|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
423-1020 |
3.78e-26 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 114.79 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 423 ASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQEL--KEKEKLDEkikepikeaseeplpmeteeedpkeep 500
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELlkGSEEDLDV--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 501 vkeikeepkeeemteeekaaqkakpvattpipgTPWCVVWTGDERVFFYNPTTRLSMWDRPDDligRADVDKIIQEpphK 580
Cdd:COG5104 56 ---------------------------------DPWKECRTADGKVYYYNSITRESRWKIPPE---RKKVEPIAEQ---K 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 581 KGLEDMKKLRHPAPTMLSIQKWQFSmsaiKEEQELMEEMNEDEPIKAKKRKrddnkdidsekeaameaeikaareraivP 660
Cdd:COG5104 97 HDERSMIGGNGNDMAITDHETSEPK----YLLGRLMSQYGITSTKDAVYRL----------------------------T 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 661 LEARMKQFKDMLLERGVSAFSTWEKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMM 738
Cdd:COG5104 145 KEEAEKEFITMLKENQVDSTWPIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKML 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 739 E-EAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWS 817
Cdd:COG5104 224 AgNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETFIIWL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 818 KVKDKVESDPRYKAvdSSSM----REDLFKQYIeKIAKNLdsekekelerqarieaslrerEREVQKARSEQTKEIDReR 893
Cdd:COG5104 304 LNHYVFDSVVRYLK--NKEMkpldRKDILFSFI-RYVRRL---------------------EKELLSAIEERKAAAAQ-N 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 894 EQHKREeaiqNFKALLSDMVRSSDVS----WSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDE 969
Cdd:COG5104 359 ARHHRD----EFRTLLRKLYSEGKIYyrmkWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYERE 434
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 87196334 970 TSaITLTSTW--KEVKKIIKEDPRciKFSSSDRKKQREFEE---YIRDKYITAKAD 1020
Cdd:COG5104 435 TR-TGQISPTdrRAVDEIFEAIAE--KKEEGEIKFDKVDKEdisLIVDGLIKQRNE 487
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
796-845 |
1.03e-13 |
|
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: 66.33 E-value: 1.03e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 87196334 796 KIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQY 845
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
957-1012 |
8.21e-10 |
|
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: 55.27 E-value: 8.21e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 87196334 957 KKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCiKFSSSDRKKQREFEEYIRD 1012
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
435-464 |
9.75e-09 |
|
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: 51.76 E-value: 9.75e-09
10 20 30
....*....|....*....|....*....|
gi 87196334 435 SEWTEYKTADGKTYYYNNRTLESTWEKPQE 464
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
137-162 |
5.78e-08 |
|
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: 49.43 E-value: 5.78e-08
10 20
....*....|....*....|....*.
gi 87196334 137 WVENKTPDGKVYYYNARTRESAWTKP 162
Cdd:pfam00397 5 WEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 |
6.09e-08 |
|
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: 49.52 E-value: 6.09e-08
10 20 30
....*....|....*....|....*....|...
gi 87196334 132 PTEEIWVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
611-1052 |
1.33e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 611 EEQELMEEMNEDEPIKAKKRKRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLErgvsafstwekelhki 690
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE---------------- 1409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 691 vfdpryllLNPKERKQVFDQYVKTRAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIE 766
Cdd:PTZ00121 1410 --------LKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 767 KMKDREAlfNEFVAAARKKEKEDSKTRGEKIKSDffELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYI 846
Cdd:PTZ00121 1482 AKKADEA--KKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 847 EKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAiqnfKALLSDMVRSSDVSWSDTRRt 926
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEK- 1632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 927 lRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAitltstwKEVKKIIKEDPRCIKFSSSDRKKQREF 1006
Cdd:PTZ00121 1633 -KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA-------EEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 87196334 1007 EEyIRDKYITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKI 1052
Cdd:PTZ00121 1705 EE-LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
137-164 |
1.65e-07 |
|
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: 48.29 E-value: 1.65e-07
10 20
....*....|....*....|....*...
gi 87196334 137 WVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
124-173 |
1.22e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 49.31 E-value: 1.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 87196334 124 APGAPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDgvKVIQQSEL 173
Cdd:COG5104 4 ALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
298-435 |
9.63e-05 |
|
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: 46.49 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 298 VSTPTTQDQTPSSAVSVATPTVSvSAPAPTatpvqtvPQPHPQTLPPAVPHSVPQPAAAIPAFPPVMVppfRVPlPGMPI 377
Cdd:pfam17823 296 AAPMGAQAQGPIIQVSTDQPVHN-TAGEPT-------PSPSNTTLEPNTPKSVASTNLAVVTTTKAQA---KEP-SASPV 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87196334 378 PLPGVAMMqivscPYVK-TVATTKTGVLP---GMAPPIVPMIHPQVAIAASPATL-AGATAVS 435
Cdd:pfam17823 364 PVLHTSMI-----PEVEaTSPTTQPSPLLptqGAAGPGILLAPEQVATEATAGTAsAGPTPRS 421
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1017-1076 |
1.62e-04 |
|
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: 40.13 E-value: 1.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 1017 AKADFRTLLKETKfITYRSkkliqesdqHLKDVEKILQNDKRYLVLDcVPEERRKLIVAY 1076
Cdd:pfam01846 2 AREAFKELLKEHK-ITPYS---------TWSEIKKKIENDPRYKALL-DGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1015-1079 |
1.85e-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: 40.25 E-value: 1.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 87196334 1015 ITAKADFRTLLKETKFITYrskkliqesDQHLKDVEKILQNDKRYLVLDcVPEERRKLIVAYVDD 1079
Cdd:smart00441 1 EEAKEAFKELLKEHEVITP---------DTTWSEARKKLKNDPRYKALL-SESEREQLFEDHIEE 55
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1055 |
7.48e-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: 40.44 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 846 IEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQT---KEIDREREQ-HKREEAIQNFKALLSD-MVRSSDVSW 920
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDlHKLEEALNDLEARLSHsRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 921 SDtrrtLRKDHRWESGSL--LEREEKEKLFNEHIEaltKKKREHFRQLLDEtsaitLTSTWKEVKKIIKEDPRCIKFSSS 998
Cdd:TIGR02169 801 SK----LEEEVSRIEARLreIEQKLNRLTLEKEYL---EKEIQELQEQRID-----LKEQIKSIEKEIENLNGKKEELEE 868
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 999 DRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKL---IQESDQHLKDVEKILQN 1055
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEA 928
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
423-1020 |
3.78e-26 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 114.79 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 423 ASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQEL--KEKEKLDEkikepikeaseeplpmeteeedpkeep 500
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELlkGSEEDLDV--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 501 vkeikeepkeeemteeekaaqkakpvattpipgTPWCVVWTGDERVFFYNPTTRLSMWDRPDDligRADVDKIIQEpphK 580
Cdd:COG5104 56 ---------------------------------DPWKECRTADGKVYYYNSITRESRWKIPPE---RKKVEPIAEQ---K 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 581 KGLEDMKKLRHPAPTMLSIQKWQFSmsaiKEEQELMEEMNEDEPIKAKKRKrddnkdidsekeaameaeikaareraivP 660
Cdd:COG5104 97 HDERSMIGGNGNDMAITDHETSEPK----YLLGRLMSQYGITSTKDAVYRL----------------------------T 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 661 LEARMKQFKDMLLERGVSAFSTWEKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMM 738
Cdd:COG5104 145 KEEAEKEFITMLKENQVDSTWPIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKML 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 739 E-EAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWS 817
Cdd:COG5104 224 AgNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETFIIWL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 818 KVKDKVESDPRYKAvdSSSM----REDLFKQYIeKIAKNLdsekekelerqarieaslrerEREVQKARSEQTKEIDReR 893
Cdd:COG5104 304 LNHYVFDSVVRYLK--NKEMkpldRKDILFSFI-RYVRRL---------------------EKELLSAIEERKAAAAQ-N 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 894 EQHKREeaiqNFKALLSDMVRSSDVS----WSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDE 969
Cdd:COG5104 359 ARHHRD----EFRTLLRKLYSEGKIYyrmkWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYERE 434
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 87196334 970 TSaITLTSTW--KEVKKIIKEDPRciKFSSSDRKKQREFEE---YIRDKYITAKAD 1020
Cdd:COG5104 435 TR-TGQISPTdrRAVDEIFEAIAE--KKEEGEIKFDKVDKEdisLIVDGLIKQRNE 487
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
796-845 |
1.03e-13 |
|
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: 66.33 E-value: 1.03e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 87196334 796 KIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQY 845
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
729-778 |
1.09e-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: 60.55 E-value: 1.09e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 87196334 729 QAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEF 778
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
664-711 |
7.19e-10 |
|
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: 55.54 E-value: 7.19e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 87196334 664 RMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYL-LLNPKERKQVFDQY 711
Cdd:pfam01846 2 AREAFKELLKEHKITPYSTWSEIKKKIENDPRYKaLLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
957-1012 |
8.21e-10 |
|
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: 55.27 E-value: 8.21e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 87196334 957 KKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCiKFSSSDRKKQREFEEYIRD 1012
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
795-848 |
1.78e-09 |
|
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: 54.50 E-value: 1.78e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 87196334 795 EKIKSDFFELLSNHHLD-SQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEK 848
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
900-951 |
2.49e-09 |
|
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: 54.00 E-value: 2.49e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 87196334 900 EAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWEsgSLLEREEKEKLFNEH 951
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYK--ALLDGSEREELFEDY 50
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
435-464 |
9.75e-09 |
|
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: 51.76 E-value: 9.75e-09
10 20 30
....*....|....*....|....*....|
gi 87196334 435 SEWTEYKTADGKTYYYNNRTLESTWEKPQE 464
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
435-462 |
3.41e-08 |
|
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: 50.20 E-value: 3.41e-08
10 20
....*....|....*....|....*...
gi 87196334 435 SEWTEYKTADGKTYYYNNRTLESTWEKP 462
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
137-162 |
5.78e-08 |
|
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: 49.43 E-value: 5.78e-08
10 20
....*....|....*....|....*.
gi 87196334 137 WVENKTPDGKVYYYNARTRESAWTKP 162
Cdd:pfam00397 5 WEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 |
6.09e-08 |
|
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: 49.52 E-value: 6.09e-08
10 20 30
....*....|....*....|....*....|...
gi 87196334 132 PTEEIWVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
437-464 |
6.59e-08 |
|
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: 49.52 E-value: 6.59e-08
10 20
....*....|....*....|....*...
gi 87196334 437 WTEYKTADGKTYYYNNRTLESTWEKPQE 464
Cdd:smart00456 6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
611-1052 |
1.33e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 611 EEQELMEEMNEDEPIKAKKRKRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLErgvsafstwekelhki 690
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE---------------- 1409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 691 vfdpryllLNPKERKQVFDQYVKTRAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIE 766
Cdd:PTZ00121 1410 --------LKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 767 KMKDREAlfNEFVAAARKKEKEDSKTRGEKIKSDffELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYI 846
Cdd:PTZ00121 1482 AKKADEA--KKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 847 EKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAiqnfKALLSDMVRSSDVSWSDTRRt 926
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEK- 1632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 927 lRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAitltstwKEVKKIIKEDPRCIKFSSSDRKKQREF 1006
Cdd:PTZ00121 1633 -KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA-------EEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 87196334 1007 EEyIRDKYITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKI 1052
Cdd:PTZ00121 1705 EE-LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
728-781 |
1.42e-07 |
|
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: 49.11 E-value: 1.42e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 87196334 728 MQAKEDFKKMMEEAKFN-PRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAA 781
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
137-164 |
1.65e-07 |
|
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: 48.29 E-value: 1.65e-07
10 20
....*....|....*....|....*...
gi 87196334 137 WVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
958-1009 |
2.51e-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: 48.22 E-value: 2.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 87196334 958 KKREHFRQLLDETSaITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQrEFEEY 1009
Cdd:pfam01846 1 KAREAFKELLKEHK-ITPYSTWSEIKKKIENDPRYKALLDGSEREE-LFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
899-954 |
2.66e-06 |
|
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: 45.64 E-value: 2.66e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 87196334 899 EEAIQNFKALLSDMVRS-SDVSWSDTRRTLRKDHRWESgsLLEREEKEKLFNEHIEA 954
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKA--LLSESEREQLFEDHIEE 55
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
662-713 |
7.03e-06 |
|
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: 44.10 E-value: 7.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 87196334 662 EARMKQFKDMLLERGVS-AFSTWEKELHKIVFDPRY-LLLNPKERKQVFDQYVK 713
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYkALLSESEREQLFEDHIE 54
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
535-563 |
1.08e-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: 42.97 E-value: 1.08e-05
10 20
....*....|....*....|....*....
gi 87196334 535 PWCVVWTGDERVFFYNPTTRLSMWDRPDD 563
Cdd:smart00456 5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
124-173 |
1.22e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 49.31 E-value: 1.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 87196334 124 APGAPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDgvKVIQQSEL 173
Cdd:COG5104 4 ALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
703-953 |
1.90e-05 |
|
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: 48.97 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 703 ERKQVfDQYVKTRAEEERREKKNKIMQAKEdfKKMMEEAKFNPRATFSEFAAKHAKDSRFkAIEKMKDREALFNEfvaaa 782
Cdd:pfam17380 286 ERQQQ-EKFEKMEQERLRQEKEEKAREVER--RRKLEEAEKARQAEMDRQAAIYAEQERM-AMERERELERIRQE----- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 783 rKKEKEDSKTRGEKIKSDFFEL--LSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMRE-DLFKQYIEKIaknldsEKEK 859
Cdd:pfam17380 357 -ERKRELERIRQEEIAMEISRMreLERLQMERQQKNERVRQELEAARKVKILEEERQRKiQQQKVEMEQI------RAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 860 ELERQARIEASLREREREVQKARSEQ---TKEIDREREQhkrEEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESG 936
Cdd:pfam17380 430 EEARQREVRRLEEERAREMERVRLEEqerQQQVERLRQQ---EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250
....*....|....*..
gi 87196334 937 SLLEREEKEKLFNEHIE 953
Cdd:pfam17380 507 AMIEEERKRKLLEKEME 523
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
534-563 |
1.91e-05 |
|
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: 42.52 E-value: 1.91e-05
10 20 30
....*....|....*....|....*....|
gi 87196334 534 TPWCVVWTGDERVFFYNPTTRLSMWDRPDD 563
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
439-1031 |
3.29e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 439 EYKTADGKTYYYNNRTLESTWEKPQELKEKEKLDEKIKEPIKEASEepLPMETEEEDPKEEPVKEIKEEPKEEEMTEEEK 518
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 519 AAQKAKPVATtpipgtpwcvvwTGDERVFFYNPTTRLSMWDRPDDLIGRADVDKIIQEPphKKGLEDMKKLRHPAptmls 598
Cdd:PTZ00121 1442 EAKKADEAKK------------KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKADEA----- 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 599 iQKWQFSMSAIKEEQELMEEMNEDEPIKAKKRKRDDNKDIDSEKEAAMEA----EIKAARERAIVPLEARMKQFKDMLLE 674
Cdd:PTZ00121 1503 -KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 675 RGVSAFSTWEKELhkivfdprylllnpKERKQVFDQYVKTRAEEERREKKNKImqAKEDFKKMMEEAKfnpratFSEFAA 754
Cdd:PTZ00121 1582 KAEEAKKAEEARI--------------EEVMKLYEEEKKMKAEEAKKAEEAKI--KAEELKKAEEEKK------KVEQLK 1639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 755 KHAKDSRFKAIEKMKDREAlfNEFVAAARKKEKEDSKTRGEKIKSDffellsnhhlDSQSRWSKVKDKVESDPRYKAvds 834
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEE--NKIKAAEEAKKAEEDKKKAEEAKKA----------EEDEKKAAEALKKEAEEAKKA--- 1704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 835 ssmrEDLFKQYIEKIAKNLDSEKEKElERQARIEASLREREREVQKARSEQTKEIDREREQH-------KREEAIQNFKA 907
Cdd:PTZ00121 1705 ----EELKKKEAEEKKKAEELKKAEE-ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHlkkeeekKAEEIRKEKEA 1779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 908 LLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFnehiealTKKKREHFRQLLDETsAITLTSTWKEVKKIIK 987
Cdd:PTZ00121 1780 VIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV-------INDSKEMEDSAIKEV-ADSKNMQLEEADAFEK 1851
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 87196334 988 EDPRCIKFSSSDRKKQREFEeyiRDKYItaKADFRTLLKETKFI 1031
Cdd:PTZ00121 1852 HKFNKNNENGEDGNKEADFN---KEKDL--KEDDEEEIEEADEI 1890
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
611-984 |
6.15e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 611 EEQELMEEM---NEDEPIKAKKRKRDDNKDidseKEAAMEAEIKAARERAIVPLEARMKQFKdmlleRGVSAFSTWEKEl 687
Cdd:PTZ00121 1209 EEERKAEEArkaEDAKKAEAVKKAEEAKKD----AEEAKKAEEERNNEEIRKFEEARMAHFA-----RRQAAIKAEEAR- 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 688 hkivfdpRYLLLNPKERKQVFDQYVKTRAEEERREKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAI 765
Cdd:PTZ00121 1279 -------KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 766 EKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRwskvKDKVESDPRYKAVDSSSMREDLfKQY 845
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE----EDKKKADELKKAAAAKKKADEA-KKK 1426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 846 IEKIAKNLDSEKEKELERQARieaSLREREREVQKARSEQTKEIDREREQHKREEAIQNFKAllSDMVRSSDVSWSDTRR 925
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKAD---EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADE 1501
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 87196334 926 TLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTwKEVKK 984
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA-EELKK 1559
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
137-172 |
8.25e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 46.61 E-value: 8.25e-05
10 20 30
....*....|....*....|....*....|....*.
gi 87196334 137 WVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSE 172
Cdd:COG5104 58 WKECRTADGKVYYYNSITRESRWKIPPERKKVEPIA 93
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
298-435 |
9.63e-05 |
|
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: 46.49 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 298 VSTPTTQDQTPSSAVSVATPTVSvSAPAPTatpvqtvPQPHPQTLPPAVPHSVPQPAAAIPAFPPVMVppfRVPlPGMPI 377
Cdd:pfam17823 296 AAPMGAQAQGPIIQVSTDQPVHN-TAGEPT-------PSPSNTTLEPNTPKSVASTNLAVVTTTKAQA---KEP-SASPV 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87196334 378 PLPGVAMMqivscPYVK-TVATTKTGVLP---GMAPPIVPMIHPQVAIAASPATL-AGATAVS 435
Cdd:pfam17823 364 PVLHTSMI-----PEVEaTSPTTQPSPLLptqGAAGPGILLAPEQVATEATAGTAsAGPTPRS 421
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
258-346 |
1.36e-04 |
|
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: 46.06 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 258 VGAPTPTTSSPAPAVSTSTPTSTPSSTTATTTtatsvAQTVSTPTTQDQTPSSAVSVATPTVSVSAPAPTaTPVQTVPQP 337
Cdd:pfam05109 513 VTTPTPNATSPTPAVTTPTPNATSPTLGKTSP-----TSAVTTPTPNATSPTPAVTTPTPNATIPTLGKT-SPTSAVTTP 586
|
....*....
gi 87196334 338 HPQTLPPAV 346
Cdd:pfam05109 587 TPNATSPTV 595
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1017-1076 |
1.62e-04 |
|
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: 40.13 E-value: 1.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 1017 AKADFRTLLKETKfITYRSkkliqesdqHLKDVEKILQNDKRYLVLDcVPEERRKLIVAY 1076
Cdd:pfam01846 2 AREAFKELLKEHK-ITPYS---------TWSEIKKKIENDPRYKALL-DGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1015-1079 |
1.85e-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: 40.25 E-value: 1.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 87196334 1015 ITAKADFRTLLKETKFITYrskkliqesDQHLKDVEKILQNDKRYLVLDcVPEERRKLIVAYVDD 1079
Cdd:smart00441 1 EEAKEAFKELLKEHEVITP---------DTTWSEARKKLKNDPRYKALL-SESEREQLFEDHIEE 55
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
534-561 |
2.03e-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: 2.03e-04
10 20
....*....|....*....|....*...
gi 87196334 534 TPWCVVWTGDERVFFYNPTTRLSMWDRP 561
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
699-1071 |
5.07e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 699 LNPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMMEEAKfnpratFSEFAAKHAKDSRfKAIEKMKDREALFNEf 778
Cdd:PTZ00121 1072 LKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEAR------KAEEAKKKAEDAR-KAEEARKAEDARKAE- 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 779 vaAARKKEkEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVE---SDPRYKAVDSSSMREDLFKQYIEKIAKNLDS 855
Cdd:PTZ00121 1144 --EARKAE-DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrkAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 856 EKEKELERQARIEaSLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsdtrrTLRK-DHRWE 934
Cdd:PTZ00121 1221 EDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD--------ELKKaEEKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 935 SGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDET--SAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRD 1012
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 87196334 1013 KYITAKADFRTLLK--ETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRK 1071
Cdd:PTZ00121 1372 KKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
718-1072 |
7.29e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 718 EERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRF-----KAIEKMKDREALFNEFVAAARKKEKEDSKT 792
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELreeleKLEKEVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 793 RGEKIKsdffelLSNhhldSQSRWSKVKDKVEsDPRYKAVDSSSMREDLfKQYIEkiaknLDSEKEKELERQARIE---A 869
Cdd:PRK03918 255 RKLEEK------IRE----LEERIEELKKEIE-ELEEKVKELKELKEKA-EEYIK-----LSEFYEEYLDELREIEkrlS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 870 SLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsDTRRTLRKDHRWESGslLEREEKEKLFN 949
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE----EAKAKKEELERLKKR--LTGLTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 950 EhIEALTKKKREHFRQLLdetsaiTLTSTWKEVKKIIKEDPRCIKFSSSDRKK----QREFEEYIRDKYITA-KADFRTL 1024
Cdd:PRK03918 392 E-LEELEKAKEEIEEEIS------KITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEyTAELKRI 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 87196334 1025 LKETKFITYRSKKLIQEsdqhLKDVEKILQNDKRYLVLDCVPEERRKL 1072
Cdd:PRK03918 465 EKELKEIEEKERKLRKE----LRELEKVLKKESELIKLKELAEQLKEL 508
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
260-345 |
1.36e-03 |
|
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: 42.64 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 260 APTPTTSSPAPAVSTSTPTSTPSSTTATTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVS-VSAPAPTATPVQTVPQPH 338
Cdd:pfam17823 165 ASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPAAGtALAAVGNSSPAAGTVTAA 244
|
....*..
gi 87196334 339 PQTLPPA 345
Cdd:pfam17823 245 VGTVTPA 251
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
700-1092 |
1.40e-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: 43.04 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 700 NPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDfkkmmeeakfnpratfsefaakhakdsrfKAIEKMKDREALFNEFV 779
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETEN-----------------------------LAELIIDLEELKLQELK 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 780 AAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKavDSSSMREDLFKQYIEKIAKNLDSEKEK 859
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE--IESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 860 ELERQARIEASLREREREVQKAR--SEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsdtRRTLRKDHRWESGS 937
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELlkLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE------LEKELKELEIKREA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 938 LLEREE----KEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIkedprcikfsSSDRKKQREFEEYIRDK 1013
Cdd:pfam02463 354 EEEEEEelekLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE----------AQLLLELARQLEDLLKE 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 87196334 1014 YITAKADFrtLLKETKFITYRSKKLIQESDqHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDRRGPPPPPTAS 1092
Cdd:pfam02463 424 EKKEELEI--LEEEEESIELKQGKLTEEKE-ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
715-997 |
2.30e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 715 RAEEERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSrfKAIEKMKDREALFNEFVAAARKKEKEDSKTRG 794
Cdd:COG5185 257 KLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYT--KSIDIKKATESLEEQLAAAEAEQELEESKRET 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 795 EKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSekekelerqarIEASLRER 874
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDE-----------IPQNQRGY 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 875 EREVQKARSEQTKEIDREREQHKR---------EEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKE 945
Cdd:COG5185 404 AQEILATLEDTLKAADRQIEELQRqieqatssnEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDL 483
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 87196334 946 --------------KLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSS 997
Cdd:COG5185 484 neeltqiesrvstlKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASE 549
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
610-1052 |
3.08e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 610 KEEQELMEEMNEDEPIKAKKRKRDDNKDIDSEKEAAMEAEIKAARERaIVPLEARMKQFKDmlLERGVSAFSTWEKELHK 689
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE-IEELEEKVKELKE--LKEKAEEYIKLSEFYEE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 690 IVFDPRYLllnpKERKQVFDQYVKTRAE--EERREKKNKIMQAKEDFKKMMEE-AKFNPRA-TFSEFAAKHAKDSRFKAI 765
Cdd:PRK03918 305 YLDELREI----EKRLSRLEEEINGIEEriKELEEKEERLEELKKKLKELEKRlEELEERHeLYEEAKAKKEELERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 766 EKMKDREALFNEFVAAARKKEK--EDSKTRGEKIKSdfFELLSNHHLDSQSRWSKVKDKVesdPRYKAVDSSSMREDLFK 843
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEieEEISKITARIGE--LKKEIKELKKAIEELKKAKGKC---PVCGRELTEEHRKELLE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 844 QYIEKIAKnldseKEKELERQARIEASLREREREVQKARS------------EQTKEIDREREQHKREEAIQNFKALLSD 911
Cdd:PRK03918 456 EYTAELKR-----IEKELKEIEEKERKLRKELRELEKVLKkeseliklkelaEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 912 MVRSsdvswsdtrRTLRKDHRwesgSLLEREEKEKLFNEHIEALTKKKREHFRQLldetsaitltstwKEVKKIIKEdpr 991
Cdd:PRK03918 531 KEKL---------IKLKGEIK----SLKKELEKLEELKKKLAELEKKLDELEEEL-------------AELLKELEE--- 581
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 87196334 992 cIKFSSSD--RKKQREFEEYIRdKYIT---AKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKI 1052
Cdd:PRK03918 582 -LGFESVEelEERLKELEPFYN-EYLElkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
838-969 |
4.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 838 REDLFKQYIEKIAKNLDSEKEKELERQARIEAsLREREREVQKARSEQ--------TKEIDR-EREQHKREEAIQNFKAL 908
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDA-LREELDELEAQIRGNggdrleqlEREIERlERELEERERRRARLEAL 367
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 87196334 909 LSDMvrssDVSWSDTRRTLRKDHRwESGSLLER--EEKEKLFNEHIEALTKKK--REHFRQLLDE 969
Cdd:COG4913 368 LAAL----GLPLPASAEEFAALRA-EAAALLEAleEELEALEEALAEAEAALRdlRRELRELEAE 427
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
259-433 |
5.06e-03 |
|
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: 41.06 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 259 GAPTPTTSSP----------APAVSTSTPTSTPSSTTATTTTATSVAQTVSTPTTQDQ-TPSSAVSVATPTVSVSAPAPT 327
Cdd:pfam05109 440 AAPNTTTGLPssthvptnltAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNgTESKAPDMTSPTSAVTTPTPN 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 328 AT-PVQTVPQPHPQTLPPAVPHSvpqpaaAIPAFPPVMVPPFRVPLPGMPIPLPGvAMMQIVSCPYVKTVATTKTgvlPG 406
Cdd:pfam05109 520 ATsPTPAVTTPTPNATSPTLGKT------SPTSAVTTPTPNATSPTPAVTTPTPN-ATIPTLGKTSPTSAVTTPT---PN 589
|
170 180
....*....|....*....|....*..
gi 87196334 407 MAPPIVPMIHPQVaiAASPATLAGATA 433
Cdd:pfam05109 590 ATSPTVGETSPQA--NTTNHTLGGTSS 614
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1055 |
7.48e-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: 40.44 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 846 IEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQT---KEIDREREQ-HKREEAIQNFKALLSD-MVRSSDVSW 920
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDlHKLEEALNDLEARLSHsRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 921 SDtrrtLRKDHRWESGSL--LEREEKEKLFNEHIEaltKKKREHFRQLLDEtsaitLTSTWKEVKKIIKEDPRCIKFSSS 998
Cdd:TIGR02169 801 SK----LEEEVSRIEARLreIEQKLNRLTLEKEYL---EKEIQELQEQRID-----LKEQIKSIEKEIENLNGKKEELEE 868
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 999 DRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKL---IQESDQHLKDVEKILQN 1055
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEA 928
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
835-920 |
8.75e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.24 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196334 835 SSMREDLFKQYiekiaknLDSEKEKELERQARIEASlREREREVQKARSEQTKEIDREREQHKREEAIQNFKA--LLSDM 912
Cdd:PLN02316 239 GGMDEHSFEDF-------LLEEKRRELEKLAKEEAE-RERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLqnLLKKA 310
|
....*...
gi 87196334 913 VRSSDVSW 920
Cdd:PLN02316 311 SRSADNVW 318
|
|
| |
