|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
424-1005 |
2.78e-21 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 99.38 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 424 WSAHKTEAGVVYYYNALTGESTYQKPPGY-KGEPEKVAAQPvpvswdklagtdWSIVTTSDGKKYYYDNKLKVSSWQLPP 502
Cdd:COG5104 17 WEELKAPDGRIYYYNKRTGKSSWEKPKELlKGSEEDLDVDP------------WKECRTADGKVYYYNSITRESRWKIPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 503 EvaeliKNAESGPLKGSSTSLQDAGTIGNKeeisididtPAVQTGgrdslplrQTVAPasssaldlikKKLQdagassvp 582
Cdd:COG5104 85 E-----RKKVEPIAEQKHDERSMIGGNGND---------MAITDH--------ETSEP----------KYLL-------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 583 splatpssaselngskttdaapmGHQVSISGEKSKDNSgdgnmsdsssnsddeEHGPSEEECTRQFKEMLKERGVLPFSK 662
Cdd:COG5104 125 -----------------------GRLMSQYGITSTKDA---------------VYRLTKEEAEKEFITMLKENQVDSTWP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 663 WEKELpKIVFDPRFKAI---PSHsrRRSTFEQYVRTRADEERKEKRAAQRAAVEAYKQLLeEASEDINSNKDYKEFKRKW 739
Cdd:COG5104 167 IFRAI-EELRDPRYWMVdtdPLW--RKDLFKKYFENQEKDQREEEENKQRKYINEFCKML-AGNSHIKYYTDWFTFKSIF 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 740 GTDPRFEAL-DRKERDALFNE-KVKSIEEKVQS---VRNAVIAEFKSMLRESKDITSTsRWTKVKENFRSDARYKAMKHE 814
Cdd:COG5104 243 SKHPYYSSVvNEKTKRQTFQKyKDKLGCYEKYVgkhMGGTALGRLEEVLRSLGSETFI-IWLLNHYVFDSVVRYLKNKEM 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 815 E---REVAFNEYIAELKSAEKEAeqaakakldeQAKLKEReremRKRKEREEQemervklkIRRKEAVSSYQALLVEIIK 891
Cdd:COG5104 322 KpldRKDILFSFIRYVRRLEKEL----------LSAIEER----KAAAAQNAR--------HHRDEFRTLLRKLYSEGKI 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 892 DPKASWTESKPRLEKDPqgRAVNPDLGKGDAEK-LFRDHVKDLYERCVRDFRALLSEVITPEIAARTTdegkTAINSWTE 970
Cdd:COG5104 380 YYRMKWKNAYPLIKDDP--RFLNLLGRTGSSPLdLFFDFIVDLENMYGFARRSYERETRTGQISPTDR----RAVDEIFE 453
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1002302520 971 --AKGLLRSDPRYNKLASKD----RESIWRRYADDMKTKLK 1005
Cdd:COG5104 454 aiAEKKEEGEIKFDKVDKEDisliVDGLIKQRNEKIQQKLQ 494
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2-360 |
4.59e-15 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 80.75 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAP-ASESEGPFDSGVVAAATTPAVVDSAVEGDAPA---APAPTSGSGPAAPSMPANPAS 77
Cdd:PHA03247 2596 ARPRAPVDDRGDPRGPAPPSPLPpDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERprdDPAPGRVSRPRRARRLGRAAQ 2675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 78 P-ATPGPPRPQFAGSPAYASPpapafSYNVLPRPSPRPQVGSGAAQQQLASPPGTNHAVQVSRFVPPSSLQPPAPMNlar 156
Cdd:PHA03247 2676 AsSPPQRPRRRAARPTVGSLT-----SLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG--- 2747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 157 psSAFPGAGAMPPNPPGSIRLPFPGPPR-----PSINTFVASPQQAQPQASQLPSNSGSSDVSTSRsdTRSVPEASPQTM 231
Cdd:PHA03247 2748 --PATPGGPARPARPPTTAGPPAPAPPAapaagPPRRLTRPAVASLSESRESLPSPWDPADPPAAV--LAPAAALPPAAS 2823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 232 QLSTGPPSTSTAGSPSITVQMPTNPSLPTRpevfgaiGASVPGQPSTILSAPPSLLGRPMTPSASPF-----PQTSQSPT 306
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLG-------GSVAPGGDVRRRPPSRSPAAKPAAPARPPVrrlarPAVSRSTE 2896
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1002302520 307 AFQQPGQQQLYPSYPSAHgVQPQPLWGYPPQPTGFQQPPFQSYPSGLLGPLGRP 360
Cdd:PHA03247 2897 SFALPPDQPERPPQPQAP-PPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDP 2949
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
37-419 |
1.31e-14 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 79.21 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 37 VAAATTPAVVDSAVEGD--APAAPAPTSGSGPAAPSMPANPASPATPGPPRPQFAGSPAYASPPAPAFSYNVlPRPSPRP 114
Cdd:PHA03247 2555 LPPAAPPAAPDRSVPPPrpAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDP-PPPSPSP 2633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 115 QVGSGAAQQQLASPPgtnhavqvsrfvPPSSLQPPAPMNLARPSSA-FPGAGAMPPNPPGSIRLPFPGPPRPSINTFVAS 193
Cdd:PHA03247 2634 AANEPDPHPPPTVPP------------PERPRDDPAPGRVSRPRRArRLGRAAQASSPPQRPRRRAARPTVGSLTSLADP 2701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 194 PQQAQPQASQLPSNSGSSDVSTSRSDTRSVPEASPqtmqLSTGPPSTSTAGSPSITVQMPTNPSLPTrpevfgaiGASVP 273
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALP----AAPAPPAVPAGPATPGGPARPARPPTTA--------GPPAP 2769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 274 GQPSTILSAPPSLLGRPMTPSASPFPQTSQSPTAFQQPGQQQLYPSypSAHGVQPQPLWGYPPQPTGFQ-QPPFQSYPSG 352
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA--AALPPAASPAGPLPPPTSAQPtAPPPPPGPPP 2847
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002302520 353 LLGPLGRPMVGSSSVTAYLPSIQPPGVSTTDRDSKELSSANPGSEQPTQQGSQNSDQLEDKRTTAIQ 419
Cdd:PHA03247 2848 PSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAP 2914
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
646-692 |
4.99e-14 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 67.10 E-value: 4.99e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1002302520 646 RQFKEMLKERGVLPFSKWEKELPKIVFDPRFKAIPSHSRRRSTFEQY 692
Cdd:pfam01846 4 EAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2-423 |
1.91e-12 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 71.89 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATP 81
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAP 2769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 82 GPPRPQFAGSpayasppapafsynvlPRPSPRPQVGSGAAQQQLASPPGTNHAvqvsrfvPPSSLQPPAPmnlARPSSAF 161
Cdd:PHA03247 2770 APPAAPAAGP----------------PRRLTRPAVASLSESRESLPSPWDPAD-------PPAAVLAPAA---ALPPAAS 2823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 162 PGAGAMPPNPPGSIRLPFPGPPRPsintfvaspqqaqpqasqlpsnsgssdvsTSRSDTRSVPEASPqtmqLSTGPPSTS 241
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPP-----------------------------PSLPLGGSVAPGGD----VRRRPPSRS 2870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 242 TagspsitvqmPTNPSLPTRPEVfGAIGASVPGQPSTILSAPPSLLGRPMTPSASPFPQTSQSPTAFQQPGQQQLYPSYP 321
Cdd:PHA03247 2871 P----------AAKPAAPARPPV-RRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 322 SAHgVQPQPLWGYPPQPTGFQQPPFQSYPSGLLGPLGRPMVGSS--SVTAYLPSIQPPGVSTTDRDSKELSS------AN 393
Cdd:PHA03247 2940 QPP-LAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPapSREAPASSTPPLTGHSLSRVSSWASSlalheeTD 3018
|
410 420 430
....*....|....*....|....*....|
gi 1002302520 394 PGSEQpTQQGSQNSDQLEDKRTTAIQDSDS 423
Cdd:PHA03247 3019 PPPVS-LKQTLWPPDDTEDSDADSLFDSDS 3047
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
3-340 |
3.40e-12 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 70.97 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 3 TPATAASDATNPEAAE----VPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASP 78
Cdd:PHA03307 107 TPPGPSSPDPPPPTPPpaspPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 79 ATPGPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPPGTNHAVQVS----------RFVPPSSLQP 148
Cdd:PHA03307 187 SSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGcgwgpenecpLPRPAPITLP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 149 PAPMNLARPSSAFPGAGAMPPNPPGSIRLPFPGPPRPSintfvasPQQAQPQASQLPSNSGSSDVSTSRSDTRSVPEASP 228
Cdd:PHA03307 267 TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPG-------SGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 229 QtmqlSTGPPSTSTAGSPSITVQMPTNPSLPTRPEVFGAIGASVPGQPSTILSAPPSLLGRPMTPSASPFPQTSQSPTAF 308
Cdd:PHA03307 340 A----VSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPS 415
|
330 340 350
....*....|....*....|....*....|....
gi 1002302520 309 QQPGQQQLYPSYPSAHGVQP--QPLWGYPPQPTG 340
Cdd:PHA03307 416 PLDAGAASGAFYARYPLLTPsgEPWPGSPPPPPG 449
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
776-823 |
3.15e-11 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 59.01 E-value: 3.15e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1002302520 776 IAEFKSMLRESKdITSTSRWTKVKENFRSDARYKAMK-HEEREVAFNEY 823
Cdd:pfam01846 3 REAFKELLKEHK-ITPYSTWSEIKKKIENDPRYKALLdGSEREELFEDY 50
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
37-377 |
2.50e-10 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 64.79 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 37 VAAATTPAVVDSAVEGDAPAApAPTSGSGPAAPSMPANPASPATPGPPRPQFAGSPAYASPPAPAFSYNVLPRPSPrpqv 116
Cdd:pfam03154 173 VLQAQSGAASPPSPPPPGTTQ-AATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHP---- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 117 gsgaAQQQLASPPGTNHavqvsrfVPPSSLQPPAPMnlarpssafpgaGAMPPNP----PGSIRLPFPGPPRPSINTFVA 192
Cdd:pfam03154 248 ----PLQPMTQPPPPSQ-------VSPQPLPQPSLH------------GQMPPMPhslqTGPSHMQHPVPPQPFPLTPQS 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 193 SPQQAQPQASQLPSNSGSSDVSTSRSDTRSVPEASPQTMQLSTGPPSTSTAGSPSIT--VQMPTNPSLPTRPEVFGaiga 270
Cdd:pfam03154 305 SQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTpiPQLPNPQSHKHPPHLSG---- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 271 SVPGQPSTILSAPPSL-----LGRPMTPSASP-----FPQTSQSPTAFQQPGQQQLYPSYPSAHGVQPQP--LWGYPPQP 338
Cdd:pfam03154 381 PSPFQMNSNLPPPPALkplssLSTHHPPSAHPpplqlMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTsgLHQVPSQS 460
|
330 340 350
....*....|....*....|....*....|....*....
gi 1002302520 339 TGFQQPPFQSYPSGLLGPLGRPMVGSSSvtayLPSIQPP 377
Cdd:pfam03154 461 PFPQHPFVPGGPPPITPPSGPPTSTSSA----MPGIQPP 495
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2-345 |
1.29e-09 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 62.31 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASE--SEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPA 79
Cdd:PRK07764 413 AAAAPAAAAAPAPAAAPQPAPAPAPApaPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAA 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 80 TPGPPRPQFAGSPAYASPPA-----------PAFSYNVLPRPSPRPQVG------------SGAAQQQLASPPGTNHAVQ 136
Cdd:PRK07764 493 APAAPAAPAAPAGADDAATLrerwpeilaavPKRSRKTWAILLPEATVLgvrgdtlvlgfsTGGLARRFASPGNAEVLVT 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 137 V----------------------SRFVPPSSLQPPAPMNLARPSSAFPGAGAMPPNPPGSirlpfPGPPRPSINTFVASP 194
Cdd:PRK07764 573 AlaeelggdwqveavvgpapgaaGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA-----AAAPAEASAAPAPGV 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 195 QQAQPQASQLPSNSGSSDVSTSRSDTRSVPEASPQTMQLSTGPPSTSTAGSPsitvqmPTNPSLPTRPevfgaigasVPG 274
Cdd:PRK07764 648 AAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPA------QPAPAPAATP---------PAG 712
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002302520 275 QPSTILSAPPSLLGRPMTPSASPFPQTSQSPTAFQQPGQQQLYPSYPSAHGVQPQPLWGYPPQPTGFQQPP 345
Cdd:PRK07764 713 QADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
642-694 |
1.21e-08 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 52.19 E-value: 1.21e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1002302520 642 EECTRQFKEMLKERGVL-PFSKWEKELPKIVFDPRFKAIPSHSRRRSTFEQYVR 694
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
777-826 |
1.81e-08 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 51.42 E-value: 1.81e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1002302520 777 AEFKSMLRESKDITSTSRWTKVKENFRSDARYKAM-KHEEREVAFNEYIAE 826
Cdd:smart00441 5 EAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALlSESEREQLFEDHIEE 55
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2-186 |
2.27e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 58.35 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATP 81
Cdd:PRK12323 388 AAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAA 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 82 GPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPPGTNHAVQVSRFVPPSSLQPPAPMNLARPSsaf 161
Cdd:PRK12323 468 GPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPA--- 544
|
170 180
....*....|....*....|....*
gi 1002302520 162 PGAGAMPPNPPGSIRLPFPGPPRPS 186
Cdd:PRK12323 545 PAAAPAPRAAAATEPVVAPRPPRAS 569
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2-382 |
2.53e-08 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 58.26 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATP 81
Cdd:PHA03307 53 VTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 82 GPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPPGTNHavqvsrfvPPSSlqPPAPMNLARPSSAF 161
Cdd:PHA03307 133 DLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETAR--------APSS--PPAEPPPSTPPAAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 162 PGAGAmPPNPPGSIRLPFPGPPRP-----------SINTFVASPQQAQPQASQLPSNSGSSDVSTSRSDTRSVPEASPqT 230
Cdd:PHA03307 203 SPRPP-RRSSPISASASSPAPAPGrsaaddagassSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPS-S 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 231 MQLSTGPPSTSTAGSPSITVQMPTNPSLPTRPEVFGAIGASVPGQPSTILSAPPSLLGRPMTPSASPfpqtSQSPTafQQ 310
Cdd:PHA03307 281 RPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSP----SRSPS--PS 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002302520 311 PGQQQLYPSYPSAHGvQPQPLWGYPPQPTGFQQPPFQSYpsgLLGPLGRPMVGSSSVTAYLPSIQPPGVSTT 382
Cdd:PHA03307 355 RPPPPADPSSPRKRP-RPSRAPSSPAASAGRPTRRRARA---AVAGRARRRDATGRFPAGRPRPSPLDAGAA 422
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
690-878 |
2.84e-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: 56.85 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 690 EQYVRTRADEERKEKRAAQRAAveayKQLLEEASEDINSNKDYKEFKRKwgtdpRFEALDRK---------ERDALFNEK 760
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQ----RQLREEIDEFNEEQAEWKELEKE-----EEREEDERileylkekaEREEEREAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 761 VKSIEEKVQSVRNAVIAEfKSMLRESKDItstsrwtkvKENFRSDaRYkamkHEEREVAFNEyiAELKSAEKEAEQAAKA 840
Cdd:pfam13868 175 REEIEEEKEREIARLRAQ-QEKAQDEKAE---------RDELRAK-LY----QEEQERKERQ--KEREEAEKKARQRQEL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002302520 841 K--LDEQAKLKEREREMRKRKEREE-QEMERVKLKIRRKEA 878
Cdd:pfam13868 238 QqaREEQIELKERRLAEEAEREEEEfERMLRKQAEDEEIEQ 278
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
4-405 |
3.24e-08 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 57.69 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 4 PATAASDATNPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATPGP 83
Cdd:PRK07764 386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 84 PRPQFAGSPAYASPPAPAFSYNvlPRPSPRPQVGSGAAQQQLASPPGT-----NHAVQV----SRFVPPSSLQ------- 147
Cdd:PRK07764 466 PAPAPAAAPEPTAAPAPAPPAA--PAPAAAPAAPAAPAAPAGADDAATlrerwPEILAAvpkrSRKTWAILLPeatvlgv 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 148 -----------PPAPMNLARPSSA-----------------------FPGAGAMPPNPPGSIRLPFPGPPRPSintfvAS 193
Cdd:PRK07764 544 rgdtlvlgfstGGLARRFASPGNAevlvtalaeelggdwqveavvgpAPGAAGGEGPPAPASSGPPEEAARPA-----AP 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 194 PQQAQPQASQLPSNSGSSDVSTSRSDTRSVPEASPQTMQLSTGPPSTSTAGSPSITVQMPTNPSLPTRPEVFGAIGASVP 273
Cdd:PRK07764 619 AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAP 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 274 GQPSTilsappsllgrpmTPSASPFPQTSQSPTAFQQPGQQQLYPSYPSAHGVQPQPlwGYPPQPTGFQQPPFQSYPSGl 353
Cdd:PRK07764 699 AQPAP-------------APAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLP--PEPDDPPDPAGAPAQPPPPP- 762
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1002302520 354 lgplgrpmvgssSVTAYLPSIQPPGVSTTDRDSKELSSANPGSEQPTQQGSQ 405
Cdd:PRK07764 763 ------------APAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAE 802
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
4-284 |
3.65e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 57.55 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 4 PATAASDAT-NPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAP-SMPANPASPATP 81
Cdd:PRK07003 360 PAVTGGGAPgGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPpAAPAPPATADRG 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 82 GPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPPGTNHAvqVSRFVPPSSLQPPAPMNLARPSSA- 160
Cdd:PRK07003 440 DDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEP--APRAAAPSAATPAAVPDARAPAAAs 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 161 FPGAGAMPPNPPGSIRLPFPGPPRPSintfvaSPQQAQPQASQLPSNSGSSdVSTSRSdtrsvpEASPQTMQLSTGPPST 240
Cdd:PRK07003 518 REDAPAAAAPPAPEARPPTPAAAAPA------ARAGGAAAALDVLRNAGMR-VSSDRG------ARAAAAAKPAAAPAAA 584
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1002302520 241 STAGSPSITVQMPTnPSLPTRPEVFGAIGASVPGQPSTILSAPP 284
Cdd:PRK07003 585 PKPAAPRVAVQVPT-PRARAATGDAPPNGAARAEQAAESRGAPP 627
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
691-881 |
5.39e-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: 54.93 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 691 QYVRTRADEERKEKRAAQrAAVEAYKQLLEEASEDI-NSNKDYKEFKRKwgtdprfeaLDRKERD-ALFNEKVKSIEEKV 768
Cdd:COG1579 13 QELDSELDRLEHRLKELP-AELAELEDELAALEARLeAAKTELEDLEKE---------IKRLELEiEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 769 QSVRNAViaEFKSMLREskdITSTSRwtkvkenfrsdaryKAMKHEEREVAFNEYIAELKSAEKEAEQAAKAKldeQAKL 848
Cdd:COG1579 83 GNVRNNK--EYEALQKE---IESLKR--------------RISDLEDEILELMERIEELEEELAELEAELAEL---EAEL 140
|
170 180 190
....*....|....*....|....*....|...
gi 1002302520 849 KEREREMRKRKEREEQEMErvKLKIRRKEAVSS 881
Cdd:COG1579 141 EEKKAELDEELAELEAELE--ELEAEREELAAK 171
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
694-878 |
8.31e-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: 55.31 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 694 RTRADEERKEKRAAQRAAVEAYKQLLEEASEDinsnkdyKEFKRKwgtdprfEALDRKERDA-LFNEKVKSIEEKvqsvr 772
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEE-------REQKRQ-------EEYEEKLQEReQMDEIVERIQEE----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 773 naviaEFKSMLReskditstsrwtkvkenfrsdaRYKAMKHEEREVA-FNEYIAELKSAEKEAEQAAKAKLDEQAKLKER 851
Cdd:pfam13868 114 -----DQAEAEE----------------------KLEKQRQLREEIDeFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166
|
170 180
....*....|....*....|....*...
gi 1002302520 852 EREMRKRKERE-EQEMERVKLKIRRKEA 878
Cdd:pfam13868 167 REEEREAEREEiEEEKEREIARLRAQQE 194
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
696-1011 |
3.23e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 696 RADEERK---EKRAAQRAAVEAYKQLLEEA--SEDINSNKDYKEFKRKWGTDPRFEALDRKERDALFNEKVKSIEEKvQS 770
Cdd:PTZ00121 1213 KAEEARKaedAKKAEAVKKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK-KK 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 771 VRNAVIAEFKSMLRESKditstsrwTKVKENFRSD-ARYKAMKHEEREVAFNEYIAELKSAEKEAEQAAKAKLDEQAKLK 849
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAK--------KKAEEAKKADeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 850 EREREMRKRKEREEQEMERVKLKIRRKEavssyqallveiikdpKASwtESKPRLEKDpqgRAVNPDLGKGDAEKLFRDH 929
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKK----------------KAD--EAKKKAEED---KKKADELKKAAAAKKKADE 1422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 930 VKDLYE--RCVRDFRALLSEVITPEIAARTTDEGKTAINSWTEAKGLLRSDPRYNKLASKDRESIWRRYADDMKTKLKQS 1007
Cdd:PTZ00121 1423 AKKKAEekKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502
|
....
gi 1002302520 1008 DMKE 1011
Cdd:PTZ00121 1503 KKAA 1506
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1-396 |
4.41e-07 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 54.15 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 1 MATPATAASDATN--PEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSaveGDAPAAPAPT---SGSGPAAPSMPANP 75
Cdd:pfam05109 434 LNTTGFAAPNTTTglPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTS---GASPVTPSPSprdNGTESKAPDMTSPT 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 76 ASPATPGP----PRPqfagspayasppapafsynVLPRPSPR---PQVGSGAAQQQLASPpgtnhavqvsrfvPPSSLQP 148
Cdd:pfam05109 511 SAVTTPTPnatsPTP-------------------AVTTPTPNatsPTLGKTSPTSAVTTP-------------TPNATSP 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 149 PAPMNLARPSSAFPGAGAMPP-----NPPGSIRLPFPGPPRPSINTFVAS-PQQAQPQASQLPSNSGSSDVSTSRSDTrs 222
Cdd:pfam05109 559 TPAVTTPTPNATIPTLGKTSPtsavtTPTPNATSPTVGETSPQANTTNHTlGGTSSTPVVTSPPKNATSAVTTGQHNI-- 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 223 vpeASPQTMQLSTGPPSTSTAGSPSITVQMPTNPSLPTRPEVFGA--IGASVPGQPSTILSAPPSLLGRPMTPSASPFPQ 300
Cdd:pfam05109 637 ---TSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGenITQVTPASTSTHHVSTSSPAPRPGTTSQASGPG 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 301 TSQSPTafqQPGQQQLYPSYPSAHGVQPQPLWGYPPQ-PTGFQQPPFQSYPSGllgplGRPMVGSSSVTAYLPSIQPPGV 379
Cdd:pfam05109 714 NSSTST---KPGEVNVTKGTPPKNATSPQAPSGQKTAvPTVTSTGGKANSTTG-----GKHTTGHGARTSTEPTTDYGGD 785
|
410
....*....|....*..
gi 1002302520 380 STTDRDSKELSSANPGS 396
Cdd:pfam05109 786 STTPRTRYNATTYLPPS 802
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2-152 |
5.61e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 53.84 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAP-APTSGSGPAAPSMPANPASPAT 80
Cdd:PRK07764 634 AAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPaAPAGAAPAQPAPAPAATPPAGQ 713
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002302520 81 PGPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPPGTNHAVQVSRFVPPSSLQPPAPM 152
Cdd:PRK07764 714 ADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEM 785
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
711-759 |
6.20e-07 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 47.07 E-value: 6.20e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1002302520 711 AVEAYKQLLEEAseDINSNKDYKEFKRKWGTDPRFEAL-DRKERDALFNE 759
Cdd:pfam01846 2 AREAFKELLKEH--KITPYSTWSEIKKKIENDPRYKALlDGSEREELFED 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
699-1010 |
1.13e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 699 EERKEKRAAQRAAVEAYKQLLE-----EASEDINSNKDYKEFKRKWGTDPRFEALDRKERDAlfnEKVKSIEEKVQSVRN 773
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEkkkadEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA---KKADEAKKKAEEAKK 1484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 774 AviAEFKSMLRESKditstsrwtKVKENFRSDARYKAMKHEEREVAFNEYIAELKSAE--------KEAEQAAKAklDEQ 845
Cdd:PTZ00121 1485 A--DEAKKKAEEAK---------KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEeakkadeaKKAEEKKKA--DEL 1551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 846 AKLKE-REREMRKRKEREEQEMERVKLKIRRKE-AVSSYQALLVEIIKDPKASWTESKPRLEKDPQGRAVNPDLGKGDAE 923
Cdd:PTZ00121 1552 KKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 924 KLFRDHVKDLYERCVRDFRALLSEviTPEIAARTTDEGKTAINSWTEAKGLLRSDPRYNKLASK-DRESIWRRYADDMKT 1002
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlKKEAEEAKKAEELKK 1709
|
....*...
gi 1002302520 1003 KLKQSDMK 1010
Cdd:PTZ00121 1710 KEAEEKKK 1717
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
696-1014 |
1.22e-06 |
|
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: 52.67 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 696 RADEERKEKRAAQRAAVEAYKQLLEEasedinsNKDYKEFKRKWGTDprfEALDRKERDALFNEKVKSIEEKVQSVRNAV 775
Cdd:pfam02463 206 AKKALEYYQLKEKLELEEEYLLYLDY-------LKLNEERIDLLQEL---LRDEQEEIESSKQEIEKEEEKLAQVLKENK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 776 IAEFKSMLRESKDITSTSRWTKVKENFRSDARYKamKHEEREVAFNEyiAELKSAEKEAEQAAKAKLDEQAKLKEREREM 855
Cdd:pfam02463 276 EEEKEKKLQEEELKLLAKEEEELKSELLKLERRK--VDDEEKLKESE--KEKKKAEKELKKEKEEIEELEKELKELEIKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 856 RKRKEREEQEMER-VKLKIRRKEAVSSYQALLVEIIKDPKASWteskprLEKDPQGRAVNPDLGKGDAEKLFRDHVKDLY 934
Cdd:pfam02463 352 EAEEEEEEELEKLqEKLEQLEEELLAKKKLESERLSSAAKLKE------EELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 935 ERcvrdfraLLSEVITPEIaARTTDEGKTAINSWTEAKGLLRSDpryNKLASKDRESIWRRYADDMKTKLKQSDMKERSD 1014
Cdd:pfam02463 426 KE-------ELEILEEEEE-SIELKQGKLTEEKEELEKQELKLL---KDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
877-929 |
1.23e-06 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 46.30 E-value: 1.23e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1002302520 877 EAVSSYQALLVEIIKDPKASWTESKPRLEKDPQGRAVNPdlgKGDAEKLFRDH 929
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLD---GSEREELFEDY 50
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
696-890 |
1.40e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.46 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 696 RADEERKEKRAAQRAAVEAYKQ-LLEEASEDINSNKDYKEFKRKWGTDPRFEALDRKERdalfnEKVKSIEEKVQSVRNA 774
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKErEIARLRAQQEKAQDEKAERDELRAKLYQEEQERKER-----QKEREEAEKKARQRQE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 775 VIAEFKSMLREskditstsrwtkvKENFRsdARYKAMKHEEREVAFNEYiAELKSAEKEAEQAAKAKLDEQAKLKER--- 851
Cdd:pfam13868 237 LQQAREEQIEL-------------KERRL--AEEAEREEEEFERMLRKQ-AEDEEIEQEEAEKRRMKRLEHRRELEKqie 300
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002302520 852 EREMRKRKEREEQEMERVKLKIRRKEavssYQALLVEII 890
Cdd:pfam13868 301 EREEQRAAEREEELEEGERLREEEAE----RRERIEEER 335
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
2-131 |
1.60e-06 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 52.02 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEvPSAAPASESegpfdsgvvAAATTPAVVDSAVEgDAPAAPAPTSGSGPAAPSMPANPASPATP 81
Cdd:PRK14951 372 AAAPAEKKTPARPEAAA-PAAAPVAQA---------AAAPAPAAAPAAAA-SAPAAPPAAAPPAPVAAPAAAAPAAAPAA 440
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1002302520 82 GP-PRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPPGT 131
Cdd:PRK14951 441 APaAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPT 491
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
4-393 |
1.88e-06 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 51.98 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 4 PATAASDATNPEA--AEVPSAAPASESE-GPFDSGVVAAattPAVVdsaveGDAPAAPAPTSGSGPAAPSMPANPASPAT 80
Cdd:PHA03379 425 PEVPQSLETATSHgsAQVPEPPPVHDLEpGPLHDQHSMA---PCPV-----AQLPPGPLQDLEPGDQLPGVVQDGRPACA 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 81 PGPP------RPQFAGSPAYASPPAPAFSYNVLP-RPSPRPQVGSGAAQQQLAS------PPGTNHAVQVS-RFVP---- 142
Cdd:PHA03379 497 PVPApagpivRPWEASLSQVPGVAFAPVMPQPMPvEPVPVPTVALERPVCPAPPliamqgPGETSGIVRVReRWRPapwt 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 143 PSSLQPPAPMNL-ARPSSAFPGAGA-------MPPN-PPGSIRLPFPGPPRPSINTFVASPQQAQPQASQLPSnsgssdV 213
Cdd:PHA03379 577 PNPPRSPSQMSVrDRLARLRAEAQPyqasvevQPPQlTQVSPQQPMEYPLEPEQQMFPGSPFSQVADVMRAGG------V 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 214 STSRSDTRSVPEASPQTMQLSTGPPSTSTAGSPSITVQMPTNPSLP-TRPEVFGAIGAS-VPGQPSTILSAPPSLLGRPM 291
Cdd:PHA03379 651 PAMQPQYFDLPLQQPISQGAPLAPLRASMGPVPPVPATQPQYFDIPlTEPINQGASAAHfLPQQPMEGPLVPERWMFQGA 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 292 TPSASPFPQTSQSpTAFQQPGQQQLYPSYPSAHGV-QP----------QPLWGYPPQPtGFQQPPFQ----SYPSGLLGP 356
Cdd:PHA03379 731 TLSQSVRPGVAQS-QYFDLPLTQPINHGAPAAHFLhQPpmegpwvpeqWMFQGAPPSQ-GTDVVQHQldalGYVLHVLNH 808
|
410 420 430
....*....|....*....|....*....|....*..
gi 1002302520 357 LGRPMvgSSSVTAYLPSIQPPGVSTTDRDSKELSSAN 393
Cdd:PHA03379 809 PGVPV--SPAVNQYHVSQAAFGLPIDEDESGEGSDTS 843
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
690-878 |
3.06e-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: 50.69 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 690 EQYVRTRADEERKEKRAAQRAAVEAYKQLLEeasedinsnkdyKEFKRKwgtdprfEALDRKERDA-LFNEKVKSIEE-- 766
Cdd:pfam13868 54 ERALEEEEEKEEERKEERKRYRQELEEQIEE------------REQKRQ-------EEYEEKLQEReQMDEIVERIQEed 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 767 ---------KVQSVRNAvIAEFKSMLRESKDItstsrwtkvkenfrsdaRYKAMKHEEREVAfnEYIAELksAEKEAEQA 837
Cdd:pfam13868 115 qaeaeekleKQRQLREE-IDEFNEEQAEWKEL-----------------EKEEEREEDERIL--EYLKEK--AEREEERE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002302520 838 AKAKLDEQAKLKERER----EMRKRKEREEQE-------MERVKLKIRRKEA 878
Cdd:pfam13868 173 AEREEIEEEKEREIARlraqQEKAQDEKAERDelraklyQEEQERKERQKER 224
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
424-449 |
3.48e-06 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 44.42 E-value: 3.48e-06
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
424-451 |
6.45e-06 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 43.67 E-value: 6.45e-06
10 20
....*....|....*....|....*...
gi 1002302520 424 WSAHKTEAGVVYYYNALTGESTYQKPPG 451
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
682-909 |
8.60e-06 |
|
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: 50.06 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 682 HSRRRSTFEQYVRTRADEERKE-------------KRAAQRAavEAYKQL---LEEASEDInSNKDYKEFKRKWgtDPRF 745
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEdilnelerqlkslERQAEKA--ERYKELkaeLRELELAL-LVLRLEELREEL--EELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 746 EALDRKERD-----ALFNEKVKSIEE------KVQSVRNAVIAEFKSMLRESKDITSTSRwtKVKENFRSDARYKAMKHE 814
Cdd:TIGR02168 246 EELKEAEEEleeltAELQELEEKLEElrlevsELEEEIEELQKELYALANEISRLEQQKQ--ILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 815 EREVAFN---EYIAELKSAEKEAEQAAKAKLDEQAKLKEREREMRKRKERE---EQEMERVK---LKIRRKEAVS----S 881
Cdd:TIGR02168 324 QLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeelEEQLETLRskvAQLELQIASLnneiE 403
|
250 260
....*....|....*....|....*...
gi 1002302520 882 YQALLVEIIKDPKASWTESKPRLEKDPQ 909
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLE 431
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
2-187 |
1.25e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 49.46 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASESE------GPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANP 75
Cdd:PRK07003 395 AVPAVTAVTGAAGAALAPKAAAAAAATRaeappaAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADS 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 76 ASPATPGPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPPGTNhavqvSRFVPPSSLQPP------ 149
Cdd:PRK07003 475 GSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPE-----ARPPTPAAAAPAaragga 549
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002302520 150 ---------APMNLARPSSAFPGAGAMPPNPPGSIrlPFPGPPRPSI 187
Cdd:PRK07003 550 aaaldvlrnAGMRVSSDRGARAAAAAKPAAAPAAA--PKPAAPRVAV 594
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
2-273 |
1.32e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 49.31 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVdsavEGDAPAAPAPTSGSGPAAPSMPANPAS---- 77
Cdd:PRK10263 323 AAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQ----TGEPVIAPAPEGYPQQSQYAQPAVQYNeplq 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 78 -PATPGPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPPgtnhavQVSRFVPPSSLQPPAPmnLAR 156
Cdd:PRK10263 399 qPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEE------QQSTFAPQSTYQTEQT--YQQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 157 PSSAFPGAGAMPPNPPGSIRLPFPG-----PPRPSINTFVASPQQAQPQASQLPS----------------NSGSSDVST 215
Cdd:PRK10263 471 PAAQEPLYQQPQPVEQQPVVEPEPVveetkPARPPLYYFEEVEEKRAREREQLAAwyqpipepvkepepikSSLKAPSVA 550
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002302520 216 SRSDTRSVPEASPQTMQLSTGPPSTSTAGSPSITVQMPTNPSLPtRPEVFGAIGASVP 273
Cdd:PRK10263 551 AVPPVEAAAAVSPLASGVKKATLATGAAATVAAPVFSLANSGGP-RPQVKEGIGPQLP 607
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2-253 |
1.47e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 49.10 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAAS--DATNPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAP------TSGSGPAAPSMPA 73
Cdd:PRK12323 372 AGPATAAAapVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEAlaaarqASARGPGGAPAPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 74 nPASPATPGP-PRPQFAGspayasppapafsynvlPRPSPRPQVGSGAAQQQLASPPGTNHAVqvsrfvPPSSLQPPAPm 152
Cdd:PRK12323 452 -PAPAAAPAAaARPAAAG-----------------PRPVAAAAAAAPARAAPAAAPAPADDDP------PPWEELPPEF- 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 153 nlarpssAFPGAGAMPPNPPGSIRLPFPGPprpsintfvASPQQAQPQASQLPSNSGSSDVSTSRSDTRSVPEASPQtmQ 232
Cdd:PRK12323 507 -------ASPAPAQPDAAPAGWVAESIPDP---------ATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPR--A 568
|
250 260
....*....|....*....|.
gi 1002302520 233 LSTGPPSTSTAGSPSITVQMP 253
Cdd:PRK12323 569 SASGLPDMFDGDWPALAARLP 589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
635-950 |
1.50e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 635 EEHGPSEEECTRQFKEMLKERgvlpfSKWEKELPKIVfdPRFKAIPSHSRRRSTFEQYVRTRADEERK-EKRAA----QR 709
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEEL-----KKEIEELEEKV--KELKELKEKAEEYIKLSEFYEEYLDELREiEKRLSrleeEI 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 710 AAVEAYKQLLEEASEDINS-NKDYKEFKRKWGT-DPRFEALD---------RKERDALFNEKVKSIEEKVQSVRNAViae 778
Cdd:PRK03918 324 NGIEERIKELEEKEERLEElKKKLKELEKRLEElEERHELYEeakakkeelERLKKRLTGLTPEKLEKELEELEKAK--- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 779 fKSMLRESKDITSTSRWTKVKENFRSDA--RYKAMK-----------HEEREVAFNEYIAELKSAEKeaeqaakakldEQ 845
Cdd:PRK03918 401 -EEIEEEISKITARIGELKKEIKELKKAieELKKAKgkcpvcgreltEEHRKELLEEYTAELKRIEK-----------EL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 846 AKLKEREREMRKRKEREEQEMERVKLKIRRKEavssyqalLVEIIKDpkaswTESKprlekdpqgravnpdLGKGDAEKL 925
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIKLKE--------LAEQLKE-----LEEK---------------LKKYNLEEL 520
|
330 340
....*....|....*....|....*
gi 1002302520 926 frdhvkdlyERCVRDFRALLSEVIT 950
Cdd:PRK03918 521 ---------EKKAEEYEKLKEKLIK 536
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-877 |
2.30e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 693 VRTRADEERKEKRAAQRAAVEAYKQLLEEASEDINSNKDYKEFKRKWGTDPRFEALDRKERDALFN-EKVKSIEEKVQSV 771
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKaEELKKAEEKKKAE 1567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 772 RNAVIAEFKSMLRESKDITSTSRWTKVKENFRSDARYKAMKHEEREVAFNEYIA--ELKSAE-----------KEAEQAA 838
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKAEeekkkveqlkkKEAEEKK 1647
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002302520 839 KAkldEQAKLKEREREMRKRKEREEQEMERVKLKIRRKE 877
Cdd:PTZ00121 1648 KA---EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
57-332 |
2.35e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 48.31 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 57 APAPTSGSGPAAPSMPANPASPATPGPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASP-PGTNHAV 135
Cdd:PRK07003 359 EPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPaPPATADR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 136 QVSRFVPPSSLQPPAPmNLARPSSAFPGAGAMPPNPPGSIRLPfPGPPRPSINTFVASPQQAQPQASQLPSNSGSSDVST 215
Cdd:PRK07003 439 GDDAADGDAPVPAKAN-ARASADSRCDERDAQPPADSGSASAP-ASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAA 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 216 SRSDtRSVPEASPQTMQLSTGPPSTST---AGSPSITVQMPTNPSLPT---RPEVFGAIGASVPGQPSTILSAPPsllgR 289
Cdd:PRK07003 517 SRED-APAAAAPPAPEARPPTPAAAAPaarAGGAAAALDVLRNAGMRVssdRGARAAAAAKPAAAPAAAPKPAAP----R 591
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1002302520 290 PMTPSASPfpqtsQSPTAFQQPGQQQLYPSYPSAHGVQPQPLW 332
Cdd:PRK07003 592 VAVQVPTP-----RARAATGDAPPNGAARAEQAAESRGAPPPW 629
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
2-184 |
3.09e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 47.92 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAV-EGDAPAAPAPTSGSGPAAPSMPA---NPAS 77
Cdd:PRK07003 415 AAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCdERDAQPPADSGSASAPASDAPPDaafEPAP 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 78 PATPGPPRPQFAGSPAYASPPAPAFSYNVLPR-PSPRPQVGSGAAQQQLASPPGTNHAVQVSRF--VPPSSLQPPAPMNL 154
Cdd:PRK07003 495 RAAAPSAATPAAVPDARAPAAASREDAPAAAApPAPEARPPTPAAAAPAARAGGAAAALDVLRNagMRVSSDRGARAAAA 574
|
170 180 190
....*....|....*....|....*....|
gi 1002302520 155 ARPSSAfPGAGAMPPNPPGSIRLPFPGPPR 184
Cdd:PRK07003 575 AKPAAA-PAAAPKPAAPRVAVQVPTPRARA 603
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
11-151 |
3.85e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 47.79 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 11 ATNPEAAEvpSAAPASESEGPFDsgVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATPGPPRPQFAG 90
Cdd:PRK14951 363 AFKPAAAA--EAAAPAEKKTPAR--PEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAP 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002302520 91 SPAYASPPAPAFSYNVLPRP--SPRPQVGSGAAQQQLASPPGTnhavqvsrfVPPSSLQPPAP 151
Cdd:PRK14951 439 AAAPAAVALAPAPPAQAAPEtvAIPVRVAPEPAVASAAPAPAA---------APAAARLTPTE 492
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
52-297 |
4.25e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.56 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 52 GDAPAAPAPTSGSGPAAPSMPANPASPATPGPPRPQFAGSPAYASPPAPAFSynvlpRPSPRPQVGSGAAQQQLASPPGT 131
Cdd:PRK12323 373 GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPA-----RRSPAPEALAAARQASARGPGGA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 132 nhavqvsrfVPPSSLQPPAPMNLARPSSAfpgagamPPNPPGSIRLPFPGPPRPsintfvaspqqaqpqasqlPSNSGSS 211
Cdd:PRK12323 448 ---------PAPAPAPAAAPAAAARPAAA-------GPRPVAAAAAAAPARAAP-------------------AAAPAPA 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 212 DVSTSRSDTRSVPEASPQTMQLSTGPPSTSTAGSPSITVQMPTNPSLPTRPEVFGAIGASVPGQPSTILSAPPSLLGRPM 291
Cdd:PRK12323 493 DDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASG 572
|
....*.
gi 1002302520 292 TPSASP 297
Cdd:PRK12323 573 LPDMFD 578
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
424-451 |
4.30e-05 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 41.43 E-value: 4.30e-05
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
207-405 |
1.01e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 46.30 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 207 NSGSSDVSTSRSDTRSVPEASPQTMQLSTGPPststagspsiTVQMPTNPSLPTRPEVFGAIGASVPGQPSTILSAPPSl 286
Cdd:pfam03154 141 NRSTSPSIPSPQDNESDSDSSAQQQILQTQPP----------VLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQ- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 287 lGRPMTPSASPFPQTSQSPTAFQQPGQQQLYPSYPSAHGVQpQPLWGYPPQPTGFQQPPFQSYPSGLLGPLGRPMVGSSS 366
Cdd:pfam03154 210 -GSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPL-QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPS 287
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002302520 367 VTAYLPSIQPPGVSTTDRDSKELSSANPGSEQPTQQGSQ 405
Cdd:pfam03154 288 HMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIH 326
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
807-891 |
1.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 807 RYKAMKHEEREVAFNEYIAELKSAEKEAEQAAKAKLDEQAKLKEREREMRKR-KEREEQEMERVKLKIRRKEAVSSYQAL 885
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELeAELEELRLELEELELELEEAQAEEYEL 293
|
....*.
gi 1002302520 886 LVEIIK 891
Cdd:COG1196 294 LAELAR 299
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
474-503 |
1.29e-04 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 39.82 E-value: 1.29e-04
10 20 30
....*....|....*....|....*....|
gi 1002302520 474 TDWSIVTTSDGKKYYYDNKLKVSSWQLPPE 503
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| KREPA2 |
cd23959 |
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ... |
11-183 |
1.32e-04 |
|
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.
Pssm-ID: 467780 [Multi-domain] Cd Length: 424 Bit Score: 45.63 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 11 ATNPEAAEVP-SAAPASESEGPFDSG--VVAAATTPAVVDSA----VEGDAPAAPAPTSGSGPAAPSMPANPASPATPG- 82
Cdd:cd23959 47 AARPSDQEEPlYGAVSPEGENPFDGPglVTASTVSDCYVGNAnfyeVDMSDAFAMAPDESLGPFRAARVPNPFSASSSTq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 83 --PPRPQFAGSPAYASPPAPAFSYNVLP----RPSPRPQVGSGAAQQQLASPPGTNHAVQVSRFVPPSSLQPPAPMNLAR 156
Cdd:cd23959 127 reTHKTAQVAPPKAEPQTAPVTPFGQLPmfgqHPPPAKPLPAAAAAQQSSASPGEVASPFASGTVSASPFATATDTAPSS 206
|
170 180
....*....|....*....|....*....
gi 1002302520 157 PSSAFPGAGAMPPNP--PGSIRLPFPGPP 183
Cdd:cd23959 207 GAPDGFPAEASAPSPfaAPASAASFPAAP 235
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
4-129 |
1.37e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 45.86 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 4 PATAASDATNPEAAEVPSAAPASESEGPfdsGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATPGP 83
Cdd:PRK14951 387 AAPAAAPVAQAAAAPAPAAAPAAAASAP---AAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIP 463
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1002302520 84 PRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPP 129
Cdd:PRK14951 464 VRVAPEPAVASAAPAPAAAPAAARLTPTEEGDVWHATVQQLAAAEA 509
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
698-876 |
1.57e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 698 DEERKEKRAAQRAAVEAYkqlLEEASEDINSNKDYKEFKRkwgtdpRFEALDRKERDA--LFNEKVKSIEEKvqsvrnav 775
Cdd:PRK02224 473 DRERVEELEAELEDLEEE---VEEVEERLERAEDLVEAED------RIERLEERREDLeeLIAERRETIEEK-------- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 776 iAEFKSMLRESKDITSTSrwTKVKENFRSDARYKAMKHEEREVAFNEYIAELKSaEKEAEQAAKAKLDEQAKLKEREREM 855
Cdd:PRK02224 536 -RERAEELRERAAELEAE--AEEKREAAAEAEEEAEEAREEVAELNSKLAELKE-RIESLERIRTLLAAIADAEDEIERL 611
|
170 180
....*....|....*....|....*
gi 1002302520 856 RKRK----EREEQEMERVKLKIRRK 876
Cdd:PRK02224 612 REKRealaELNDERRERLAEKRERK 636
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
677-891 |
1.65e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 677 KAIPSHSRRRSTFEQYVRTRAdEERKEKRAAQRAAVEAYKQLLEEASEDINSNKDYKEfkrkwgtdprfealdrkERDAL 756
Cdd:COG1340 22 EEIEELKEKRDELNEELKELA-EKRDELNAQVKELREEAQELREKRDELNEKVKELKE-----------------ERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 757 fNEKVKSIEEKVQSVRNaviaEFKSMLRESKDITSTSRwtkvkenfrsdaRYKAM----------KHEEREVAfnEYIAE 826
Cdd:COG1340 84 -NEKLNELREELDELRK----ELAELNKAGGSIDKLRK------------EIERLewrqqtevlsPEEEKELV--EKIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 827 LksaEKEAEqAAKAKLDEQAKLKEREREMRK-RKEREE---------QEMERVKLKIR---------RKEAvSSYQALLV 887
Cdd:COG1340 145 L---EKELE-KAKKALEKNEKLKELRAELKElRKEAEEihkkikelaEEAQELHEEMIelykeadelRKEA-DELHKEIV 219
|
....
gi 1002302520 888 EIIK 891
Cdd:COG1340 220 EAQE 223
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
474-501 |
1.74e-04 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 39.41 E-value: 1.74e-04
10 20
....*....|....*....|....*...
gi 1002302520 474 TDWSIVTTSDGKKYYYDNKLKVSSWQLP 501
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
820-892 |
1.88e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 1.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002302520 820 FNEYIAELKSAEKEAEQAAK---AKLDEQAKLKER-EREMRKRKEREEQEMERVKLKIrrKEAVSSYQALLVEIIKD 892
Cdd:PRK00409 518 LNELIASLEELERELEQKAEeaeALLKEAEKLKEElEEKKEKLQEEEDKLLEEAEKEA--QQAIKEAKKEADEIIKE 592
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
873-932 |
2.09e-04 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 39.86 E-value: 2.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002302520 873 IRRKEAvssYQALLVEIIKD-PKASWTESKPRLEKDPQGRAVnpdLGKGDAEKLFRDHVKD 932
Cdd:smart00441 1 EEAKEA---FKELLKEHEVItPDTTWSEARKKLKNDPRYKAL---LSESEREQLFEDHIEE 55
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
118-361 |
2.27e-04 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 45.38 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 118 SGAAQQQLASPPGTNHAVQVSRFVPP--SSLQppapmNLARPSSAFPGAGAMPPNPPGsirlPFPGPPRPsintfvaspq 195
Cdd:pfam09606 56 KAAQQQQPQGGQGNGGMGGGQQGMPDpiNALQ-----NLAGQGTRPQMMGPMGPGPGG----PMGQQMGG---------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 196 qaqpqasqlPSNSGSSDVSTSRSDTRSVPEASPQTMQ--LSTGPPSTSTAGS-PSITVQMPTNPS--LPTRPEVFGAIGA 270
Cdd:pfam09606 117 ---------PGTASNLLASLGRPQMPMGGAGFPSQMSrvGRMQPGGQAGGMMqPSSGQPGSGTPNqmGPNGGPGQGQAGG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 271 SVPGQPSTILSAPPSLLGRPMTPSASPfpqtsqsptafqqpGQQQLYPSYPSAHGVQPQPLWGYPPQPTGFQQPPFQSYP 350
Cdd:pfam09606 188 MNGGQQGPMGGQMPPQMGVPGMPGPAD--------------AGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQ 253
|
250
....*....|.
gi 1002302520 351 SGLLGPLGRPM 361
Cdd:pfam09606 254 QSQLGMGINQM 264
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
699-907 |
2.43e-04 |
|
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: 45.35 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 699 EERKEKRAAQRAAVEAYKQLLEEASED-INSNKDYKEFKRKwgTDPRFEALDRKERDALFNEKVKSIEEkvqsvrnavia 777
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAqDKINEELKLLKQK--IDEEEEEEEKSRLKKEEKEEEKSELS----------- 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 778 efksmLRESKDITSTSRWTKVKENFRSDARYKAMKHEEREVAF-NEYIAELKSAEKEAEQAAKAKLDEQAKLKEREREMR 856
Cdd:pfam02463 771 -----LKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEeLKEEAELLEEEQLLIEQEEKIKEEELEELALELKEE 845
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002302520 857 KRKEREEQEMERVKLKIRRKEAVSSYQAL-LVEIIKDPKASWTESKPRLEKD 907
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLkEEELEEQKLKDELESKEEKEKE 897
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1-305 |
2.60e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 44.95 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 1 MATPATAASDAtNPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPAT 80
Cdd:pfam17823 97 LSEPATREGAA-DGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 81 PGPPRPQFAGSPAYASPPAPAFSYNVLPrPSPRPQVGSGAAQQQLASPPGTNHAVQVSRFVP-PSSLQPPAPMNLARPSS 159
Cdd:pfam17823 176 RTAASSTTAASSTTAASSAPTTAASSAP-ATLTPARGISTAATATGHPAAGTALAAVGNSSPaAGTVTAAVGTVTPAALA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 160 AFPGAGAMPPNPPGSIRLPFPGPPRPSintfvaspqqaqpqasqlPSNSGSSDVSTSRSDTRSVPEASPQTMQLSTGPPS 239
Cdd:pfam17823 255 TLAAAAGTVASAAGTINMGDPHARRLS------------------PAKHMPSDTMARNPAAPMGAQAQGPIIQVSTDQPV 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002302520 240 TSTAGSPSitvqmptnPSlPTRPEVFGAIGASVPGQPSTILSAPPSLLGRPmTPSASPFPQTSQSP 305
Cdd:pfam17823 317 HNTAGEPT--------PS-PSNTTLEPNTPKSVASTNLAVVTTTKAQAKEP-SASPVPVLHTSMIP 372
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
702-888 |
2.67e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 702 KEKRAAQRAAVEAYKQLLE---EASEDINSN-KDYKEFKRKWGT--DPRFEALDRKERDALFNEKVKSIEEKVQSVrNAV 775
Cdd:PRK03918 563 KKLDELEEELAELLKELEElgfESVEELEERlKELEPFYNEYLElkDAEKELEREEKELKKLEEELDKAFEELAET-EKR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 776 IAEFKSMLRESKDITSTSRWTKVKENFRSdarykamkhEEREVAFNEyiAELKSAEKEAEQAAKAkLDeqaKLKEREREM 855
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELREEYLE---------LSRELAGLR--AELEELEKRREEIKKT-LE---KLKEELEER 706
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002302520 856 RKRKEREE------QEMERVKLKIRRkeavssYQALLVE 888
Cdd:PRK03918 707 EKAKKELEklekalERVEELREKVKK------YKALLKE 739
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
809-878 |
2.70e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.04 E-value: 2.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002302520 809 KAMkhEEREvafnEYIAE-LKSAEKEAEQAAKAKLDEQAKLKEREREMRKRKEREEQEMERVKLKIR---RKEA 878
Cdd:cd06503 26 KAL--DERE----EKIAEsLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILaeaKEEA 93
|
|
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
206-428 |
2.75e-04 |
|
Hamartin protein; This family includes the hamartin protein which is thought to function as a tumour suppressor. The hamartin protein interacts with the tuberin protein pfam03542. Tuberous sclerosis complex (TSC) is an autosomal dominant disorder and is characterized by the presence of hamartomas in many organs, such as brain, skin, heart, lung, and kidney. It is caused by mutation either TSC1 or TSC2 tumour suppressor gene. TSC1 encodes a protein, hamartin, containing two coiled-coil regions, which have been shown to mediate binding to tuberin. The TSC2 gene codes for tuberin pfam03542. These two proteins function within the same pathway(s) regulating cell cycle, cell growth, adhesion, and vesicular trafficking.
Pssm-ID: 461287 [Multi-domain] Cd Length: 730 Bit Score: 45.05 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 206 SNSGSSDVSTSRSDTRSVPEASPQ--TMQLSTGPPSTSTAGSPSITVQMPTNPS----LPTRPEVFgaigASVPGQPSTI 279
Cdd:pfam04388 289 GSSTSTPSSTPRLQLSSSSGTSPPylSPPSIRLKTDSFPLWSPSSVCGMTTPPTspgmVPTTPSEL----SPSSSHLSSR 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 280 LSAPPSLLGRPmTPSASPfpqtSQSPTAFQQPgqqqlyPSYPSAHGVQPQPLWGYPPQPTGFQQPPFQSYPsgllgplgr 359
Cdd:pfam04388 365 GSSPPEAAGEA-TPETTP----AKDSPYLKQP------PPLSDSHVHRALPASSQPSSPPRKDGRSQSSFP--------- 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002302520 360 PMVGSSSVTAYLPSIQPPGVSTTDRDSKELSsanpgseQPTQQGSQNSDQLEDKrttaiqDSDSWSAHK 428
Cdd:pfam04388 425 PLSKQAPTNPNSRGLLEPPGDKSSVTLSELP-------DFIKDLALSSEDSVEG------AEEEAAISQ 480
|
|
| DUF3729 |
pfam12526 |
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
5-87 |
3.54e-04 |
|
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.
Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 41.22 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 5 ATAASDATNPEAAeVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATP--- 81
Cdd:pfam12526 23 SGFSSCFSPPESA-HPDPPPPVGDPRPPVVDTPPPVSAVWVLPPPSEPAAPEPDLVPPVTGPAGPPSPLAPPAPAQKppl 101
|
....*.
gi 1002302520 82 GPPRPQ 87
Cdd:pfam12526 102 PPPRPQ 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
783-878 |
3.82e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 783 LRESKDITSTSRWTKVKENFRSDARYKAMKHEEREVAFNEYIAELKSAEKEAEQAAKAKLDEQAKLKE---REREMRKRK 859
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAEL 297
|
90
....*....|....*....
gi 1002302520 860 EREEQEMERVKLKIRRKEA 878
Cdd:COG1196 298 ARLEQDIARLEERRRELEE 316
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
749-876 |
3.92e-04 |
|
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: 44.67 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 749 DRKERDALfnEKVKSIEEKvqsvrnavIAEFKSMLRESKDitstsRWTKVKENfRSDA-RYKAMKHEEREVAFNEYIAEL 827
Cdd:TIGR02169 169 DRKKEKAL--EELEEVEEN--------IERLDLIIDEKRQ-----QLERLRRE-REKAeRYQALLKEKREYEGYELLKEK 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002302520 828 KSAEKEaeqaaKAKLDEQAKLKERERE--------MRKRKEREEQEMERVKLKIRRK 876
Cdd:TIGR02169 233 EALERQ-----KEAIERQLASLEEELEklteeiseLEKRLEEIEQLLEELNKKIKDL 284
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
696-953 |
4.34e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 696 RADEERKEKRAaqRAAVEAYKQLLEEASEDINSNKDYKEFKRKWGTDPRFEALDRKERDALFNEKVKSIEEKVQSVRNAV 775
Cdd:PTZ00121 1523 KADEAKKAEEA--KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 776 IAEFKSM----LRESKDITSTSRWTKVKENFRSDARYKAMKHEER-----EVAFNEYIAELKSAE---------KEAEQA 837
Cdd:PTZ00121 1601 YEEEKKMkaeeAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaeELKKAEEENKIKAAEeakkaeedkKKAEEA 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 838 AKA-----KLDEQAKLKERER----EMRKRKEREEQEMERVklkiRRKEAVSSYQAllveiiKDPKASWTESKPRLEkdp 908
Cdd:PTZ00121 1681 KKAeedekKAAEALKKEAEEAkkaeELKKKEAEEKKKAEEL----KKAEEENKIKA------EEAKKEAEEDKKKAE--- 1747
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1002302520 909 qgravnpDLGKGDAEKLFRDHVKDLYERCVRDFRALLSEVITPEI 953
Cdd:PTZ00121 1748 -------EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
797-859 |
5.07e-04 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 43.33 E-value: 5.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002302520 797 KVKENfRSDAR---YKAMKHEEREvafnEYIAELKSAEKEAEQAAKAKLD--EQAKLKEREREMRKRK 859
Cdd:pfam07946 261 KAKKT-REEEIekiKKAAEEERAE----EAQEKKEEAKKKEREEKLAKLSpeEQRKYEEKERKKEQRK 323
|
|
| RhoGAP-FF1 |
pfam16512 |
p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating ... |
875-933 |
5.34e-04 |
|
p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating proteins (GAPs). These are the key proteins that make the switch between the active guanosine-triphosphate-bound form of Rho guanosine triphosphatases (GTPases) and the inactive guanosine-diphosphate-bound form. Rho guanosine triphosphatases (GTPases) are a family of proteins with key roles in the regulation of actin cytoskeleton dynamics. The RhoGAP-FF1 region contains the FF domain that has been implicated in binding to the transcription factor TFII-I; and phosphorylation of Tyr308 within the first FF domain inhibits this interaction. The RhoGAPFF1 domain constitutes the first solved structure of an FF domain that lacks the first of the two highly conserved Phe residues, but the substitution of Phe by Tyr does not affect the domain fold.
Pssm-ID: 465153 Cd Length: 80 Bit Score: 39.49 E-value: 5.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 875 RKEAVSS----YQALLVEIIKDPKASWTESKPRLEKdpqgravNPD-------LGKGDAEKLFRDHVKDL 933
Cdd:pfam16512 6 RKELLDSatdaFERLIRSQVTDYRALWKTVSKKLSQ-------HPEyqeyvelFGTDKAKRLFRKHIKKL 68
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
2-175 |
5.87e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.93 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPAtAASDATNPEAAEV---PSAAPASESE--------GPFDSGVVA---AATTPAVV-------DSAVEGDAPAAPAP 60
Cdd:PRK14951 302 AVPQ-AAAAATDPEAAEVarlAALMPADETQllysiclhGRAELGLAPdeyAALTMVLLrllafkpAAAAEAAAPAEKKT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 61 TSGSGPAAPSMPANPASPATPGPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPPGTNHAVQVSRF 140
Cdd:PRK14951 381 PARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETV 460
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002302520 141 VPPSSLQP-PAPMNLARPSSAFPGAGAMPPNPPGSI 175
Cdd:PRK14951 461 AIPVRVAPePAVASAAPAPAAAPAAARLTPTEEGDV 496
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1-166 |
6.64e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.90 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 1 MATPATAASDATNPEAAEVPSAAP-ASESEGPFDSGVVAAATTPAvvdSAVEGDAPAAPAPTSGSGPAAPSMPANP--AS 77
Cdd:PHA03378 694 MQPPPRAPTPMRPPAAPPGRAQRPaAATGRARPPAAAPGRARPPA---AAPGRARPPAAAPGRARPPAAAPGRARPpaAA 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 78 PATPGPPRPQFAGSPAYASPPAPafsynvlPRPSPRPQVGSGAAQQQLASPPGTNH-AVQVSRFVPPSSLQPpapmnlAR 156
Cdd:PHA03378 771 PGAPTPQPPPQAPPAPQQRPRGA-------PTPQPPPQAGPTSMQLMPRAAPGQQGpTKQILRQLLTGGVKR------GR 837
|
170
....*....|
gi 1002302520 157 PSSAFPGAGA 166
Cdd:PHA03378 838 PSLKKPAALE 847
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
2-90 |
7.01e-04 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 43.73 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASESEGPfdsgvvAAATTPAvvdsavegDAPAAPAPTSGSGPAAPSMPANPASPATP 81
Cdd:PRK12270 40 STAAPTAAAAAAAAAASAPAAAPAAKAPAA------PAPAPPA--------AAAPAAPPKPAAAAAAAAAPAAPPAAAAA 105
|
....*....
gi 1002302520 82 GPPRPQFAG 90
Cdd:PRK12270 106 AAPAAAAVE 114
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
804-892 |
8.04e-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: 214922 [Multi-domain] Cd Length: 140 Bit Score: 40.64 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 804 SDARYKAMKHEEREvaFNEYIAELKSAEKEAE------QAAKAKLDEQAKlKEREREMRKRKE---REEQEMERvKLKIR 874
Cdd:smart00935 13 SPAGKAAQKQLEKE--FKKRQAELEKLEKELQklkeklQKDAATLSEAAR-EKKEKELQKKVQefqRKQQKLQQ-DLQKR 88
|
90
....*....|....*...
gi 1002302520 875 RKEAVSSYQALLVEIIKD 892
Cdd:smart00935 89 QQEELQKILDKINKAIKE 106
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2-176 |
8.49e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAevPSAAPASESEGPFDSG--VVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPA 79
Cdd:PHA03307 280 SRPGPASSSSSPRERS--PSPSPSSPGSGPAPSSprASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 80 TPGPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPPGTNHAVQVSRFVPPSSLQPPAPMNLARPS- 158
Cdd:PHA03307 358 PPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSg 437
|
170
....*....|....*...
gi 1002302520 159 SAFPGAgamPPNPPGSIR 176
Cdd:PHA03307 438 EPWPGS---PPPPPGRVR 452
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
802-868 |
9.61e-04 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 42.55 E-value: 9.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002302520 802 FRSDARYKAMKheEREvafnEYIAELKSAEKEAEQAAKAKLDEQAKLKEREREM--------RKRKERE-EQEMER 868
Cdd:pfam07946 254 LRPEALKKAKK--TRE----EEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLaklspeeqRKYEEKErKKEQRK 323
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
699-878 |
9.78e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 699 EERKEKRAAQRAAVEAYKQLLEEASEDINSNKDYKEFKRkwgtdpRFEALDRKERDA--LFNEKVKSIEEKvqsvrnavi 776
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED------RIERLEERREDLeeLIAERRETIEEK--------- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 777 AEFKSMLRESKDITSTSrwTKVKENFRSDARYKAMKHEEREVAFNEYIAELKS---------------AEKEAE------ 835
Cdd:PRK02224 536 RERAEELRERAAELEAE--AEEKREAAAEAEEEAEEAREEVAELNSKLAELKErieslerirtllaaiADAEDEierlre 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002302520 836 -QAAKAKLDEQAK--LKE-RER--------------EMRKRKEREEQEMERVKLKIRRKEA 878
Cdd:PRK02224 614 kREALAELNDERRerLAEkRERkreleaefdearieEAREDKERAEEYLEQVEEKLDELRE 674
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
690-878 |
1.05e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 690 EQYVRTRADEERKEKRAAQR-AAVEAYKQLLEEASEDINS-NKDYKEFKRKWGTDPRFEALDRKERDALfNEKVKSIEEK 767
Cdd:COG1196 246 AELEELEAELEELEAELAELeAELEELRLELEELELELEEaQAEEYELLAELARLEQDIARLEERRREL-EERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 768 VQSVRNAVIAEFKSMLRESKDITSTSRWTKVKENFRSDARYKAMKHEEREVAFNEYIAELKSAEKEAEQAAKAKLDEQAK 847
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190
....*....|....*....|....*....|.
gi 1002302520 848 LKEREREMRKRKEREEQEMERVKLKIRRKEA 878
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEE 435
|
|
| COG5373 |
COG5373 |
Uncharacterized membrane protein [Function unknown]; |
15-86 |
1.33e-03 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 444140 [Multi-domain] Cd Length: 854 Bit Score: 42.68 E-value: 1.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002302520 15 EAAEVPSAAPASESEGPFdSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATPGPPRP 86
Cdd:COG5373 36 ELAEAAEAASAPAEPEPE-AAAAATAAAPEAAPAPVPEAPAAPPAAAEAPAPAAAAPPAEAEPAAAPAAASS 106
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
696-935 |
1.35e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 696 RADEERKEKRAAQRAAVEAYKQLLEEASEDINSNKDYKEFKRKWGTDPRFEALDRKERDALFNEKVKSIEE--------K 767
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERirqeerkrE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 768 VQSVRNAVIAEFKSMLRESK--DITSTSRWTKVKENFRSDARYKAMKhEEREVAFNEYIAELKSAEKEAEQAakakldeq 845
Cdd:pfam17380 362 LERIRQEEIAMEISRMRELErlQMERQQKNERVRQELEAARKVKILE-EERQRKIQQQKVEMEQIRAEQEEA-------- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 846 aklkeREREMRKRKEREEQEMERVklkiRRKEAVSSYQallVEIIKDPKASWTESKPRLEKDPQGRAVNPDLGKGDAEKL 925
Cdd:pfam17380 433 -----RQREVRRLEEERAREMERV----RLEEQERQQQ---VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKE 500
|
250
....*....|
gi 1002302520 926 FRDHVKDLYE 935
Cdd:pfam17380 501 LEERKQAMIE 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
675-892 |
1.35e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 675 RFKAIpshSRRRSTFEQYVRTRADEERKEKRAAQRAAVEAYKQLLEEASEDInsnkdykefkrkwgtdprfeALDRKERD 754
Cdd:COG1196 214 RYREL---KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL--------------------AELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 755 ALfNEKVKSIEEKVQSVRNAVIAEFKSMLRESKDITST----SRWTKVKENFRSDARYKAMKHEEREVAFNEYIAELKSA 830
Cdd:COG1196 271 EL-RLELEELELELEEAQAEEYELLAELARLEQDIARLeerrRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002302520 831 EKEAEQAAKAKLDEQAKLKEREREMRKRKEREEQEMERVKLKIRRKEAVSSYQALLVEIIKD 892
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
684-877 |
1.37e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 42.33 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 684 RRRSTFEQyvRTRADEERK------EKRAAQRAAVEAYKQ-LLEEASEDINSNKDYKEFKRKwgtdpRFEALDRKERDal 756
Cdd:pfam15558 71 KARLGREE--RRRADRREKqviekeSRWREQAEDQENQRQeKLERARQEAEQRKQCQEQRLK-----EKEEELQALRE-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 757 fnekvksiEEKVQSVRNAVIAEFKSMLRES---KDITSTSRWTKVKEnfrsDARYKAMKHEERevafneyiAELKSAEKE 833
Cdd:pfam15558 142 --------QNSLQLQERLEEACHKRQLKEReeqKKVQENNLSELLNH----QARKVLVDCQAK--------AEELLRRLS 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1002302520 834 AEQAA-KAKLDEQAKLKEREREMRKRKEREEQEMERVKLKIRRKE 877
Cdd:pfam15558 202 LEQSLqRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKE 246
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
5-127 |
1.44e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 42.26 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 5 ATAASDATNPEAAEVPSAAPASESEGPfdsGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAA--PSMPANPASPATPG 82
Cdd:PRK06995 50 ALAPPAAAAPAAAQPPPAAAPAAVSRP---AAPAAEPAPWLVEHAKRLTAQREQLVARAAAPAApeAQAPAAPAERAAAE 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1002302520 83 PPRPQFAGSPAYasppapafsynvLPRPSPRPQVGSGAAQQQLAS 127
Cdd:PRK06995 127 NAARRLARAAAA------------APRPRVPADAAAAVADAVKAR 159
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
699-944 |
1.48e-03 |
|
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: 42.75 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 699 EERKEKRAAQRAAVEAYKQLLEEASEDINSNKDykefkrkwgtdpRFEALDRKERDALFNEKVK---SIEEKVQSVRnAV 775
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEE------------ALNDLEARLSHSRIPEIQAelsKLEEEVSRIE-AR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 776 IAEFKSMLRES---KDITSTSRWTKVKENFRSDARYKAMKHEEREVafNEYIAELKSAEKEAeQAAKAKLDEQ-----AK 847
Cdd:TIGR02169 814 LREIEQKLNRLtleKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL--NGKKEELEEELEEL-EAALRDLESRlgdlkKE 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 848 LKEREREMRKRKEREEQemerVKLKIRRKEAVSSYQALLVEIIKDPKASWTESKPRLEKDPqgrAVNPDLGKgdaeklfr 927
Cdd:TIGR02169 891 RDELEAQLRELERKIEE----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP---EEELSLED-------- 955
|
250
....*....|....*..
gi 1002302520 928 dhVKDLYERCVRDFRAL 944
Cdd:TIGR02169 956 --VQAELQRVEEEIRAL 970
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
58-186 |
1.55e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 42.39 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 58 PAPTSGSGPAAPSMPANPASPATPGP-PRPQFAGSPAYASPPAPAFSynvLPRPSPRPQVGSGAAQQQLASPPGTNHAVQ 136
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAaPVAQAAAAPAPAAAPAAAAS---APAAPPAAAPPAPVAAPAAAAPAAAPAAAP 442
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1002302520 137 VSRFVPPSSLQPPAPMNLARPSSAFPGAGAMPPNPPgSIRLPFPGPPRPS 186
Cdd:PRK14951 443 AAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPA-PAAAPAAARLTPT 491
|
|
| PHA02030 |
PHA02030 |
hypothetical protein |
4-82 |
1.72e-03 |
|
hypothetical protein
Pssm-ID: 222843 [Multi-domain] Cd Length: 336 Bit Score: 41.89 E-value: 1.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002302520 4 PATAASDATNPEAAEVPSAAPAsesegpfdsgvvAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATPG 82
Cdd:PHA02030 269 VPNVAADAGSAAAPAVPAAAAA------------VAQAAPSVPQVPNVAVLPDVPQVAPVAAPAAPEVPAVPVVPAAPQ 335
|
|
| DUF1720 |
pfam08226 |
Domain of unknown function (DUF1720); This domain is found in different combinations with ... |
292-352 |
1.90e-03 |
|
Domain of unknown function (DUF1720); This domain is found in different combinations with cortical patch components EF hand, SH3 and ENTH and is therefore likely to be involved in cytoskeletal processes. This family contains many hypothetical proteins.
Pssm-ID: 369766 [Multi-domain] Cd Length: 75 Bit Score: 37.81 E-value: 1.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002302520 292 TPSASPFPQTSQSPTAFQQPGQQQLYPSYPSAHGVQPQP-----LWGYPPQPTGFQ---QPPFQSYPSG 352
Cdd:pfam08226 6 TGYMPPQQQQPQQTQQPLQPQPTGFMPQQQTGQGLQPQPtgmgqFQPLQPQQTGFQpqaQQGLQPQATG 74
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
814-883 |
2.35e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 39.09 E-value: 2.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002302520 814 EEREVAFNEYI----AELKSAEKEAEQAAKAKldeqaklKEREREMRKRKereeQEMERVKLKIRR-KEAVSSYQ 883
Cdd:pfam13863 44 KEDLIKFDKFLkendAKRRRALKKAEEETKLK-------KEKEKEIKKLT----AQIEELKSEISKlEEKLEEYK 107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
686-878 |
2.38e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 686 RSTFEQYVRTRADE-ERKEKRAAQRAAVEaykqlLEEASEDINSNKDYKEfkrkwgtdpRFEALdRKERDALfNEKVKSI 764
Cdd:COG4717 44 RAMLLERLEKEADElFKPQGRKPELNLKE-----LKELEEELKEAEEKEE---------EYAEL-QEELEEL-EEELEEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 765 EEKVQSVRNaviaEFKSMLRESKDITSTSRWTKVKENFRS-DARYKAMKHEEREVAfnEYIAELKSAEKEAEQAAK---- 839
Cdd:COG4717 108 EAELEELRE----ELEKLEKLLQLLPLYQELEALEAELAElPERLEELEERLEELR--ELEEELEELEAELAELQEelee 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002302520 840 -------AKLDEQAKLKEREREMRKRKEREEQEMERVKLKIRRKEA 878
Cdd:COG4717 182 lleqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
797-877 |
2.46e-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: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 797 KVKENFRSDARyKAMKHEErevAFNEYiaeLKSAEKEAE----------QAAKAKLDEQAKLKEREREMRKRKEREEQEM 866
Cdd:cd16269 153 KLVEKYRQVPR-KGVKAEE---VLQEF---LQSKEAEAEailqadqaltEKEKEIEAERAKAEAAEQERKLLEEQQRELE 225
|
90
....*....|.
gi 1002302520 867 ERVKLKIRRKE 877
Cdd:cd16269 226 QKLEDQERSYE 236
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
2-80 |
2.99e-03 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 41.17 E-value: 2.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASESEGPFDSGVVaAATTPAVVDSAVEGDAPAAPAPTSGSgpAAPSMPANPASPAT 80
Cdd:PRK10856 174 TTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAV-VAPSQANVDTAATPAPAAPATPDGAA--PLPTDQAGVSTPAA 249
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
808-892 |
3.17e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.43 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 808 YKAMKhEEREVAFNEYIAELKSAEKEAeQAAKAKLDEQAKL------KEREREMRKRKE--REEQEMERVKLKIRRKEAV 879
Cdd:COG2825 41 GKAAQ-KKLEKEFKKRQAELQKLEKEL-QALQEKLQKEAATlseeerQKKERELQKKQQelQRKQQEAQQDLQKRQQELL 118
|
90
....*....|...
gi 1002302520 880 SSYQALLVEIIKD 892
Cdd:COG2825 119 QPILEKIQKAIKE 131
|
|
| DUF1720 |
pfam08226 |
Domain of unknown function (DUF1720); This domain is found in different combinations with ... |
299-361 |
3.32e-03 |
|
Domain of unknown function (DUF1720); This domain is found in different combinations with cortical patch components EF hand, SH3 and ENTH and is therefore likely to be involved in cytoskeletal processes. This family contains many hypothetical proteins.
Pssm-ID: 369766 [Multi-domain] Cd Length: 75 Bit Score: 37.43 E-value: 3.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002302520 299 PQTSQSPTAFQQPGQQQLYPSYPSAHGVQPQPLWGYP--PQPTGF-QQPPFQSYPSGLLGPLGRPM 361
Cdd:pfam08226 3 PQQTGYMPPQQQQPQQTQQPLQPQPTGFMPQQQTGQGlqPQPTGMgQFQPLQPQQTGFQPQAQQGL 68
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
699-895 |
3.41e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 699 EERKEKRAAQRAAVEAYKQLLEEASEDINSNKDYKEfkrkwgtdprfEALDRKERD-ALFNEKVKSIEEKVQSVRNA-VI 776
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE-----------EELKELEEQlESLQEELAALEQELQALSEAeAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 777 AEFKSMLRESKDITSTSRWTK---VKENFRSDARYKAMKHEEREVAFNEYIAELKSAEKEAEQAAKAKLDEQAKLKERER 853
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAeaeKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002302520 854 EMRKRKEREEQEMERVKLKIRRKEAVSSYQALLVEIIKDPKA 895
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
709-759 |
3.56e-03 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 36.40 E-value: 3.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1002302520 709 RAAVEAYKQLLEEASEDInSNKDYKEFKRKWGTDPRFEAL-DRKERDALFNE 759
Cdd:smart00441 1 EEAKEAFKELLKEHEVIT-PDTTWSEARKKLKNDPRYKALlSESEREQLFED 51
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
476-503 |
3.80e-03 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 36.04 E-value: 3.80e-03
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
641-853 |
3.84e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 641 EEECTRQFKEMLKERGVLPfskwekelpkIVFDPRFKAIpsHSRRRSTFEQYVRTRADEERKEKRAAQRAAVEaykQLLE 720
Cdd:COG4717 48 LERLEKEADELFKPQGRKP----------ELNLKELKEL--EEELKEAEEKEEEYAELQEELEELEEELEELE---AELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 721 EASEDInsnKDYKEFKRKWGTDPRFEALdrKERDALFNEKVKSIEEKVQSVRNAV---------IAEFKSMLRESKDITS 791
Cdd:COG4717 113 ELREEL---EKLEKLLQLLPLYQELEAL--EAELAELPERLEELEERLEELRELEeeleeleaeLAELQEELEELLEQLS 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002302520 792 TSRWTKVKENFRS-DARYKAMKHEEREVAFNEYIAELKSAEKEAEQAAKAKLDEQAKLKERER 853
Cdd:COG4717 188 LATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| SOBP |
pfam15279 |
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ... |
39-287 |
3.97e-03 |
|
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.
Pssm-ID: 464609 [Multi-domain] Cd Length: 325 Bit Score: 40.57 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 39 AATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATPGPPRPqfagSPAYASPPAPAFSYNVLPRPSPRPQVGS 118
Cdd:pfam15279 86 ASTRSESVSPGPSSSASPSSSPTSSNSSKPLISVASSSKLLAPKPHEP----PSLPPPPLPPKKGRRHRPGLHPPLGRPP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 119 GAA------QQQLASPPGTNHAVQVSRFVPPSSLQPPAPMnlARPSSAFPGAGAMPPNPPGSirLPFPGPPRPsintfva 192
Cdd:pfam15279 162 GSPpmsmtpRGLLGKPQQHPPPSPLPAFMEPSSMPPPFLR--PPPSIPQPNSPLSNPMLPGI--GPPPKPPRN------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 193 spqqaqpqasQLPSNSGSSDVSTSRSDTRSVPEASPQTMQLSTGPPSTSTA--GSPSITVQMPTNPslptrPEVFGAIGA 270
Cdd:pfam15279 231 ----------LGPPSNPMHRPPFSPHHPPPPPTPPGPPPGLPPPPPRGFTPpfGPPFPPVNMMPNP-----PEMNFGLPS 295
|
250
....*....|....*..
gi 1002302520 271 SVPGQPstilsaPPSLL 287
Cdd:pfam15279 296 LAPLVP------PVTVL 306
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
699-877 |
4.61e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 699 EERKEKRAAQRAAVEAYKQLLEEASEDInsnkdykefkRKWgtdprfealdRKERDALfNEKVKSIEEKVQSvrnaviae 778
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEEL----------KEL----------AEKRDEL-NAQVKELREEAQE-------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 779 fksmLRESKDitstsrwtkvkenfrsdarykamkheerevAFNEYIAELKSAEKEAEQAAKAKLDEQAKLKErEREMRKR 858
Cdd:COG1340 62 ----LREKRD------------------------------ELNEKVKELKEERDELNEKLNELREELDELRK-ELAELNK 106
|
170
....*....|....*....
gi 1002302520 859 KEREEQEMERvklKIRRKE 877
Cdd:COG1340 107 AGGSIDKLRK---EIERLE 122
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
4-239 |
4.64e-03 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 41.17 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 4 PATAASDATNPEAAEVPSAAPAS----ESEGPFDSGVVAAATTPAV----VDSAVEGDAPAAPAPTSgSGPAAPSMPANP 75
Cdd:pfam09770 108 AARAAQSSAQPPASSLPQYQYASqqsqQPSKPVRTGYEKYKEPEPIpdlqVDASLWGVAPKKAAAPA-PAPQPAAQPASL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 76 ASP---------------ATPGPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASPPGTNHAVQVSRF 140
Cdd:pfam09770 187 PAPsrkmmsleeveaamrAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTIL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 141 VPPSSLQPPAPMNLARPSsAFPGAGAMPPNPPGSIRLpFPGPPRPSintfvaspqqaqPQASQLPSNSGSSDVSTSRSDT 220
Cdd:pfam09770 267 QRPQSPQPDPAQPSIQPQ-AQQFHQQPPPVPVQPTQI-LQNPNRLS------------AARVGYPQNPQPGVQPAPAHQA 332
|
250
....*....|....*....
gi 1002302520 221 RSVPEASPQTMQLSTGPPS 239
Cdd:pfam09770 333 HRQQGSFGRQAPIITHPQQ 351
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
808-892 |
4.72e-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: 38.33 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 808 YKAMKhEEREVAFNEYIAELKSAEKEAeQAAKAKLDEQAKL-----KEREREMRKRKER--EEQEMERVKLKIRRKEAVS 880
Cdd:pfam03938 17 GKAAQ-AQLEKKFKKRQAELEAKQKEL-QKLYEELQKDGALleeerEEKEQELQKKEQElqQLQQKAQQELQKKQQELLQ 94
|
90
....*....|..
gi 1002302520 881 SYQALLVEIIKD 892
Cdd:pfam03938 95 PIQDKINKAIKE 106
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
56-286 |
5.04e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 40.51 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 56 AAPAPTSGSGPAAPSMPANPASPATPGPPRPQFAGSPAYASPPAPAFSYNVLprpSPRPQVGSGAAQQQLASPPGTNHav 135
Cdd:COG3469 1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVA---ASGSAGSGTGTTAASSTAATSST-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 136 qvsrfvpPSSLQPPAPMNLARPSSAFPGAGAMPPNPPgsirlpfPGPPRPSINTFVASPQQAQPQASQLPSNSGSSDVST 215
Cdd:COG3469 76 -------TSTTATATAAAAAATSTSATLVATSTASGA-------NTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASAT 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002302520 216 SRSDTRSVPEASPQTMQLSTGPPSTSTAGSPSITVQMPTNPSLPTRPEVFGAIGASVPGQPSTILSAPPSL 286
Cdd:COG3469 142 SSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGL 212
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
256-377 |
5.08e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 40.84 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 256 PSLPTRPEVFGAIGASVPGQPSTILSAPPSLLGRPMTPSA-SPFPQTSQSPTAFQQPGQQQLYPSYPSAHGVQPQPLWGY 334
Cdd:PRK10263 747 PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVApQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP 826
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1002302520 335 PPQPTGFQQPPFQSYPSGLLGPL------GRPMVGSSSVTAYLPSIQPP 377
Cdd:PRK10263 827 QPQYQQPQQPVAPQPQDTLLHPLlmrngdSRPLHKPTTPLPSLDLLTPP 875
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
233-339 |
5.20e-03 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 40.75 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 233 LSTGPPSTSTAGSPSITVQMPTNPSLPTRPEvfgaigaSVPGQPSTILSAPPSllgrPMTPSASPFpqtsqSPTAFQQPG 312
Cdd:PHA03369 351 ASLTAPSRVLAAAAKVAVIAAPQTHTGPADR-------QRPQRPDGIPYSVPA----RSPMTAYPP-----VPQFCGDPG 414
|
90 100
....*....|....*....|....*..
gi 1002302520 313 QQQLYPSYPSAHGVQPQPLWGYPPQPT 339
Cdd:PHA03369 415 LVSPYNPQSPGTSYGPEPVGPVPPQPT 441
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
108-379 |
5.32e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 40.81 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 108 PRPSPRPQV------GSGAAQQQLASPPGTNHA----VQVSRFVPPSSLQ--PPAPMNLARPSSAFPGagamPPNPPGSI 175
Cdd:PHA03379 419 PVEKPRPEVpqsletATSHGSAQVPEPPPVHDLepgpLHDQHSMAPCPVAqlPPGPLQDLEPGDQLPG----VVQDGRPA 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 176 RLPFPGPPRPSINTFVASPQQAQPQASQLPSN---SGSSDVSTSRSDTRSVPEASPQTMQLSTGPPSTS----------- 241
Cdd:PHA03379 495 CAPVPAPAGPIVRPWEASLSQVPGVAFAPVMPqpmPVEPVPVPTVALERPVCPAPPLIAMQGPGETSGIvrvrerwrpap 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 242 -TAGSPSITVQMPTNPSLPT-RPEVFgAIGASVPGQPSTILSAPPSL-LGRPMTPSASPFPQT--SQSPTAFQQPGQQQL 316
Cdd:PHA03379 575 wTPNPPRSPSQMSVRDRLARlRAEAQ-PYQASVEVQPPQLTQVSPQQpMEYPLEPEQQMFPGSpfSQVADVMRAGGVPAM 653
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002302520 317 YPSYPSAHGVQPQPLwGYPPQP----TGFQQPPFQSYPSGLLGPLGRPMVGSSSVTAYLPS--IQPPGV 379
Cdd:PHA03379 654 QPQYFDLPLQQPISQ-GAPLAPlrasMGPVPPVPATQPQYFDIPLTEPINQGASAAHFLPQqpMEGPLV 721
|
|
| PABP-1234 |
TIGR01628 |
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
290-402 |
5.39e-03 |
|
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.
Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 40.56 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 290 PMTPSASPFPqTSQSPTAFQQPGQQQLYPSYPSAHGVQPQPLW----GYPPQPTGFQQPPFQSYPSG----LLGPLGRPM 361
Cdd:TIGR01628 383 RQLPMGSPMG-GAMGQPPYYGQGPQQQFNGQPLGWPRMSMMPTpmgpGGPLRPNGLAPMNAVRAPSRnaqnAAQKPPMQP 461
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1002302520 362 VGSSSVTAYLPSIQP---PGVSTTDRDSKELSSANPGSEQPTQQ 402
Cdd:TIGR01628 462 VMYPPNYQSLPLSQDlpqPQSTASQGGQNKKLAQVLASATPQMQ 505
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
698-906 |
5.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 698 DEERKEKRAAQRAAVEAYkqllEEASEdiNSNKDYKEFKRkwgtdprfealdRKERDALFNEKVKSIEEKVQSVRnaviA 777
Cdd:PRK03918 143 SDESREKVVRQILGLDDY----ENAYK--NLGEVIKEIKR------------RIERLEKFIKRTENIEELIKEKE----K 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 778 EFKSMLRESKDITSTSRWTKVK-ENFRSdaRYKAMkhEEREVAFNEYIAELKSAEKEaeqaaKAKLDEqaKLKERErEMR 856
Cdd:PRK03918 201 ELEEVLREINEISSELPELREElEKLEK--EVKEL--EELKEEIEELEKELESLEGS-----KRKLEE--KIRELE-ERI 268
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002302520 857 KRKEREEQEMERvklKIRRKEAVSSYqALLVEIIKDPKASWTESKPRLEK 906
Cdd:PRK03918 269 EELKKEIEELEE---KVKELKELKEK-AEEYIKLSEFYEEYLDELREIEK 314
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
810-892 |
5.52e-03 |
|
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: 40.73 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 810 AMKHEEREVAFNEYIAELKSAEKEAEQAAK------AKLDEQAKLKEREREMRKRKEREEQEMERVKLK-----IRRKEA 878
Cdd:pfam02463 148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKlieeteNLAELIIDLEELKLQELKLKEQAKKALEYYQLKeklelEEEYLL 227
|
90
....*....|....
gi 1002302520 879 VSSYQALLVEIIKD 892
Cdd:pfam02463 228 YLDYLKLNEERIDL 241
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
2-80 |
5.77e-03 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 40.64 E-value: 5.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPAT 80
Cdd:PRK12270 38 PGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDE 116
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-59 |
6.46e-03 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 40.24 E-value: 6.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002302520 2 ATPATAASdatnPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDA---PAAPA 59
Cdd:TIGR01348 194 STPATAPA----PASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAkvdHAAPA 250
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
699-878 |
7.35e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 699 EERKEKRAAQRAAVEAYKQLLEEASEDINSNKDYKEFKRK-----WgtdpRFE--ALDRKERDALFnEKVKSIEEKVQSV 771
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEierleW----RQQteVLSPEEEKELV-EKIKELEKELEKA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 772 RNAV-----IAEFKSMLRESKDITSTSRwTKVKENF-RSDARYKAM-----KHEE-REVAfNEYIAELKSAEKEAEQ--- 836
Cdd:COG1340 153 KKALeknekLKELRAELKELRKEAEEIH-KKIKELAeEAQELHEEMielykEADElRKEA-DELHKEIVEAQEKADElhe 230
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002302520 837 AAKAKLDEQAKLKEREREMRKRKEREEQEMERVKLKIRRKEA 878
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
20-186 |
7.73e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 40.19 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 20 PSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSG-PAAPSMPANPASPATPGPPRPQFAgSPAYASPP 98
Cdd:PRK14086 124 PRADDRPPGLPRQDQLPTARPAYPAYQQRPEPGAWPRAADDYGWQQqRLGFPPRAPYASPASYAPEQERDR-EPYDAGRP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 99 APAFSYNVLPRPSPRPQVGSGAAQQQLASPPGTNHAVqvsRFVPPSSLQPPAPMNLARPSSafpgagampPNPPGSIRLP 178
Cdd:PRK14086 203 EYDQRRRDYDHPRPDWDRPRRDRTDRPEPPPGAGHVH---RGGPGPPERDDAPVVPIRPSA---------PGPLAAQPAP 270
|
....*...
gi 1002302520 179 FPGPPRPS 186
Cdd:PRK14086 271 APGPGEPT 278
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
818-907 |
7.91e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 37.62 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 818 VAFNEYIAELKSAEKEAE---QAAKAKLDEQAKLKER-----EREMRK-----------RKEREEQEMERVKLKIRRKEA 878
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEaqlQKLQEDLEKQAEIAREaqqnyERELVLhaedikalqalREELNELKAEIAELKAEAESA 83
|
90 100
....*....|....*....|....*....
gi 1002302520 879 VSSYQALlveiikdpKASWTESKPRLEKD 907
Cdd:pfam07926 84 KAELEES--------EESWEEQKKELEKE 104
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
800-894 |
8.28e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 38.77 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 800 ENFRSDARYKAmkHEEREVAFNEYIAELKSAEKEAEQAAKAKLDEQAKLKEREREMRKRKEREEQEME--RVKLKIRRK- 876
Cdd:COG1390 5 EKIIEEILEEA--EAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEarKELLEAKEEl 82
|
90 100
....*....|....*....|
gi 1002302520 877 --EAVSSYQALLVEIIKDPK 894
Cdd:COG1390 83 ieEVFEEALEKLKNLPKDPE 102
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
44-185 |
8.42e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 40.19 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 44 AVVDSAVEGDAPAAPAPTSGSGPAAPSMPANP-----ASPATPGPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGS 118
Cdd:PRK14086 86 ITVDPSAGEPAPPPPHARRTSEPELPRPGRRPyegygGPRADDRPPGLPRQDQLPTARPAYPAYQQRPEPGAWPRAADDY 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 119 GAAQQQLASPPGTNHAV------QVSRFVPPSSLQPPApMNLARPSSAFPGAGAMPPN---------PPGSIRLPFPGPP 183
Cdd:PRK14086 166 GWQQQRLGFPPRAPYASpasyapEQERDREPYDAGRPE-YDQRRRDYDHPRPDWDRPRrdrtdrpepPPGAGHVHRGGPG 244
|
..
gi 1002302520 184 RP 185
Cdd:PRK14086 245 PP 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
679-906 |
8.74e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 679 IPSHSRRR---STFEQYVR-TRAD-EERKEKRAAQRAAVEAYKQLLEEASEDINSNKDYKEFkrkwgTDPRFEALDrKER 753
Cdd:PRK02224 243 LEEHEERReelETLEAEIEdLRETiAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL-----DDADAEAVE-ARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 754 DALFNEKVkSIEEKVQSVRnaviaefksmlreskdiTSTSRWTKVKENFRSDARykamKHEEREVAFNEYIAELKSAEKE 833
Cdd:PRK02224 317 EELEDRDE-ELRDRLEECR-----------------VAAQAHNEEAESLREDAD----DLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002302520 834 AEQAAKAKLDEQAKLKEREREMRKRKEREEQEMERVKlkiRRKEAVSSYQALLVEIIKDPKASWTESKPRLEK 906
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE---DFLEELREERDELREREAELEATLRTARERVEE 444
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
16-86 |
9.11e-03 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 40.26 E-value: 9.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002302520 16 AAEVPSAAPASESEGpfdsgvvAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATPGPPRP 86
Cdd:PRK12270 34 ADYGPGSTAAPTAAA-------AAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPA 97
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
2-184 |
9.25e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 39.74 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 2 ATPATAASDATNPEAAEVPSAAPASESEGPFDSGVVAAATTPAVVDSAVEGDAPAAPAPTSGSGPAAPSMPANPASPATP 81
Cdd:COG3469 29 AASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATSTASGANTG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302520 82 GPPRPQFAGSPAYASPPAPAFSYNVLPRPSPRPQVGSGAAQQQLASP--PGTNHAVQVSRFVPPSSLQP-PAPMNLARPS 158
Cdd:COG3469 109 TSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGteTATGGTTTTSTTTTTTSASTtPSATTTATAT 188
|
170 180
....*....|....*....|....*.
gi 1002302520 159 SAFPGAGAMPPNPPGSIRLPFPGPPR 184
Cdd:COG3469 189 TASGATTPSATTTATTTGPPTPGLPK 214
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
939-996 |
9.87e-03 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 35.13 E-value: 9.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002302520 939 RDFRALLSEvitPEIAARTTdegktainsWTEAKGLLRSDPRYNKLASK-DRESIWRRY 996
Cdd:pfam01846 4 EAFKELLKE---HKITPYST---------WSEIKKKIENDPRYKALLDGsEREELFEDY 50
|
|
| |
