681 DQVN------QRDFESEKRlrkDLKRTKALLADAQIMLDHLKNNA-PSKRE-IAQLKNQLEESEFT 1738
Cdd:COG4913 787 EELEramrafNREWPAETA---DLDADLESLPEYLALLDRLEEDGlPEYEErFKELLNENSIEFVA 849
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1494-1852 |
8.19e-10 |
|
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: 64.10 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1494 HELEKKQRRFDSELSQ--AHEETQREKLQ--REKLQREKDMLLAEAFS-------LKQQMEEKDLDIAGFTQKVVS---L 1559
Cdd:pfam06160 96 DDIEEDIKQILEELDEllESEEKNREEVEelKDKYRELRKTLLANRFSygpaideLEKQLAEIEEEFSQFEELTESgdyL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1560 EAE--LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGSIQMLEQ----AKLRLEMEMERMRQTHSKEMES- 1632
Cdd:pfam06160 176 EARevLEKLEEETDALEELMEDIPPLYEELKTELPDQLEEL--KEGYREMEEEgyalEHLNVDKEIQQLEEQLEENLALl 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1633 ---RDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQ----------------------VNQRD 1687
Cdd:pfam06160 254 enlELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnkelkeelervqqsytlnenelERVRG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1688 FESE-KRLRKDLKRTKALLADAQI----MLDHLKnnapskreiaQLKNQLEEseftcaaavkarkaMEVEMEDLHLQIDD 1762
Cdd:pfam06160 334 LEKQlEELEKRYDEIVERLEEKEVayseLQEELE----------EILEQLEE--------------IEEEQEEFKESLQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1763 IAKAKTALEEQLSRLQREKNEIQNRLEEDQ-----EDMNELMKKHKAAVAQASRDMAQ----MNDLQAQIEESNKEKQEL 1833
Cdd:pfam06160 390 LRKDELEAREKLDEFKLELREIKRLVEKSNlpglpESYLDYFFDVSDEIEDLADELNEvplnMDEVNRLLDEAQDDVDTL 469
|
410
....*....|....*....
gi 1907082213 1834 QEKLQALQSQVEFLEQSMV 1852
Cdd:pfam06160 470 YEKTEELIDNATLAEQLIQ 488
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1723-1904 |
1.11e-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: 61.09 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1723 REIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkh 1802
Cdd:COG1579 17 SELDRLEHRLKELP-------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1803 kaavaqasRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEKtqvKRLE 1882
Cdd:COG1579 86 --------RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE------LAELEAELAELEAELEEKK---AELD 148
|
170 180
....*....|....*....|..
gi 1907082213 1883 NLASRLKETMEKLTEERDQRAA 1904
Cdd:COG1579 149 EELAELEAELEELEAEREELAA 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1217-1633 |
1.15e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1217 LARLEEQRDEQTSRHLTLFQAacRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRP-LIQVQLSEEQ 1295
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1296 IRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELT-SELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYD 1374
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1375 ALKKQMEVMEMEVMEARLIRAAEINGEV------DDDDAGGEWRLK---------------YERAVREVDFTKKRLQQEL 1433
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALlallglGGSLLSLILTIAgvlflvlgllallflLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1434 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE---LEKKQRRFDSELSQA 1510
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1511 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAgfTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-- 1588
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEed 468
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907082213 1589 -------AKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESR 1633
Cdd:COG4717 469 gelaellQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1293-1894 |
1.19e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.15 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1293 EEQIRNKDEEIQQLRSKLEKVEKernELRLSSDRLEtRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTq 1372
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEK---SHSITLKEIE-RLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAES- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1373 yDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYeravrevDFTKKRlqqELEDKMEVEQQSRRQLERRLG 1452
Cdd:PRK01156 264 -DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKN-------DIENKK---QILSNIDAEINKYHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1453 DLQADSDEsqraLQQLKKKCQRLTAELQDTKLHLEGQQ--VRNHELEKKQRRfdselsqahEETQREKLQREKLQREKDM 1530
Cdd:PRK01156 333 VLQKDYND----YIKKKSRYDDLNNQILELEGYEMDYNsyLKSIESLKKKIE---------EYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1531 LLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR------DL-EAKVKDQEEELDEQAG 1603
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLgEEKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1604 SiqmLEQAKLRLEMEMERM--RQTHSKEMESR--DEEVEEARQScQKKLKQMEVQLeEEYEDKQKALREKrelESKLSTL 1679
Cdd:PRK01156 480 R---LEEKIREIEIEVKDIdeKIVDLKKRKEYleSEEINKSINE-YNKIESARADL-EDIKIKINELKDK---HDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1680 SDQVNQRDFESekrlrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavKARKAMEVEMEDLHLQ 1759
Cdd:PRK01156 552 KNRYKSLKLED-----LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLE----------SRLQEIEIGFPDDKSY 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1760 IDDIAKaktALEEQLSRLQREKNEIQNrLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ- 1838
Cdd:PRK01156 617 IDKSIR---EIENEANNLNNKYNEIQE-NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDd 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1839 ALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLaSRLKETMEK 1894
Cdd:PRK01156 693 AKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDL-KRLREAFDK 747
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1425-1844 |
1.71e-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: 63.39 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1425 TKKRLQQELEDKMEVEQQSRRQLerrlgdlqadSDESQR---ALQQLKKKCQRLT-AELQDTKLHLEGQQVRNhELEKKQ 1500
Cdd:pfam15964 301 TIERLTKERDDLMSALVSVRSSL----------AEAQQRessAYEQVKQAVQMTEeANFEKTKALIQCEQLKS-ELERQK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1501 RRFDSEL-SQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAK 1579
Cdd:pfam15964 370 ERLEKELaSQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1580 VKKQLRDLEAKVKDQEEELdeqagsiqmleqaklrlEMEMERMRQTHSKEMESRDEEVEEARQscqkKLKQMEVQLEEEY 1659
Cdd:pfam15964 450 VCGEMRYQLNQTKMKKDEA-----------------EKEHREYRTKTGRQLEIKDQEIEKLGL----ELSESKQRLEQAQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1660 EDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQLEESEFTC 1739
Cdd:pfam15964 509 QDAARAREECLKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELT------QKMQQMEAQHDKTVNEQ 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1740 AAAVKARKAMEVEMED----LHLQIDDIAKAKTALEEQLSR----LQREKNEIQNRLEEDQED------MNELMK----- 1800
Cdd:pfam15964 583 YSLLTSQNTFIAKLKEecctLAKKLEEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQcvqhgrMHERMKqrlrq 662
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907082213 1801 --KHKAAVAQasrdmaQMNDLQAQIEESNKEKQELQEKLQALQSQV 1844
Cdd:pfam15964 663 ldKHCQATAQ------QLVQLLSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1429-1843 |
1.95e-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: 63.12 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1429 LQQELEDKMEVEQQSrrqLERRLGDLQADSDESQRALQQLKkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELS 1508
Cdd:pfam05667 216 LAAAQEWEEEWNSQG---LASRLTPEEYRKRKRTKLLKRIA---EQLRSAALAGTEATSGASRSAQDLAELLSSFSGSST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1509 QAHEETQREKLQR-EKLQREKDMLLAEAFSLKQQMEEKDLDIAGfTQKVVSLEAELQDISSqeskdeaSLAKVKKQLRDL 1587
Cdd:pfam05667 290 TDTGLTKGSRFTHtEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLES-------SIQELEKEIKKL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1588 EAKVKDQEEELDEQagsiqmlEQAKLRLEMEMERMRQTHsKEMESRDEEVEEARQSCQKKLKQMeVQLEEEYEDKQKAL- 1666
Cdd:pfam05667 362 ESSIKQVEEELEEL-------KEQNEELEKQYKVKKKTL-DLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLi 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1667 REKRELESKLSTlsdqvnqRDFESEKRLR--KDLK-RTKALLADAQimldhlknnapSKRE-IAQLKNQLEE-------S 1735
Cdd:pfam05667 433 EEYRALKEAKSN-------KEDESQRKLEeiKELReKIKEVAEEAK-----------QKEElYKQLVAEYERlpkdvsrS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1736 EFTcaaavkaRKAMEVeMEDLHLQIDDIAKaktALEEQLSrLQREKNEIQNRLEEDQEDMNELM---KKHKAAVAQASRD 1812
Cdd:pfam05667 495 AYT-------RRILEI-VKNIKKQKEEITK---ILSDTKS-LQKEINSLTGKLDRTFTVTDELVfkdAKKDESVRKAYKY 562
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907082213 1813 MAQMNDLQAQ----IEESNK---EKQELQEKLQALQSQ 1843
Cdd:pfam05667 563 LAALHENCEQliqtVEETGTimrEIRDLEEQIETESGK 600
|
|
| PDZ5_MAGI-1_3-like |
cd06735 |
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
222-309 |
3.42e-09 |
|
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467217 [Multi-domain] Cd Length: 84 Bit Score: 55.66 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 222 ELQRRPTGdFGFSLRrttmldrapEGQAYRR----VVHFAEPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMI 296
Cdd:cd06735 5 ELERGPKG-FGFSIR---------GGREYNNmplyVLRLAEDGPAQRD---GrLRVGDQILEINGESTQGMTHAQAIELI 71
|
90
....*....|...
gi 1907082213 297 RQSGDSVRLKVQP 309
Cdd:cd06735 72 RSGGSVVRLLLRR 84
|
|
| PDZ_FRMPD1_3_4-like |
cd06769 |
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ... |
220-307 |
4.04e-09 |
|
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This FRMPD1,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467250 [Multi-domain] Cd Length: 75 Bit Score: 54.94 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPTGDFGFSLRRTTMLdrapegqayrrVVHFAEPGaGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQ 298
Cdd:cd06769 1 TVEIQRDAVLGFGFVAGSERPV-----------VVRSVTPG-GPSE---GkLLPGDQILKINNEPVEDLPRERVIDLIRE 65
|
....*....
gi 1907082213 299 SGDSVRLKV 307
Cdd:cd06769 66 CKDSIVLTV 74
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1320-1849 |
4.10e-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: 62.28 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1320 LRLSSDR------LETRI-----SELTSELTD---ERNTG-ESASQLLDAETAERLRTEKEMKELQTQYDaLKKQMEVME 1384
Cdd:COG3096 187 LRSSSDRskfyrlIEASLyggisSAITRSLRDyllPENSGvRKAFQDMEAALRENRMTLEAIRVTQSDRD-LFKHLITEA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1385 MEVMEARLIRAAEingevddddaggEWRLKYERAV--REVDFTKKRLQQELEDKM-----EVEQQSRRQ--LERrlgDLQ 1455
Cdd:COG3096 266 TNYVAADYMRHAN------------ERRELSERALelRRELFGARRQLAEEQYRLvemarELEELSAREsdLEQ---DYQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1456 ADSDESQRALQ--QLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDML-- 1531
Cdd:COG3096 331 AASDHLNLVQTalRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqt 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1532 -----------LAEAfslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQeskdeaslakvkkqLRDLEAKVKDQEEELDE 1600
Cdd:COG3096 411 raiqyqqavqaLEKA---RALCGLPDLTPENAEDYLAAFRAKEQQATEE--------------VLELEQKLSVADAARRQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1601 QAGSIQMLEqaklRLEMEMERmrqthSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLS 1680
Cdd:COG3096 474 FEKAYELVC----KIAGEVER-----SQAWQTARELLRRYRS--QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFC 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1681 dqvnqrdfeseKRLRKDLkrtkallaDAQIMLDHLKnnapskreiAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQI 1760
Cdd:COG3096 543 -----------QRIGQQL--------DAAEELEELL---------AELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1761 D---DIAKAKTALEEQLSRLQREKNEiqnrleedqedmnelmkkhkaAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL 1837
Cdd:COG3096 595 KelaARAPAWLAAQDALERLREQSGE---------------------ALADSQEVTAAMQQLLEREREATVERDELAARK 653
|
570
....*....|..
gi 1907082213 1838 QALQSQVEFLEQ 1849
Cdd:COG3096 654 QALESQIERLSQ 665
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1410-1751 |
4.20e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.06 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1410 EWRLKYE-RAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRlgdlqadsdeSQRALQQLKKKCQRltaELQDTKLHLEG 1488
Cdd:pfam17380 255 EYTVRYNgQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM----------EQERLRQEKEEKAR---EVERRRKLEEA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1489 QQVRNHELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMLLAEAFSLK-QQMEEKDLDIAGFTQKVVSLEAELQDI 1566
Cdd:pfam17380 322 EKARQAEMDRQAAIYAEQERMAMErERELERIRQEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1567 SSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQagsIQMLEQAKLRlemEMERMRQTHSKEMES----RDEEVEEARQ 1642
Cdd:pfam17380 402 RKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE---VRRLEEERAR---EMERVRLEEQERQQQverlRQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1643 SCQKKLKQMEVQLEEEY----------EDKQKALREKR-------ELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALL 1705
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQrrkilekeleERKQAMIEEERkrkllekEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907082213 1706 ADAQIMLDHLKNNAPSKREiAQLKNQLEESEftcaaavKARKAMEV 1751
Cdd:pfam17380 556 EQMRKATEERSRLEAMERE-REMMRQIVESE-------KARAEYEA 593
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1300-1921 |
4.82e-09 |
|
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: 61.76 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1300 DEEIQQLRSKLEKVEKERNELRLSSDRLETRIS--ELTSELTDE-----------RNTGESASQLLDAETAERLRTEKEM 1366
Cdd:pfam10174 115 EENFRRLQSEHERQAKELFLLRKTLEEMELRIEtqKQTLGARDEsikkllemlqsKGLPKKSGEEDWERTRRIAEAEMQL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1367 KELQTQYD-------ALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgewrlKYERAVREVDFTKKRLQQELEDKMEV 1439
Cdd:pfam10174 195 GHLEVLLDqkekeniHLREELHRRNQLQPDPAKTKALQTVIEMKDTKIS-----SLERNIRDLEDEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1440 EQQSRRQLE----------RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEgqqVRNHELEKKQRR---FDSE 1506
Cdd:pfam10174 270 REEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIE---VLKESLTAKEQRaaiLQTE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1507 ---LSQAHEETQR------EKLQRekLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDissqesKDeasl 1577
Cdd:pfam10174 347 vdaLRLRLEEKESflnkktKQLQD--LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD------KD---- 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1578 akvkKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQsCQKKLKQMEVQLEE 1657
Cdd:pfam10174 415 ----KQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKK-ENKDLKEKVSALQP 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1658 EYEDKQKALREKRELESKLST----LSDQVNQRDFESEKRlRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQL- 1732
Cdd:pfam10174 490 ELTEKESSLIDLKEHASSLASsglkKDSKLKSLEIAVEQK-KEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVa 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1733 ---EESEfTCAAAVKARKAM--EVEMEDlhlqiDDIAKAKTALEEQLSRLQREkneiQNRLEEDQEDMNELMKKHKAAVA 1807
Cdd:pfam10174 569 rykEESG-KAQAEVERLLGIlrEVENEK-----NDKDKKIAELESLTLRQMKE----QNKKVANIKHGQQEMKKKGAQLL 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1808 QASR---DMAQMNDLQAQIEES----NKEKQELQEKLQALQSQVEFLEQSmvDKSLVSRQEAKIRELETRLEF------- 1873
Cdd:pfam10174 639 EEARrreDNLADNSQQLQLEELmgalEKTRQELDATKARLSSTQQSLAEK--DGHLTNLRAERRKQLEEILEMkqealla 716
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1907082213 1874 ---EK-TQVKRLENLASRLKETMEKLteerdqraAAENREKEqnkRLQRQLR 1921
Cdd:pfam10174 717 aisEKdANIALLELSSSKKKKTQEEV--------MALKREKD---RLVHQLK 757
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1286-1689 |
5.30e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 61.45 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1286 LIQVQLsEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgESASQLLDAETaerlRTEKE 1365
Cdd:pfam07888 31 LLQNRL-EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK---EELRQSREKHE----ELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1366 MKELQTQYDALKKQMevmemevmearliraaeingevdddDAGGEWRLKYERAVREVDFTKKRLQQ---ELEDKMEVEQQ 1442
Cdd:pfam07888 103 YKELSASSEELSEEK-------------------------DALLAQRAAHEARIRELEEDIKTLTQrvlERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1443 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETqreklqre 1522
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKE-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1523 klqrekdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQA 1602
Cdd:pfam07888 230 ----------AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1603 GSIQMlEQAKLRLEMEMERMR-QTHSKEMESRDEEVEEARQSCQKklkqMEVQLEEEYEDKQKALRE-KRELESKLSTLs 1680
Cdd:pfam07888 300 ARWAQ-ERETLQQSAEADKDRiEKLSAELQRLEERLQEERMEREK----LEVELGREKDCNRVQLSEsRRELQELKASL- 373
|
....*....
gi 1907082213 1681 dQVNQRDFE 1689
Cdd:pfam07888 374 -RVAQKEKE 381
|
|
| PDZ4_MAGI-1_3-like |
cd06734 |
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
270-309 |
5.54e-09 |
|
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467216 [Multi-domain] Cd Length: 84 Bit Score: 54.93 E-value: 5.54e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907082213 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06734 45 LKVGDRILAVNGISILNLSHGDIVNLIKDSGLSVTLTIVP 84
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1780-2018 |
6.08e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1780 EKNEIQNRLEEDQEDMNELMKKHKAAVaQASRdmaQMNDLQaQIEESNKEKQELQEKLQALQSQVEFLEqsmvdkslVSR 1859
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALE-DARE---QIELLE-PIRELAERYAAARERLAELEYLRAALR--------LWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1860 QEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERD----QRAAAENREKEQnkrLQRQLRDTKEEMSELARKEA 1935
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDeleaQIRGNGGDRLEQ---LEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1936 EASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMesDENEDLINSLQDMVTKYQKKKNKLE-GDSDVDS 2014
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL--AEAEAALRDLRRELRELEAEIASLErRKSNIPA 440
|
....
gi 1907082213 2015 ELED 2018
Cdd:COG4913 441 RLLA 444
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1726-1990 |
6.41e-09 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 59.93 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1726 AQLKNQLEESEFTCAAAVKARKAM-EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedmnELMKKHKA 1804
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED------ELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1805 AvaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFEKTQVK----R 1880
Cdd:pfam00038 102 E--------NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN---------HEEEVRELQAQVSDTQVNVEmdaaR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1881 LENLASRLKETMEKLTEE-RDQRAAAENREKEQNKRLQRQ-------LRDTKEEMSELarkeaeaSRKKHELEMDLESLE 1952
Cdd:pfam00038 165 KLDLTSALAEIRAQYEEIaAKNREEAEEWYQSKLEELQQAaarngdaLRSAKEEITEL-------RRTIQSLEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1953 AANQSLQA-----------DLKLAFKRIGDLQAA---IEDEMES--DENEDLIN 1990
Cdd:pfam00038 238 KQKASLERqlaeteeryelQLADYQELISELEAElqeTRQEMARqlREYQELLN 291
|
|
| PDZ |
pfam00595 |
PDZ domain; PDZ domains are found in diverse signaling proteins. |
220-308 |
9.66e-09 |
|
PDZ domain; PDZ domains are found in diverse signaling proteins.
Pssm-ID: 395476 [Multi-domain] Cd Length: 81 Bit Score: 54.21 E-value: 9.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPTGDFGFSLRRttMLDRAPEGQAYRRVVHFaepGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:pfam00595 1 QVTLEKDGRGGLGFSLKG--GSDQGDPGIFVSEVLPG---GAAEAG---GLKVGDRILSINGQDVENMTHEEAVLALKGS 72
|
....*....
gi 1907082213 300 GDSVRLKVQ 308
Cdd:pfam00595 73 GGKVTLTIL 81
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1719-1914 |
9.70e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1719 APSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNEL 1798
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1799 ---MKKHKAAVAQ-----------------------ASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV 1852
Cdd:COG3883 92 araLYRSGGSVSYldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 1853 D-KSLVSRQEAKIRELETRlefEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNK 1914
Cdd:COG3883 172 ElEAQQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1584-1934 |
1.59e-08 |
|
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: 59.16 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1584 LRDLEAKV------KDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEE-VEEARQSCQKKLKQMEVQLE 1656
Cdd:pfam13868 8 LRELNSKLlaakcnKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEErKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1657 EEYEDKQKALREKRELesklstLSDQVNQRDFESEKRLRKDLKRTKAlladaqimldhlknnapsKREIAQLKNQLEESe 1736
Cdd:pfam13868 88 KRQEEYEEKLQEREQM------DEIVERIQEEDQAEAEEKLEKQRQL------------------REEIDEFNEEQAEW- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1737 ftcaaavKARKAMEVEMEDlhLQIDDIAKAKTALEEQLSRLQ----REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRD 1812
Cdd:pfam13868 143 -------KELEKEEEREED--ERILEYLKEKAEREEEREAEReeieEEKEREIARLRAQQEKAQDEKAERDELRAKLYQE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1813 MAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV-----DKSLVSRQEAKIRELEtRLEFEKTQVKRLENLasR 1887
Cdd:pfam13868 214 EQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAeeaerEEEEFERMLRKQAEDE-EIEQEEAEKRRMKRL--E 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907082213 1888 LKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKE 1934
Cdd:pfam13868 291 HRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1669-1934 |
1.65e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 60.31 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1669 KRELESKLSTLSDQvnqRDFESEKrlrkdlkrtKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaAAVKARKA 1748
Cdd:PRK11281 38 EADVQAQLDALNKQ---KLLEAED---------KLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ------APAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1749 MEvEMEDlhLQIDDIAKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESN 1827
Cdd:PRK11281 100 QA-ELEA--LKDDNDEETRETLSTLsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1828 K---------------EKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELET----RLEfekTQVKRLENLAS-- 1886
Cdd:PRK11281 177 NllkggkvggkalrpsQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTariqRLE---HQLQLLQEAINsk 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1887 RLKETMEKLTEERDQRAAAEN-------REKEQNKRLQRQLRDTKEEMSELARKE 1934
Cdd:PRK11281 254 RLTLSEKTVQEAQSQDEAARIqanplvaQELEINLQLSQRLLKATEKLNTLTQQN 308
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1292-1965 |
2.26e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1292 SEEQIRNKDEEIQQLRSKLEKVEKERNEL----RLSSDRL------------ETRISELTSELTDERNTGESASQLLDAE 1355
Cdd:PRK04863 298 SRRQLAAEQYRLVEMARELAELNEAESDLeqdyQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1356 TAER----LRTEKEMKELQTQ-------YDALkkQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAvREVDF 1424
Cdd:PRK04863 378 QEENearaEAAEEEVDELKSQladyqqaLDVQ--QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQA-KEQEA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1425 TKKRLQqeLEDKMEVEQQSRRQLERRLGDLQADSDESQR--ALQQLKKKCQRL-TAELQDTKLhlegQQVRNHElekkqr 1501
Cdd:PRK04863 455 TEELLS--LEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRseAWDVARELLRRLrEQRHLAEQL----QQLRMRL------ 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1502 rfdSELSQAHEETQR-EKLQREKLQREKDMLLAEAFsLKQQMEEkdldiagftqkvvsLEAELQDISSQeskdeaslakv 1580
Cdd:PRK04863 523 ---SELEQRLRQQQRaERLLAEFCKRLGKNLDDEDE-LEQLQEE--------------LEARLESLSES----------- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1581 KKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRdEEVEEARQSCQKKLKQMEVQlEEEYE 1660
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-QDVTEYMQQLLERERELTVE-RDELA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1661 dkqkalREKRELESKLSTLSdqvnQRDFESEKRLRKDLKRTKA-LLAD--AQIMLDhlknNAP----------------- 1720
Cdd:PRK04863 652 ------ARKQALDEEIERLS----QPGGSEDPRLNALAERFGGvLLSEiyDDVSLE----DAPyfsalygparhaivvpd 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1721 ---SKREIAQLKNQLEE------------------SEFTCAAAVK-----------------ARKAMEVEMEDLHLQIDD 1762
Cdd:PRK04863 718 lsdAAEQLAGLEDCPEDlyliegdpdsfddsvfsvEELEKAVVVKiadrqwrysrfpevplfGRAAREKRIEQLRAEREE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1763 IAkaktaleEQLSRLQREKNEIQnRLeedQEDMNELMKKHkAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQS 1842
Cdd:PRK04863 798 LA-------ERYATLSFDVQKLQ-RL---HQAFSRFIGSH-LAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRS 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1843 QVEFLEQSMV-------------DKSLVSRQEAkIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEnRE 1909
Cdd:PRK04863 866 QLEQAKEGLSalnrllprlnllaDETLADRVEE-IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLK-QD 943
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082213 1910 KEQNKRLQRQLRDTKEEMSEL-ARKEAEASrkkHELEMDLESLEAANQSLQADLKLA 1965
Cdd:PRK04863 944 YQQAQQTQRDAKQQAFALTEVvQRRAHFSY---EDAAEMLAKNSDLNEKLRQRLEQA 997
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1667-2021 |
2.58e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1667 REKRELESKLSTLSDQVNQRDfesEKRLRKDLKRTKALLADAQIMLDHLKnnapSKREIAqlKNQLEESEFTCAAAVKAR 1746
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKE---EKDLHERLNGLESELAELDEEIERYE----EQREQA--RETRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1747 KamevEMEDLHLQIDDIAKAKTALEeqlsrlqREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEES 1826
Cdd:PRK02224 251 E----ELETLEAEIEDLRETIAETE-------REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1827 NKEKQELQEKL-QALQSQVEFLEQsmvdkslVSRQEAKIRELETRLEFEKTQVKRLEnlaSRLKETMEKLTEERDQRAAA 1905
Cdd:PRK02224 320 EDRDEELRDRLeECRVAAQAHNEE-------AESLREDADDLEERAEELREEAAELE---SELEEAREAVEDRREEIEEL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1906 ENREKEQNKRLQR---QLRDTKEEMSELARKEAEASRKKHELEMDLESLE---AANQSLQADLKLA-----FKRIGDLQA 1974
Cdd:PRK02224 390 EEEIEELRERFGDapvDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEAGKCPecgqpVEGSPHVET 469
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907082213 1975 AIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELEDRVD 2021
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEE 516
|
|
| PDZ_SNX27-like |
cd23070 |
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ... |
231-307 |
2.62e-08 |
|
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SNX27-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467283 [Multi-domain] Cd Length: 93 Bit Score: 53.57 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 231 FGFSLRRTTMLD---RAPEGQAYRRVVHFA---EPGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVR 304
Cdd:cd23070 12 FGFNVRGQVSEGgqlRSINGELYAPLQHVSavlEGGAADKA---GVRKGDRILEVNGVNVEGATHKQVVDLIKSGGDELT 88
|
...
gi 1907082213 305 LKV 307
Cdd:cd23070 89 LTV 91
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1722-1938 |
2.78e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1722 KREIAQLKNQLEESEftcaAAVKARKAmEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedMNELMKK 1801
Cdd:COG3206 181 EEQLPELRKELEEAE----AALEEFRQ-KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1802 HKAAVAQASRDmAQMNDLQAQIEESNKEKQELQEKL-------QALQSQVEFLEQSmvdksLVSRQEAKIRELETRLEFE 1874
Cdd:COG3206 252 GPDALPELLQS-PVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-----LQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1875 KTQVKRLENLASRLKETMEKLTEERDQRAaaenrekeqnkRLQRQLRDTKEEMSELARKEAEAS 1938
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR-----------RLEREVEVARELYESLLQRLEEAR 378
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1459-1673 |
3.41e-08 |
|
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: 56.21 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1459 DESQRALQQLKK----KCQRLTAELQDTKLHLEGQQVRNHELEKKqrrfdselSQAHEETQREKlqreklQREKDMLLAE 1534
Cdd:pfam15665 10 DEHEAEIQALKEaheeEIQQILAETREKILQYKSKIGEELDLKRR--------IQTLEESLEQH------ERMKRQALTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1535 AFSLKQQMEEKDL-DIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL-RDLEAKVKDQEEELDEQAGSIQMLEQAK 1612
Cdd:pfam15665 76 FEQYKRRVEERELkAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFeQEKRKALEELRAKHRQEIQELLTTQRAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1613 LRLEM-EMERMRQTHSKEMESRDEEVEEarqscqkkLKQMEVQLEEEYEDK---QKALREkRELE 1673
Cdd:pfam15665 156 SASSLaEQEKLEELHKAELESLRKEVED--------LRKEKKKLAEEYEQKlskAQAFYE-RELE 211
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1536-1920 |
3.75e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 58.69 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1536 FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ-------EEELDEQAGSIQML 1608
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANrfsfgpaLDELEKQLENLEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1609 -------------EQAK---LRLEMEMERMRQThskeMesrdEEVEEARQSCQKKLKQmevQLEEEYEDKQKALREKREL 1672
Cdd:PRK04778 181 fsqfveltesgdyVEAReilDQLEEELAALEQI----M----EEIPELLKELQTELPD---QLQELKAGYRELVEEGYHL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1673 ESKlstlsdqvnqrDFESE-KRLRKDLKRTKALLADAQimLDHLK-NNAPSKREIAQLKNQLEeseftcaAAVKARKAME 1750
Cdd:PRK04778 250 DHL-----------DIEKEiQDLKEQIDENLALLEELD--LDEAEeKNEEIQERIDQLYDILE-------REVKARKYVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1751 VEMEDLHLQIDDIAKAKTALEEQLSRLQ-----------------REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM 1813
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEEIDRVKqsytlneselesvrqleKQLESLEKQYDEITERIAEQEIAYSELQEELEEIL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1814 AQMNDLQAQIEESN-------KEKQELQEKLQALQSQVE----FLEQS---------MVDKSLVSRQeakIRELETRLE- 1872
Cdd:PRK04778 390 KQLEEIEKEQEKLSemlqglrKDELEAREKLERYRNKLHeikrYLEKSnlpglpedyLEMFFEVSDE---IEALAEELEe 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082213 1873 --FEKTQVKRLENLASRLKETMEKLTEE-RDQRAAAE------NREKEQNKRLQRQL 1920
Cdd:PRK04778 467 kpINMEAVNRLLEEATEDVETLEEETEElVENATLTEqliqyaNRYRSDNEEVAEAL 523
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1663-1839 |
5.09e-08 |
|
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: 56.09 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1663 QKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESEFTCAAA 1742
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELE-DELAALEARLEAAKTELEDLEKEIKRLEL------EIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1743 VKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdmaqmnDLQ 1820
Cdd:COG1579 86 RNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA----------ELE 155
|
170
....*....|....*....
gi 1907082213 1821 AQIEESNKEKQELQEKLQA 1839
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1499-1927 |
5.47e-08 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 58.33 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1499 KQRRFDSELSQAheETQREKLQ----REKLQREKDMLLA-EAFSLKQQMEEKDLDIAgfTQKVVSLEAELQDIssQESKD 1573
Cdd:pfam06160 4 LRKKIYKEIDEL--EERKNELMnlpvQEELSKVKKLNLTgETQEKFEEWRKKWDDIV--TKSLPDIEELLFEA--EELND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1574 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQaklrlememermrqthsKEMESRdEEVEEAR---QSCQKKLKQ 1650
Cdd:pfam06160 78 KYRFKKAKKALDEIEELLDDIEEDIKQILEELDELLE-----------------SEEKNR-EEVEELKdkyRELRKTLLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1651 MEVQLEEEYEDKQKALrekRELESKLSTLSDQVNQRDFESEK----RLRKDLKRTKALLADAQIMLDHLKNNAPskREIA 1726
Cdd:pfam06160 140 NRFSYGPAIDELEKQL---AEIEEEFSQFEELTESGDYLEARevleKLEEETDALEELMEDIPPLYEELKTELP--DQLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1727 QLKN---QLEESEFtcaaaVKARKAMEVEMEDLHlqiDDIAKAKTALEE-QLSRLQREKNEIQNRLEEDQEDM------- 1795
Cdd:pfam06160 215 ELKEgyrEMEEEGY-----ALEHLNVDKEIQQLE---EQLEENLALLENlELDEAEEALEEIEERIDQLYDLLekevdak 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1796 NELMKKHKAAVAQASRDMAQMNDLQAQIEESNK----------EKQELQEKLQALQSQVEFLEQSMVDKSLV-SRQEAKI 1864
Cdd:pfam06160 287 KYVEKNLPEIEDYLEHAEEQNKELKEELERVQQsytlneneleRVRGLEKQLEELEKRYDEIVERLEEKEVAySELQEEL 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1865 RELETRLE-FEKTQVKrlenlasrLKETMEKLTEErdqraaaENREKEQNKRLQRQLRDTKEEM 1927
Cdd:pfam06160 367 EEILEQLEeIEEEQEE--------FKESLQSLRKD-------ELEAREKLDEFKLELREIKRLV 415
|
|
| cpPDZ_CPP-like |
cd06782 |
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ... |
269-309 |
7.32e-08 |
|
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.
Pssm-ID: 467623 [Multi-domain] Cd Length: 88 Bit Score: 52.10 E-value: 7.32e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1907082213 269 GLVPGDRLVEINGQNVENKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:cd06782 31 GIKPGDVIVAVDGESVRGMSLDEVVKLLRgPKGTKVKLTIRR 72
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1294-2024 |
7.90e-08 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 58.30 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1294 EQIRNKDEEIQQLRSKLEKVEKER------NELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAeRLRTEKEMK 1367
Cdd:PTZ00440 1190 EEIESYKKDIDQVKKNMSKERNDHlttfeyNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEI-KLQVFSYLQ 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1368 ELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEwrlKYER-AVREVDFTKkRLQQELEDKMEVEQQSRRQ 1446
Cdd:PTZ00440 1269 QVIKENNKMENALHEIKNMYEFLISIDSEKILKEILNSTKKAE---EFSNdAKKELEKTD-NLIKQVEAKIEQAKEHKNK 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1447 LERRLGDLQADSDesqraLQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAH------------EET 1514
Cdd:PTZ00440 1345 IYGSLEDKQIDDE-----IKKIEQIKEEISNKRKEINKYLS-------NIKSNKEKCDLHVRNASrgkdkidflnkhEAI 1412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1515 QREKLQREKLQREKDML------LAEAFSLKQQMEEKDLDIAGFTQKVVSLeaeLQD--ISSQESKDEaslaKVKKQLRD 1586
Cdd:PTZ00440 1413 EPSNSKEVNIIKITDNInkckqySNEAMETENKADENNDSIIKYEKEITNI---LNNssILGKKTKLE----KKKKEATN 1485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1587 LEAKVKDQEEELDEQAGSIQmleqaklrlememERMRQTHSKEMESRDEEV------EEARQSCQKKLKQMEVQLEEEYE 1660
Cdd:PTZ00440 1486 IMDDINGEHSIIKTKLTKSS-------------EKLNQLNEQPNIKREGDVlnndksTIAYETIQYNLGRVKHNLLNILN 1552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1661 DKQKA---LREKRELESKLSTLSDQVNQRDFES-EKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEES- 1735
Cdd:PTZ00440 1553 IKDEIetiLNKAQDLMRDISKISKIVENKNLENlNDKEADYVKYLDNILKEKQLMEAEYKKLNEIYSDVDNIEKELKKHk 1632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1736 --------EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL-------EEQLSRLQREKNEIQNRLEEDQEDMNELMK 1800
Cdd:PTZ00440 1633 knyeigllEKVIEINKNIKLYMDSTKESLNSLVNNFSSLFNNFylnkyniNENLEKYKKKLNEIYNEFMESYNIIQEKMK 1712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1801 KhkaavaqASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsMVDKSLVSRQEAKIRELETRLEFEKTQVKR 1880
Cdd:PTZ00440 1713 E-------VSNDDVDYNEAKTLREEAQKEEVNLNNKEEEAKKYLNDIKK-QESFRFILYMKEKLDELSKMCKQQYNIVDE 1784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1881 LENLASRLKETMEKLTEErDQRAAAENREKEQNKRLQRQLRDT-KEE-------------------MSELARKE--AEAS 1938
Cdd:PTZ00440 1785 GYNYIKKKIEYIKTLNDE-NNLSDSLNQAEDKNKEVANLTHYTnKNEaknllghvvksanfigikiMTGLQPTEltPDAS 1863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1939 RKK-------HELEMDLESLEAANQSLQAD---------------LKLAF---KRIGDLQAAIEDEMESDENEDLINSLQ 1993
Cdd:PTZ00440 1864 LETapeltfeSENNSDLELDHLSSNKNELDvykniqdayksslqiLKYSDdidKKQRDCNKLVEDGNEIYLKSTAINELK 1943
|
810 820 830
....*....|....*....|....*....|.
gi 1907082213 1994 DMVTKYQKKKNKLEGDSDVDSELEDRVDGVK 2024
Cdd:PTZ00440 1944 NMINSVKNKESAISNKIDNVSNKLSELNKIT 1974
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1645-2019 |
1.06e-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: 57.27 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1645 QKKLKQMEVQ-LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLR--KDLKRTKALLadaQIMLDHLKNNAPS 1721
Cdd:COG5185 165 FGKLTQELNQnLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGseSTLLEKAKEI---INIEEALKGFQDP 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1722 KREIAQLKNQLEESEFtcaaAVKARKamEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE-----DQEDMN 1796
Cdd:COG5185 242 ESELEDLAQTSDKLEK----LVEQNT--DLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSidikkATESLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1797 ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqSMVDKSLVSRQEAKIRELETRLEFEKT 1876
Cdd:COG5185 316 EQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIE----NIVGEVELSKSSEELDSFKDTIESTKE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1877 ----QVKRLENLASRLKETMEKLTEERDQraaaenrekeQNKRLQRQLRDTKEEMSELARK--EAEASRKKHELEMDLES 1950
Cdd:COG5185 392 sldeIPQNQRGYAQEILATLEDTLKAADR----------QIEELQRQIEQATSSNEEVSKLlnELISELNKVMREADEES 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1951 LE-------AANQSLQADLKLAFKRIGDLQAAI-----EDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELED 2018
Cdd:COG5185 462 QSrleeaydEINRSVRSKKEDLNEELTQIESRVstlkaTLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
.
gi 1907082213 2019 R 2019
Cdd:COG5185 542 E 542
|
|
| PDZ_tamalin_CYTIP-like |
cd06713 |
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ... |
223-307 |
1.22e-07 |
|
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This tamalin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467197 [Multi-domain] Cd Length: 91 Bit Score: 51.47 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 223 LQRRPTGDFGF-------------SLRRTTMLDRapegqayrrvVHFAEPGagtkDLAlGLVPGDRLVEINGQNVENKSR 289
Cdd:cd06713 8 LEKQDNETFGFeiqtyglhhknsnEVEMCTYVCR----------VHEDSPA----YLA-GLTAGDVILSVNGVSVEGASH 72
|
90
....*....|....*...
gi 1907082213 290 DEIVEMIRQSGDSVRLKV 307
Cdd:cd06713 73 QEIVELIRSSGNTLRLET 90
|
|
| PDZ_SYNJ2BP-like |
cd06709 |
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ... |
220-308 |
1.41e-07 |
|
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNJ2BP-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467193 [Multi-domain] Cd Length: 86 Bit Score: 51.14 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPTGdFGFSLRRTTMLDRAPEGQA-YrrVVHFAEPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIR 297
Cdd:cd06709 2 EITLKRGPSG-LGFNIVGGTDQPYIPNDSGiY--VAKIKEDGAAAID---GrLQEGDKILEINGQSLENLTHQDAVELFR 75
|
90
....*....|.
gi 1907082213 298 QSGDSVRLKVQ 308
Cdd:cd06709 76 NAGEDVKLKVQ 86
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1293-1790 |
1.58e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 57.14 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1293 EEQIRNKDEEIQQLRSKLEKVEKERNE-------LRLSSDRLETRISELTSELTderntgesasqlldaetaerlRTEKE 1365
Cdd:pfam10174 246 ERNIRDLEDEVQMLKTNGLLHTEDREEeikqmevYKSHSKFMKNKIDQLKQELS---------------------KKESE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1366 MKELQTQYDALK------KQMEVMEMEVMEARLIRAAEINGEVDdddaggEWRLKYERAVREVDFTKKRLQQELEDK--- 1436
Cdd:pfam10174 305 LLALQTKLETLTnqnsdcKQHIEVLKESLTAKEQRAAILQTEVD------ALRLRLEEKESFLNKKTKQLQDLTEEKstl 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1437 ----------MEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHL--------EGQQV-----RN 1493
Cdd:pfam10174 379 ageirdlkdmLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALttleealsEKERIierlkEQ 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1494 HELEKKQRRFDSELSQAHEETQREK---LQREKLQREKDM--LLAEAFSLKQQMEEKD-----LDIAGFTQK--VVSLEA 1561
Cdd:pfam10174 459 REREDRERLEELESLKKENKDLKEKvsaLQPELTEKESSLidLKEHASSLASSGLKKDsklksLEIAVEQKKeeCSKLEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1562 ELQDISSQESKDEASlAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAkLRlEMEMERmrqtHSKEMESRDEEVEEAR 1641
Cdd:pfam10174 539 QLKKAHNAEEAVRTN-PEINDRIRLLEQEVARYKEESGKAQAEVERLLGI-LR-EVENEK----NDKDKKIAELESLTLR 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1642 QSCQKKLKQMEVQLEEEyEDKQKALREKRELESKLSTLSDQVNQRDFE----SEKRLRKDLKRTKALLADAQIMLD---- 1713
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQ-EMKKKGAQLLEEARRREDNLADNSQQLQLEelmgALEKTRQELDATKARLSSTQQSLAekdg 690
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082213 1714 HLKNNAPSKREiaQLKNQLEESEFTCAAAVKARKAmevemeDLHLQIDDIAKAKTALEEQLSrLQREKNEIQNRLEE 1790
Cdd:pfam10174 691 HLTNLRAERRK--QLEEILEMKQEALLAAISEKDA------NIALLELSSSKKKKTQEEVMA-LKREKDRLVHQLKQ 758
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1574-1936 |
2.14e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1574 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQ----AKLRLEMEMERMRQThskemesrdeeveEARQSCQKKLK 1649
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQdyqaASDHLNLVQTALRQQ-------------EKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1650 QMEVQLEEEYEDKQKALREKRELESKLSTLSDQVnqrdfesekrlrkdlKRTKALLADAQIMLDHLKnnapsKREIA--Q 1727
Cdd:PRK04863 359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEV---------------DELKSQLADYQQALDVQQ-----TRAIQyqQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1728 LKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQreknEIQNRLEEdqedmneLMKKHKAAVA 1807
Cdd:PRK04863 419 AVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ----AAHSQFEQ-------AYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1808 QASRDMAQmNDLQAQIEESNKEKQELQeKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASR 1887
Cdd:PRK04863 488 EVSRSEAW-DVARELLRRLREQRHLAE-QLQQLRMRLSELEQ---RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907082213 1888 LKETMEKLTEErdQRAAAENREkeqnkRLQRQLRDTKEEMSELARKEAE 1936
Cdd:PRK04863 563 LEARLESLSES--VSEARERRM-----ALRQQLEQLQARIQRLAARAPA 604
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1561-1744 |
2.19e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.18 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1561 AELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMER------MRQTH------SK 1628
Cdd:PHA02562 216 ARKQNKYDELVEEAKTI---KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQfqkvikMYEKGgvcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1629 EMESRDEEVEEARQS---CQKKLKQMEVQLEEEYE---DKQKALREKRELESKLSTLsDQVNQRDFESEKRLRKDLKRTK 1702
Cdd:PHA02562 293 QISEGPDRITKIKDKlkeLQHSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTN-KQSLITLVDKAKKVKAAIEELQ 371
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907082213 1703 ALLADaqimldhlknnapSKREIAQLKNQLEESEFTCAAAVK 1744
Cdd:PHA02562 372 AEFVD-------------NAEELAKLQDELDKIVKTKSELVK 400
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1432-1807 |
3.13e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1432 ELEDKMEVEQQSRRQLERRLGDLQADSDESQRA----LQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSEL 1507
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKalfeLDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1508 SQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEkdldiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDL 1587
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1588 EAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEearqscqKKLKQMEVQLEEEYEDKQKALR 1667
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE-------KLIESLPRELAEELLEAKDSLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1668 EKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARK 1747
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1748 AMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1807
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| PDZ2_L-delphilin-like |
cd06744 |
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ... |
224-308 |
3.23e-07 |
|
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which it is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467226 [Multi-domain] Cd Length: 75 Bit Score: 49.58 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 224 QRRPTGDFGFSLRrttmlDRAPegqAYRRVVhfaEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSV 303
Cdd:cd06744 4 VYRGNGSFGFTLR-----GHAP---VYIESV---DPG-SAAERA-GLKPGDRILFLNGLDVRNCSHDKVVSLLQGSGSMP 70
|
....*
gi 1907082213 304 RLKVQ 308
Cdd:cd06744 71 TLVVE 75
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1723-2007 |
3.60e-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: 55.90 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1723 REIAQlKNQLEESEFTCAAAVKARKAMEVEMEDLHLQiddiakaktaLEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1802
Cdd:pfam17380 310 REVER-RRKLEEAEKARQAEMDRQAAIYAEQERMAME----------RERELERIRQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1803 KAAVAQASRdmaQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLE 1882
Cdd:pfam17380 379 ELERLQMER---QQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1883 NLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKE-EMSELARKEAEASRKKHELEMDLESLEAANQSLQAd 1961
Cdd:pfam17380 456 QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEkELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER- 534
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907082213 1962 lklafKRIGDLQAAIEDEMESDENedlinsLQDMVTKYQKKKNKLE 2007
Cdd:pfam17380 535 -----RREAEEERRKQQEMEERRR------IQEQMRKATEERSRLE 569
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1288-1981 |
4.27e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.73 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1288 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNEL------------RLSSDRLETRISELTSELTDERNTGESASQllDAE 1355
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqALEKARALCGLPDLTPENAEDYLAAFRAKE--QQA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1356 TAERLRTEKEM---KELQTQYDAlkkqmevmemevmEARLIRAaeINGEVDDDDAggewrlkYERAvREVdftkkrLQQE 1432
Cdd:COG3096 454 TEEVLELEQKLsvaDAARRQFEK-------------AYELVCK--IAGEVERSQA-------WQTA-REL------LRRY 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1433 LEDKMEVEQQSrrQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhlegqqvrNHELEKKQRRFDSELSQAHE 1512
Cdd:COG3096 505 RSQQALAQRLQ--QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-----------AEELEELLAELEAQLEELEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1513 ETQREKLQREKLQREKDMLLAEAFSLKQQmeekdldiAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK 1592
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAAR--------APAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREAT 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1593 DQEEEldeqagsiqmLEQAKLRLEMEMERMRQTHSkemesrdeeVEEARqscqkkLKQME-----VQLEEEYEDkqKALR 1667
Cdd:COG3096 644 VERDE----------LAARKQALESQIERLSQPGG---------AEDPR------LLALAerlggVLLSEIYDD--VTLE 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1668 EKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKRE-----IAQLKN-QLEESEFTcAA 1741
Cdd:COG3096 697 DAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEGDPDSFDDSVFDAEEledavVVKLSDrQWRYSRFP-EV 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1742 AVKARKAMEVEMEDLHLQIDDIAK--AKTA--------LEEQLSR--------------------LQREKNEIQNRLEED 1791
Cdd:COG3096 776 PLFGRAAREKRLEELRAERDELAEqyAKASfdvqklqrLHQAFSQfvgghlavafapdpeaelaaLRQRRSELERELAQH 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1792 QEDmnelMKKHKAAVAQASRDMAQMNDLQAQIEESNKEkqELQEKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRL 1871
Cdd:COG3096 856 RAQ----EQQLRQQLDQLKEQLQLLNKLLPQANLLADE--TLADRLEELREELDAAQE---AQAFIQQHGKALAQLEPLV 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1872 ----------EFEKTQVKRLENLASRLKETMEKLTEERDQRAA----------AENRekEQNKRLQRQLRDTKEEMSElA 1931
Cdd:COG3096 927 avlqsdpeqfEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyedavgllGENS--DLNEKLRARLEQAEEARRE-A 1003
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1932 RKEAEASRKKHE----LEMDLES-LEAANQSLQAdlklAFKRIGDLQAAIEDEME 1981
Cdd:COG3096 1004 REQLRQAQAQYSqynqVLASLKSsRDAKQQTLQE----LEQELEELGVQADAEAE 1054
|
|
| PDZ4_GRIP1-2-like |
cd06686 |
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
220-308 |
4.41e-07 |
|
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467174 [Multi-domain] Cd Length: 99 Bit Score: 50.04 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPTGDFGFSLR----RTTMLDRAPegqayrrVVHFAEPGAGTKDLALgLVPGDRLVEINGQNVENKSRDEIVEM 295
Cdd:cd06686 9 EVILRGDPLKGFGIQLQggvfATETLSSPP-------LISFIEPDSPAERCGV-LQVGDRVLSINGIPTEDRTLEEANQL 80
|
90
....*....|...
gi 1907082213 296 IRQSGDSVRLKVQ 308
Cdd:cd06686 81 LRDSASKVTLEIE 93
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1613-1963 |
5.21e-07 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 55.25 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1613 LRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQmevQLEEEYEDKQKALrekrELESKLSTLSDqvnqrdfESEK 1692
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKK---EIDLEYTEAVIAM----GLQERLENLRE-------EFSK 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1693 RLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavkarkamevemedlhlQIDDIAKAKTALEE 1772
Cdd:PLN03229 498 ANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLD-------------------------MLNEFSRAKALSEK 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1773 QlSRLQREKNEIQNRLEE--DQEDMNELMKKHKAAVAQ--ASRDMAQMNDLQAQIEESNKEKQ-ELQEKLQALQSQVEFL 1847
Cdd:PLN03229 553 K-SKAEKLKAEINKKFKEvmDRPEIKEKMEALKAEVASsgASSGDELDDDLKEKVEKMKKEIElELAGVLKSMGLEVIGV 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1848 EQsmvdKSLVSRQEAKIRELETRLEFEKTQV-KRLENL--ASRLKETMEKLTEERDQRAAAEN-REKEQNKRLQRQLRDT 1923
Cdd:PLN03229 632 TK----KNKDTAEQTPPPNLQEKIESLNEEInKKIERVirSSDLKSKIELLKLEVAKASKTPDvTEKEKIEALEQQIKQK 707
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907082213 1924 -KEEMSELARKEaeasrKKHELEMDLESLEAANQSLQADLK 1963
Cdd:PLN03229 708 iAEALNSSELKE-----KFEELEAELAAARETAAESNGSLK 743
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1630-1843 |
5.59e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1630 MESRDEEVEEARQSCQKKLKQMEVQLEEeyedKQKALREKRElESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQ 1709
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQ-KNGLVDLSEEAKLLL-QQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1710 IMLDHLKNNAPSKRE----------IAQLKNQLEESEFTCAAAVK-------ARKAMEVEMEDLHLQIDD-IAKAKTALE 1771
Cdd:COG3206 240 ARLAALRAQLGSGPDalpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQeAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082213 1772 EQLSRLQREKNEIQNRLEEdqedmnelmkkHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1843
Cdd:COG3206 320 AELEALQAREASLQAQLAQ-----------LEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1441-1774 |
6.19e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1441 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQ 1520
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1521 REKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR-----DLEAKVKDQE 1595
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1596 EELDEQAGSIQMLEQAKLRLEMEMERMRQTHS--KEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELE 1673
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1674 SKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEM 1753
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
|
330 340
....*....|....*....|.
gi 1907082213 1754 EDLHLQIDDIAKAKTALEEQL 1774
Cdd:COG4372 350 LLDNDVLELLSKGAEAGVADG 370
|
|
| PDZ2-PTPN13_FRMPD2-like |
cd06792 |
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ... |
273-308 |
6.42e-07 |
|
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467254 [Multi-domain] Cd Length: 87 Bit Score: 49.13 E-value: 6.42e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1907082213 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06792 51 GDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLVLE 86
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1410-2032 |
6.55e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.44 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1410 EWRLK------YERAVREvDFTK----KRLQQELEDKMEVEQQSRRQLERRLGDL------------------------- 1454
Cdd:TIGR01612 531 DQNIKaklykeIEAGLKE-SYELaknwKKLIHEIKKELEEENEDSIHLEKEIKDLfdkyleiddeiiyinklklelkeki 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1455 --QADSDESQRALQQLKKKCQRLTA---ELQDTKLHLEGQQVRNHEleKKQRRFDSELSQAHEEtQREKLQRE--KLQRE 1527
Cdd:TIGR01612 610 knISDKNEYIKKAIDLKKIIENNNAyidELAKISPYQVPEHLKNKD--KIYSTIKSELSKIYED-DIDALYNElsSIVKE 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1528 KDMLLAEAfslKQQMEEKDLDIAGFTQKVVSLEAE-----LQDISSQESKDEASLAKVKKQL-----RDLEAKVKDQEEE 1597
Cdd:TIGR01612 687 NAIDNTED---KAKLDDLKSKIDKEYDKIQNMETAtvelhLSNIENKKNELLDIIVEIKKHIhgeinKDLNKILEDFKNK 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1598 LDEQAGSIQMLEQAKLRLEM---EMERMRQTHSKEMESRDEEVEEARQSCQKK---LKQMEVQLEEEYEDKQKALREKRE 1671
Cdd:TIGR01612 764 EKELSNKINDYAKEKDELNKyksKISEIKNHYNDQINIDNIKDEDAKQNYDKSkeyIKTISIKEDEIFKIINEMKFMKDD 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1672 LESKLSTLSDQVN--QRDFESEKRLRKDL-KRTKALLADAQIMlDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKA 1748
Cdd:TIGR01612 844 FLNKVDKFINFENncKEKIDSEHEQFAELtNKIKAEISDDKLN-DYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEY 922
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1749 MEVeMEDLHLQIDDIAKAKTALEEQLSR---LQREKNEIQ----NRLEEDQED-MNELMKKHKAAV-----AQASRDMAQ 1815
Cdd:TIGR01612 923 IKI-CENTKESIEKFHNKQNILKEILNKnidTIKESNLIEksykDKFDNTLIDkINELDKAFKDASlndyeAKNNELIKY 1001
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1816 MNDLQA------------QIEESNKEKQELQEKLQALQSQVEFLEQSmVDKSLVSRQEAKIRELETRLEFEKTQV-KRLE 1882
Cdd:TIGR01612 1002 FNDLKAnlgknkenmlyhQFDEKEKATNDIEQKIEDANKNIPNIEIA-IHTSIYNIIDEIEKEIGKNIELLNKEIlEEAE 1080
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1883 NLASRLKETMEKLT---------EERDQRAAAENREKEQNKRLQRQLRDTKEEMSELarkeaeasRKKHELEMDleslEA 1953
Cdd:TIGR01612 1081 INITNFNEIKEKLKhynfddfgkEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI--------KKKSENYID----EI 1148
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082213 1954 ANQslqadlklafkrIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELEdRVDGVKSWLSKNKG 2032
Cdd:TIGR01612 1149 KAQ------------INDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIA-EIEKDKTSLEEVKG 1214
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1554-1839 |
8.80e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1554 QKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQmleqaKLRLEMemermrQTHSKEMESR 1633
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK-----ELREEA------QELREKRDEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1634 DEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQVNQ---------RDFESEKRLRKDLKRTKAL 1704
Cdd:COG1340 70 NEKVKELKEERDELNEKLN-ELREELDELRKELAELNKAGGSIDKLRKEIERlewrqqtevLSPEEEKELVEKIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1705 LADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEI 1784
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADEL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1785 QNRLEEDQEDMNELMKKHKAAvaqasRDMAQMNDLQAQIEESNKEKQELQEKLQA 1839
Cdd:COG1340 229 HEEIIELQKELRELRKELKKL-----RKKQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1506-1696 |
9.08e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 9.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1506 ELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQlR 1585
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1586 DLEAKVKdqeeELDEQAGSIQMLEQAKLRLEMEMERMRqthskemesrdEEVEEArqscQKKLKQMEVQLEE---EYEDK 1662
Cdd:COG1579 90 EYEALQK----EIESLKRRISDLEDEILELMERIEELE-----------EELAEL----EAELAELEAELEEkkaELDEE 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1907082213 1663 QKALREKRE-LESKLSTLSDQVNQRDFESEKRLRK 1696
Cdd:COG1579 151 LAELEAELEeLEAEREELAAKIPPELLALYERIRK 185
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1294-1719 |
1.01e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1294 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESAsqlldaeTAERLRTEKEMKELQTQY 1373
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA-------PVDLGNAEDFLEELREER 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1374 DALKKQMEVMEMEVMEAR-LIRAAEingevddddaggewRLKYERAVREVDftkkrlqQELEDKMEVEQQSRRqlERRLG 1452
Cdd:PRK02224 422 DELREREAELEATLRTAReRVEEAE--------------ALLEAGKCPECG-------QPVEGSPHVETIEED--RERVE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1453 DLQADSDESQRALQQLKKKCQRLTaELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLL 1532
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIE-------RLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1533 AEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESkdeaSLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAK 1612
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE----SLERIRTLLAAIADAEDEIERLREKREALAELNDERR 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1613 LRLEMEMERMRQTHSKEMESRdeeVEEARQScqkklKQMEVQLEEEYEDKQKALREKR-ELESKLSTLsdqvnQRDFESE 1691
Cdd:PRK02224 627 ERLAEKRERKRELEAEFDEAR---IEEARED-----KERAEEYLEQVEEKLDELREERdDLQAEIGAV-----ENELEEL 693
|
410 420
....*....|....*....|....*...
gi 1907082213 1692 KRLRKDLKRtkalLADAQIMLDHLKNNA 1719
Cdd:PRK02224 694 EELRERREA----LENRVEALEALYDEA 717
|
|
| PDZ2_DLG5-like |
cd06765 |
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
270-308 |
1.04e-06 |
|
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PSZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467246 [Multi-domain] Cd Length: 77 Bit Score: 48.50 E-value: 1.04e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1907082213 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06765 35 LTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLM 73
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1434-1856 |
1.39e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1434 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKkkcqRLTAelqdTKLHLEGQQVRNHELEKKQRR---FDSELSQA 1510
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFS----RFIG----SHLAVAFEADPEAELRQLNRRrveLERALADH 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1511 HEETQREKLQREKLQREKDML--LAEAFSLkqqmeekdLDIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLrdle 1588
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALnrLLPRLNL--------LADETLADRVEEIREQLD----EAEEAKRFVQQHGNAL---- 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1589 akvkdqeEELDEQAGSIQMLEQaklrlemEMERMRQthskemesrdeEVEEARQScQKKLKQ--------MEVQLEEEYE 1660
Cdd:PRK04863 921 -------AQLEPIVSVLQSDPE-------QFEQLKQ-----------DYQQAQQT-QRDAKQqafaltevVQRRAHFSYE 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1661 DKQKALREKRELESKLSTLSDQVNQ-RDfesekRLRKDLKRTKALLADAQIMLDHLKNNAPSKREI-AQLKNQLEesEFT 1738
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQeRT-----RAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMlQELKQELQ--DLG 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1739 CAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA--QASRDMAQM 1816
Cdd:PRK04863 1048 VPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwCAVLRLVKD 1127
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907082213 1817 NDLqaqieesnkEKQELQEKLQALQSQVeflEQSMVDKSL 1856
Cdd:PRK04863 1128 NGV---------ERRLHRRELAYLSADE---LRSMSDKAL 1155
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1445-1601 |
1.44e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1445 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLhlegqQVRNHELEKKQrrfdselSQAHEETQREKLQREKL 1524
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK-----EIKRLELEIEE-------VEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082213 1525 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1601
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1300-1601 |
1.64e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1300 DEEIQQLRSKLEKVEKERNELRLSSDRLEtrisELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQ 1379
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1380 MEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMeveqqsrRQLERRLGDLQADSD 1459
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAM-------RAFNREWPAETADLD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1460 ESQRALQQLKKKCQRLTAElqdtklHLEGQQVRNHELEKKQ-----RRFDSELSQAHEETqreklqREKLQREKDMLLAE 1534
Cdd:COG4913 809 ADLESLPEYLALLDRLEED------GLPEYEERFKELLNENsiefvADLLSKLRRAIREI------KERIDPLNDSLKRI 876
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 1535 AFS----LKQQMEE-KDLDIAGFTQkvvsleaELQDISSQESKDEASLAKVK-KQLRDLEAKVKDQEEELDEQ 1601
Cdd:COG4913 877 PFGpgryLRLEARPrPDPEVREFRQ-------ELRAVTSGASLFDEELSEARfAALKRLIERLRSEEEESDRR 942
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1689-1988 |
1.75e-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: 52.51 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1689 ESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMevemedlhlqiddiAKAKT 1768
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSL--------------SASVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1769 ALEEQLSRLQREKNEIQNRLEED--QEDMN----ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQS 1842
Cdd:pfam15905 126 SLEKQLLELTRVNELLKAKFSEDgtQKKMSslsmELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1843 QVEFLEQSMVDkslvsrqeakireletrlefEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD 1922
Cdd:pfam15905 206 KLVSTEKEKIE--------------------EKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQS 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1923 TKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKlafKRIGDLQAAIedEMESDENEDL 1988
Cdd:pfam15905 266 LEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN---AELEELKEKL--TLEEQEHQKL 326
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1474-1839 |
2.22e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1474 RLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFT 1553
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAAL---SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1554 QKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMErMRQTHSKEMESR 1633
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA-EREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1634 DEEVEEARQSCQKKLKQMEVQleEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLD 1713
Cdd:COG4372 159 LESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1714 HLKNNAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE 1793
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIE-ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1794 DM----NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQA 1839
Cdd:COG4372 316 ALlaalLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1293-1962 |
2.40e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1293 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQ 1372
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1373 YDALKKQMEVMEMEVmeARLIRAAEINGE-VDDDDAGGEWRLKYERAVREVDFTKKRLQQEledKMEVEQQSRRQLerrl 1451
Cdd:COG3096 594 IKELAARAPAWLAAQ--DALERLREQSGEaLADSQEVTAAMQQLLEREREATVERDELAAR---KQALESQIERLS---- 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1452 gdlQADSDESQRaLQQLkkkCQRLTAEL-----QDTKLH-------LEGQQ-----VRNHELEKKQ-------------- 1500
Cdd:COG3096 665 ---QPGGAEDPR-LLAL---AERLGGVLlseiyDDVTLEdapyfsaLYGPArhaivVPDLSAVKEQlagledcpedlyli 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1501 ----RRFDSELSQAHEETQREKLQREKLQ----------------REK--DMLLAEAFSLKQQMEEKDLDIagftQKVVS 1558
Cdd:COG3096 738 egdpDSFDDSVFDAEELEDAVVVKLSDRQwrysrfpevplfgraaREKrlEELRAERDELAEQYAKASFDV----QKLQR 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1559 LEAELQDISSQ------ESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAgsiQMLEQAKLRLEMEMERMRQTHSKEMES 1632
Cdd:COG3096 814 LHQAFSQFVGGhlavafAPDPEAELAALRQRRSELERELAQHRAQEQQLR---QQLDQLKEQLQLLNKLLPQANLLADET 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1633 RDEEVEEARqscqkklkqmevqleEEYEDKQKALREKRELESKLSTLSDQVN--QRDFESEKRLRKDLKRTKALLADAQI 1710
Cdd:COG3096 891 LADRLEELR---------------EELDAAQEAQAFIQQHGKALAQLEPLVAvlQSDPEQFEQLQADYLQAKEQQRRLKQ 955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1711 MLDHLKNnapskreiaqlknqleeseftcaaaVKARKAmevemedlHLQIDDIAKaktaleeqlsrlqrekneiqnRLEE 1790
Cdd:COG3096 956 QIFALSE-------------------------VVQRRP--------HFSYEDAVG---------------------LLGE 981
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1791 DQeDMNELMKkHKAAVAQASRDMA--QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA 1862
Cdd:COG3096 982 NS-DLNEKLR-ARLEQAEEARREAreQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqADAEAEERARI 1059
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1863 KIRELETRL--------EFEKTQVKR---LENLASRLKETMEKLTEERDQRAAAenreKEQNKRLQRQLRDTKEE----M 1927
Cdd:COG3096 1060 RRDELHEELsqnrsrrsQLEKQLTRCeaeMDSLQKRLRKAERDYKQEREQVVQA----KAGWCAVLRLARDNDVErrlhR 1135
|
730 740 750
....*....|....*....|....*....|....*
gi 1907082213 1928 SELARKEAEASRkkhelEMDLESLEAANQSlQADL 1962
Cdd:COG3096 1136 RELAYLSADELR-----SMSDKALGALRLA-VADN 1164
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1444-1956 |
2.72e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 52.72 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1444 RRQLERRLGDLQADSDESQRALQ-------QLKKKCQRLTAELQDTKLHLEGQQVrnhelEKKQRRFDSELSQ------- 1509
Cdd:pfam05701 37 RKLVELELEKVQEEIPEYKKQSEaaeaakaQVLEELESTKRLIEELKLNLERAQT-----EEAQAKQDSELAKlrveeme 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1510 ---AHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEkdldiagfTQKVVSLEAELQDISSQESKDEASLAK-VKKQLR 1585
Cdd:pfam05701 112 qgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELES--------LRKEYASLVSERDIAIKRAEEAVSASKeIEKTVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1586 DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKlKQMEVQLEEEYEdkqKA 1665
Cdd:pfam05701 184 ELTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQLLSA-KDLKSKLETASA---LL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1666 LREKREL----ESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIA-QLKNQLEEsEFTCA 1740
Cdd:pfam05701 260 LDLKAELaaymESKLKEEADG-EGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAaSLRSELEK-EKAEL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1741 AAVKARKAMEvemedlhlqiddiAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKhkaaVAQASRDMAQMNDL- 1819
Cdd:pfam05701 338 ASLRQREGMA-------------SIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQ----LQQAAQEAEEAKSLa 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1820 QAQIEESNKEKQElQEKLQALQSQVEfleqsmvdkslvSRQEAKIRELETRLEFEKT------------QVKRLENLASR 1887
Cdd:pfam05701 401 QAAREELRKAKEE-AEQAKAAASTVE------------SRLEAVLKEIEAAKASEKLalaaikalqeseSSAESTNQEDS 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082213 1888 LKETMEKLTEERDQRAAAENREKEQNKRLQR---QLRDTKEEMSELARKEAEASRkkhELEMDLESLEAANQ 1956
Cdd:pfam05701 468 PRGVTLSLEEYYELSKRAHEAEELANKRVAEavsQIEEAKESELRSLEKLEEVNR---EMEERKEALKIALE 536
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1292-1908 |
2.81e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1292 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQT 1371
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1372 QYDALKKQMEVMEMEVmeARLIRAAEINGEVDDDDAGGEwrlkyeravrevDFTKKRLQQELEDKMEVEQ--QSRRQLER 1449
Cdd:PRK04863 594 RIQRLAARAPAWLAAQ--DALARLREQSGEEFEDSQDVT------------EYMQQLLERERELTVERDElaARKQALDE 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1450 RLGDLQADSDESQRALQQLkkkCQRLTAEL-----QDTKLH-------LEGQQ-----VRNHELEKKQ------------ 1500
Cdd:PRK04863 660 EIERLSQPGGSEDPRLNAL---AERFGGVLlseiyDDVSLEdapyfsaLYGPArhaivVPDLSDAAEQlagledcpedly 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1501 ------RRFDSELSQAhEETQREKLQRE-----------------KLQREK--DMLLAEAFSLKQQMEEKDLDIagftQK 1555
Cdd:PRK04863 737 liegdpDSFDDSVFSV-EELEKAVVVKIadrqwrysrfpevplfgRAAREKriEQLRAEREELAERYATLSFDV----QK 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1556 VVSLEAELQDISSQ------ESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAgsiQMLEQAKLRLEMEMERMRQTHSKE 1629
Cdd:PRK04863 812 LQRLHQAFSRFIGShlavafEADPEAELRQLNRRRVELERALADHESQEQQQR---SQLEQAKEGLSALNRLLPRLNLLA 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1630 MESRDEEVEEARQscqkklkqmevQLEEEYEDK------QKALrekRELESKLSTLsdQVNQRDFEsekRLRKDLKRTKA 1703
Cdd:PRK04863 889 DETLADRVEEIRE-----------QLDEAEEAKrfvqqhGNAL---AQLEPIVSVL--QSDPEQFE---QLKQDYQQAQQ 949
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1704 LLADAQIMLDHLKNnapskreiaqlknqleeseftcaaaVKARKAmevemedlHLQIDDIAK---AKTALEEQLSRlqre 1780
Cdd:PRK04863 950 TQRDAKQQAFALTE-------------------------VVQRRA--------HFSYEDAAEmlaKNSDLNEKLRQ---- 992
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1781 kneiqnRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEF--LEQSMVDKS--- 1855
Cdd:PRK04863 993 ------RLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSgaEERARARRDelh 1066
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1856 -LVSRQEAKIRELETRLEFEKTqvkRLENLASRLKETMEKLTEERDQRAAAENR 1908
Cdd:PRK04863 1067 aRLSANRSRRNQLEKQLTFCEA---EMDNLTKKLRKLERDYHEMREQVVNAKAG 1117
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1515-1705 |
3.06e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1515 QREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQK--VVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK 1592
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1593 DQEEELDE---------QAGSIQMLEQAKLRLEMEMERMRQTHSKE---MESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1660
Cdd:COG3206 244 ALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082213 1661 DKQKALREKRELESKLSTLSDQVNQRDFESEkRLRKDLKRTKALL 1705
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELR-RLEREVEVARELY 367
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1354-1602 |
3.32e-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: 52.07 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1354 AETAERLRTEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDDDDaggewrlkyeravREVDFTKKRLqQEL 1433
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK--------EEKALLKQLAALE-------------RRIAALARRI-RAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1434 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLtAELQDTKLHLEGQQVRnhELEKKQRRFDSELSQAHEE 1513
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1514 TQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1593
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
....*....
gi 1907082213 1594 QEEELDEQA 1602
Cdd:COG4942 232 LEAEAAAAA 240
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1635-1943 |
3.55e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 52.27 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1635 EEVEEARQSCQKKLKQMEvQLEEEYED--------KQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRtkallA 1706
Cdd:COG5185 232 EEALKGFQDPESELEDLA-QTSDKLEKlveqntdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKS-----I 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1707 DAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaAAVKARKA-MEVEMEDLHLQIDDIAKAKTAL--EEQLSRLQREKNE 1783
Cdd:COG5185 306 DIKKATESLEEQLAAAEAEQELEESKRETE----TGIQNLTAeIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1784 IQNRLE----EDQEDMNELMKKHKAAVAQASRDMA----QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKS 1855
Cdd:COG5185 382 FKDTIEstkeSLDEIPQNQRGYAQEILATLEDTLKaadrQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEES 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1856 LVSRQEAK---IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELAR 1932
Cdd:COG5185 462 QSRLEEAYdeiNRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
330
....*....|.
gi 1907082213 1933 KEAEASRKKHE 1943
Cdd:COG5185 542 ENLIPASELIQ 552
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1635-1953 |
3.62e-06 |
|
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: 52.37 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1635 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDF----------ESEKRLRKDLKRTKAL 1704
Cdd:pfam15070 18 ENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAeeeqppagpsEEEQRLQEEAEQLQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1705 LADAQIML-DHLKNNAPSKREIAQLKNQLEESEFTC---AAAVKARKAMeveMEDLHLQIDDIAKAKT---ALEEQLSRL 1777
Cdd:pfam15070 98 LEALAGQLqAQVQDNEQLSRLNQEQEQRLLELERAAerwGEQAEDRKQI---LEDMQSDRATISRALSqnrELKEQLAEL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1778 Q-------REKNEIQNRLEEDQEDMNELMKKhkaavaqasrdMAQMN----DLQAQIEESNKEKQELQEK----LQALQS 1842
Cdd:pfam15070 175 QngfvkltNENMELTSALQSEQHVKKELAKK-----------LGQLQeelgELKETLELKSQEAQSLQEQrdqyLAHLQQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1843 QVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVK-RLENLASRLKETMEKLTeerdqrAAAenrekEQNKRLQRQLR 1921
Cdd:pfam15070 244 YVAAYQQLASEKEELHKQYLLQTQLMDRLQHEEVQGKvAAEMARQELQETQERLE------ALT-----QQNQQLQAQLS 312
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907082213 1922 DTKEEMS----ELARKEAEASRKKHELEMDLESLEA 1953
Cdd:pfam15070 313 LLANPGEgdglESEEEEEEAPRPSLSIPEDFESREA 348
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1571-1686 |
3.82e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.45 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1571 SKDEASLAKVkkqLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthskemESRDEEVEEARQSCQKKLKQ 1650
Cdd:COG1193 510 GEESIDVEKL---IEELERERRELEEEREEAERLREELEKLREELEEKLEELE-------EEKEEILEKAREEAEEILRE 579
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907082213 1651 MEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQR 1686
Cdd:COG1193 580 ARKEAEElirELREAQAEEEELKEARKKLEELKQELEEK 618
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1579-1734 |
4.08e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1579 KVKKQLRDLEAKVKDQEEELDEQAGSIQmlEQAKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEE 1658
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKL----EKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1659 YEDKQKALREKRELESKLSTLSDQVNQRDFESEK---RLRKDLKRTKALLAD--AQIMLDHLKNNApsKREIAQLKNQLE 1733
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEElieEQLQELERISGLTAEeaKEILLEKVEEEA--RHEAAVLIKEIE 179
|
.
gi 1907082213 1734 E 1734
Cdd:PRK12704 180 E 180
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1574-1934 |
4.11e-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: 52.65 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1574 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQ----AKLRLEMEMERMRQThsKEMESRDEEVEEArqscQKKLK 1649
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQdyqaASDHLNLVQTALRQQ--EKIERYQEDLEEL----TERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1650 QMEVQLEEEYEDKQKAlREKRElesklstlsdqvnqrdfesekRLRKDLKRTKALLADAQIMLDHLKNNAPSKReiaQLK 1729
Cdd:COG3096 365 EQEEVVEEAAEQLAEA-EARLE---------------------AAEEEVDSLKSQLADYQQALDVQQTRAIQYQ---QAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1730 NQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEedqedmneLMKKHKAAV-AQ 1808
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE--------LVCKIAGEVeRS 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1809 ASRDMAQmndlqaQIEESNKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELEtrlEFEKTQVKRLENlASRL 1888
Cdd:COG3096 492 QAWQTAR------ELLRRYRSQQALAQRLQQLRAQLAELEQ------RLRQQQNAERLLE---EFCQRIGQQLDA-AEEL 555
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907082213 1889 KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKE 1934
Cdd:COG3096 556 EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1728-1962 |
5.24e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.82 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1728 LKNQLEESEFTCAAAVKARKAMEVEMEDlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1807
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREK---EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1808 QASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSR--QEAKIRELETRLEFEKTQVK 1879
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELermkerAKKAGAQRkeEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1880 RL--------------ENLASRLKETMEKLTeerdQRAAAENREKEQNKRLQRQLRDTKEEmselarkeAEASRKKHE-L 1944
Cdd:pfam07888 189 SLskefqelrnslaqrDTQVLQLQDTITTLT----QKLTTAHRKEAENEALLEELRSLQER--------LNASERKVEgL 256
|
250
....*....|....*...
gi 1907082213 1945 EMDLESLEAANQSLQADL 1962
Cdd:pfam07888 257 GEELSSMAAQRDRTQAEL 274
|
|
| PDZ_Par6-like |
cd06718 |
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ... |
222-297 |
5.78e-06 |
|
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par6-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467202 [Multi-domain] Cd Length: 84 Bit Score: 46.41 E-value: 5.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 222 ELQRRPTGDFGFSLRRTTMLDRAPeGQAYRRVVhfaePGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIR 297
Cdd:cd06718 4 ELIKPPGKPLGFYIRDGNGVERVP-GIFISRLV----LG-SLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMV 73
|
|
| PDZ4_PTPN13-like |
cd06696 |
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ... |
220-307 |
6.07e-06 |
|
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)] and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467182 [Multi-domain] Cd Length: 85 Bit Score: 46.53 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPTGDFGFSLRRTTMldraPEGQAYRRVVHfaEPgagtkdlALG---LVPGDRLVEINGQNVENKSRDEIVEMI 296
Cdd:cd06696 5 EVTLTKSEKGSLGFTVTKGKD----DNGCYIHDIVQ--DP-------AKSdgrLRPGDRLIMVNGVDVTNMSHTEAVSLL 71
|
90
....*....|.
gi 1907082213 297 RQSGDSVRLKV 307
Cdd:cd06696 72 RAAPKEVTLVL 82
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1287-1606 |
6.20e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1287 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEM 1366
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1367 KELQTQYDALKKQMevmemevmearliraaeingevddddaggewrlkyeravrevdftkKRLQQELEDKmeveQQSRRQ 1446
Cdd:COG4372 104 ESLQEEAEELQEEL----------------------------------------------EELQKERQDL----EQQRKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1447 LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlegQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQR 1526
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALE-----QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1527 EKDMLLAEAfslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQ 1606
Cdd:COG4372 209 IESLPRELA---EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1509-1735 |
6.31e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1509 QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagfTQKVVSLEAELQDIssqeskdEASLAKVKKQLRDLE 1588
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEEL-------NEEYNELQAELEAL-------QAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1589 AKVKDQEEELDEQAGSIQMLEQAKLRLEM---------------EMERMRQTHSKEMesrdEEVEEARQSCQKKLKQMEV 1653
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDVllgsesfsdfldrlsALSKIADADADLL----EELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1654 QLEEEYEDKQKALREKRELESKLSTLSDQVNQrdfesekrLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLE 1733
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQ--------LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
..
gi 1907082213 1734 ES 1735
Cdd:COG3883 227 AA 228
|
|
| PDZ3_Dlg1-2-4-like |
cd06795 |
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ... |
237-312 |
6.46e-06 |
|
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467257 [Multi-domain] Cd Length: 91 Bit Score: 46.58 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 237 RTTMLDRAPEGQAYRRV---------VHFAEPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06795 3 RKIVLHKGSTGLGFNIVggedgegifISFILAG-GPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTIIA 81
|
....*
gi 1907082213 308 QPIPE 312
Cdd:cd06795 82 QYKPE 86
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1430-1929 |
6.58e-06 |
|
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: 51.45 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1430 QQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhleGQQVRNHELEKKQRrfDSELSQ 1509
Cdd:pfam15964 219 RLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAST----SSRVGGLCLKCAQH--EAVLAQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1510 AHEETQREKLQRekLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSleaelqdisSQESKDEASLAKVKK--QLRDL 1587
Cdd:pfam15964 293 THTNVHMQTIER--LTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQ---------AVQMTEEANFEKTKAliQCEQL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1588 EAKVKDQEEELDEQAGSiqmlEQAKLRLEMEMERmrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqKALR 1667
Cdd:pfam15964 362 KSELERQKERLEKELAS----QQEKRAQEKEALR------KEMKKEREELGATMLALSQNVAQLEAQVE-------KVTR 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1668 EKRELESKLSTLSDQVNQRDFESEK---RLRKDLKRTKALLADAQimLDHLKNNAPSKR-------EIAQLKNQLEESef 1737
Cdd:pfam15964 425 EKNSLVSQLEEAQKQLASQEMDVTKvcgEMRYQLNQTKMKKDEAE--KEHREYRTKTGRqleikdqEIEKLGLELSES-- 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1738 tcaaavkaRKAMEVEMEDLHLQIDDIAKaktaLEEQLSRLQREKNeiqnrleedqedmneLMKKHKAAVAQASRDMAQMN 1817
Cdd:pfam15964 501 --------KQRLEQAQQDAARAREECLK----LTELLGESEHQLH---------------LTRLEKESIQQSFSNEAKAQ 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1818 DLQAQIEEsnkekQELQEKLQALQSQvefleqsmvdkslvsrQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTE 1897
Cdd:pfam15964 554 ALQAQQRE-----QELTQKMQQMEAQ----------------HDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQ 612
|
490 500 510
....*....|....*....|....*....|..
gi 1907082213 1898 ERDQRAAAENREKEQNKRLQRQLRDTKEEMSE 1929
Cdd:pfam15964 613 KSRSEVEQLSQEKEYLQDRLEKLQKRNEELEE 644
|
|
| PDZ_MPP-like |
cd06726 |
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ... |
273-309 |
6.93e-06 |
|
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467208 [Multi-domain] Cd Length: 80 Bit Score: 46.10 E-value: 6.93e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1907082213 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06726 44 GDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLIP 80
|
|
| PDZ1_PTPN13_FRMPD2-like |
cd06694 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ... |
258-305 |
7.32e-06 |
|
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467180 [Multi-domain] Cd Length: 92 Bit Score: 46.62 E-value: 7.32e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907082213 258 EPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRL 305
Cdd:cd06694 38 IPG-GPADKDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVEL 84
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1645-2016 |
7.34e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.98 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1645 QKKLKQMEVQLEEEYEDKQKALREKRelesklsTLSDQVNQrdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKRE 1724
Cdd:TIGR01612 458 KSKLKALEKRFFEIFEEEWGSYDIKK-------DIDENSKQ-----DNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNI 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1725 IAqlknqleeseFTCAAAVKARKAMEVEmedlhlqiddiAKAKTALEeQLSRLQREKNEIQNRLEEDQEDMNELMKkhka 1804
Cdd:TIGR01612 526 IG----------FDIDQNIKAKLYKEIE-----------AGLKESYE-LAKNWKKLIHEIKKELEEENEDSIHLEK---- 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1805 avaqasrdmaQMNDLQAQ----IEES---NKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQ 1877
Cdd:TIGR01612 580 ----------EIKDLFDKyleiDDEIiyiNKLKLELKEKIKNISDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQVPE 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1878 -VKRLENLASRLKETMEKLTEerDQRAAAENrekEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELE-MDLESLEAAN 1955
Cdd:TIGR01612 650 hLKNKDKIYSTIKSELSKIYE--DDIDALYN---ELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQnMETATVELHL 724
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1956 QSLQADLKLAFKRIGDLQAAIEDEMesdeNEDLINSLQDMVTKYQKKKNKLEGDSDVDSEL 2016
Cdd:TIGR01612 725 SNIENKKNELLDIIVEIKKHIHGEI----NKDLNKILEDFKNKEKELSNKINDYAKEKDEL 781
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1298-1623 |
7.49e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 50.30 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1298 NKDEEIQQLRSKL----EKVEkernELRLSSDRLETRISELTSELTDERN--------TGESASQLLDAETAERLRTEKE 1365
Cdd:pfam00038 1 NEKEQLQELNDRLasyiDKVR----FLEQQNKLLETKISELRQKKGAEPSrlyslyekEIEDLRRQLDTLTVERARLQLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1366 MKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDAGGEWRLKYERAVR----EVDFTKKRLQQELedkmeveq 1441
Cdd:pfam00038 77 LDNLRLAAEDFRQKYEDELNLRTSAE----NDLVGLRKDLDEATLARVDLEAKIEslkeELAFLKKNHEEEV-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1442 qsrRQLERRLGDlqadsdeSQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN-HELEKKQRRFDSELSQAhEETQREKLQ 1520
Cdd:pfam00038 145 ---RELQAQVSD-------TQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNrEEAEEWYQSKLEELQQA-AARNGDALR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1521 REKlqrekdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDIssqESKDEASLAKVKKQLRDLEAKVKDQEEELDE 1600
Cdd:pfam00038 214 SAK---------EEITELRRTIQSLEIELQSLKKQKASLERQLAET---EERYELQLADYQELISELEAELQETRQEMAR 281
|
330 340
....*....|....*....|...
gi 1907082213 1601 QAGSIQMLEQAKLRLEMEMERMR 1623
Cdd:pfam00038 282 QLREYQELLNVKLALDIEIATYR 304
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1434-1987 |
7.65e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.72 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1434 EDKMEVEQQSRRQLE----RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNH---------ELEKKQ 1500
Cdd:PRK10246 231 EEKQLLTAQQQQQQSlnwlTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHweriqeqsaALAHTR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1501 RRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDlDIAGFTQKVVSLEAELqdisSQESKDEASLAKV 1580
Cdd:PRK10246 311 QQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHD-RFRQWNNELAGWRAQF----SQQTSDREQLRQW 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1581 KKQLRDLEAKVKDQEE-----ELDEQAGSI-QMLEQAKLRlememERMRQTHSK--EMESRDEEVEEARQSCQKKLKQME 1652
Cdd:PRK10246 386 QQQLTHAEQKLNALPAitltlTADEVAAALaQHAEQRPLR-----QRLVALHGQivPQQKRLAQLQVAIQNVTQEQTQRN 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1653 VQLEEeyedKQKALREKRELESKLSTLSDQvnqrdfesEKRLrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKnqL 1732
Cdd:PRK10246 461 AALNE----MRQRYKEKTQQLADVKTICEQ--------EARI-KDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALE--P 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1733 EESEFTCAAAVKARKAMEVEMEDLHLQIDdiakaktALEEQLsrlQREKNEIQNRLEEDQEdmneLMKKHKAAVAQASRD 1812
Cdd:PRK10246 526 GVNQSRLDALEKEVKKLGEEGAALRGQLD-------ALTKQL---QRDESEAQSLRQEEQA----LTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1813 MAQMNDLQAQIEESNKEKQELQE--KLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFEKTQVK-RLENLASRLK 1889
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHERQLRLlsQRHELQGQIA-------------AHNQQIIQYQQQIEQRQQQLLtALAGYALTLP 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1890 ETMEKLT--EERDQRAAAENREKEQNKRLQRQ------LRDTKEEMSELARKEAEAS----RKKHElemDLESLEAANQS 1957
Cdd:PRK10246 659 QEDEEASwlATRQQEAQSWQQRQNELTALQNRiqqltpLLETLPQSDDLPHSEETVAldnwRQVHE---QCLSLHSQLQT 735
|
570 580 590
....*....|....*....|....*....|
gi 1907082213 1958 LQADLKLAFKRIGDLQAAIEDEMESDENED 1987
Cdd:PRK10246 736 LQQQDVLEAQRLQKAQAQFDTALQASVFDD 765
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1416-1673 |
8.86e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.30 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1416 ERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRlgdlqadsdESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnHE 1495
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERKRYRQELEEQIEER---------EQKRQEEYEEKLQEREQMDEIVERIQEEDQAEA-EE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1496 LEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftqkvvsLEAELQDIssqeskdEA 1575
Cdd:pfam13868 121 KLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEE-------------REAEREEI-------EE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1576 SLAKVKKQLRDLEAKVKDQEEELDEQagsiqmleQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQK----KLKQM 1651
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDEL--------RAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEqielKERRL 252
|
250 260
....*....|....*....|..
gi 1907082213 1652 EVQLEEEYEDKQKALREKRELE 1673
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDE 274
|
|
| PDZ4_Scribble-like |
cd06701 |
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ... |
220-307 |
8.87e-06 |
|
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467185 [Multi-domain] Cd Length: 98 Bit Score: 46.45 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPTGDFGFSLR------RTTMLDRAPEGQAYRRVVHfaePGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEI 292
Cdd:cd06701 6 ELTIVKEPGEKLGISIRggakghAGNPLDPTDEGIFISKINP---DGAAARD---GrLKVGQRILEVNGQSLLGATHQEA 79
|
90
....*....|....*
gi 1907082213 293 VEMIRQSGDSVRLKV 307
Cdd:cd06701 80 VRILRSVGDTLTLLV 94
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1784-2007 |
9.07e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1784 IQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKE----KQELQEKLQALQSQVEFLEQSMvdKSLVSR 1859
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRElesrVAELKEELRQSREKHEELEEKY--KELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1860 QEAKIRELETRLEFEKTQVKRLEnlasRLKETMEKLTEERDQRAAAENREKEQNKRLQRQlrdtkeemselaRKEAEASR 1939
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIR----ELEEDIKTLTQRVLERETELERMKERAKKAGAQ------------RKEEEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1940 KkhELEMDLESLEAANQSLQADLKLAFKRIGdlqaaiEDEMESDENEDLINSLQDMVTKYQKKKNKLE 2007
Cdd:pfam07888 174 K--QLQAKLQQTEEELRSLSKEFQELRNSLA------QRDTQVLQLQDTITTLTQKLTTAHRKEAENE 233
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
586-721 |
9.95e-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: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 586 LLEAFGNSPTIMNGSATRFSQILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEA------TFNVFYYLLACGD 654
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 655 A-----TLRTELHLNHL----------AENNVFGIVplSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYH 719
Cdd:cd14894 335 AfpfmrLLAKELHLDGIdcsaltylgrSDHKLAGFV--SKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLW 412
|
..
gi 1907082213 720 LG 721
Cdd:cd14894 413 LG 414
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1499-1906 |
1.01e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.06 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1499 KQRRFDSElsqaheETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLD-IAGFTQKVVSLEAELQDISSQesKDEASL 1577
Cdd:PLN02939 38 RRRGFSSQ------QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtVMELPQKSTSSDDDHNRASMQ--RDEAIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1578 AKVKKQLRdleaKVKDQEEELDEQAGS-IQMLEQAklrlEMEMERMRQTHSKEMESRDEEVEEaRQSCQKKLKQMEVQLE 1656
Cdd:PLN02939 110 AIDNEQQT----NSKDGEQLSDFQLEDlVGMIQNA----EKNILLLNQARLQALEDLEKILTE-KEALQGKINILEMRLS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1657 EEYEDKQKALREKRELEsklsTLSDQVNQRDFESEKRLRKDLKRTKALLADaqimLDHLK-NNAPSKREIAQLKNQL--- 1732
Cdd:PLN02939 181 ETDARIKLAAQEKIHVE----ILEEQLEKLRNELLIRGATEGLCVHSLSKE----LDVLKeENMLLKDDIQFLKAELiev 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1733 EESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEIqnrLEEDQEDMNELMKKHKAAVAQASRD 1812
Cdd:PLN02939 253 AETEERVFKLEKERSLLDASLRELESKF-------IVAQEDVSKLSPLQYDC---WWEKVENLQDLLDRATNQVEKAALV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1813 MAQMNDLQAQI---EESNKEKQELQEKLQalqsQVEFLEQSMvdKSLVSRQEAKIRELETrlefektQVKRLENLASRLK 1889
Cdd:PLN02939 323 LDQNQDLRDKVdklEASLKEANVSKFSSY----KVELLQQKL--KLLEERLQASDHEIHS-------YIQLYQESIKEFQ 389
|
410
....*....|....*..
gi 1907082213 1890 ETMEKLTEERDQRAAAE 1906
Cdd:PLN02939 390 DTLSKLKEESKKRSLEH 406
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1459-1836 |
1.12e-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: 50.19 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1459 DESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMllaeafs 1537
Cdd:pfam15905 24 EKSQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKElEKEIRALVQERGEQDKRL------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1538 lkQQMEEKdldiagftqkVVSLEAELQDISSQESKDEASLAKVKKQLRDLeAKVKDqeeeldeqagsiqmLEQAKLRLEM 1617
Cdd:pfam15905 97 --QALEEE----------LEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNE--------------LLKAKFSEDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1618 EMERMRQTHSKEMESRDEeVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRkd 1697
Cdd:pfam15905 150 TQKKMSSLSMELMKLRNK-LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLE-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1698 lkrtkalladaqimldhlknnapskrEIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1777
Cdd:pfam15905 227 --------------------------YITELSCVSEQVE-------KYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082213 1778 QREKNEIQNRLEEDQEDMNELMKKHKAavaQASRDMAQMNDLQAQIEESNKEKQELQEK 1836
Cdd:pfam15905 274 SKQIKDLNEKCKLLESEKEELLREYEE---KEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1527-1849 |
1.37e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1527 EKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEAS-------LAKVKKQLR-------------D 1586
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDyqaasdhLNLVQTALRqqekieryqadleE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1587 LEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMR-------------QTHSKEMESRDEEVEEARQSCQK---KLKQ 1650
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqaldvqQTRAIQYQQAVQALERAKQLCGLpdlTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1651 MEVQLEEeYEDKQKALREK-RELESKLSTLSDQVNQRD------------------FESEKRLRKDLKRTKALLADAQIM 1711
Cdd:PRK04863 440 AEDWLEE-FQAKEQEATEElLSLEQKLSVAQAAHSQFEqayqlvrkiagevsrseaWDVARELLRRLREQRHLAEQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1712 LDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE- 1790
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRl 598
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1791 ---------DQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQ 1849
Cdd:PRK04863 599 aarapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1692-1978 |
1.58e-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: 49.53 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1692 KRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE-----MEDLHLQIDDIAKA 1766
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEerkryRQELEEQIEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1767 KtalEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQE-KLQALQSQVE 1845
Cdd:pfam13868 89 R---QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRILEYLKEKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1846 FLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKR-----LQRQL 1920
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQelqqaREEQI 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1921 RDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRigDLQAAIED 1978
Cdd:pfam13868 246 ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR--ELEKQIEE 301
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1280-1655 |
1.62e-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: 50.29 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1280 FTTVRPLIQV-QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRlssdrletriSELTSELTDERNTGESASQLLDAETAE 1358
Cdd:pfam15964 349 FEKTKALIQCeQLKSELERQKERLEKELASQQEKRAQEKEALR----------KEMKKEREELGATMLALSQNVAQLEAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1359 RLRTEKEMKELQTQYDALKKQMEVMemevmearliraaeingEVDDDDAGGEWR-------LKYERAVREVDFTKKRLQQ 1431
Cdd:pfam15964 419 VEKVTREKNSLVSQLEEAQKQLASQ-----------------EMDVTKVCGEMRyqlnqtkMKKDEAEKEHREYRTKTGR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1432 ELEDKmeveQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDT--KLHLEGQqvrnhELEKKQRRFDSEL-S 1508
Cdd:pfam15964 482 QLEIK----DQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESehQLHLTRL-----EKESIQQSFSNEAkA 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1509 QAHEETQREK----------LQREKLQREKDMLLAEAFSLkqqmeekdldIAGFTQKVVSLEAELQDISSQESKDEASLA 1578
Cdd:pfam15964 553 QALQAQQREQeltqkmqqmeAQHDKTVNEQYSLLTSQNTF----------IAKLKEECCTLAKKLEEITQKSRSEVEQLS 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1579 KVKKQLRDLEAKVKDQEEELDEQAgsIQ---MLEQAKLRLEmEMERMRQTHSK---EMESRDEEVEEARQSCQKKLKQME 1652
Cdd:pfam15964 623 QEKEYLQDRLEKLQKRNEELEEQC--VQhgrMHERMKQRLR-QLDKHCQATAQqlvQLLSKQNQLFKERQNLTEEVQSLR 699
|
...
gi 1907082213 1653 VQL 1655
Cdd:pfam15964 700 SQV 702
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1633-1974 |
1.69e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1633 RDEEVEEArQSCQKKLKQMEVQLEEEyedkQKALREkreLESKLSTLSdqvnqrdfESEKRLRKDLKRTKALLADAQIML 1712
Cdd:PRK04863 281 RRVHLEEA-LELRRELYTSRRQLAAE----QYRLVE---MARELAELN--------EAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1713 DHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKA----KTALEEQLSRLQREKNEIQnRL 1788
Cdd:PRK04863 345 RQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladyQQALDVQQTRAIQYQQAVQ-AL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1789 EEDQEdMNELMKkhkAAVAQASRDMAQmndLQAQIEESNKEKQELQEKL---QALQSQVEF---LEQSMVDKslVSRQEA 1862
Cdd:PRK04863 424 ERAKQ-LCGLPD---LTADNAEDWLEE---FQAKEQEATEELLSLEQKLsvaQAAHSQFEQayqLVRKIAGE--VSRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1863 K--IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDqraaAENREKEQNKRLQRQLRDtkEEMSELARKEAEASRK 1940
Cdd:PRK04863 495 WdvARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQR----AERLLAEFCKRLGKNLDD--EDELEQLQEELEARLE 568
|
330 340 350
....*....|....*....|....*....|....
gi 1907082213 1941 khELEMDLESLEAANQSLQADLKLAFKRIGDLQA 1974
Cdd:PRK04863 569 --SLSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1453-1948 |
1.69e-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: 50.07 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1453 DLQADSDESQralqQLKKKCQRL---TAELQDTKLHLegqQVRNHELEKKQRRFDSELSQA--------HEETQREKLQR 1521
Cdd:pfam05622 1 DLSEAQEEKD----ELAQRCHELdqqVSLLQEEKNSL---QQENKKLQERLDQLESGDDSGtpggkkylLLQKQLEQLQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1522 EKLQREKDmllAEAFSLKQQMEEKD-LDIAGFTQKVVSLEAElqdisSQESKDE-----ASLAKVKKqlrdLEAKV---K 1592
Cdd:pfam05622 74 ENFRLETA---RDDYRIKCEELEKEvLELQHRNEELTSLAEE-----AQALKDEmdilrESSDKVKK----LEATVetyK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1593 DQEEELDEQAGSIQMLEqaklrlEMEMERMRQTHSKEMESRDEEVEEAR-QSCQKKLKQMEVQLEEEYEDKQKALREKRE 1671
Cdd:pfam05622 142 KKLEDLGDLRRQVKLLE------ERNAEYMQRTLQLEEELKKANALRGQlETYKRQVQELHGKLSEESKKADKLEFEYKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1672 LESKLSTLsdqvnQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS--------------------KREIAQLknQ 1731
Cdd:pfam05622 216 LEEKLEAL-----QKEKERLIIERDTLRETNEELRCAQLQQAELSQADALlspssdpgdnlaaeimpaeiREKLIRL--Q 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1732 LEESEFTCaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLsRLQREK-NEIQNRLEEDQEDMNELMKKHKAAVAqas 1810
Cdd:pfam05622 289 HENKMLRL----GQEGSYRERLTELQQLLEDANRRKNELETQN-RLANQRiLELQQQVEELQKALQEQGSKAEDSSL--- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1811 rdmaqmndLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdkSLVSRQEAKIRELETRLefektQVKRLENLA--SRL 1888
Cdd:pfam05622 361 --------LKQKLEEHLEKLHEAQSELQKKKEQIEELEP-----KQDSNLAQKIDELQEAL-----RKKDEDMKAmeERY 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1889 KETMEKLTEE-RDQRAAAENREKEQNKRLQRQLRDtKEEMSELARKEAEASRKKHELEMDL 1948
Cdd:pfam05622 423 KKYVEKAKSViKTLDPKQNPASPPEIQALKNQLLE-KDKKIEHLERDFEKSKLQREQEEKL 482
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1645-1960 |
1.77e-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: 50.14 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1645 QKKLKQMEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS 1721
Cdd:pfam09731 124 QEKEKALEEVLKEaisKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1722 KREIAQLKNQLEESEFTCAAAVKARKAME--VEMEDLHLQIDDIAKAKTALEEQLSRLQREK--NEIQNRLEEDQEDMNE 1797
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEekVEKAQSLAKLVDQYKELVASERIVFQQELVSifPDIIPVLKEDNLLSND 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1798 lmkKHKAAVAQASRDMAQmndLQAQIEEsnKEKQELQEKLQALQSQVEFLEQSmvDKSLVSRQEAKIRELET--RLEFEK 1875
Cdd:pfam09731 284 ---DLNSLIAHAHREIDQ---LSKKLAE--LKKREEKHIERALEKQKEELDKL--AEELSARLEEVRAADEAqlRLEFER 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1876 TQVKRLENLASRLKETMEKLTEERDQRaaAENREKEQNKRLQRQ-LRDTKEEMSE----LARKEAEASRKKHELEMDLES 1950
Cdd:pfam09731 354 EREEIRESYEEKLRTELERQAEAHEEH--LKDVLVEQEIELQREfLQDIKEKVEEeragRLLKLNELLANLKGLEKATSS 431
|
330
....*....|.
gi 1907082213 1951 -LEAANQSLQA 1960
Cdd:pfam09731 432 hSEVEDENRKA 442
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1552-1619 |
1.81e-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: 47.62 E-value: 1.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1552 FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQML--EQAKLRLEMEM 1619
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLqdELVALQLQLNM 145
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1785-1978 |
1.84e-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: 48.45 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1785 QNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvDKSLVSRQEAKI 1864
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAE-------AAPKEILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1865 RELETRLEFEKTQvkrLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQR------QLRDTKEEMSELARKEAEAS 1938
Cdd:pfam12795 81 EELEQRLLQTSAQ---LQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQirnrlnGPAPPGEPLSEAQRWALQAE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082213 1939 RKKHELEMDLESLEAANQSLQADL-----KLAFKRIGDLQAAIED 1978
Cdd:pfam12795 158 LAALKAQIDMLEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQA 202
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1805-1986 |
2.04e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1805 AVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEqsmvdkslvsrqeAKIRELETRLEFEKTQVKRLENL 1884
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALE-------------ARLEAAKTELEDLEKEIKRLELE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1885 ASRLKETMEKLTEErdQRAAAENREKEQnkrLQRQLRDTKEEMSELARKEAEasrkkheLEMDLESLEAANQSLQADLKL 1964
Cdd:COG1579 68 IEEVEARIKKYEEQ--LGNVRNNKEYEA---LQKEIESLKRRISDLEDEILE-------LMERIEELEEELAELEAELAE 135
|
170 180
....*....|....*....|..
gi 1907082213 1965 AFKRIGDLQAAIEDEMESDENE 1986
Cdd:COG1579 136 LEAELEEKKAELDEELAELEAE 157
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1634-1993 |
2.23e-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: 49.30 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1634 DEEVEEARQScQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesekRLRKDLKRTKALLADAQIMLD 1713
Cdd:pfam19220 37 EAILRELPQA-KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELE--------ELVARLAKLEAALREAEAAKE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1714 HLKnnapskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLqREKNEIqnrLEEDQE 1793
Cdd:pfam19220 108 ELR------IELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATA-RERLAL---LEQENR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1794 DMNELMKKHKAAVAQASRDMAqmndlqaqieesnkekqELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLE 1872
Cdd:pfam19220 178 RLQALSEEQAAELAELTRRLA-----------------ELETQLDATRARLRALEGQLAAeQAERERAEAQLEEAVEAHR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1873 FEKT-QVKRLENLASRLKETMEKLTEERDQ--RAAAENREKEQN--------KRLQRQLRDTKEEMSELARKEAEASRKK 1941
Cdd:pfam19220 241 AERAsLRMKLEALTARAAATEQLLAEARNQlrDRDEAIRAAERRlkeasierDTLERRLAGLEADLERRTQQFQEMQRAR 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1942 HELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE---DEMESDE------NEDLINSLQ 1993
Cdd:pfam19220 321 AELEERAEMLTKALAAKDAALERAEERIASLSDRIAeltKRFEVERaaleqaNRRLKEELQ 381
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1434-1643 |
2.51e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1434 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEE 1513
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1514 TQREKLQREKLqrekDMLL-AEAFS--------LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL 1584
Cdd:COG3883 95 LYRSGGSVSYL----DVLLgSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082213 1585 RDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS 1643
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1814-2024 |
2.61e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 48.10 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1814 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETrlEFEKTQvKRLENLASRLKEtME 1893
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAE------VAALNRRIQLLEE--ELERTE-ERLAEALEKLEE-AE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1894 KLTEERDQ-RAAAENREKEQNKR---LQRQLRDTKEEMSELARKEAEASRKKHELEMDLE-------SLEAANQSLQADL 1962
Cdd:pfam00261 71 KAADESERgRKVLENRALKDEEKmeiLEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraeeraeLAESKIVELEEEL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1963 KLAFKRIGDLQAAIEDEMES-DENEDLINSLQD----MVTKYQ---KKKNKLEGDSDvdsELEDRVDGVK 2024
Cdd:pfam00261 151 KVVGNNLKSLEASEEKASEReDKYEEQIRFLTEklkeAETRAEfaeRSVQKLEKEVD---RLEDELEAEK 217
|
|
| CtpA |
COG0793 |
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
269-309 |
2.65e-05 |
|
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440556 [Multi-domain] Cd Length: 341 Bit Score: 48.71 E-value: 2.65e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1907082213 269 GLVPGDRLVEINGQNVENKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:COG0793 88 GIKPGDIILAIDGKSVAGLTLDDAVKLLRgKAGTKVTLTIKR 129
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1290-1661 |
3.01e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.19 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1290 QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETrisELTSELTDERNTGESASQlldaETAERLRTEKEMKEL 1369
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENA---ESSKRLNENANNLIKQFE----NTKEKIAEYTKSIDI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1370 QTQYDALKKQmevmemevmearlIRAAEINGEvddddaggewrlkYERAVREVDFTKKRLQQELEdkmeveqQSRRQLER 1449
Cdd:COG5185 308 KKATESLEEQ-------------LAAAEAEQE-------------LEESKRETETGIQNLTAEIE-------QGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1450 RLGDLQADSDESQRALQQlkkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKL-QREKLQREK 1528
Cdd:COG5185 355 NLEAIKEEIENIVGEVEL-----SKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADrQIEELQRQI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1529 DmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAK--VKKQLRDLEAKVKDQEEELDEQAGSiq 1606
Cdd:COG5185 430 E-------QATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINrsVRSKKEDLNEELTQIESRVSTLKAT-- 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1607 mLEQAKLRLEMEMERMRQTHSKEMESRDEEvEEARQSCQKKLKQMEVQLEEEYED 1661
Cdd:COG5185 501 -LEKLRAKLERQLEGVRSKLDQVAESLKDF-MRARGYAHILALENLIPASELIQA 553
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1689-1962 |
3.05e-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: 48.43 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1689 ESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREIAQLKNQL-EESEFTCAAAVKARKAMEVEMEDLHLQIDdiaKAK 1767
Cdd:pfam09311 16 EQEAETRDQVKKLQEMLRQAN---DQLEKTMKDKKELEDKMNQLsEETSNQVSTLAKRNQKSETLLDELQQAFS---QAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1768 TALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqaSRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFL 1847
Cdd:pfam09311 90 RNFQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHV---SLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADHM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1848 EQSMVDKSLVSRQEAKiRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLqRQLRDTKEEM 1927
Cdd:pfam09311 167 EEKLKAEILFLKEQIQ-AEQCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQLENGLTEKI-RQLEDLQTTK 244
|
250 260 270
....*....|....*....|....*....|....*
gi 1907082213 1928 SELARKEAEASRKKHELEMDLESLEAANQSLQADL 1962
Cdd:pfam09311 245 GSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTEL 279
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
1598-1950 |
3.17e-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: 48.29 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1598 LDEQAGSIQMLEQAKLRLEMEMERMRqTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKREleskls 1677
Cdd:pfam09755 23 REQLQKRIESLQQENRVLKMELETYK-LRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKE------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1678 TLSDQVNQRdfesEKRLRKDLKRTkalladaqimLDHLKnnapskREIAQLKNQLEeseftcaaavkarKAMEVEMEDLH 1757
Cdd:pfam09755 96 TLAMNYEQE----EEFLTNDLSRK----------LTQLR------QEKVELEQTLE-------------QEQEYQVNKLM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1758 LQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM-NELMKKhkaavaqasrdmaqMNDLQAqieesnkEKQELQEK 1836
Cdd:pfam09755 143 RKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQEALvNRLWKR--------------MDKLEA-------EKRLLQEK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1837 LQALQSQVEFLEQSMVDKSLVSRQEAKIRELetrlefeKTQVKRLENlasRLKETMEKLTEERDQRAAAENREKEQNKRL 1916
Cdd:pfam09755 202 LDQPVSAPPSPRDSTSEGDTAQNLTAHIQYL-------RKEVERLRR---QLATAQQEHTEKMAQYAQEERHIREENLRL 271
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907082213 1917 QRQLRDTKEEMSELARK--EAEASrkkheLEMDLES 1950
Cdd:pfam09755 272 QRKLQLEMERREALCRHlsESESS-----LEMDEER 302
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1619-1965 |
3.21e-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: 49.36 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1619 MERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQ----LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFE----- 1689
Cdd:pfam07111 21 LERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEgsqaLSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRleaqa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1690 --------SEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEMEDLHLQID 1761
Cdd:pfam07111 101 meldalavAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLT-QAHEEALSSLTSKAEGLEKSLN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1762 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMN---ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ 1838
Cdd:pfam07111 180 SLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEaqvTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1839 ALQSQVEFLE---QSMVdKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEerdQRAAAENREKEQNKR 1915
Cdd:pfam07111 260 DLQATVELLQvrvQSLT-HMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---QLKAQDLEHRDSVKQ 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1916 LQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLA 1965
Cdd:pfam07111 336 LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRA 385
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1591-1925 |
3.57e-05 |
|
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: 48.52 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1591 VKDQEEELDEQAGSIQMLEQAKLRL---------EMEMER-----MRQTHSKEMESRDEEVEEARQSCQKKL--KQMEVQ 1654
Cdd:pfam15742 1 VSSGEKLKYQQQEEVQQLRQNLQRLqilctsaekELRYERgknldLKQHNSLLQEENIKIKAELKQAQQKLLdsTKMCSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1655 LEEEYEDKQKALREkRELESKLSTLSDQvnqrdfeSEKRLRKDLKRTKALLADAQIMldhlknnapskreIAQLKNQLEE 1734
Cdd:pfam15742 81 LTAEWKHCQQKIRE-LELEVLKQAQSIK-------SQNSLQEKLAQEKSRVADAEEK-------------ILELQQKLEH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1735 SEFTCAAAVKA--RKAMEVEMEDLhlqIDDIAKAKTAL-EEQLSR--LQREKNEIQNRLEEDQEDMNELMKKHKAAVAQA 1809
Cdd:pfam15742 140 AHKVCLTDTCIleKKQLEERIKEA---SENEAKLKQQYqEEQQKRklLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1810 SRDMAQMNDLQAQI---EESNKEKQELQEKLQALQSQVEFL--EQSMVDKSL----------VSRQEAKIRELETRLEFE 1874
Cdd:pfam15742 217 QQQEAQLKQLENEKrksDEHLKSNQELSEKLSSLQQEKEALqeELQQVLKQLdvhvrkynekHHHHKAKLRRAKDRLVHE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1875 KTQ----VKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKE 1925
Cdd:pfam15742 297 VEQrderIKQLENEIGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQEE 351
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1544-1703 |
3.86e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1544 EKDLDIAGFTQKVVSLEAELQDIssqeskdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEmemERMR 1623
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAEL-------EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1624 QTHS-KEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKALRE-KRELESKLSTLSDQVNQRDfESEKRLRKDLKRT 1701
Cdd:COG1579 84 NVRNnKEYEALQKEIESLKRR-ISDLEDEILELMERIEELEEELAElEAELAELEAELEEKKAELD-EELAELEAELEEL 161
|
..
gi 1907082213 1702 KA 1703
Cdd:COG1579 162 EA 163
|
|
| PDZ_6 |
pfam17820 |
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. |
269-308 |
4.00e-05 |
|
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
Pssm-ID: 436067 [Multi-domain] Cd Length: 54 Bit Score: 43.29 E-value: 4.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1907082213 269 GLVPGDRLVEINGQNVENKsrDEIVEMIRQSGDS-VRLKVQ 308
Cdd:pfam17820 15 GLRVGDVILAVNGKPVRSL--EDVARLLQGSAGEsVTLTVR 53
|
|
| PDZ2_Par3-like |
cd23058 |
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ... |
260-307 |
4.10e-05 |
|
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP, Drosophila Bazooka) and related domains. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include Par3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467271 [Multi-domain] Cd Length: 93 Bit Score: 44.17 E-value: 4.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 260 GAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQS--GDSVRLKV 307
Cdd:cd23058 43 GAAIQD---GrLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTklGGTVSLVV 90
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1287-1597 |
4.19e-05 |
|
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: 48.95 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1287 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEM 1366
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1367 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDK---MEVEQQS 1443
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1444 RRQLERRlgdlqadSDESQRALQQLKKKCQRLTAELQDTKLHLeGQQVRNHELEKKQRRFDSElsQAHEETQREKLQRE- 1522
Cdd:pfam05483 617 NKALKKK-------GSAENKQLNAYEIKVNKLELELASAKQKF-EEIIDNYQKEIEDKKISEE--KLLEEVEKAKAIADe 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1523 --KLQREKDML----LAEAFSLKQQ--------MEEKDLDIAGFTQK-------VVSLEAELQDIssqeskdEASLAKVK 1581
Cdd:pfam05483 687 avKLQKEIDKRcqhkIAEMVALMEKhkhqydkiIEERDSELGLYKNKeqeqssaKAALEIELSNI-------KAELLSLK 759
|
330
....*....|....*....
gi 1907082213 1582 KQL---RDLEAKVKDQEEE 1597
Cdd:pfam05483 760 KQLeieKEEKEKLKMEAKE 778
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1434-1838 |
4.26e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 48.86 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1434 EDKMEVEQQSRRQLERRLGDLQADSDESQ--------RALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQRrfdS 1505
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKhtqnvalnKKLSDIKTEYLYELNVLKEKS---------EAELTSKTK---K 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1506 ELSQAHEETQREKLQREKLQREKDMLLAEA-FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESkdEASLAKVKKQL 1584
Cdd:NF033838 122 ELDAAFEQFKKDTLEPGKKVAEATKKVEEAeKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--ELELVKEEAKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1585 RDLEAKVKDQEEELDEQAGSIQMLEQAKlrlememermrqTHSKEMEsrdeevEEARQSCQKKLKQ-MEVQLEEEYEDKQ 1663
Cdd:NF033838 200 PRDEEKIKQAKAKVESKKAEATRLEKIK------------TDREKAE------EEAKRRADAKLKEaVEKNVATSEQDKP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1664 KAlREKRELESKLSTlsdqvnqrdfesekrlrKDLKRTKALLADAQIMLDHLKNnaPSKREiaqlKNQLEESEFTCAAAV 1743
Cdd:NF033838 262 KR-RAKRGVLGEPAT-----------------PDKKENDAKSSDSSVGEETLPS--PSLKP----EKKVAEAEKKVEEAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1744 KARKAMEVE---------MEDLHLQiddIAKAKTALEE-QLSRLQREKNEIQNrleedQEDMNELMKKHKAAVAQASRdM 1813
Cdd:NF033838 318 KKAKDQKEEdrrnyptntYKTLELE---IAESDVKVKEaELELVKEEAKEPRN-----EEKIKQAKAKVESKKAEATR-L 388
|
410 420
....*....|....*....|....*
gi 1907082213 1814 AQMNDLQAQIEESNKEKQELQEKLQ 1838
Cdd:NF033838 389 EKIKTDRKKAEEEAKRKAAEEDKVK 413
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1778-1957 |
5.98e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.41 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1778 QREKNEIQNRLEEDQEDMNELMKKHkaaVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVE----FLEQSMVD 1853
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREE---LELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAqeraRQQQEEFR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1854 KSLVSRQEAKIRELETRLEFEKTQVKRLE-NLASRLKETMEKLTEERDQraaaenrekeqnkrLQRQlrdtKEEMSELAR 1932
Cdd:pfam15709 430 RKLQELQRKKQQEEAERAEAEKQRQKELEmQLAEEQKRLMEMAEEERLE--------------YQRQ----KQEAEEKAR 491
|
170 180
....*....|....*....|....*
gi 1907082213 1933 KEAEASRKKHELEMDLESLEAANQS 1957
Cdd:pfam15709 492 LEAEERRQKEEEAARLALEEAMKQA 516
|
|
| PDZ_syntrophin-like |
cd06801 |
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ... |
270-308 |
7.08e-05 |
|
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntrophin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467262 [Multi-domain] Cd Length: 83 Bit Score: 43.33 E-value: 7.08e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1907082213 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06801 44 LFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTLTVK 82
|
|
| PDZ2_MAGI-1_3-like |
cd06732 |
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
269-308 |
7.63e-05 |
|
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467214 [Multi-domain] Cd Length: 82 Bit Score: 43.31 E-value: 7.63e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1907082213 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQS--GDSVRLKVQ 308
Cdd:cd06732 39 GLQEGDLIVEINGQNVQNLSHAQVVDVLKECpkGSEVTLLVQ 80
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1426-1624 |
7.88e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.06 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1426 KKRLQQELEDKMEVEQ-QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhLEGQqvrnHELEKKQRRfd 1504
Cdd:pfam09787 23 KEKLIASLKEGSGVEGlDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE----LEAQ----QQEEAESSR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1505 SELSQAHEETQREKLQREKLQrekdmllAEAFSLKQQM----EEKDLDIAGFTQKVVSLEAELQDISSQ-ESKDEASLAK 1579
Cdd:pfam09787 93 EQLQELEEQLATERSARREAE-------AELERLQEELryleEELRRSKATLQSRIKDREAEIEKLRNQlTSKSQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082213 1580 vkkqlRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQ 1624
Cdd:pfam09787 166 -----SELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQ 205
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1288-1657 |
9.10e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.91 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1288 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRIseltseLTDERNTGESASQLldaetaerlrtEKEMK 1367
Cdd:PRK04778 113 LLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL------LANRFSFGPALDEL-----------EKQLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1368 ELQTQYDalkkqmevmemevmearliRAAEINGEVDdddaggewrlkYERAVREVDFTKKRLQQeLEDKME------VEQ 1441
Cdd:PRK04778 176 NLEEEFS-------------------QFVELTESGD-----------YVEAREILDQLEEELAA-LEQIMEeipellKEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1442 QSR------------RQLER---RLGDLQADSDesqraLQQLKKKCQRLTAELQDtkLHLEGQQVRNHELEKK------- 1499
Cdd:PRK04778 225 QTElpdqlqelkagyRELVEegyHLDHLDIEKE-----IQDLKEQIDENLALLEE--LDLDEAEEKNEEIQERidqlydi 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1500 -QRRFDSElSQAHEETQREKLQREKLQREKDMLLAEAFSLKQ--QMEEKDLDIA-GFTQKVVSLEAELQDISSQESKDEA 1575
Cdd:PRK04778 298 lEREVKAR-KYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsyTLNESELESVrQLEKQLESLEKQYDEITERIAEQEI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1576 SLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQ---THSKEMESRD-----EEVEEARQSCQKK 1647
Cdd:PRK04778 377 AYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklhEIKRYLEKSNlpglpEDYLEMFFEVSDE 456
|
410
....*....|
gi 1907082213 1648 LKQMEVQLEE 1657
Cdd:PRK04778 457 IEALAEELEE 466
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1300-1479 |
9.44e-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: 46.46 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1300 DEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQT--QYDALK 1377
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1378 KQmevmemEVMEARLIRAAeingevddddaggewrlkyERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLGDLQAD 1457
Cdd:COG1579 96 KE------IESLKRRISDL-------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 1907082213 1458 SDESQRALQQLKKKCQRLTAEL 1479
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1864-2029 |
1.02e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1864 IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLqRQLRDTKEEMSELARKEAEASRKKHE 1943
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1944 LEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSdvdSELEDRVDGV 2023
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL---SRLEEEINGI 326
|
....*.
gi 1907082213 2024 KSWLSK 2029
Cdd:PRK03918 327 EERIKE 332
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1459-1602 |
1.03e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1459 DESQRALQQLKKKCQrLTA--ELQDTKLHLEGQ-QVRNHELEKKQRRFdselsQAHEETQREKLqrEKLQREKDMLLAEA 1535
Cdd:PRK12704 45 EEAKKEAEAIKKEAL-LEAkeEIHKLRNEFEKElRERRNELQKLEKRL-----LQKEENLDRKL--ELLEKREEELEKKE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1536 FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQeSKDEAS---LAKVKKQLR-DLEAKVKDQEEELDEQA 1602
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEEQLQELERISGL-TAEEAKeilLEKVEEEARhEAAVLIKEIEEEAKEEA 186
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1857-1974 |
1.04e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1857 VSRQEAKIRELEtrlefekTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRDTKEEMSELARKEAE 1936
Cdd:COG2433 408 LTEEEEEIRRLE-------EQVERLEAEVEELEAELEEK--------------DERIERLERELSEARSEERREIRKDRE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907082213 1937 ASRKKHE---LEMDLESLEAANQSLQADLKLaFKRIGDLQA 1974
Cdd:COG2433 467 ISRLDREierLERELEEERERIEELKRKLER-LKELWKLEH 506
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
1862-1987 |
1.07e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 43.93 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1862 AKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEnrekEQNKRLQRQLRDTKEEMSELARKEAEASRKK 1941
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELE----AEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907082213 1942 HELEMDLESLEAANQSLQADLKlafKRIGDLQAAIEDEMESDENED 1987
Cdd:pfam04871 77 DDLLLLLGDLEEKVEKYKARLK---ELGEEVLSDDEDDDEDDEEDD 119
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1489-1963 |
1.10e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.90 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1489 QQVRNHELEKKQRRFDSE--LSQAHEETQR----EKLQREKLQREkdmLLAEAFSLKQQMEEK------------DLDIA 1550
Cdd:NF041483 76 QLLRNAQIQADQLRADAEreLRDARAQTQRilqeHAEHQARLQAE---LHTEAVQRRQQLDQElaerrqtveshvNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1551 GFTQKVVSLEAE---LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEM-------- 1619
Cdd:NF041483 153 WAEQLRARTESQarrLLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAERLLnaastqaq 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1620 ------ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesEKR 1693
Cdd:NF041483 233 eatdhaEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESAN------EQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1694 LRKdlkrtkalladaqimldhlknnapSKREIAQLKNQ-LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE 1772
Cdd:NF041483 307 TRT------------------------AKEEIARLVGEaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1773 --QLSRLQREKNEIQNRLEEDQEDM-----NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQ--------ELQEKL 1837
Cdd:NF041483 363 aaQLAKAARTAEEVLTKASEDAKATtraaaEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTkeyraktvELQEEA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1838 QALQSQVEFLEQSMVDKSLVSRQEAKireletrlefeKTQVKRLENLASRLKETMEKLTEERDQ--RAAAENREKEQNKR 1915
Cdd:NF041483 443 RRLRGEAEQLRAEAVAEGERIRGEAR-----------REAVQQIEEAARTAEELLTKAKADADElrSTATAESERVRTEA 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1916 LQR--QLRDTKEEMSELARKEAEasRKKHELEMDLESLEAANQSLQADLK 1963
Cdd:NF041483 512 IERatTLRRQAEETLERTRAEAE--RLRAEAEEQAEEVRAAAERAARELR 559
|
|
| PDZ3_DLG5-like |
cd06767 |
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
1.14e-04 |
|
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467248 [Multi-domain] Cd Length: 82 Bit Score: 42.70 E-value: 1.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907082213 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06767 42 GLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLVQ 81
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1768-1953 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1768 TALEEQLSRLQREKN----EIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1843
Cdd:pfam09787 43 TALTLELEELRQERDllreEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1844 VEFLEQSMVdKSLVSRQEaKIRELETRLEFEKTQVK--------------RLENLASRL--KETM-EKLTEERDQRAAAE 1906
Cdd:pfam09787 123 LRYLEEELR-RSKATLQS-RIKDREAEIEKLRNQLTsksqssssqselenRLHQLTETLiqKQTMlEALSTEKNSLVLQL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907082213 1907 NREKEQNKRLQ-RQLRDTKEEMSELARKEAEASRKKHELEMDLESLEA 1953
Cdd:pfam09787 201 ERMEQQIKELQgEGSNGTSINMEGISDGEGTRLRNVPGLFSESDSDRA 248
|
|
| PDZ_MPP3-MPP4-MPP7-like |
cd06799 |
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ... |
269-309 |
1.18e-04 |
|
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467260 [Multi-domain] Cd Length: 81 Bit Score: 42.62 E-value: 1.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1907082213 269 GLV-PGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06799 40 GLIhVGDELREVNGISVEGKDPEEVIQILANSQGPITFKLIP 81
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1765-2016 |
1.26e-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: 47.63 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1765 KAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA----QASRDMAQMND------LQAQIEEsnKEKQELQ 1834
Cdd:pfam15818 21 EAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAvfkkQLQMKMCALEEekgkyqLATEIKE--KEIEGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1835 EKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEKTQVKRLEN----LASR---LKETMEKLtEERDQRAAAEN 1907
Cdd:pfam15818 99 ETLKALQVSKYSLQKK------VSEMEQKLQLHLLAKEDHHKQLNEIEKyyatITGQfglVKENHGKL-EQNVQEAIQLN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1908 -REKEQNKRLQRQLRDTKEEM----SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFkrigDLQAAIEDEME- 1981
Cdd:pfam15818 172 kRLSALNKKQESEICSLKKELkkvtSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMEL----ELNKKINEEITh 247
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907082213 1982 -SDENEDLINSLQDMVTKYQKkknKLEGDSDVDSEL 2016
Cdd:pfam15818 248 iQEEKQDIIISFQHMQQLLQQ---QTQANTEMEAEL 280
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1549-1793 |
1.32e-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: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1549 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQaklrlememermrqthsk 1628
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1629 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESK-LSTLSDQVNQRDF--ESEKRLRKDLKRTKALL 1705
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsFSDFLDRLSALSKiaDADADLLEELKADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1706 ADAQIMLDHLKNnapskrEIAQLKNQLEEseftcaaavkARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ 1785
Cdd:COG3883 146 EAKKAELEAKLA------ELEALKAELEA----------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
....*...
gi 1907082213 1786 NRLEEDQE 1793
Cdd:COG3883 210 AAAAAAAA 217
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1722-1932 |
1.38e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.00 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1722 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEiQNRLEEDQEDMNELMKK 1801
Cdd:PRK11637 67 QQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQI-------DELNASIAKLEQQQAA-QERLLAAQLDAAFRQGE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1802 HKAAVAQASRDMAQ-------------------MNDLQAQIEESNKEKQELQEKlQALQSQVEFLEQSMVDKSLVSRQEA 1862
Cdd:PRK11637 139 HTGLQLILSGEESQrgerilayfgylnqarqetIAELKQTREELAAQKAELEEK-QSQQKTLLYEQQAQQQKLEQARNER 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082213 1863 K--IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD-------TKEEMSELAR 1932
Cdd:PRK11637 218 KktLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREAREAARVRDKQKQAKRkgstykpTESERSLMSR 296
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1765-2137 |
1.46e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 47.35 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1765 KAKTALEEQLSRLQ--REKNEIQNRLEEDQedmnelmkkhkaavAQASRDMAQMNDLQAQIEESNKEKQELQEKLqaLQS 1842
Cdd:PTZ00108 1031 AKKKDLVKELKKLGyvRFKDIIKKKSEKIT--------------AEEEEGAEEDDEADDEDDEEELGAAVSYDYL--LSM 1094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1843 QVEFLEQSMVDKsLVSRQEAKIRELEtrlEFEKTQVKR--LENLAsRLKETMEKlTEERDQRAAAENREKEQNKRL-QRQ 1919
Cdd:PTZ00108 1095 PIWSLTKEKVEK-LNAELEKKEKELE---KLKNTTPKDmwLEDLD-KFEEALEE-QEEVEEKEIAKEQRLKSKTKGkASK 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1920 LRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKY 1999
Cdd:PTZ00108 1169 LRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKN 1248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 2000 QKKKNKLEGDSDVDSELED-----RVDGVKSWLSKNKGPSKAPSDDGSLKSSRTalNSLPKEGKGPEERPSSVLSSLSYR 2074
Cdd:PTZ00108 1249 NSSKSSEDNDEFSSDDLSKegkpkNAPKRVSAVQYSPPPPSKRPDGESNGGSKP--SSPTKKKVKKRLEGSLAALKKKKK 1326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 2075 KRLTlkdsiggTGDQDSLLTTLSERATSPERPPRKARggPREEPDQaqgrrcEELDDCSSIFS 2137
Cdd:PTZ00108 1327 SEKK-------TARKKKSKTRVKQASASQSSRLLRRP--RKKKSDS------SSEDDDDSEVD 1374
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1741-1932 |
1.47e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.59 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1741 AAVKARKAMEVEMEDLHlqiDDIAKAKTALEEQLSRLQRekneIQNRLEEDQEDMNELMKKHKAAVAQASRDMA------ 1814
Cdd:COG1842 20 KAEDPEKMLDQAIRDME---EDLVEARQALAQVIANQKR----LERQLEELEAEAEKWEEKARLALEKGREDLArealer 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1815 ------QMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFEKTQVKRLENLAS-R 1887
Cdd:COG1842 93 kaeleaQAEALEAQLAQLEEQVEKLKEALRQLESKLE-------------ELKAKKDTLKARAKAAKAQEKVNEALSGiD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 1888 LKETMEKLT--EERDQRAAAEN---REKEQNKRLQRQLRDTKEEMS---ELAR 1932
Cdd:COG1842 160 SDDATSALErmEEKIEEMEARAeaaAELAAGDSLDDELAELEADSEvedELAA 212
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1684-1955 |
1.51e-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: 45.76 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1684 NQRDFESEKRLRKDLKRTKALLADAQImldhlknnapSKREIAQLKNQLEEseftcaAAVKARKAMEvemEDLHLQIDDI 1763
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDA----------SKQRAAAYQKALDD------APAELRELRQ---ELAALQAKAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1764 AKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNELMKkhkaavaqasrdmaQMNDLQAQIEESNKEKQELQEKLQALQS 1842
Cdd:pfam12795 69 AAPKEILASLsLEELEQRLLQTSAQLQELQNQLAQLNS--------------QLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1843 QvefLEQSMVDKSLVSrqEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRaaaenreKEQNKRLQRQLRD 1922
Cdd:pfam12795 135 R---LNGPAPPGEPLS--EAQRWALQAELAALKAQIDMLEQELLSNNNRQDLLKARRDLL-------TLRIQRLEQQLQA 202
|
250 260 270
....*....|....*....|....*....|...
gi 1907082213 1923 TKEEMSELARKEAEASRKkhELEMDLESLEAAN 1955
Cdd:pfam12795 203 LQELLNEKRLQEAEQAVA--QTEQLAEEAAGDH 233
|
|
| PDZ_rhophilin-like |
cd06712 |
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
225-307 |
1.55e-04 |
|
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This rhophilin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467196 [Multi-domain] Cd Length: 78 Bit Score: 42.19 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 225 RRPTGDFGFSLRrttmlDRAPegqayrrV-VHFAEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIVEMIRQSG-DS 302
Cdd:cd06712 7 TKEEGGFGFTLR-----GDSP-------VqVASVDPG-SCAAEA-GLKEGDYIVSVGGVDCKWSKHSEVVKLLKSAGeEG 72
|
....*
gi 1907082213 303 VRLKV 307
Cdd:cd06712 73 LELQV 77
|
|
| PDZ_SYNPO2-like |
cd10820 |
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ... |
269-308 |
1.73e-04 |
|
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNPO2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467264 [Multi-domain] Cd Length: 78 Bit Score: 42.30 E-value: 1.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907082213 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd10820 39 GLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
|
|
| PDZ1_L-delphilin-like |
cd06743 |
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ... |
269-299 |
2.25e-04 |
|
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467225 [Multi-domain] Cd Length: 76 Bit Score: 41.88 E-value: 2.25e-04
10 20 30
....*....|....*....|....*....|.
gi 1907082213 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:cd06743 36 GLQPGDQILELDGQDVSSLSCEAIIALARRC 66
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1581-1761 |
2.35e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1581 KKQLRDLEAKVKDQEEELDEQAgsiqMLEQAKLRLEMEMERMRqtHSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYE 1660
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEE----KLEAALLEAKELLLRER--NQQRQEARREREELQRE--EERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1661 DKQKALREKRELESKLSTLSDQVNQRdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEsEFTCA 1740
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEEL----EKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE-EADLE 173
|
170 180
....*....|....*....|.
gi 1907082213 1741 AAVKARKAMEVEMEDLHLQID 1761
Cdd:PRK12705 174 AERKAQNILAQAMQRIASETA 194
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1480-2001 |
2.45e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.75 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1480 QDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQreKLQREKLQREK-DMLLAEAFSLKQQMEEKDLDIagFTQKVVS 1558
Cdd:PTZ00440 617 EKNDLQEKVKYILNKFYKGDLQELLDELSHFLDDHK--YLYHEAKSKEDlQTLLNTSKNEYEKLEFMKSDN--IDNIIKN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1559 LEAELQDISSQesKDEAslakVKKQLRDLEAKVKDQEEELDEQAGSIQM-LEQAKlrlemEMERMRQTHSKEMESRDEEV 1637
Cdd:PTZ00440 693 LKKELQNLLSL--KENI----IKKQLNNIEQDISNSLNQYTIKYNDLKSsIEEYK-----EEEEKLEVYKHQIINRKNEF 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1638 EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQV--NQRDFESEKRLRKDLK--------RTKALL-- 1705
Cdd:PTZ00440 762 ILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKknNQDLLNSYNILIQKLEahtekndeELKQLLqk 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1706 ---ADAQIMLDHLKNNAPSKREIAQ-LKNQLEESEFTCAAAVKARKAMEVEMEDLHLqIDDIAKAKTALEEQLS------ 1775
Cdd:PTZ00440 842 fptEDENLNLKELEKEFNENNQIVDnIIKDIENMNKNINIIKTLNIAINRSNSNKQL-VEHLLNNKIDLKNKLEqhmkii 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1776 ----------------RLQREKNEIQNRLeeDQEDMNEL-MKKHKA-AVAQASRDMAQMND--LQAQIEESNKEKQELQE 1835
Cdd:PTZ00440 921 ntdniiqkneklnllnNLNKEKEKIEKQL--SDTKINNLkMQIEKTlEYYDKSKENINGNDgtHLEKLDKEKDEWEHFKS 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1836 KLQALQSQVEFLEQSMVDksLVSRQEAKIRELETRLEFEKTQ-----VKRLENLASRLKETMEKLTeerdqraAAENREK 1910
Cdd:PTZ00440 999 EIDKLNVNYNILNKKIDD--LIKKQHDDIIELIDKLIKEKGKeieekVDQYISLLEKMKTKLSSFH-------FNIDIKK 1069
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1911 EQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAF----KRIGDLQAAIE---DEMESD 1983
Cdd:PTZ00440 1070 YKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYnkkkKSLEKIYKQMEktlKELENM 1149
|
570
....*....|....*....
gi 1907082213 1984 ENEDL-INSLQDMVTKYQK 2001
Cdd:PTZ00440 1150 NLEDItLNEVNEIEIEYER 1168
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1299-1604 |
2.49e-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: 46.49 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1299 KDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAE---TAERLRTEKEMKELQTQYDA 1375
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEaeqELEESKRETETGIQNLTAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1376 LKKQMEVMEmevmearliRAAEINGEVDDDDAGGEWRLKYER---AVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLG 1452
Cdd:COG5185 346 EQGQESLTE---------NLEAIKEEIENIVGEVELSKSSEEldsFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1453 DLQADSDESQRALQQLKKKcqrlTAELQDTKLHLEgqqvrnHELEKKQRRFDSELSQAHEETQREKLQR-----EKLQRE 1527
Cdd:COG5185 417 AADRQIEELQRQIEQATSS----NEEVSKLLNELI------SELNKVMREADEESQSRLEEAYDEINRSvrskkEDLNEE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1528 KDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLE---AELQDISSQESKDEASLAKVKKQlRDLEAKvKDQEEELDEQAGS 1604
Cdd:COG5185 487 LTQIESRVSTLKATLEKLRAKLERQLEGVRSKLdqvAESLKDFMRARGYAHILALENLI-PASELI-QASNAKTDGQAAN 564
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1770-1959 |
2.56e-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: 46.21 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1770 LEEQLSRLQREKNEIQNRLEEDQEDMNELmkKHKAAVAQASRDM------AQMNDLQAQIEESNKEKQELQEKLQAlqsQ 1843
Cdd:pfam15070 34 LSEQVRTLREEKERSVSQVQELETSLAEL--KNQAAVPPAEEEQppagpsEEEQRLQEEAEQLQKELEALAGQLQA---Q 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1844 VEFLEQSmvdKSLVSRQEAKIRELETRLEFEKTQVKRLEnlasRLKETME--KLTeerDQRAAAENRE-KEQNKRLQRQ- 1919
Cdd:pfam15070 109 VQDNEQL---SRLNQEQEQRLLELERAAERWGEQAEDRK----QILEDMQsdRAT---ISRALSQNRElKEQLAELQNGf 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1920 LRDTKEEM-------------SELARKEAEASRKKHEL--EMDLESLEAanQSLQ 1959
Cdd:pfam15070 179 VKLTNENMeltsalqseqhvkKELAKKLGQLQEELGELkeTLELKSQEA--QSLQ 231
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1288-1509 |
2.60e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1288 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNElRLSSDRLETRISELTSELTDERNT-GESASQLLDAETAERlRTEKEM 1366
Cdd:PRK11281 88 QLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLESRLAQTLDQLQNAQNDlAEYNSQLVSLQTQPE-RAQAAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1367 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQQELEDKMEVEQQsrrQ 1446
Cdd:PRK11281 166 YANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNA----QNDLQRKSLEGNTQLQDLLQKQRDYLTARIQ---R 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 1447 LERRLGDLQADSdeSQRALQQLKKKCQRltAELQDtklhlEGQQVRNHELEKKQRRFDSELSQ 1509
Cdd:PRK11281 239 LEHQLQLLQEAI--NSKRLTLSEKTVQE--AQSQD-----EAARIQANPLVAQELEINLQLSQ 292
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1729-1903 |
2.69e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1729 KNQLEESEFTCAAAVK-ARKAMEVEMEDLHLQI-DDIAKAKTALEEQLsrlqREKNEIQNRLEEDQEDMNELMKKHKAAV 1806
Cdd:PRK12704 30 EAKIKEAEEEAKRILEeAKKEAEAIKKEALLEAkEEIHKLRNEFEKEL----RERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1807 AQASRDMAQMNDLQAQIEESNKEKQELQEKLQalQSQVEFLEQSMvdkSLvSRQEAK---IRELETRLEFEKtqvkrlen 1883
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELI--EEQLQELERIS---GL-TAEEAKeilLEKVEEEARHEA-------- 171
|
170 180
....*....|....*....|
gi 1907082213 1884 lASRLKETMEKLTEERDQRA 1903
Cdd:PRK12704 172 -AVLIKEIEEEAKEEADKKA 190
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1517-1668 |
2.80e-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: 44.51 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1517 EKLQREKLQREKDMLLAEAFSLKQQMEEKdldIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLRDLEAKVKDQEE 1596
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEP---LQKAQEEVEELRKQLE----NYEKDKQSLKNLKARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1597 ELDeqagsiqMLEQAKLRLEMEMErmrqthskEMESRDEE-VEEARQSCQKK---LKQMEVQLEEEYEDKQKALRE 1668
Cdd:pfam13851 107 EHE-------VLEQRFEKVERERD--------ELYDKFEAaIQDVQQKTGLKnllLEKKLQALGETLEKKEAQLNE 167
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1669-1843 |
3.07e-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: 45.39 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1669 KRELESKLSTLSdqvnqrdfESEKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQleeseftcaaavkarka 1748
Cdd:smart00787 146 KEGLDENLEGLK--------EDYKLLMKELELLNSIKPKLRDRKDALE------EELRQLKQL----------------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1749 mEVEMEDLHLQIDDIAKAKtaleeqLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEE--- 1825
Cdd:smart00787 195 -EDELEDCDPTELDRAKEK------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQcrg 267
|
170
....*....|....*....
gi 1907082213 1826 -SNKEKQELQEKLQALQSQ 1843
Cdd:smart00787 268 fTFKEIEKLKEQLKLLQSL 286
|
|
| PDZ5_MUPP1-like |
cd06669 |
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ... |
269-311 |
3.20e-04 |
|
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467157 [Multi-domain] Cd Length: 98 Bit Score: 41.83 E-value: 3.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1907082213 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSG-DSVRLKV-QPIP 311
Cdd:cd06669 54 RLLPGDRLVFVNDVSLENASLDEAVQALKSAPpGTVRIGVaKPLP 98
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1352-1618 |
3.30e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.84 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1352 LDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVMEARliraaEINGEV-----------DDDDAGGEWRLKYERAVR 1420
Cdd:pfam05622 199 LSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLR-----ETNEELrcaqlqqaelsQADALLSPSSDPGDNLAA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1421 EV---DFTKKRLQQELEDKMEVEQQSrRQLERRLGDLQADSDESQRALQ----QLKKKCQR---LTAELQDTKLHLEGQQ 1490
Cdd:pfam05622 274 EImpaEIREKLIRLQHENKMLRLGQE-GSYRERLTELQQLLEDANRRKNeletQNRLANQRileLQQQVEELQKALQEQG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1491 VRNHELEKKQRRFDS---ELSQAHEETQREKLQREKLQREKDMLLAE-AFSLKQQMEEKDLDIAGFTQK----------- 1555
Cdd:pfam05622 353 SKAEDSSLLKQKLEEhleKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEERykkyvekaksv 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 1556 VVSLEAELQDISSQEskdeasLAKVKKQLRDLEAKVKDQEEEldeqagsiqmLEQAKLRLEME 1618
Cdd:pfam05622 433 IKTLDPKQNPASPPE------IQALKNQLLEKDKKIEHLERD----------FEKSKLQREQE 479
|
|
| PDZ_MPP1-like |
cd10830 |
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ... |
273-309 |
3.41e-04 |
|
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1, and related domains. MPP1 (also known as MAGUK p55 subfamily member 1, erythrocyte membrane protein p55, EMP55) is a membrane-associated guanylate kinase (MAGUK)-like protein which forms a complex with protein 4.1 and glycophorin C (GPC) at the cytoplasmic face of the plasma membrane; this complex is essential for cytoskeleton-membrane linkage in erythrocytes and many non-erythroid cells, and participates in the determination of membrane stability and cell shape. MPP1, by interacting with various scaffold proteins and cytoskeletal proteins in the postsynaptic density, also plays an important role in organizing synaptic and non-synaptic structures. MPP1 is also a component of the Crumbs protein complex in the mammalian retina and may link the Usher protein network and the Crumbs protein complex. The MPP1 PDZ domain binding partners include GPC, ABCC4, and CADM1/Necl-2/SynCAM1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467266 [Multi-domain] Cd Length: 81 Bit Score: 41.39 E-value: 3.41e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1907082213 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd10830 45 GDEILEINGKSVTNHSVDQLQKMLKETKGMVSLKVIP 81
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1620-1945 |
3.46e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1620 ERMRQTHSKEMESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKalrekrelesklstLSDQVNQRDFESEKRLRKDL 1698
Cdd:pfam02029 18 ERRRQKEEEEPSGQvTESVEPNEHNSYEEDSELKPSGQGGLDEEEA--------------FLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1699 KRTKALLadaqimldhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhlqiddiakaktalEEQLSRlq 1778
Cdd:pfam02029 84 ERQKEFD----------PTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYK----------------EEETEI-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1779 REKNEIQNRLEEDQEDMNELMKKHKAAVAQASR-DMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS------M 1851
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEvPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKsqngeeE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1852 VDKSLVS--RQEAKIRELETRLEFEKTQV---KRLENLASRLKET----MEKLtEERDQRAAAE----NREKEQNKRL-- 1916
Cdd:pfam02029 216 VTKLKVTtkRRQGGLSQSQEREEEAEVFLeaeQKLEELRRRRQEKeseeFEKL-RQKQQEAELEleelKKKREERRKLle 294
|
330 340
....*....|....*....|....*....
gi 1907082213 1917 QRQLRDTKEEMSELARKEAEASRKKHELE 1945
Cdd:pfam02029 295 EEEQRRKQEEAERKLREEEEKRRMKEEIE 323
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1765-1929 |
3.49e-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: 43.05 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1765 KAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQV 1844
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1845 EFLEQSmvdkslvsrqeakireletrLEFEKTQVKRLENLASRLKETMEKLTEERDQraaaenrEKEQNKRLQRQLRDTK 1924
Cdd:pfam10473 83 ENLTKE--------------------LQKKQERVSELESLNSSLENLLEEKEQEKVQ-------MKEESKTAVEMLQTQL 135
|
....*
gi 1907082213 1925 EEMSE 1929
Cdd:pfam10473 136 KELNE 140
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1287-1682 |
3.75e-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: 45.90 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1287 IQVQLSEEQIRNKDEeIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEM 1366
Cdd:pfam07111 318 LMVQLKAQDLEHRDS-VKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQT 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1367 K--ELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDddaggewRLKYerAVREVDFTKKRLQQeledKMEVEQQSR 1444
Cdd:pfam07111 397 AsaEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSN-------RLSY--AVRKVHTIKGLMAR----KVALAQLRQ 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1445 RQLERRLGDLQADSDESQRaLQQLKKKCQRLTAELQdTKLHLEGQQV-RNHELEKKQRRFDSELSQAHEetqreklqrEK 1523
Cdd:pfam07111 464 ESCPPPPPAPPVDADLSLE-LEQLREERNRLDAELQ-LSAHLIQQEVgRAREQGEAERQQLSEVAQQLE---------QE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1524 LQREKDMLLaeafSLKQQMEEKDLDIAGFTQKVVSLEAEL---QDISSQESKDEasLAKVKKQLRDLEAKVKDQ-EEELD 1599
Cdd:pfam07111 533 LQRAQESLA----SVGQQLEVARQGQQESTEEAASLRQELtqqQEIYGQALQEK--VAEVETRLREQLSDTKRRlNEARR 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1600 EQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTL 1679
Cdd:pfam07111 607 EQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSG 686
|
...
gi 1907082213 1680 SDQ 1682
Cdd:pfam07111 687 LDK 689
|
|
| PDZ4_DLG5-like |
cd06766 |
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
237-308 |
3.83e-04 |
|
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467247 [Multi-domain] Cd Length: 81 Bit Score: 41.22 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 237 RTTMLDRAPE--------GQAYRRVVHFAEPGAGTKDLAlGLVPGDRLVEINGQNVENKSRDEI-VEMIRQSgDSVRLKV 307
Cdd:cd06766 3 RLVFLKKSQVelgiqlcgGNLHGIFVEDVEDDSPAKGPD-GLVPGDLILEYNSVDMRNKTAEEAyLEMLKPA-ETVTLKV 80
|
.
gi 1907082213 308 Q 308
Cdd:cd06766 81 Q 81
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1824-1946 |
3.93e-04 |
|
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: 42.21 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1824 EESNKEKQELQEKLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKL------TE 1897
Cdd:pfam20492 2 EEAEREKQELEERLKQYEEETKKAQEEL------EESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLeesaemEA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907082213 1898 ERDQRAAAENREKEQnkRLQRQlrdtkeeMSELARKEAEASRKKHELEM 1946
Cdd:pfam20492 76 EEKEQLEAELAEAQE--EIARL-------EEEVERKEEEARRLQEELEE 115
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1795-2011 |
4.15e-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: 45.05 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1795 MNELMKKHKAAVAQASRDMAqMNDLQAQIEESNKEKQELQEKLQALQSQV-EFLEQSMVDKSlvsrqeaKIRELETRLEf 1873
Cdd:cd22656 96 ILELIDDLADATDDEELEEA-KKTIKALLDDLLKEAKKYQDKAAKVVDKLtDFENQTEKDQT-------ALETLEKALK- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1874 ektqvkrlenlasrlketmEKLTEErdqraaAENREKEQNKRLQRQLrdtKEEMSELARKEAEASRKKHELEMDLESLEA 1953
Cdd:cd22656 167 -------------------DLLTDE------GGAIARKEIKDLQKEL---EKLNEEYAAKLKAKIDELKALIADDEAKLA 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1954 ANQSLQADLKLAFKRIGDLQAAIEDEMESDENedLINSLQDMVTKYQKKKNKLEGDSD 2011
Cdd:cd22656 219 AALRLIADLTAADTDLDNLLALIGPAIPALEK--LQGAWQAIATDLDSLKDLLEDDIS 274
|
|
| secA |
PRK12903 |
preprotein translocase subunit SecA; Reviewed |
1811-1987 |
4.16e-04 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237258 [Multi-domain] Cd Length: 925 Bit Score: 45.82 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1811 RDMAQMNDLQAQIEESNKEKQELQEKLqALQSQVEFLEQSMVDKSLvsrqeaKIRELETRLEFEKTQVKRLENLASRL-K 1889
Cdd:PRK12903 741 VQYSQKNPYQVYTEEGTKKFNILLQEI-AYDVIVSLFNNPNAEKIL------IITEILSDGINNSDINDRPQELIDQIiE 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1890 ETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFK-R 1968
Cdd:PRK12903 814 SEEERLKALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEFKNDPKKLNKLIIAKdV 893
|
170
....*....|....*....
gi 1907082213 1969 IGDLQAAIEDEMESDENED 1987
Cdd:PRK12903 894 LIKLVISSDEIKQDEKTTK 912
|
|
| PDZ_PDLIM-like |
cd06753 |
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
4.19e-04 |
|
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467235 [Multi-domain] Cd Length: 79 Bit Score: 40.98 E-value: 4.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907082213 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06753 39 NLRPGDVILAINGESTEGMTHLEAQNKIKAATGSLSLTLE 78
|
|
| PDZ2_Dlg1-2-4-like |
cd06724 |
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ... |
258-308 |
4.22e-04 |
|
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467207 [Multi-domain] Cd Length: 85 Bit Score: 41.10 E-value: 4.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 258 EPGAGTKDLALGLvpGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06724 37 EGGAAQKDGRLQV--GDKLLAVNDVSLEEVTHEEAVAALKNTSDVVYLKVA 85
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1301-1795 |
4.57e-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: 45.44 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1301 EEIQQLRSKLEKVEKERnelrlssDRLETRISELTSELTDERNTGESASQLLDAETA----ERLRTEKEMKELQTQYDAL 1376
Cdd:pfam15070 29 QKMQQLSEQVRTLREEK-------ERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgpseEEQRLQEEAEQLQKELEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1377 kkqmevmemevmearlirAAEINGEVDDDDagGEWRLKYERAVREVDftkkrLQQELEDKMEVEQQSRRQLErrlgDLQA 1456
Cdd:pfam15070 102 ------------------AGQLQAQVQDNE--QLSRLNQEQEQRLLE-----LERAAERWGEQAEDRKQILE----DMQS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1457 DSDESQRALQQLKKKCQRLtAELQD-------------TKLHLEgQQVRNhELEKKQRRFDSELSQAHEETQREKLQREK 1523
Cdd:pfam15070 153 DRATISRALSQNRELKEQL-AELQNgfvkltnenmeltSALQSE-QHVKK-ELAKKLGQLQEELGELKETLELKSQEAQS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1524 LQREKDMLLAE----AFSLKQQMEEKDLdiagfTQKVVSLEAELQD-ISSQESKDEASLAKVKKQLRD----LEAKVKDQ 1594
Cdd:pfam15070 230 LQEQRDQYLAHlqqyVAAYQQLASEKEE-----LHKQYLLQTQLMDrLQHEEVQGKVAAEMARQELQEtqerLEALTQQN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1595 EEEldeQAGSIQMLEQAK---LRLEMEMERMRQTH---SKEMESRDEEVE---EARQSCQKKLKQMEVQLEEEYedkqka 1665
Cdd:pfam15070 305 QQL---QAQLSLLANPGEgdgLESEEEEEEAPRPSlsiPEDFESREAMVAffnSALAQAEEERAELRRQLKEQK------ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1666 lREKRELESKLSTLSDQvnQRDFESEKRLRKD---LKRTKALladaQIMLDHLKNNAPS-KREIAQLKNQLEESEFTCAa 1741
Cdd:pfam15070 376 -RRCRRLAQQAAPAQEE--PEHEAHAPGTGGDsvpVEVHQAL----QVAMEKLQSRFTElMQEKADLKERVEELEHRCI- 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082213 1742 avkarkamevemeDLHLQIDDIAKAKTALEEQ---LSRLQREKNEIQNRLEEDQEDM 1795
Cdd:pfam15070 448 -------------QLSGETDTIGEYIALYQSQraiLKQRHREKEEYISRLAQDKEEM 491
|
|
| DUF1633 |
pfam07794 |
Protein of unknown function (DUF1633); This family contains sequences derived from a group of ... |
1581-1777 |
5.06e-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: 45.65 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1581 KKQLRDLEAKVK-DQEEELDEQAgsiQMLEQAKLRLEMEMermrqTHSKEMESRDEEveearqscqkKLKQMEVQLEEEY 1659
Cdd:pfam07794 457 ERAIREEDPHLGaDQDREVRFGA---EGIVPGIERLKIEL-----STSKDLEKGYAE----------KIGFMEMEFGGLE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1660 EDKQKALREKRELESKLSTLSDQVnqRDFESEKR-LRKDLKRTKALLADAQI-MLDHLKNNAPSKREIAQLKNQLEESEF 1737
Cdd:pfam07794 519 ADKQMARNQIHRLEEKKDELSKKV--LDLTSIAQgAKKAVHDAKVELAAAYLkLLAGIKDKWVAKKEFTVLEGQAAEVES 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907082213 1738 TCA---AAVKARKAMEVEMEDLHLQIDDIaKAKTALEE----QLSRL 1777
Cdd:pfam07794 597 NLAlidQITKAAIDLTLEKPRFQAEIDDL-EARCKLKEvsdfTLSKL 642
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1442-1685 |
6.21e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.07 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1442 QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLT-AELQdtklhlEGQQVrnhELEKKQRRfdseLSQAheetqrEKLq 1520
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELEaAALQ------PGEEE---ELEEERRR----LSNA------EKL- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1521 REKLQREKDML----------LAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESK-------DEASLAKVKK- 1582
Cdd:COG0497 225 REALQEALEALsggeggaldlLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRyldslefDPERLEEVEEr 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1583 --QLRDLEAKVKDQEEELdeqagsIQMLEQAKLRLEmemermrqthskEMESRDEEVEEarqscqkkLKQMEVQLEEEYE 1660
Cdd:COG0497 305 laLLRRLARKYGVTVEEL------LAYAEELRAELA------------ELENSDERLEE--------LEAELAEAEAELL 358
|
250 260
....*....|....*....|....*
gi 1907082213 1661 DKQKALREKRELESKlsTLSDQVNQ 1685
Cdd:COG0497 359 EAAEKLSAARKKAAK--KLEKAVTA 381
|
|
| PDZ1_PTPN13-like |
cd23072 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ... |
259-309 |
6.24e-04 |
|
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467285 [Multi-domain] Cd Length: 92 Bit Score: 40.94 E-value: 6.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907082213 259 PGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV-QP 309
Cdd:cd23072 39 PG-GPADLDGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTLVVsQP 89
|
|
| PDZ2_MUPP1-like |
cd06667 |
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ... |
259-307 |
6.31e-04 |
|
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467155 [Multi-domain] Cd Length: 80 Bit Score: 40.73 E-value: 6.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1907082213 259 PGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06667 31 PG-GVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSHVRLVV 78
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1444-1661 |
6.37e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1444 RRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTK-----LHLEGQQvrnHELEKKQRRFDSELSQAHEETQREK 1518
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEA---KLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1519 LQREKLQREKDMLLAEAFSLKQqmeekDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ---- 1594
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaqri 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1595 ----EEELDEQAGSIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQ---SCQKKLKQMEVQLEEEYED 1661
Cdd:COG3206 315 laslEAELEALQAREASLQAQLAQLEARLAELPEL-EAELRRLEREVEVARElyeSLLQRLEEARLAEALTVGN 387
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1914-2008 |
7.39e-04 |
|
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: 42.18 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1914 KRLQRQLRDTKEEM-SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEdLINSL 1992
Cdd:pfam03938 18 KAAQAQLEKKFKKRqAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQE-LLQPI 96
|
90
....*....|....*.
gi 1907082213 1993 QDMVTKYQKKKNKLEG 2008
Cdd:pfam03938 97 QDKINKAIKEVAKEKG 112
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1300-1480 |
7.81e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1300 DEEIQQLRSKLEKVEKERNELRLSSDrletriseltseLTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQ 1379
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNG------------LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1380 MEVMEMEVMEAR--------LIRAAEINGEVDdddaggEWRLKY-------ERAVREVDFTKKRLQQELEDKMEVEQQSR 1444
Cdd:COG3206 249 LGSGPDALPELLqspviqqlRAQLAELEAELA------ELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907082213 1445 RQLERRLGDLQADSDESQRALQQLKKKCQRLtAELQ 1480
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAEL-RRLE 357
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1292-1378 |
9.01e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1292 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldAETAERLRTEKEMKELQT 1371
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKDREISRLDR 472
|
....*..
gi 1907082213 1372 QYDALKK 1378
Cdd:COG2433 473 EIERLER 479
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1429-1590 |
9.06e-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: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1429 LQQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRrfds 1505
Cdd:pfam13851 27 LIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELK---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1506 ELSQAHEEtqreKLQR-EKLQREKDMLLAE----AFSLKQQMEEKDLDIAgftQKVVSL-------EAELQDISSQESKD 1573
Cdd:pfam13851 103 DLKWEHEV----LEQRfEKVERERDELYDKfeaaIQDVQQKTGLKNLLLE---KKLQALgetlekkEAQLNEVLAAANLD 175
|
170
....*....|....*...
gi 1907082213 1574 EASLAKVKKQLRD-LEAK 1590
Cdd:pfam13851 176 PDALQAVTEKLEDvLESK 193
|
|
| PDZ5_DrPTPN13-like |
cd23060 |
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ... |
220-307 |
9.09e-04 |
|
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of Danio rerio Ptpn13, and related domains. Protein-tyrosine phosphatases (PTPs) dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases (PTKs). Danio rerio Ptpn13 is a classical non-receptor-like PTP. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467273 [Multi-domain] Cd Length: 80 Bit Score: 40.03 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPTGDFGFSLRRttmldrAPEGQAYRrvVHFAEPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:cd23060 1 QIELEKPANGGLGFSLVG------GEGGSGIF--VKSISPG-GVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKA 71
|
....*...
gi 1907082213 300 GDSVRLKV 307
Cdd:cd23060 72 KGTVQLTV 79
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1429-1566 |
9.56e-04 |
|
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: 43.82 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1429 LQQELEDKmEVEQQSRRQLERRLgdlqadsDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnheLEKKQRRFDSELS 1508
Cdd:pfam02841 178 LQEFLQSK-EAVEEAILQTDQAL-------TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQM---MEAQERSYQEHVK 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1509 QAHEETQREklqREKLQREKDMLLAeafslKQQMEEKDLDIAGFTQKVVSLEAELQDI 1566
Cdd:pfam02841 247 QLIEKMEAE---REQLLAEQERMLE-----HKLQEQEELLKEGFKTEAESLQKEIQDL 296
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1583-1897 |
9.68e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1583 QLRDLeaKVKDQEEELDEQAGSIQMLEQA--KLRLEMEMERMRQthSKEMESRDEEVEEARQSCQKKLKQmevqLEEEYE 1660
Cdd:PRK05771 32 HIEDL--KEELSNERLRKLRSLLTKLSEAldKLRSYLPKLNPLR--EEKKKVSVKSLEELIKDVEEELEK----IEKEIK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1661 DKQKALR----EKRELESKLSTLSdqvNQRDFESEKRLRKDLKRTKALLADAQimldhlKNNAPSKREIAQLKNQLEESE 1736
Cdd:PRK05771 104 ELEEEISelenEIKELEQEIERLE---PWGNFDLDLSLLLGFKYVSVFVGTVP------EDKLEELKLESDVENVEYIST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1737 F----TCAAAVKARKAMEV--EMEDLHLQIDDIAKAKTALEEqLSRLQREKNEIQNRLEEDQEDMNELMKKHKaavaqas 1810
Cdd:PRK05771 175 DkgyvYVVVVVLKELSDEVeeELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELAKKYL------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1811 rdmaqmNDLQAQIEESNKEKQELQEKLQALQS----QVE-FLEQSMVD--KSLVSRQEAK---IRELETRLEFEKTQVKr 1880
Cdd:PRK05771 247 ------EELLALYEYLEIELERAEALSKFLKTdktfAIEgWVPEDRVKklKELIDKATGGsayVEFVEPDEEEEEVPTK- 319
|
330
....*....|....*..
gi 1907082213 1881 LENlaSRLKETMEKLTE 1897
Cdd:PRK05771 320 LKN--PKFIKPFESLTE 334
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1697-1953 |
9.99e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.51 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1697 DLKRTKALladaqIMLDHLKNNAPSKREiaQLKNQLE-ESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLS 1775
Cdd:pfam15964 348 NFEKTKAL-----IQCEQLKSELERQKE--RLEKELAsQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1776 RLQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDMA-QMNDLQAQIEESNKEKQELQEKlqaLQSQVEFLEQsmvdk 1854
Cdd:pfam15964 421 KVTREKNSLVSQLEEAQKQ----LASQEMDVTKVCGEMRyQLNQTKMKKDEAEKEHREYRTK---TGRQLEIKDQ----- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1855 slvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDqraaaenrEKEQNKRLQRQLRDTKEE-MSELARK 1933
Cdd:pfam15964 489 --------EIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG--------ESEHQLHLTRLEKESIQQsFSNEAKA 552
|
250 260
....*....|....*....|.
gi 1907082213 1934 EA-EASRKKHELEMDLESLEA 1953
Cdd:pfam15964 553 QAlQAQQREQELTQKMQQMEA 573
|
|
| PDZ_RGS12-like |
cd06710 |
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ... |
222-308 |
1.04e-03 |
|
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467194 [Multi-domain] Cd Length: 76 Bit Score: 39.92 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 222 ELQRRPTGdFGFSLRrttmldrapeGQAYRRVVHFaepGAGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGD 301
Cdd:cd06710 4 EIARGRAG-YGFTIS----------GQAPCVLSCV---VRGSPADVAGLKAGDQILAVNGINVSKASHEDVVKLIGKCTG 69
|
....*..
gi 1907082213 302 SVRLKVQ 308
Cdd:cd06710 70 VLRLVIA 76
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1753-1844 |
1.07e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 43.90 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1753 MEDLHLQIDDIAKAKTALE--------EQLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRDMAQMNDLQA 1821
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAkrgfpldvDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKE 80
|
90 100
....*....|....*....|...
gi 1907082213 1822 QIEESNKEKQELQEKLQALQSQV 1844
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRI 103
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1882-1991 |
1.09e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1882 ENLASRLKETMEKLTEERDQRAaaenREKEQNKRLQRQLRDTKEEMSELArKEAEAsrKKHELEMDLESLEAANQSLQAD 1961
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQA----REKAQSQALAEAQQQELVALEGLA-AELEE--KQQELEAQLEQLQEKAAETSQE 213
|
90 100 110
....*....|....*....|....*....|
gi 1907082213 1962 LKLAFKRIGDlQAAIEDEMESDENEDLINS 1991
Cdd:PRK11448 214 RKQKRKEITD-QAAKRLELSEEETRILIDQ 242
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1723-1966 |
1.14e-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: 43.09 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1723 REIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1802
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1803 KAAVAQASRDMAQMNDLQAQI-------EESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEK 1875
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLkeakeiaEEADRKYEEVARKLVVVEGDLERAEER------AELAESKIVELEEELKVVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1876 TQVKRLENLAsrlketmekltEERDQRaaaENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAAN 1955
Cdd:pfam00261 155 NNLKSLEASE-----------EKASER---EDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKY 220
|
250
....*....|.
gi 1907082213 1956 QSLQADLKLAF 1966
Cdd:pfam00261 221 KAISEELDQTL 231
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1581-1668 |
1.25e-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: 41.41 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1581 KKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1660
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQ 97
|
....*....
gi 1907082213 1661 DK-QKALRE 1668
Cdd:pfam03938 98 DKiNKAIKE 106
|
|
| RseP |
COG0750 |
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ... |
269-308 |
1.26e-03 |
|
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];
Pssm-ID: 440513 [Multi-domain] Cd Length: 349 Bit Score: 43.54 E-value: 1.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1907082213 269 GLVPGDRLVEINGQNVEnkSRDEIVEMIRQS-GDSVRLKVQ 308
Cdd:COG0750 145 GLQPGDRIVAINGQPVT--SWDDLVDIIRASpGKPLTLTVE 183
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1800-1947 |
1.30e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1800 KKHKAAVAQASRDMAQMndlqaqIEESNKEKQELQeKLQALQSQVEFLE-QSMVDKSLVSRqEAKIRELETRLEFEKTQV 1878
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRI------LEEAKKEAEAIK-KEALLEAKEEIHKlRNEFEKELRER-RNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1879 KRLENLASRLKETMEKLTEERDQR--------AAAENREKEQNKRLQRQLRDTKEE-----MSELARK-EAEASRKKHEL 1944
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKqqelekkeEELEELIEEQLQELERISGLTAEEakeilLEKVEEEaRHEAAVLIKEI 178
|
...
gi 1907082213 1945 EMD 1947
Cdd:PRK12704 179 EEE 181
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1618-1791 |
1.54e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1618 EMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQV-NQRDFES-EKRLr 1695
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEAlQKEI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1696 KDLKRTKALLADaqimldhlknnapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAktaLEEQLS 1775
Cdd:COG1579 99 ESLKRRISDLED----------------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELE 159
|
170
....*....|....*.
gi 1907082213 1776 RLQREKNEIQNRLEED 1791
Cdd:COG1579 160 ELEAEREELAAKIPPE 175
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1292-1510 |
1.57e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1292 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDerntgesasqlldaetaerlrTEKEMKELQT 1371
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA---------------------LQAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1372 QYDALKKQmeVMEMEVMEARLIRAAEINGEVDDDDA---GGE------WRLKYERAVREVDFTKKRLQQELEDKMEVEQQ 1442
Cdd:COG3883 73 EIAEAEAE--IEERREELGERARALYRSGGSVSYLDvllGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1443 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQA 1510
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1860-1968 |
1.63e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1860 QEAKIRELETRLEFEKTQVKRLENLASRLKETMEklteERDQRAAaenREKEQNKRLQRQLRDTKEEMSELARKEAEASR 1939
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELE----EKDERIE---RLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|..
gi 1907082213 1940 KKHELE---MDLESLEAANQSLQADLKLAFKR 1968
Cdd:COG2433 477 LERELEeerERIEELKRKLERLKELWKLEHSG 508
|
|
| PDZ5_GRIP1-2-like |
cd06682 |
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
270-308 |
1.77e-03 |
|
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family domain PDZ5 is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467170 [Multi-domain] Cd Length: 85 Bit Score: 39.64 E-value: 1.77e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1907082213 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06682 46 LEPGDKLLAIDNIRLDNCSMEDAAQILQQAEDIVKLKIR 84
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1789-1939 |
1.79e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1789 EEDQEDMNELMKKHKAAVAQASRDMAQ-MNDLQAQIEESNKEKQELQEKLQalqsqvefleqsmvdkslvsRQEAKIREL 1867
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEeIRRLEEQVERLEAEVEELEAELE--------------------EKDERIERL 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082213 1868 ETRLEFEKTQVKRlenlasrlketmekltEERDQRaAAENREKEqNKRLQRQLRDTKEEMSELARKEAEASR 1939
Cdd:COG2433 447 ERELSEARSEERR----------------EIRKDR-EISRLDRE-IERLERELEEERERIEELKRKLERLKE 500
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1803-1945 |
1.81e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1803 KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFEKTqvKRLE 1882
Cdd:TIGR02794 39 QAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAA---------EQARQKELEQRAAAEKA--AKQA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 1883 NLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELE 1945
Cdd:TIGR02794 108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEE 170
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1569-1933 |
1.91e-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: 43.51 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1569 QESKD-EASLAKVKKQLRDLEAKVKDQEEELdeqagsiqmlEQAKLRLEMEMERMRQTHSKEMESR-DEEVEEARQSCQK 1646
Cdd:pfam13166 89 EESIEiQEKIAKLKKEIKDHEEKLDAAEANL----------QKLDKEKEKLEADFLDECWKKIKRKkNSALSEALNGFKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1647 KLKQMEVQLEE--EYEDKQKALREKRELESKLSTLSDQ---------VNQRDFESEKRLRKDLKRTKALLADAQIMLDHL 1715
Cdd:pfam13166 159 EANFKSRLLREieKDNFNAGVLLSDEDRKAALATVFSDnkpeiapltFNVIDFDALEKAEILIQKVIGKSSAIEELIKNP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1716 KNNAPSKREIAQLKNQLEESEFtC--------AAAVKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQL----------S 1775
Cdd:pfam13166 239 DLADWVEQGLELHKAHLDTCPF-CgqplpaerKAALEAHfdDEFTEFQNRLQKLIEKVESAISSLLAQLpavsdlasllS 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1776 RLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASR---------DMAQMNDLQAQIEES----NKEKQELQEKLQALQS 1842
Cdd:pfam13166 318 AFELDVEDIESEAEVLNSQLDGLRRALEAKRKDPFKsieldsvdaKIESINDLVASINELiakhNEITDNFEEEKNKAKK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1843 QVEfleqsmvdKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRD 1922
Cdd:pfam13166 398 KLR--------LHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKL--------------REEIKELEAQLRD 455
|
410
....*....|....
gi 1907082213 1923 TK---EEMSELARK 1933
Cdd:pfam13166 456 HKpgaDEINKLLKA 469
|
|
| PDZ3_MUPP1-like |
cd06791 |
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ... |
272-307 |
1.94e-03 |
|
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467253 [Multi-domain] Cd Length: 89 Bit Score: 39.52 E-value: 1.94e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1907082213 272 PGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06791 52 VNDQIIAVDGVNLQGFTNQEAVEVLRNTGQVVHLTL 87
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
1814-1898 |
1.94e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 39.90 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1814 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS--------MVDKSLVSR-QEAKIRELETRLEFEKTQVKRLENL 1884
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLdedtkvykLIGDVLVKQdKEEVKEQLEERKETLEKEIKTLEKQ 81
|
90
....*....|....
gi 1907082213 1885 ASRLKETMEKLTEE 1898
Cdd:pfam01920 82 LEKLEKELEELKEE 95
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1529-2006 |
1.98e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1529 DMLLAEAFSLKQQMEEKDLDIagfTQKVVSLEAELQDISSQESKDEASL-----------AKVKKQLRDLEAKVKDQEEE 1597
Cdd:PTZ00440 601 EELINEALFNKEKFINEKNDL---QEKVKYILNKFYKGDLQELLDELSHflddhkylyheAKSKEDLQTLLNTSKNEYEK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1598 LDEQAGSI--QMLEQAKLRLEmemermrqtHSKEMESR--DEEVEEARQSCQKKLKQMEvqleEEYEDKQKALREKRELE 1673
Cdd:PTZ00440 678 LEFMKSDNidNIIKNLKKELQ---------NLLSLKENiiKKQLNNIEQDISNSLNQYT----IKYNDLKSSIEEYKEEE 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1674 SKLSTLSDQVNQRdfesEKRLRKDLKRTKALLADAQIMLDHLKNNapsKREIAQLKNQLEESEFTCAAAVKARKAMEVEM 1753
Cdd:PTZ00440 745 EKLEVYKHQIINR----KNEFILHLYENDKDLPDGKNTYEEFLQY---KDTILNKENKISNDINILKENKKNNQDLLNSY 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1754 EDLHLQIDDIAKAKTALEEQLsrLQREKNEIQN-RLEEDQEDMNELMKKhkaavaqasrdmaqMNDLQAQIEESNKekqe 1832
Cdd:PTZ00440 818 NILIQKLEAHTEKNDEELKQL--LQKFPTEDENlNLKELEKEFNENNQI--------------VDNIIKDIENMNK---- 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1833 lqeKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEfektqvkrlenlaSRLKETMEKLTEERDQRAAAENREKEQ 1912
Cdd:PTZ00440 878 ---NINIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLE-------------QHMKIINTDNIIQKNEKLNLLNNLNKE 941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1913 NKRLQRQLRDTKeeMSELarkeaeasrkKHELEMDLESLEAANQSLQADLKLafkrigDLQAAIEDEMESDENEDLINSL 1992
Cdd:PTZ00440 942 KEKIEKQLSDTK--INNL----------KMQIEKTLEYYDKSKENINGNDGT------HLEKLDKEKDEWEHFKSEIDKL 1003
|
490
....*....|....
gi 1907082213 1993 QdmvTKYQKKKNKL 2006
Cdd:PTZ00440 1004 N---VNYNILNKKI 1014
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1429-1668 |
2.07e-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: 42.05 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1429 LQQELEDKMEVEQQSRRQLERRLGDLQADSDESQraLQQLKKKCQRLTAELQdtklhleGQQVRNHELEKKQRRFDSELS 1508
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLES--VEALLKKHEALEAELA-------AHEERVEALNELGEQLIEEGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1509 QAHEETQReklQREKLQREKDMLLAEAFSLKQQMEEKdLDIAGFTQKVVSLEAELQDISSQESKDE--ASLAKVKKQLRD 1586
Cdd:cd00176 72 PDAEEIQE---RLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1587 LeakvKDQEEELDEQAGSIQMLEQAKLRLEmemermrqthskemESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKAL 1666
Cdd:cd00176 148 H----KELEEELEAHEPRLKSLNELAEELL--------------EEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
|
..
gi 1907082213 1667 RE 1668
Cdd:cd00176 210 EE 211
|
|
| PDZ2_GRIP1-2-like |
cd06681 |
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
220-308 |
2.07e-03 |
|
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467169 [Multi-domain] Cd Length: 89 Bit Score: 39.52 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPtGDFGFSLR----RTTMLDRA-------PEGQAYRRvvhfaepgaGTkdlalgLVPGDRLVEINGQNVENKS 288
Cdd:cd06681 4 EVTLEKEG-NSFGFVIRggahEDRNKSRPltvthvrPGGPADRE---------GT------IKPGDRLLSVDGISLHGAT 67
|
90 100
....*....|....*....|
gi 1907082213 289 RDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06681 68 HAEAMSILKQCGQEATLLIE 87
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1753-1920 |
2.11e-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: 42.03 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1753 MEDLHLQIDDIAKAKTALEEQ----LSRL----QRE----------KNEIQN----------RLEEDQEDMNELMKKHKA 1804
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQsqnlLSKLeiaqQKEskflenlaslKHENDNlssmlnrkerRLKDLEDQLSELKNSYEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1805 AVaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqSMVDKSLVSRQ--EAKIRELETRLE-FEKTQVKRL 1881
Cdd:pfam17078 85 LT-------ESNKQLKKRLENSSASETTLEAELERLQIQYD----ALVDSQNEYKDhyQQEINTLQESLEdLKLENEKQL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907082213 1882 ENLASRL----KETMEKLTEERDQRAAAENREKEQNKRLQRQL 1920
Cdd:pfam17078 154 ENYQQRIssndKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKL 196
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1558-1962 |
2.14e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1558 SLEAeLQDISSQESKDEASLAKVKKQLRDLeAKVKDQEEELDEqagsiqmLEQaklRLEMEMERMRQThSKEMES-RDEE 1636
Cdd:PRK11281 44 QLDA-LNKQKLLEAEDKLVQQDLEQTLALL-DKIDRQKEETEQ-------LKQ---QLAQAPAKLRQA-QAELEAlKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1637 VEEARQSCQK-KLKQMEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL---RKDLKRT----KALL 1705
Cdd:PRK11281 111 DEETRETLSTlSLRQLESRLAQtldQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLqqiRNLLKGGkvggKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1706 ADAQIMLdhlknNApskrEIAQLKNQLEESEFTCAAAVKarkameveMEDLHLQIDDIAKAKTA-LEEQLSRLQREKNei 1784
Cdd:PRK11281 191 PSQRVLL-----QA----EQALLNAQNDLQRKSLEGNTQ--------LQDLLQKQRDYLTARIQrLEHQLQLLQEAIN-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1785 QNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQI--------EESNK-EKQELQEKLQ---ALQSQVEFLEQSMV 1852
Cdd:PRK11281 252 SKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLsqrllkatEKLNTlTQQNLRVKNWldrLTQSERNIKEQISV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1853 DK-SLV-SR----------QEAKIREL-----ETRLE-FEKTQvKRleNLASRLKETMEKLteERDQRAAAENREKEQNK 1914
Cdd:PRK11281 332 LKgSLLlSRilyqqqqalpSADLIEGLadriaDLRLEqFEINQ-QR--DALFQPDAYIDKL--EAGHKSEVTDEVRDALL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 1915 rlqrQLRDTKEEM-----SELARKEAEASrkkhELEMDLESLEAANQSLQADL 1962
Cdd:PRK11281 407 ----QLLDERRELldqlnKQLNNQLNLAI----NLQLNQQQLLSVSDSLQSTL 451
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1651-2072 |
2.15e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.17 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1651 MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrlrkDLKRTKALLADAQIMLDHLKNN-APSKREIAQLK 1729
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE----DLKRQNAVLQEAQVELDALQNQlALARAEMENIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1730 NQLEESEFTCAAAV-KARKAMEVEMEDLHLQIDDIAKA-----KTALEEQLSR-------LQREKNEIQNRLEEDQEDMN 1796
Cdd:pfam03528 82 AVATVSENTKQEAIdEVKSQWQEEVASLQAIMKETVREyevqfHRRLEQERAQwnqyresAEREIADLRRRLSEGQEEEN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1797 ---------ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKE-----KQELQEKLQALQSQVEFLEQSM----VDKSLVS 1858
Cdd:pfam03528 162 ledemkkaqEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKEleaskMKELNHYLEAEKSCRTDLEMYVavlnTQKSVLQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1859 RQEAKIR----ELETRLEFEKTQVKRL--------------ENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQL 1920
Cdd:pfam03528 242 EDAEKLRkelhEVCHLLEQERQQHNQLkhtwqkandqflesQRLLMRDMQRMESVLTSEQLRQVEEIKKKDQEEHKRART 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1921 RDTKEEMSE-----------LARKEAEASRKKHELEMDLESLEAANQSLQADLKL----AFKRIGDLqaaIEDEMESDEN 1985
Cdd:pfam03528 322 HKEKETLKSdrehtvsihavFSPAGVETSAPLSNVEEQINSAHGSVHSLDTDVVLgagdSFNKQEDP---FKEGLRRAQS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1986 EDLINSLQDMVTKYQKKKNKLEGDSDVD-SELEDRV--DGV-KSWLSKNKGPSKAPSDDGSLKSSRTALNSLPKEgkgpE 2061
Cdd:pfam03528 399 TDSLGSSSSLQHKFLGHNQKAKSAGNLDeSDFGPLVgaDSVsENFDTSSLGSLKMPSGFMLTKDQEKAIKAMTPE----Q 474
|
490
....*....|.
gi 1907082213 2062 ERPSSVLSSLS 2072
Cdd:pfam03528 475 EETASLLSSVT 485
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1744-1849 |
2.37e-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: 39.86 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1744 KARKAMEVEM------EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMN 1817
Cdd:pfam13863 4 KKREMFLVQLaldakrEEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIK 83
|
90 100 110
....*....|....*....|....*....|..
gi 1907082213 1818 DLQAQIEESNKEKQELQEKLQALQSQVEFLEQ 1849
Cdd:pfam13863 84 KLTAQIEELKSEISKLEEKLEEYKPYEDFLEK 115
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
1782-1907 |
2.38e-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: 41.52 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1782 NEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEK-------QELQEK--LQALQSQVEF------ 1846
Cdd:pfam16043 10 DQLQALILDLQEELEKLSETTSELSERLQQRQKHLEALYQQIEKLEKVKadkevveEELDEKadKEALASKVSRdqfdet 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1847 ---LEQSMVDK-SLVSRQEAKIR---ELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1907
Cdd:pfam16043 90 leeLNQMLQELlDKLEGQEDAWKkalETLSEELDTKLDRLELDPLKELLERRIKALQKLLQEGSEELD 157
|
|
| PDZ1_harmonin |
cd06737 |
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ... |
220-310 |
2.40e-03 |
|
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467219 [Multi-domain] Cd Length: 85 Bit Score: 39.16 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 220 ELELQRRPTGDFGFSLRR---------TTMLDraPEGQAYRRvvhfaepgagtkdlalGLVPGDRLVEINGQNVENKSRD 290
Cdd:cd06737 4 LVRLDRRGPESLGFSVRGglehgcglfVSHVS--PGSQADNK----------------GLRVGDEIVRINGYSISQCTHE 65
|
90 100
....*....|....*....|
gi 1907082213 291 EIVEMIRQSgDSVRLKVQPI 310
Cdd:cd06737 66 EVINLIKTK-KTVSLKVRHV 84
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1720-2017 |
2.47e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1720 PSKREIaqlKNQLEeseftcaaAVKARKAMEVE-------MEDLHLQIDDIAKAK---TALEEQLSRLQREKNEIQNRLE 1789
Cdd:PRK11281 36 PTEADV---QAQLD--------ALNKQKLLEAEdklvqqdLEQTLALLDKIDRQKeetEQLKQQLAQAPAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1790 EdqedmnelMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQvefleqsmvdksLVSRQEAKIReLET 1869
Cdd:PRK11281 105 A--------LKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQ------------LVSLQTQPER-AQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1870 RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELArkeaeasRKKHELemdle 1949
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLL-------QKQRDY----- 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1950 sLEAANQSLQadlklafKRIGDLQAAIedemesdeNEDLINSLQDMVTKYQ--KKKNKLEGDSDVDSELE 2017
Cdd:PRK11281 232 -LTARIQRLE-------HQLQLLQEAI--------NSKRLTLSEKTVQEAQsqDEAARIQANPLVAQELE 285
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1729-1953 |
2.68e-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: 42.90 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1729 KNQLEESEFTCAAAVKARKAMEVEMEDLHLQ--IDDIAKAKTALEEQLS---RLQREKNEIQNRLEEDQEdmnelmkkhk 1803
Cdd:pfam15066 329 KQQMQIQDLQCSNLYLEKKVKELQMKITKQQvfVDIINKLKENVEELIEdkyNVILEKNDINKTLQNLQE---------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1804 aavaqasrdmaQMNDLQAQIEESNKEKQELQEKLQALQ-SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLE 1882
Cdd:pfam15066 399 -----------ILANTQKHLQESRKEKETLQLELKKIKvNYVHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQ 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 1883 nlasRLKETMEKLTEerdqrAAAENREKEQNKRLQRQLRDTKeemsELARKEAEASRKKHELEMDLESLEA 1953
Cdd:pfam15066 468 ----QLKGELEKATT-----SALDLLKREKETREQEFLSLQE----EFQKHEKENLEERQKLKSRLEKLVA 525
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1452-1596 |
2.81e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1452 GDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAhEETQREKLQREKLQREKDML 1531
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQ---AAEQERLKQLEKERLAAQEQKKQA-EEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1532 LAEAFSLKQQMEEKDLDIAGftqKVVSLEAELQDISSQESKDEaslAKVKKQLrDLEAKVKDQEE 1596
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAA---KKAAAEAKKKAEAEAAKKAA---AEAKKKA-EAEAAAKAAAE 198
|
|
| PDZ1_Scribble-like |
cd06704 |
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ... |
226-308 |
3.40e-03 |
|
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467188 [Multi-domain] Cd Length: 87 Bit Score: 38.80 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 226 RPTGDFGFSL---RRTTMLDRAPEGQAYRRVvhfAEPGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDS 302
Cdd:cd06704 7 RQTGGLGISIaggKGSTPYKGDDEGIFISRV---TEGGPAAKA---GVRVGDKLLEVNGVDLVDADHHEAVEALKNSGNT 80
|
....*.
gi 1907082213 303 VRLKVQ 308
Cdd:cd06704 81 VTMVVL 86
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1773-1962 |
3.42e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1773 QLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRdmaQMNDLQAQIEESNKEKQELQEKLQALQSQvefleQ 1849
Cdd:PRK11637 48 QLKSIQQDIAAKEKSVRQQQQQRASLlaqLKKQEEAISQASR---KLRETQNTLNQLNKQIDELNASIAKLEQQ-----Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1850 SMVDKSLVSRQEAKIRE-----LETRLEFEKTQVK-RLENLASRL----KETMEKLTEERDQrAAAENREKEQNKRLQRQ 1919
Cdd:PRK11637 120 AAQERLLAAQLDAAFRQgehtgLQLILSGEESQRGeRILAYFGYLnqarQETIAELKQTREE-LAAQKAELEEKQSQQKT 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907082213 1920 -LRDTKEEMSELarKEAEASRKKhelemDLESLEAANQSLQADL 1962
Cdd:PRK11637 199 lLYEQQAQQQKL--EQARNERKK-----TLTGLESSLQKDQQQL 235
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
1754-2007 |
4.12e-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: 41.84 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1754 EDLHLQIDDIAKAKTALEEQLsrlqrekNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMA------QMNDLQAQIEESN 1827
Cdd:pfam13949 20 ERLEKSLDDLPKLKQRNREIL-------DEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELtatlraEIRKYREILEQAS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1828 KEKQELQEKLQALQSQVEFLEQSMVD--KSLVSRQEAKIREletrlefektqvkRLENLASRLKETMEKLTEERDQRAAA 1905
Cdd:pfam13949 93 ESDSQVRSKFREHEEDLELLSGPDEDleAFLPSSRRAKNSP-------------SVEEQVAKLRELLNKLNELKREREQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1906 EN--REKEQNKRLQRQLRDTKEEMSELARKEA---EASRKKHELEMDLESLEAANQSLQADLKLAFKRIgdLQAAIEDEM 1980
Cdd:pfam13949 160 LKdlKEKARNDDISPKLLLEKARLIAPNQEEQlfeEELEKYDPLQNRLEQNLHKQEELLKEITEANNEF--LQDKRVDSE 237
|
250 260
....*....|....*....|....*..
gi 1907082213 1981 ESDENEDLINSLQDMVTKYQKKKNKLE 2007
Cdd:pfam13949 238 KQRQREEALQKLENAYDKYKELVSNLQ 264
|
|
| PDZ_Lin-7-like |
cd06796 |
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ... |
259-311 |
4.45e-03 |
|
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Lin-7-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467258 [Multi-domain] Cd Length: 86 Bit Score: 38.57 E-value: 4.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 259 PGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQPIP 311
Cdd:cd06796 35 PG-GVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVRYTP 86
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1786-1992 |
4.51e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1786 NRLEEDQEDMNELMKKHKAAVAQASRDMAQmndlqAQIEESNKEKQELQEKLQALQSQVEFLEQSMVdkslvSRQEAKIR 1865
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQ-----KQAAEQERLKQLEKERLAAQEQKKQAEEAAKQ-----AALKQKQA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1866 ELETRLEFEKTQVKRlENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEA-------- 1937
Cdd:PRK09510 135 EEAAAKAAAAAKAKA-EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAeakkkaaa 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1938 -SRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDeneDLINSL 1992
Cdd:PRK09510 214 eAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD---DLFGGL 266
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1813-2021 |
4.52e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1813 MAQMNDLQAQIEESNKEkqeLQEKLQALQSQVEFLEQSMVdkslvsRQEAKIRELETRLEFEKTQVKRLENLAsrlKETM 1892
Cdd:pfam04012 10 RANIHEGLDKAEDPEKM---LEQAIRDMQSELVKARQALA------QTIARQKQLERRLEQQTEQAKKLEEKA---QAAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1893 EKLTEERDQRAAaenrekEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAfkrigDL 1972
Cdd:pfam04012 78 TKGNEELAREAL------AEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA-----KA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907082213 1973 QAAIEDEMESDENEDLINSLQDMvtkyQKKKNKLEGDSDVDSELEDRVD 2021
Cdd:pfam04012 147 QEAVQTSLGSLSTSSATDSFERI----EEKIEEREARADAAAELASAVD 191
|
|
| PDZ_CASK-like |
cd10831 |
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ... |
273-309 |
4.72e-03 |
|
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CASK, Caenorhabditis elegans Lin-2, and related domains. CASK and Lin-2 are membrane-associated guanylate kinase (MAGUK)-like proteins. CASK (also known as Calcium/calmodulin-dependent protein kinase, CAKI, and Camguk) has a role in synaptic transmembrane protein anchoring and ion channel trafficking. CASK may regulate transmembrane proteins that bind calcium, calmodulin, or nucleotides; it regulates the Drosophila ether a go-go (eag) potassium channel, and also regulates autophosphorylation of CaMKII. CASK binding partners include the transcription factor TBR1, and cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. Lin-2, as a component of the CLin-10-Lin-2-Lin-7 complex, plays a role in controlling the basolateral localization of the EGF receptor Let-23; this complex also associates with the neuron-specific motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. CASK may also function in targeting or scaffolding of the protein parkin which is selectively truncated by a Parkinson's disease-causing mutation; the C-terminus of parkin functions as a class II PDZ-binding motif that binds CASK. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP6-MPP2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467267 [Multi-domain] Cd Length: 81 Bit Score: 38.23 E-value: 4.72e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1907082213 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd10831 45 GDEIREINGISVANQTVEQLQKMLREARGSITFKIVP 81
|
|
| PDZ_MAST1 |
cd23073 |
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 ... |
225-314 |
4.75e-03 |
|
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST family kinase MAST1, and related domains. MAST1 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain; MAST family member MASTL is a shorter protein lacking the PDZ domain. MAST1 functions as a scaffold protein to link the dystrophin/utrophin network with microfilaments via syntrophin, and it has been identified as a main driver of cisplatin resistance in human cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST1 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467286 [Multi-domain] Cd Length: 95 Bit Score: 38.47 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 225 RRPTGDFGFSLRRTTMLDRAPEGQAYRRVVHFAEPGAGTKDLalGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVR 304
Cdd:cd23073 8 QRSGKKYGFTLRAIRVYMGDSDVYSVHHIVWHVEEGGPAQEA--GLCAGDLITHVNGEPVHGMVHPEVVELILKSGNKVA 85
|
90
....*....|
gi 1907082213 305 LKVQPIPELS 314
Cdd:cd23073 86 VTTTPFENTS 95
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1553-1650 |
4.83e-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: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.49 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1553 TQKVVSLEAELQDISSQeskDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSiqMLEQAKLRLEMEMERMRQTHSKEMES 1632
Cdd:smart00935 6 VQKILQESPAGKAAQKQ---LEKEFKKRQAELEKLEKELQKLKEKLQKDAAT--LSEAAREKKEKELQKKVQEFQRKQQK 80
|
90
....*....|....*...
gi 1907082213 1633 RDEEVEEARQSCQKKLKQ 1650
Cdd:smart00935 81 LQQDLQKRQQEELQKILD 98
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1287-2013 |
4.95e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1287 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNelrlssDRLETRISEltseltderntgesasqlLDAETAERLRTEKEM 1366
Cdd:PTZ00440 945 IEKQLSDTKINNLKMQIEKTLEYYDKSKENIN------GNDGTHLEK------------------LDKEKDEWEHFKSEI 1000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1367 KELQTQYDALKKQMEVMemevmearliraaeINGEVDD---------DDAGGEWRLKYERAVREVDFTKKRLQ-----QE 1432
Cdd:PTZ00440 1001 DKLNVNYNILNKKIDDL--------------IKKQHDDiielidkliKEKGKEIEEKVDQYISLLEKMKTKLSsfhfnID 1066
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1433 LE-DKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKcqrltaeLQDTKLHLEGQQVRNHELEKKQRRFDSELSQAH 1511
Cdd:PTZ00440 1067 IKkYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNK-------SHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQM 1139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1512 EETQREKLQREklqrEKDMLLAEAFSLKQQMEEK--DLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDL-- 1587
Cdd:PTZ00440 1140 EKTLKELENMN----LEDITLNEVNEIEIEYERIliDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDHlt 1215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1588 EAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQThsKEMESRDEEVEEARQscqkklkqmevQLEEEYEDKQKALR 1667
Cdd:PTZ00440 1216 TFEYNAYYDKATASYENIEELTTEAKGLKGEANRSTNV--DELKEIKLQVFSYLQ-----------QVIKENNKMENALH 1282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1668 EKRELESKL-STLSDQV-------NQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNApSKREIAQLKNQLEESeftC 1739
Cdd:PTZ00440 1283 EIKNMYEFLiSIDSEKIlkeilnsTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHK-NKIYGSLEDKQIDDE---I 1358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1740 AAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEI---QNRLEEDQEDMNEL-MKKHKAAVAQASRDMAQ 1815
Cdd:PTZ00440 1359 KKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASRGKDKIdflNKHEAIEPSNSKEVnIIKITDNINKCKQYSNE 1438
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1816 MNDLQAQIEESNKEKQELQEKLQALQSQVEFLEqsMVDKSLVSRQEAkiRELETRLEFEKTQVK-RLENLASRLKETMEK 1894
Cdd:PTZ00440 1439 AMETENKADENNDSIIKYEKEITNILNNSSILG--KKTKLEKKKKEA--TNIMDDINGEHSIIKtKLTKSSEKLNQLNEQ 1514
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1895 LTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELarkeaeaSRKKHELEmdlESLEAANqslqaDLKLAFKRIGDLQA 1974
Cdd:PTZ00440 1515 PNIKREGDVLNNDKSTIAYETIQYNLGRVKHNLLNI-------LNIKDEIE---TILNKAQ-----DLMRDISKISKIVE 1579
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1907082213 1975 AIE-DEMESDENE--DLINSLQDMVTKYQKKKNKLEG-DSDVD 2013
Cdd:PTZ00440 1580 NKNlENLNDKEADyvKYLDNILKEKQLMEAEYKKLNEiYSDVD 1622
|
|
| LXG |
pfam04740 |
LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of ... |
1781-1876 |
5.10e-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: 40.69 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1781 KNEIQNRLEEDQEDMNELMKKHKAAVAQASR----DMAQMNDLQAQIEESNKEKQELQEKLQAL-QSQVEFLEQSmvdKS 1855
Cdd:pfam04740 101 EHELENGLKKAKEKTEELTDEINSILASVSDivslPKLSDSEVQDSLQKAKKKVKDTIEKLYDFdQEQTSELSEL---EA 177
|
90 100
....*....|....*....|.
gi 1907082213 1856 LVSRQEAKIRELETRLEFEKT 1876
Cdd:pfam04740 178 DLQALKTYVSELEEMTSNGKI 198
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1301-1598 |
5.20e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1301 EEIQQLRSKLEKVEKERNELRlssdrletrisELTSELTDERNtgESASQLldAETAERLRTEKEMK-ELQTQYDALKKQ 1379
Cdd:COG1340 15 EKIEELREEIEELKEKRDELN-----------EELKELAEKRD--ELNAQV--KELREEAQELREKRdELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1380 mevmemevmeaRLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQeLEDKMEVEQQSR---RQLERRLGDLQA 1456
Cdd:COG1340 80 -----------RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER-LEWRQQTEVLSPeeeKELVEKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1457 DSDESQRALQQlKKKCQRLTAELQdtklhlegqqvrnhELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAF 1536
Cdd:COG1340 148 ELEKAKKALEK-NEKLKELRAELK--------------ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAD 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1537 SLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQES--KDEASLAKVKKQLRDLEAKVKDQEEEL 1598
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELQKELRELRKELKklRKKQRALKREKEKEELEEKAEEIFEKL 276
|
|
| mS26_Tt |
cd23695 |
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ... |
1410-1732 |
5.42e-03 |
|
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.
Pssm-ID: 467909 [Multi-domain] Cd Length: 496 Bit Score: 41.73 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1410 EWRLK--YERAVREVDFTKKRLQQELEDKMEveqqsrrQLERRLGDLQADSDESqraLQQLKKKCQRLTAELQDtklhle 1487
Cdd:cd23695 193 LFKLLkeYQDAKAIIIEDFRESSEEGAEKLE-------KLEKAFATLLKNYKEE---LEEPEKQLEFMQKRLLD------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1488 gqqvrnheLEKKQRRFDSELSQAH--EETQREKLQREKLQREKdmllaeaFSLKQQMEEKDLDIAGFTQKVVSLEAELQD 1565
Cdd:cd23695 257 --------LYNLLRLWGQYITIVKmpDSVVRDIMNKTQARPEV-------AKLNSKQELEDAKNRKRDTEENEFDDDYES 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1566 ISSQESKDEaslakvkkqlrdleakvkdqEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQ 1645
Cdd:cd23695 322 ADEGETSDE--------------------EDEIEEENFQLQKEKKKEEELNAEFNIAKNSLYKFSPQNDKNVVDDRDFYS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1646 KklKQMEVQLEEE------------YEDKQKALREKRELESkLSTLSDQVNQRDFESEKRLRKDLKrtkalladAQIMLD 1713
Cdd:cd23695 382 G--VDLENVFPRAllnnlndftgldFQNVKEILNNEEKLKI-IQGEDDQNDQEDFNNPRKFQTSLI--------VQTYKQ 450
|
330 340
....*....|....*....|.
gi 1907082213 1714 HLKN--NAPSKREIAQLKNQL 1732
Cdd:cd23695 451 KINNldAESLTRATQEKKNDI 471
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1347-1606 |
5.55e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1347 SASQLLDAETAERLRTEKEmkeLQTQYDALKKQMEVmemevmearliraaeingEVDDddaggewrlkyeravrevdftk 1426
Cdd:PRK11281 22 LSSAFARAASNGDLPTEAD---VQAQLDALNKQKLL------------------EAED---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1427 KRLQQELE------DKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKcqrltaELQDTKLHLEGQQVRnhELEKKQ 1500
Cdd:PRK11281 59 KLVQQDLEqtlallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD------NDEETRETLSTLSLR--QLESRL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1501 RRFDSELSQAHEE------------TQREKLQRE---KLQR---------------------EKDMLLAEAFSLKQQMEE 1544
Cdd:PRK11281 131 AQTLDQLQNAQNDlaeynsqlvslqTQPERAQAAlyaNSQRlqqirnllkggkvggkalrpsQRVLLQAEQALLNAQNDL 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082213 1545 KDLDIAGFTQkvvsleaeLQDIsSQESKDEASL--AKVKKQLRDLE----AKVKDQEEELDEQAGSIQ 1606
Cdd:PRK11281 211 QRKSLEGNTQ--------LQDL-LQKQRDYLTAriQRLEHQLQLLQeainSKRLTLSEKTVQEAQSQD 269
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
1465-1947 |
5.61e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 42.00 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1465 LQQLKKKCQRLTAELQDTKLHLEGQQVR----NHELEKKQ---RRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFS 1537
Cdd:COG5644 1 LPQPQGKHQRKGKKQLENKILHSYEEESagfdSEELEDNDeqgYSFGVNSEDDEEIDSDEAFDEEDEKRFADWSFNASKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1538 LKQQMEEKDLDiagfTQKVVSLEAELQDISSQESKDEASLAKV-KKQLRDLEaKVKDQEEELDEQAGSIQMLEQAKLRLE 1616
Cdd:COG5644 81 GKSNKDHKNLN----NTKEISLNDSDDSVNSDKLENEGSVSSIdENELVDLD-TLLDNDQPEKNESGNNDHATDKENLLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1617 MEMERMRQTHSKEMESRDEEVEEarqscqkklkqmevqlEEEYEDKQKALREKRELESKLSTLSDQVNQR------DFES 1690
Cdd:COG5644 156 SDASSSNDSESEESDSESEIESS----------------DSDHDDENSDSKLDNLRNYIVSLKKDEADAEsvlssdDNDS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1691 EKRLRKDLKRT-KALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKarkamevemedlhlQIDDIAKAKTA 1769
Cdd:COG5644 220 IEEIKYDPHETnKESGSSETIDITDLLDSIPMEQLKVSLKPLVSESSKLDAPLAK--------------SIQDRLERQAA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1770 LEEQLSRLQREKNEIQNRLEEDQE--DMNELMKKHKAAVAQASRDMAQmNDLQAQIEE-------SNKEKQELQEKLQAL 1840
Cdd:COG5644 286 YEQTKNDLEKWKPIVADNRKSDQLifPMNETARPVPSNNGLASSFEPR-TESERKMHQalldaglENESALKKQEELALN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1841 QSQVEFLEQSMVD----KSLVSRQEAKIRELETRLEFEKTQVKRLENLASR-LKETMEKLTEERDQRAAAENREKEQNKR 1915
Cdd:COG5644 365 KLSVEEVAERTRQlrfmRELMFREERKAKRVAKIKSKTYRKIRKNRKEKEMaLIPKSEDLENEKSEEARALERMTQRHKN 444
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1907082213 1916 LQRQLRD----------TKEEMSELARKEAEASRKKHELEMD 1947
Cdd:COG5644 445 TSSWTRKmlerashgegTREAVNEQIRKGDELMQRIHGKEIM 486
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1751-1845 |
5.71e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.48 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1751 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQM-NDLQAQIEESNKE 1829
Cdd:pfam03938 5 VDMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKeQELQQLQQKAQQE 84
|
90
....*....|....*..
gi 1907082213 1830 -KQELQEKLQALQSQVE 1845
Cdd:pfam03938 85 lQKKQQELLQPIQDKIN 101
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1747-1933 |
5.83e-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: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1747 KAMEVEMEDLHLQIDDIAKAktaLEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLqaQIEES 1826
Cdd:pfam04108 20 RSLLEELVVLLAKIAFLRRG---LSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNT--PVEPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1827 NKEKQELQEKLqalqsqvefleQSMVDKSLVSRQEAKIRELETRLefeKTQVKRLENLASRLKETMEKLTEERDQRAAAe 1906
Cdd:pfam04108 95 LPPGEEKQKTL-----------LDFIDEDSVEILRDALKELIDEL---QAAQESLDSDLKRFDDDLRDLQKELESLSSP- 159
|
170 180
....*....|....*....|....*..
gi 1907082213 1907 NREKEQNKRLQRQLRDTKEEMSELARK 1933
Cdd:pfam04108 160 SESISLIPTLLKELESLEEEMASLLES 186
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1797-1972 |
5.93e-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: 40.27 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1797 ELMKKHKAAVAQA------------------SRDMAQMNDLQAQIE----ESNKEKQELQEKLQALQSQVEfleqsmvdk 1854
Cdd:pfam13851 1 ELMKNHEKAFNEIknyynditrnnlelikslKEEIAELKKKEERNEklmsEIQQENKRLTEPLQKAQEEVE--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1855 slvsrqeakirELETRLEFEKTQVKRLENLASRLKET-----------------MEKLTEERDQ------RAAAENREKE 1911
Cdd:pfam13851 72 -----------ELRKQLENYEKDKQSLKNLKARLKVLekelkdlkwehevleqrFEKVERERDElydkfeAAIQDVQQKT 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1912 QNKR--LQRQLrdtkEEMSE-LARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDL 1972
Cdd:pfam13851 141 GLKNllLEKKL----QALGEtLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1428-1619 |
5.96e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1428 RLQQELEDKMEVEQQSRRQLE-RRLGDLQADSDESQRAlqQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRR---F 1503
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEqRRLQQEQLERAEKMRE--ELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLqlqA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1504 DSELSQAHEETQREKLQreKLQREKDMLLAE-AFSLKQQMEEKDLDIAGfTQKVVSLEAELQDISSQESKDEAslakvkK 1582
Cdd:pfam15709 417 AQERARQQQEEFRRKLQ--ELQRKKQQEEAErAEAEKQRQKELEMQLAE-EQKRLMEMAEEERLEYQRQKQEA------E 487
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907082213 1583 QLRDLEAKVKDQEEEldeqagsiqmlEQAKLRLEMEM 1619
Cdd:pfam15709 488 EKARLEAEERRQKEE-----------EAARLALEEAM 513
|
|
| PDZ3_MAGI-1_3-like |
cd06733 |
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
223-300 |
6.29e-03 |
|
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467215 [Multi-domain] Cd Length: 85 Bit Score: 37.98 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 223 LQRRPTGdFGFSLrrttmLDRAPEG-QAYrrVVHFAEPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQSG 300
Cdd:cd06733 6 LRRQETG-FGFRI-----LGGTEEGsQVS--IGAIVPGGAADLD---GrLRTGDELLSVDGVNVVGASHHKVVDLMGNAA 74
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1782-1963 |
6.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1782 NEIQNRLEEDQEDMNELMKKHKAAVAQASRD----MAQMNDLQAQIEESNKEKQELQEKlqalQSQVEfleqsmvdkSLV 1857
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQlrkaLFELDKLQEELEQLREELEQAREE----LEQLE---------EEL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1858 SRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEA 1937
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
170 180
....*....|....*....|....*.
gi 1907082213 1938 SRKKHELEMDLESLEAANQSLQADLK 1963
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQ 174
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
1853-1953 |
6.50e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 38.72 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1853 DKSLVSRQEAKIRELETRLE----FEK------TQVKRLENLASRLKETMEKLTEERDQRAAAENREKE---QNKRLQRQ 1919
Cdd:pfam18595 7 EKEELAELERKARELQAKIDalqvVEKdlrsciKLLEEIEAELAKLEEAKKKLKELRDALEEKEIELRElerREERLQRQ 86
|
90 100 110
....*....|....*....|....*....|....
gi 1907082213 1920 LRDTKEemsELARKEAEASRKKHELEMDLESLEA 1953
Cdd:pfam18595 87 LENAQE---KLERLREQAEEKREAAQARLEELRE 117
|
|
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
1876-1951 |
6.67e-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: 38.68 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1876 TQVKRLENLASRLKETMEKLTEERDQrAAAE----NREKEQNKRLQRQLRDTKEEMSELARKEA-------EASRKKHEL 1944
Cdd:pfam12325 19 STIRRLEGELASLKEELARLEAQRDE-ARQEivklMKENEELKELKKELEELEKELKELEQRYEttlellgEKSEEVEEL 97
|
....*..
gi 1907082213 1945 EMDLESL 1951
Cdd:pfam12325 98 KADVEDL 104
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1292-1515 |
6.79e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1292 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELtdeRNTGESASQLLDAETAERLRTekEMKELQT 1371
Cdd:COG3206 203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL---GSGPDALPELLQSPVIQQLRA--QLAELEA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1372 QYDALkkqmevmemevmearliraaeingevddddaggewRLKYERAVREVdftkKRLQQELEdkmEVEQQSRRQLERRL 1451
Cdd:COG3206 278 ELAEL-----------------------------------SARYTPNHPDV----IALRAQIA---ALRAQLQQEAQRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082213 1452 GDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSeLSQAHEETQ 1515
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES-LLQRLEEAR 378
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1654-1866 |
6.87e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.43 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1654 QLEEEYEDKQKALREK-RELESKLSTLSDQVNQ---RDFESEKRLRKDLKRTKALLADAQIMLDhlKNNAPSKREIAQLK 1729
Cdd:pfam04012 15 EGLDKAEDPEKMLEQAiRDMQSELVKARQALAQtiaRQKQLERRLEQQTEQAKKLEEKAQAALT--KGNEELAREALAEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1730 NQLEESEftcaaavkarKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEedQEDMNELMKKH--KAAVA 1807
Cdd:pfam04012 93 KSLEKQA----------EALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLK--AAKAQEAVQTSlgSLSTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082213 1808 QASRDMAQMNDLQAQIEESNkekqELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRE 1866
Cdd:pfam04012 161 SATDSFERIEEKIEEREARA----DAAAELASAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| PDZ2_APBA1_3-like |
cd06793 |
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ... |
273-309 |
7.15e-03 |
|
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, APBA3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of APBA1, APBA2, APBA3, and related domains. The APBA/X11/Mint protein family includes three members: neuron specific APBA1 (also known as X11alpha and Mint1) and APBA2 (also known as X11beta and Mint2), and the ubiquitously expressed APBA3 (also known as X12gamma and Mint3). They are involved in regulating neuronal signaling, trafficking, and plasticity. They contain two PDZ domains (PDZ1 and PDZ2) which bind a variety of proteins: Arf GTPases (APBA1 and APBA2 PDZ2) and neurexin (APBA1 and APBA2 PDZ1 and 2) which are involved in vesicle docking and exocytosis; alpha1B subunit of N-type Ca2+ channel (APBA1 PDZ1) that is involved in ion channels; KIF17 (APBA1 PDZ1) that is involved in transport and traffic; and Alzheimer's disease related proteins, APP (APBA3 PDZ2), CCS (APBA1 PDZ2), NF-kappa-B/p65 (APBA2 PDZ2), presenilin-1 (APBA1 and APBA2 PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This APBA1,3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467255 [Multi-domain] Cd Length: 78 Bit Score: 37.38 E-value: 7.15e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1907082213 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06793 42 GHRIIEINGQSVVATPHEKIVQLLSNSVGEIHMKTMP 78
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1445-1930 |
7.25e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 41.36 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1445 RQLERRLGDLQAD-------SDESQRALQQLKKKCQRLTA--ELQDTKLHLEGQQVRN--HELEKKQRRFDSELSQAHEE 1513
Cdd:pfam15450 16 KQLEQWVADLQAEvvslrghKERCEHATLSLLRELLQVRAhvQLQDSELKQLRQEVQQaaRAPEKEALEFPGPQNQNQMQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1514 TQREKL--QREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKvVSLEAELQDISS---QESKDEASlAKVKKQLRDLE 1588
Cdd:pfam15450 96 ALDKRLveVREALTQIRRKQALQDSERKGAEQEANLRLTKLTGK-LKQEEQGREAACsalQKSQEEAS-QKVDHEVARMQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1589 AKVKDQEEE-----LDEQAGSIQMLEQAKLRLEmemERMRQTHSKEMESRDEEVEEARQSCQKklkqmevqLEEEYEDKQ 1663
Cdd:pfam15450 174 AQVTKLGEEmslrfLKREAKLCSFLQKSFLALE---KRMKASESTRLKAESSLREELEGRWQK--------LQELTEERL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1664 KALREKRELESklSTLSDQVnqrdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIaqlKNQLEESEFTCAAAV 1743
Cdd:pfam15450 243 RALQGQREQEE--GHLLEQC--------RGLDAAVVQLTKFVRQNQVSLNRVLLAEQKARDA---KGQLEESQAGELASY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1744 ------KARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQN-------RLEEDQEDMNELMKKHKAAVAQAS 1810
Cdd:pfam15450 310 vqenleAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKDLSDhflalswRLDLQEQTLGLKLSEAKKEWEGAE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1811 RDmaQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV----DKSLVSRQEAKIRELET---RLE----FEKTQVK 1879
Cdd:pfam15450 390 RK--SLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVlhksDSDLKISAEGKAREFEVeamRQElaalLSSVQLL 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1880 RLENLASRLKETMEKLTEERDQRAAAENREKE----QNKRLQRQLRDTKEEMSEL 1930
Cdd:pfam15450 468 KEGNPGRKIAEIQGKLATFQNQIIKLENSIQDnktiQNLKFNTETKLRTEEIATL 522
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1578-1669 |
7.29e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1578 AKVKKQLRDLEAKVKDQEEELDEQagsiqMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQScqkKLKQMEVQLEE 1657
Cdd:cd16269 203 ERAKAEAAEQERKLLEEQQRELEQ-----KLEDQERSYEEHLRQLKEKMEEERENLLKEQERALES---KLKEQEALLEE 274
|
90
....*....|..
gi 1907082213 1658 EYEDKQKALREK 1669
Cdd:cd16269 275 GFKEQAELLQEE 286
|
|
| SynN |
cd00179 |
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ... |
1774-1929 |
7.31e-03 |
|
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain
Pssm-ID: 238105 [Multi-domain] Cd Length: 151 Bit Score: 39.19 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1774 LSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvd 1853
Cdd:cd00179 1 LEEFFEEVEEIRGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEA---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1854 ksLVSRQEAKIReletrlefeKTQVkrlENLASRLKETMEKLTEERdQRAAAENREkeqnkRLQRQLRDTKEEMSE 1929
Cdd:cd00179 77 --LNGSSVDRIR---------KTQH---SGLSKKFVEVMTEFNKAQ-RKYRERYKE-----RIQRQLEITGGEATD 132
|
|
| PDZ_ZASP52-like |
cd23068 |
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ... |
269-308 |
7.54e-03 |
|
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Drosophila melanogaster Zasp52 and related domains. Drosophila melanogaster Zasp52 (also known as Z band alternatively spliced PDZ-motif protein or Zasp) colocalizes with integrins at myotendinous junctions and with alpha-actinin at Z-disks and is required for muscle attachment as well as Z-disk assembly and maintenance. The Zasp52 actin-binding site includes the extended PDZ domain and the ZM region. The Zasp52-PDZ domain is required for myofibril assembly. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Zasp52-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467281 [Multi-domain] Cd Length: 82 Bit Score: 37.51 E-value: 7.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907082213 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd23068 42 GLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQ 81
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1497-1617 |
7.55e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 39.20 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1497 EKKQRRFDSELSQAHEETQREKLQREKLQREKDML--------------LAEAFSLKQQMEEkdldiagFTQKVVSLEAE 1562
Cdd:pfam10473 2 EKKQLHVLEKLKESERKADSLKDKVENLERELEMSeenqelaileaensKAEVETLKAEIEE-------MAQNLRDLELD 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082213 1563 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDE-QAGSIQMLEQAKLRLEM 1617
Cdd:pfam10473 75 LVTLRSEKENLTKELQKKQERVSELESLNSSLENLLEEkEQEKVQMKEESKTAVEM 130
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
1754-1847 |
7.83e-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: 40.76 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1754 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKekqEL 1833
Cdd:pfam14932 70 EALEESLEEIREATEDLEAELQELQKTKQLKINRLNKLQAQASSLSQGLRALVAEEEEAAKQLEELQEELAALNA---KT 146
|
90
....*....|....
gi 1907082213 1834 QEKLQALQSQVEFL 1847
Cdd:pfam14932 147 NNVLQSLQSEVKEL 160
|
|
| PDZ10_MUPP1-PDZ8_PATJ-like |
cd06673 |
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ... |
258-307 |
8.11e-03 |
|
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 10 of MUPP1, PDZ domain 8 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ10 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467161 [Multi-domain] Cd Length: 86 Bit Score: 37.66 E-value: 8.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907082213 258 EPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06673 37 EDGAAAKD---GrLWAGDQILEVNGEDLRKATHDEAINVLRQTPQKVRLLV 84
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1671-1941 |
8.11e-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: 41.22 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1671 ELESKLSTLSDQVNQRdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaavkarKAME 1750
Cdd:pfam04108 116 ILRDALKELIDELQAA----QESLDSDLKRFDDDLRDLQKELESLSSPSESISLIPTLLKELESLE----------EEMA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1751 VEMEDLHLQIDDIAKAKTALEEqlsrlqrEKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQmndLQAQIEESNKEK 1830
Cdd:pfam04108 182 SLLESLTNHYDQCVTAVKLTEG-------GRAEMLEVLENDARELDDVVPELQDRLDEMENNYER---LQKLLEQKNSLI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1831 QELQEKLQalqsqvefleqsmvdkslvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEE-RDQRAAAEN-- 1907
Cdd:pfam04108 252 DELLSALQ------------------------LIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSElEDLREFYEGfp 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907082213 1908 -----------REKEQNKRLQRQLRDTKEEMSELARKEAEAsRKK 1941
Cdd:pfam04108 308 saygsllleveRRREWAEKMKKILRKLAEELDRLQEEERKR-REK 351
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1496-1658 |
8.12e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1496 LEKKQRRFDSELSQAHEETQREKlqREKLQREKDmllaEAFSLKQQMEekdldiagftQKVVSLEAELQDISSQESKDEA 1575
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIK--KEALLEAKE----EIHKLRNEFE----------KELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1576 SLakvKKQLRDLEAKvkdqEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEME-----SRDE-------EVE-EARQ 1642
Cdd:PRK12704 97 NL---DRKLELLEKR----EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELErisglTAEEakeilleKVEeEARH 169
|
170
....*....|....*.
gi 1907082213 1643 SCQKKLKQMEVQLEEE 1658
Cdd:PRK12704 170 EAAVLIKEIEEEAKEE 185
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1483-1668 |
8.32e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1483 KLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQK-VVSLEA 1561
Cdd:pfam15709 337 RLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKqRLQLQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1562 ELQDISSQESKDEASLAKVKKQLRDLEAKvKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEAR 1641
Cdd:pfam15709 417 AQERARQQQEEFRRKLQELQRKKQQEEAE-RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAE 495
|
170 180
....*....|....*....|....*..
gi 1907082213 1642 QSCQKKLKQMEVQLEEEYEDKQKALRE 1668
Cdd:pfam15709 496 ERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1301-1912 |
8.34e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1301 EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQ-TQYDALKKQ 1379
Cdd:PRK10246 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASrRQQALQQAL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1380 MEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLGDLQ---- 1455
Cdd:PRK10246 271 AAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQslnt 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1456 --ADSDESQ---------RAL--------QQLKKKCQRLTAELQ------DTKLHLEGQQVRNH-ELEKKQRRFDSELSQ 1509
Cdd:PRK10246 351 wlAEHDRFRqwnnelagwRAQfsqqtsdrEQLRQWQQQLTHAEQklnalpAITLTLTADEVAAAlAQHAEQRPLRQRLVA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1510 AHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSL------EAELQDISSQESKDEA-------- 1575
Cdd:PRK10246 431 LHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVkticeqEARIKDLEAQRAQLQAgqpcplcg 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1576 -----------SLAKVKKQLR--DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMR---QTHSKEMESRDEEVEE 1639
Cdd:PRK10246 511 stshpaveayqALEPGVNQSRldALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRqeeQALTQQWQAVCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1640 ARQSCQKKLKQMEVQleEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKR---LRKDLKRTKALLADAQIMLDHLK 1716
Cdd:PRK10246 591 TLQPQDDIQPWLDAQ--EEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRqqqLLTALAGYALTLPQEDEEASWLA 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1717 NNAPSKREIAQLKNQ---LEESEFTCAAAVKARKAM-EVEMEDLHLQIDDIAKAKT---ALEEQLSRLQREKNEIQNRLE 1789
Cdd:PRK10246 669 TRQQEAQSWQQRQNEltaLQNRIQQLTPLLETLPQSdDLPHSEETVALDNWRQVHEqclSLHSQLQTLQQQDVLEAQRLQ 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1790 EDQEDMNELMKKH----KAAVAQASRDMAQMNDLQAQieesnkeKQELQEKLQALQSQVEFLEQsmvdkSLVSRQEAKIR 1865
Cdd:PRK10246 749 KAQAQFDTALQASvfddQQAFLAALLDEETLTQLEQL-------KQNLENQRQQAQTLVTQTAQ-----ALAQHQQHRPD 816
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1907082213 1866 ELETRLEFEKTQVkRLENLASRLKETMEKLTEERDQ-RAAAENREKEQ 1912
Cdd:PRK10246 817 GLDLTVTVEQIQQ-ELAQLAQQLRENTTRQGEIRQQlKQDADNRQQQQ 863
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1639-1844 |
8.96e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.36 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1639 EARQSCQKKLKQMEVQLEEeYEDKQKALRekRELESKLSTLSDQVNQRDFE-SEKRLRKDLKRTKALLADAQimldhlkn 1717
Cdd:pfam12795 30 DKIDASKQRAAAYQKALDD-APAELRELR--QELAALQAKAEAAPKEILASlSLEELEQRLLQTSAQLQELQ-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1718 napskREIAQLKNQLEESEftcAAAVKARKAMEVEMEDLHlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNE 1797
Cdd:pfam12795 99 -----NQLAQLNSQLIELQ---TRPERAQQQLSEARQRLQ-QIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQIDMLE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907082213 1798 LmkkhkaavAQASRDMAQMNdLQAQIEESNKEKQELQEKLQALQSQV 1844
Cdd:pfam12795 170 Q--------ELLSNNNRQDL-LKARRDLLTLRIQRLEQQLQALQELL 207
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1751-1844 |
9.06e-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: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1751 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDmAQMNDLQAQIEESNKEK 1830
Cdd:smart00935 4 VDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEK----LQKDAATLSEAARE-KKEKELQKKVQEFQRKQ 78
|
90
....*....|....
gi 1907082213 1831 QELQEKLQALQSQV 1844
Cdd:smart00935 79 QKLQQDLQKRQQEE 92
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1804-1920 |
9.10e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1804 AAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMvdkSLVSRQeakIRELETRLEfektqvkRLEN 1883
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAI---SQASRK---LRETQNTLN-------QLNK 103
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907082213 1884 LASRLKETMEKLteerdqraaaENREKEQNKRLQRQL 1920
Cdd:PRK11637 104 QIDELNASIAKL----------EQQQAAQERLLAAQL 130
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1795-1937 |
9.13e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 38.82 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1795 MNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEfE 1874
Cdd:pfam12718 2 MNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLT-R 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082213 1875 KTQV--KRLENLASRLKETMEKLteeRDQRAAAENREKeQNKRLQRQLRDTKEEMSELARKEAEA 1937
Cdd:pfam12718 81 KIQLleEELEESDKRLKETTEKL---RETDVKAEHLER-KVQALEQERDEWEKKYEELEEKYKEA 141
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1582-1702 |
9.32e-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: 38.36 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1582 KQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMrqthskemesrdeevEEARQSCQKKLKQMEVQLEEEYED 1661
Cdd:pfam20492 13 ERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL---------------EQKRQEAEEEKERLEESAEMEAEE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907082213 1662 KQKALREKRELESKLSTLSDQVNQRDFESEkRLRKDLKRTK 1702
Cdd:pfam20492 78 KEQLEAELAEAQEEIARLEEEVERKEEEAR-RLQEELEEAR 117
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1294-1657 |
9.42e-03 |
|
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: 41.17 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1294 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTG-----ESASQLLDAETAERLRTEKEMKE 1368
Cdd:pfam05701 70 EELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVAakaqlEVAKARHAAAVAELKSVKEELES 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1369 LQTQYDALKKQMEVMEMEVMEArLIRAAEINGEVDD------------------DDAGGEWRLkyeRAVREVDFTKKRLQ 1430
Cdd:pfam05701 150 LRKEYASLVSERDIAIKRAEEA-VSASKEIEKTVEEltieliatkeslesahaaHLEAEEHRI---GAALAREQDKLNWE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1431 QELEDKMEVEQQSRRQLeRRLGDLQADSDESQRALQQLKkkcqrltAEL---QDTKLHLEGQQVRNheLEKKQRRFDSEL 1507
Cdd:pfam05701 226 KELKQAEEELQRLNQQL-LSAKDLKSKLETASALLLDLK-------AELaayMESKLKEEADGEGN--EKKTSTSIQAAL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1508 SQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQK-------VVSLEAELQDISSQeskdeasLAKV 1580
Cdd:pfam05701 296 ASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKEKAELASLRQRegmasiaVSSLEAELNRTKSE-------IALV 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082213 1581 KKQLRDLEAKVKDQEEELDEQAgsiQMLEQAKLRLEMEMERMRQTHskemesrdEEVEEARQSCQkklkQMEVQLEE 1657
Cdd:pfam05701 369 QAKEKEAREKMVELPKQLQQAA---QEAEEAKSLAQAAREELRKAK--------EEAEQAKAAAS----TVESRLEA 430
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1495-1741 |
9.48e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1495 ELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFS-----LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQ 1569
Cdd:pfam09731 230 NVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPvlkedNLLSNDDLNSLIAHAHREIDQLSKKLAELKKR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1570 ESKDEA-SLAKVKKQLRDLEAKV-KDQEEELDEQAGSIQMLEQAKL-------RLEMEMERMRQTHSKEMESRDEEVEEA 1640
Cdd:pfam09731 310 EEKHIErALEKQKEELDKLAEELsARLEEVRAADEAQLRLEFEREReeiresyEEKLRTELERQAEAHEEHLKDVLVEQE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1641 rqscqkklkqMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQ--RDFESEKRLRKDLKRTKAL------LADAQIML 1712
Cdd:pfam09731 390 ----------IELQREFLQDIKEKVEEERAGRLLKLNELLANLKGleKATSSHSEVEDENRKAQQLwlaveaLRSTLEDG 459
|
250 260
....*....|....*....|....*....
gi 1907082213 1713 DHLKNNAPSKREIAQLKNQLEESEFTCAA 1741
Cdd:pfam09731 460 SADSRPRPLVRELKALKELASDDEVVKAA 488
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1428-1608 |
9.51e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1428 RLQQELEDKMEVEQQSRRQLER---RLGDLQADSDESQRALQQLKKKCQRLTAELQ----DTKLHLEG-------QQVrn 1493
Cdd:PHA02562 217 RKQNKYDELVEEAKTIKAEIEEltdELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfqkVIKMYEKGgvcptctQQI-- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1494 HELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLA---EAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQE 1570
Cdd:PHA02562 295 SEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907082213 1571 SKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQML 1608
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLL 412
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1559-1790 |
9.94e-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: 39.74 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1559 LEAELQDISSQESK-DEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQaklrLEMEMERMRQTHSKEMESRDEEV 1637
Cdd:cd00176 9 ADELEAWLSEKEELlSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNE----LGEQLIEEGHPDAEEIQERLEEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082213 1638 EEARQSCQKKLKQMEVQLEEEYeDKQKALREKRELESKLSTLSDQVNQRDfesekrlrkdlkrtkaLLADAQIMLDHLKN 1717
Cdd:cd00176 85 NQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASED----------------LGKDLESVEELLKK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082213 1718 NAPSKREIAQLKNQLEESEftcaaavkaRKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE 1790
Cdd:cd00176 148 HKELEEELEAHEPRLKSLN---------ELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| |
