|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
429-1043 |
4.35e-24 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 108.63 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 429 ASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQEL--KEKEKLDEkikepikeaseeplpmeteeedpkeep 506
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELlkGSEEDLDV--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 507 vkeikeepkeeemteeekaaqkakpvattpipgTPWCVVWTGDERVFFYNPTTRLSMWDRPDDligRADVDKIIQEpphK 586
Cdd:COG5104 56 ---------------------------------DPWKECRTADGKVYYYNSITRESRWKIPPE---RKKVEPIAEQ---K 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 587 KGLEDMKKLRHPAPTMLSIQKWQFSmsaiKEEQELMEemnedepikakkrkrmskksfmwiaraslfrrddnkdidsekE 666
Cdd:COG5104 97 HDERSMIGGNGNDMAITDHETSEPK----YLLGRLMS------------------------------------------Q 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 667 AAMEAEIKAARERAivpLEARMKQFKDMLLERGVSAFSTWEKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERR 744
Cdd:COG5104 131 YGITSTKDAVYRLT---KEEAEKEFITMLKENQVDSTWPIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQRE 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 745 EKKNKIMQAKEDFKKMME-EAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSD 823
Cdd:COG5104 207 EEENKQRKYINEFCKMLAgNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGR 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 824 FFELLSNHHLDSQSRWSKVKDKVESDPRYKAvdSSSM----REDLFKQYIeKIAKNLdsekekelerqarieaslrerER 899
Cdd:COG5104 287 LEEVLRSLGSETFIIWLLNHYVFDSVVRYLK--NKEMkpldRKDILFSFI-RYVRRL---------------------EK 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 900 EVQKARSEQTKEIDReREQHKREeaiqNFKALLSDMVRSSDVS----WSDTRRTLRKDHRWESGSLLEREEKEKLFNEHI 975
Cdd:COG5104 343 ELLSAIEERKAAAAQ-NARHHRD----EFRTLLRKLYSEGKIYyrmkWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFI 417
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569004224 976 EALTKKKREHFRQLLDETSaITLTSTW--KEVKKIIKEDPRciKFSSSDRKKQREFEE---YIRDKYITAKAD 1043
Cdd:COG5104 418 VDLENMYGFARRSYERETR-TGQISPTdrRAVDEIFEAIAE--KKEEGEIKFDKVDKEdisLIVDGLIKQRNE 487
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
819-868 |
9.42e-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: 66.33 E-value: 9.42e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 569004224 819 KIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQY 868
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
980-1035 |
6.38e-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: 55.66 E-value: 6.38e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 569004224 980 KKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCiKFSSSDRKKQREFEEYIRD 1035
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
441-470 |
8.68e-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: 8.68e-09
10 20 30
....*....|....*....|....*....|
gi 569004224 441 SEWTEYKTADGKTYYYNNRTLESTWEKPQE 470
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 |
5.42e-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: 5.42e-08
10 20 30
....*....|....*....|....*....|...
gi 569004224 132 PTEEIWVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
137-162 |
5.51e-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: 5.51e-08
10 20
....*....|....*....|....*.
gi 569004224 137 WVENKTPDGKVYYYNARTRESAWTKP 162
Cdd:pfam00397 5 WEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
137-164 |
1.44e-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: 1.44e-07
10 20
....*....|....*....|....*...
gi 569004224 137 WVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
124-173 |
9.40e-06 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 49.69 E-value: 9.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 569004224 124 APGAPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDgvKVIQQSEL 173
Cdd:COG5104 4 ALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
735-1075 |
1.14e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 735 VKTRAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREAlfNEFVAAARKKEK 810
Cdd:PTZ00121 1423 AKKKAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKAD 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 811 EDSKTRGEKIKSDffELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARI 890
Cdd:PTZ00121 1501 EAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 891 EASLREREREVQKARSEQTKEIDREREQHKREEAiqnfKALLSDMVRSSDVSWSDTRRtlRKDHRWESGSLLEREEKEKL 970
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEK--KKVEQLKKKEAEEKKKAEEL 1652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 971 FNEHIEALTKKKREHFRQLLDETSAitltstwKEVKKIIKEDPRCIKFSSSDRKKQREFEEyIRDKYITAKADFRTLLKE 1050
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKA-------EEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKA 1724
|
330 340
....*....|....*....|....*
gi 569004224 1051 TKFITYRSKKLIQESDQHLKDVEKI 1075
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1040-1099 |
1.49e-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: 40.52 E-value: 1.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 1040 AKADFRTLLKETKfITYRSkkliqesdqHLKDVEKILQNDKRYLVLDcVPEERRKLIVAY 1099
Cdd:pfam01846 2 AREAFKELLKEHK-ITPYS---------TWSEIKKKIENDPRYKALL-DGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1038-1102 |
1.52e-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: 40.63 E-value: 1.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569004224 1038 ITAKADFRTLLKETKFITYrskkliqesDQHLKDVEKILQNDKRYLVLDcVPEERRKLIVAYVDD 1102
Cdd:smart00441 1 EEAKEAFKELLKEHEVITP---------DTTWSEARKKLKNDPRYKALL-SESEREQLFEDHIEE 55
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
258-352 |
2.22e-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: 42.21 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 258 VGAPTPTTSSPAPAVSTSTPTstpssttattttatsvaqtvsmfsfSLAPTTQDQTPSSAVSVAT-----PTVSVSAPAP 332
Cdd:pfam05109 513 VTTPTPNATSPTPAVTTPTPN-------------------------ATSPTLGKTSPTSAVTTPTpnatsPTPAVTTPTP 567
|
90 100
....*....|....*....|....*...
gi 569004224 333 TAT--------PVQTVPQPHPQTLPPAV 352
Cdd:pfam05109 568 NATiptlgktsPTSAVTTPTPNATSPTV 595
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
869-1078 |
4.57e-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: 41.21 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 869 IEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQT---KEIDREREQ-HKREEAIQNFKALLSD-MVRSSDVSW 943
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDlHKLEEALNDLEARLSHsRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 944 SDTRRTLRkdhRWESG-SLLEREEKEKLFNEHIEaltKKKREHFRQLLDEtsaitLTSTWKEVKKIIKEDPRCIKFSSSD 1022
Cdd:TIGR02169 801 SKLEEEVS---RIEARlREIEQKLNRLTLEKEYL---EKEIQELQEQRID-----LKEQIKSIEKEIENLNGKKEELEEE 869
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569004224 1023 RKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKL---IQESDQHLKDVEKILQN 1078
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEA 928
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
429-1043 |
4.35e-24 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 108.63 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 429 ASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQEL--KEKEKLDEkikepikeaseeplpmeteeedpkeep 506
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELlkGSEEDLDV--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 507 vkeikeepkeeemteeekaaqkakpvattpipgTPWCVVWTGDERVFFYNPTTRLSMWDRPDDligRADVDKIIQEpphK 586
Cdd:COG5104 56 ---------------------------------DPWKECRTADGKVYYYNSITRESRWKIPPE---RKKVEPIAEQ---K 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 587 KGLEDMKKLRHPAPTMLSIQKWQFSmsaiKEEQELMEemnedepikakkrkrmskksfmwiaraslfrrddnkdidsekE 666
Cdd:COG5104 97 HDERSMIGGNGNDMAITDHETSEPK----YLLGRLMS------------------------------------------Q 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 667 AAMEAEIKAARERAivpLEARMKQFKDMLLERGVSAFSTWEKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERR 744
Cdd:COG5104 131 YGITSTKDAVYRLT---KEEAEKEFITMLKENQVDSTWPIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQRE 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 745 EKKNKIMQAKEDFKKMME-EAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSD 823
Cdd:COG5104 207 EEENKQRKYINEFCKMLAgNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGR 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 824 FFELLSNHHLDSQSRWSKVKDKVESDPRYKAvdSSSM----REDLFKQYIeKIAKNLdsekekelerqarieaslrerER 899
Cdd:COG5104 287 LEEVLRSLGSETFIIWLLNHYVFDSVVRYLK--NKEMkpldRKDILFSFI-RYVRRL---------------------EK 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 900 EVQKARSEQTKEIDReREQHKREeaiqNFKALLSDMVRSSDVS----WSDTRRTLRKDHRWESGSLLEREEKEKLFNEHI 975
Cdd:COG5104 343 ELLSAIEERKAAAAQ-NARHHRD----EFRTLLRKLYSEGKIYyrmkWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFI 417
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569004224 976 EALTKKKREHFRQLLDETSaITLTSTW--KEVKKIIKEDPRciKFSSSDRKKQREFEE---YIRDKYITAKAD 1043
Cdd:COG5104 418 VDLENMYGFARRSYERETR-TGQISPTdrRAVDEIFEAIAE--KKEEGEIKFDKVDKEdisLIVDGLIKQRNE 487
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
819-868 |
9.42e-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: 66.33 E-value: 9.42e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 569004224 819 KIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQY 868
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
752-801 |
9.94e-12 |
|
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: 9.94e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 569004224 752 QAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEF 801
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
980-1035 |
6.38e-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: 55.66 E-value: 6.38e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 569004224 980 KKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCiKFSSSDRKKQREFEEYIRD 1035
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
687-734 |
6.85e-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: 6.85e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 569004224 687 RMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYL-LLNPKERKQVFDQY 734
Cdd:pfam01846 2 AREAFKELLKEHKITPYSTWSEIKKKIENDPRYKaLLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
818-871 |
1.34e-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: 54.89 E-value: 1.34e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 569004224 818 EKIKSDFFELLSNHHLD-SQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEK 871
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
923-974 |
2.38e-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: 2.38e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 569004224 923 EAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWEsgSLLEREEKEKLFNEH 974
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYK--ALLDGSEREELFEDY 50
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
441-470 |
8.68e-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: 8.68e-09
10 20 30
....*....|....*....|....*....|
gi 569004224 441 SEWTEYKTADGKTYYYNNRTLESTWEKPQE 470
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
441-468 |
3.16e-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: 3.16e-08
10 20
....*....|....*....|....*...
gi 569004224 441 SEWTEYKTADGKTYYYNNRTLESTWEKP 468
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 |
5.42e-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: 5.42e-08
10 20 30
....*....|....*....|....*....|...
gi 569004224 132 PTEEIWVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
137-162 |
5.51e-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: 5.51e-08
10 20
....*....|....*....|....*.
gi 569004224 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 ... |
443-470 |
5.87e-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: 5.87e-08
10 20
....*....|....*....|....*...
gi 569004224 443 WTEYKTADGKTYYYNNRTLESTWEKPQE 470
Cdd:smart00456 6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
751-804 |
1.12e-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: 49.49 E-value: 1.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 569004224 751 MQAKEDFKKMMEEAKFN-PRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAA 804
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 |
1.44e-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: 1.44e-07
10 20
....*....|....*....|....*...
gi 569004224 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 ... |
981-1032 |
2.37e-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: 2.37e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 569004224 981 KKREHFRQLLDETSaITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQrEFEEY 1032
Cdd:pfam01846 1 KAREAFKELLKEHK-ITPYSTWSEIKKKIENDPRYKALLDGSEREE-LFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
922-977 |
2.19e-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: 2.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 569004224 922 EEAIQNFKALLSDMVRS-SDVSWSDTRRTLRKDHRWESgsLLEREEKEKLFNEHIEA 977
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKA--LLSESEREQLFEDHIEE 55
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
685-736 |
5.61e-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: 44.49 E-value: 5.61e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 569004224 685 EARMKQFKDMLLERGVS-AFSTWEKELHKIVFDPRY-LLLNPKERKQVFDQYVK 736
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYkALLSESEREQLFEDHIE 54
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
726-976 |
8.45e-06 |
|
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: 50.12 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 726 ERKQVfDQYVKTRAEEERREKKNKIMQAKEdfKKMMEEAKFNPRATFSEFAAKHAKDSRFkAIEKMKDREALFNEfvaaa 805
Cdd:pfam17380 286 ERQQQ-EKFEKMEQERLRQEKEEKAREVER--RRKLEEAEKARQAEMDRQAAIYAEQERM-AMERERELERIRQE----- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 806 rKKEKEDSKTRGEKIKSDFFEL--LSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMRE-DLFKQYIEKIaknldsEKEK 882
Cdd:pfam17380 357 -ERKRELERIRQEEIAMEISRMreLERLQMERQQKNERVRQELEAARKVKILEEERQRKiQQQKVEMEQI------RAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 883 ELERQARIEASLREREREVQKARSEQ---TKEIDREREQhkrEEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESG 959
Cdd:pfam17380 430 EEARQREVRRLEEERAREMERVRLEEqerQQQVERLRQQ---EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250
....*....|....*..
gi 569004224 960 SLLEREEKEKLFNEHIE 976
Cdd:pfam17380 507 AMIEEERKRKLLEKEME 523
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
124-173 |
9.40e-06 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 49.69 E-value: 9.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 569004224 124 APGAPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDgvKVIQQSEL 173
Cdd:COG5104 4 ALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
541-569 |
9.86e-06 |
|
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: 43.36 E-value: 9.86e-06
10 20
....*....|....*....|....*....
gi 569004224 541 PWCVVWTGDERVFFYNPTTRLSMWDRPDD 569
Cdd:smart00456 5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
735-1075 |
1.14e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 735 VKTRAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREAlfNEFVAAARKKEK 810
Cdd:PTZ00121 1423 AKKKAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKAD 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 811 EDSKTRGEKIKSDffELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARI 890
Cdd:PTZ00121 1501 EAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 891 EASLREREREVQKARSEQTKEIDREREQHKREEAiqnfKALLSDMVRSSDVSWSDTRRtlRKDHRWESGSLLEREEKEKL 970
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEK--KKVEQLKKKEAEEKKKAEEL 1652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 971 FNEHIEALTKKKREHFRQLLDETSAitltstwKEVKKIIKEDPRCIKFSSSDRKKQREFEEyIRDKYITAKADFRTLLKE 1050
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKA-------EEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKA 1724
|
330 340
....*....|....*....|....*
gi 569004224 1051 TKFITYRSKKLIQESDQHLKDVEKI 1075
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
540-569 |
1.72e-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: 1.72e-05
10 20 30
....*....|....*....|....*....|
gi 569004224 540 TPWCVVWTGDERVFFYNPTTRLSMWDRPDD 569
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
137-172 |
6.66e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 47.00 E-value: 6.66e-05
10 20 30
....*....|....*....|....*....|....*.
gi 569004224 137 WVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSE 172
Cdd:COG5104 58 WKECRTADGKVYYYNSITRESRWKIPPERKKVEPIA 93
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
738-1007 |
7.15e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 738 RAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDS 813
Cdd:PTZ00121 1297 KAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 814 KTRGEKIKSDFFELLSNHHLDSQSRwskvKDKVESDPRYKAVDSSSMREDLfKQYIEKIAKNLDSEKEKELERQARieaS 893
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAE----EDKKKADELKKAAAAKKKADEA-KKKAEEKKKADEAKKKAEEAKKAD---E 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 894 LREREREVQKARSEQTKEIDREREQHKREEAIQNFKAllSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNE 973
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
250 260 270
....*....|....*....|....*....|....
gi 569004224 974 HIEALTKKKREHFRQLLDETSAITLTSTwKEVKK 1007
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKA-EELKK 1559
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
614-1028 |
8.68e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 614 AIKEEQELMEEMNEDEPIKAKKRKRMskksfmwIARASLFRRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKD 693
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADE-------AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKK 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 694 MLLE-RGVSAFSTWEKELHKIVFDPRYL--LLNPKERKQVFDQyVKTRAEEERR--EKKNKIMQAK--EDFKKMMEEAKF 766
Cdd:PTZ00121 1406 KADElKKAAAAKKKADEAKKKAEEKKKAdeAKKKAEEAKKADE-AKKKAEEAKKaeEAKKKAEEAKkaDEAKKKAEEAKK 1484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 767 NPRA-TFSEFAAKHAKDSRFKAIEKMKDREAL-------FNEFVAAARKKEKEDSKTRGEKIKSDffELLSNHHLDSQSR 838
Cdd:PTZ00121 1485 ADEAkKKAEEAKKKADEAKKAAEAKKKADEAKkaeeakkADEAKKAEEAKKADEAKKAEEKKKAD--ELKKAEELKKAEE 1562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 839 WSKVKD-KVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELErQARIEASLREREREVQKARSEQTK-EIDRER 916
Cdd:PTZ00121 1563 KKKAEEaKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAEELKKAEEEKKKvEQLKKK 1641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 917 EQHKREEAIQNFKALLSDMVRSSDVSwsdtRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETsai 996
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEA----KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE--- 1714
|
410 420 430
....*....|....*....|....*....|..
gi 569004224 997 tlTSTWKEVKKiiKEDPRCIKFSSSDRKKQRE 1028
Cdd:PTZ00121 1715 --KKKAEELKK--AEEENKIKAEEAKKEAEED 1742
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1040-1099 |
1.49e-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: 40.52 E-value: 1.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 1040 AKADFRTLLKETKfITYRSkkliqesdqHLKDVEKILQNDKRYLVLDcVPEERRKLIVAY 1099
Cdd:pfam01846 2 AREAFKELLKEHK-ITPYS---------TWSEIKKKIENDPRYKALL-DGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1038-1102 |
1.52e-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: 40.63 E-value: 1.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569004224 1038 ITAKADFRTLLKETKFITYrskkliqesDQHLKDVEKILQNDKRYLVLDcVPEERRKLIVAYVDD 1102
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 ... |
540-567 |
1.90e-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: 1.90e-04
10 20
....*....|....*....|....*...
gi 569004224 540 TPWCVVWTGDERVFFYNPTTRLSMWDRP 567
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
741-1095 |
2.46e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 741 EERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRF-----KAIEKMKDREALFNEFVAAARKKEKEDSKT 815
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELreeleKLEKEVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 816 RGEKIKsdffelLSNhhldSQSRWSKVKDKVEsDPRYKAVDSSSMREDLfKQYIEkiaknLDSEKEKELERQARIE---A 892
Cdd:PRK03918 255 RKLEEK------IRE----LEERIEELKKEIE-ELEEKVKELKELKEKA-EEYIK-----LSEFYEEYLDELREIEkrlS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 893 SLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsDTRRTLRKDHRWESGslLEREEKEKLFN 972
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE----EAKAKKEELERLKKR--LTGLTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 973 EhIEALTKKKREHFRQLLdetsaiTLTSTWKEVKKIIKEDPRCIKFSSSDRKK----QREFEEYIRDKYITA-KADFRTL 1047
Cdd:PRK03918 392 E-LEELEKAKEEIEEEIS------KITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEyTAELKRI 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 569004224 1048 LKETKFITYRSKKLIQEsdqhLKDVEKILQNDKRYLVLDCVPEERRKL 1095
Cdd:PRK03918 465 EKELKEIEEKERKLRKE----LRELEKVLKKESELIKLKELAEQLKEL 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
722-1094 |
2.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 722 LNPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMMEEAKfnpratFSEFAAKHAKDSRfKAIEKMKDREALFNEf 801
Cdd:PTZ00121 1072 LKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEAR------KAEEAKKKAEDAR-KAEEARKAEDARKAE- 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 802 vaAARKKEkEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVE---SDPRYKAVDSSSMREDLFKQYIEKIAKNLDS 878
Cdd:PTZ00121 1144 --EARKAE-DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrkAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 879 EKEKELERQARIEaSLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsdtrrTLRK-DHRWE 957
Cdd:PTZ00121 1221 EDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD--------ELKKaEEKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 958 SGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDET--SAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRD 1035
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569004224 1036 KYITAKADFRTLLK--ETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRK 1094
Cdd:PTZ00121 1372 KKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
723-1115 |
5.62e-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: 44.19 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 723 NPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDfkkmmeeakfnpratfsefaakhakdsrfKAIEKMKDREALFNEFV 802
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETEN-----------------------------LAELIIDLEELKLQELK 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 803 AAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKavDSSSMREDLFKQYIEKIAKNLDSEKEK 882
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE--IESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 883 ELERQARIEASLREREREVQKAR--SEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsdtRRTLRKDHRWESGS 960
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELlkLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE------LEKELKELEIKREA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 961 LLEREE----KEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIkedprcikfsSSDRKKQREFEEYIRDK 1036
Cdd:pfam02463 354 EEEEEEelekLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE----------AQLLLELARQLEDLLKE 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569004224 1037 YITAKADFrtLLKETKFITYRSKKLIQESDqHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDRRGPPPPPTAS 1115
Cdd:pfam02463 424 EKKEELEI--LEEEEESIELKQGKLTEEKE-ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
738-1020 |
1.16e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 738 RAEEERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSrfKAIEKMKDREALFNEFVAAARKKEKEDSKTRG 817
Cdd:COG5185 257 KLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYT--KSIDIKKATESLEEQLAAAEAEQELEESKRET 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 818 EKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSekekelerqarIEASLRER 897
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDE-----------IPQNQRGY 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 898 EREVQKARSEQTKEIDREREQHKR---------EEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKE 968
Cdd:COG5185 404 AQEILATLEDTLKAADRQIEELQRqieqatssnEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDL 483
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004224 969 --------------KLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSS 1020
Cdd:COG5185 484 neeltqiesrvstlKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASE 549
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
258-352 |
2.22e-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: 42.21 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 258 VGAPTPTTSSPAPAVSTSTPTstpssttattttatsvaqtvsmfsfSLAPTTQDQTPSSAVSVAT-----PTVSVSAPAP 332
Cdd:pfam05109 513 VTTPTPNATSPTPAVTTPTPN-------------------------ATSPTLGKTSPTSAVTTPTpnatsPTPAVTTPTP 567
|
90 100
....*....|....*....|....*...
gi 569004224 333 TAT--------PVQTVPQPHPQTLPPAV 352
Cdd:pfam05109 568 NATiptlgktsPTSAVTTPTPNATSPTV 595
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
861-992 |
4.04e-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: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 861 REDLFKQYIEKIAKNLDSEKEKELERQARIEAsLREREREVQKARSEQ--------TKEIDR-EREQHKREEAIQNFKAL 931
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDA-LREELDELEAQIRGNggdrleqlEREIERlERELEERERRRARLEAL 367
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569004224 932 LSDMvrssDVSWSDTRRTLRKDHRwESGSLLER--EEKEKLFNEHIEALTKKK--REHFRQLLDE 992
Cdd:COG4913 368 LAAL----GLPLPASAEEFAALRA-EAAALLEAleEELEALEEALAEAEAALRdlRRELRELEAE 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
869-1078 |
4.57e-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: 41.21 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 869 IEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQT---KEIDREREQ-HKREEAIQNFKALLSD-MVRSSDVSW 943
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDlHKLEEALNDLEARLSHsRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 944 SDTRRTLRkdhRWESG-SLLEREEKEKLFNEHIEaltKKKREHFRQLLDEtsaitLTSTWKEVKKIIKEDPRCIKFSSSD 1022
Cdd:TIGR02169 801 SKLEEEVS---RIEARlREIEQKLNRLTLEKEYL---EKEIQELQEQRID-----LKEQIKSIEKEIENLNGKKEELEEE 869
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569004224 1023 RKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKL---IQESDQHLKDVEKILQN 1078
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEA 928
|
|
| half-pint |
TIGR01645 |
poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
304-490 |
5.03e-03 |
|
poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.
Pssm-ID: 130706 [Multi-domain] Cd Length: 612 Bit Score: 40.82 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 304 SLAPTTQDQ-TPSSAV--SVATPTVsVSAPAPTATPVQTVPQPHPQTLPPAvphsvpqpaaaipafppVMVPPFRVPLPG 380
Cdd:TIGR01645 323 VLGPRAQSPaTPSSSLptDIGNKAV-VSSAKKEAEEVPPLPQAAPAVVKPG-----------------PMEIPTPVPPPG 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 381 MPIPLpGVAMMQIVScpyvktvattKTGVLPG-MAPPIVPMIHPQVAIAASP--ATLAGATAVSEwtEYKTADGKTYYYN 457
Cdd:TIGR01645 385 LAIPS-LVAPPGLVA----------PTEINPSfLASPRKKMKREKLPVTFGAldDTLAWKEPSKE--DQTSEDGKMLAIM 451
|
170 180 190
....*....|....*....|....*....|...
gi 569004224 458 NRTLESTWEKPQElKEKEKLDEKIKEPIKEASE 490
Cdd:TIGR01645 452 GEAAAALALEPKK-KKKEKEGEELQPKLVMNSE 483
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
741-1075 |
7.51e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 741 EERREKKNKIMQAKEDFKKMMEE-AKFNPRA-TFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEK--EDSKTR 816
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRlEELEERHeLYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEieEEISKI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 817 GEKIKSdfFELLSNHHLDSQSRWSKVKDKVesdPRYKAVDSSSMREDLFKQYIEKIAKnldseKEKELERQARIEASLRE 896
Cdd:PRK03918 411 TARIGE--LKKEIKELKKAIEELKKAKGKC---PVCGRELTEEHRKELLEEYTAELKR-----IEKELKEIEEKERKLRK 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 897 REREVQKARS------------EQTKEIDREREQHKREEAIQNFKALLSDMVRSsdvswsdtrRTLRKDHRwesgSLLER 964
Cdd:PRK03918 481 ELRELEKVLKkeseliklkelaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL---------IKLKGEIK----SLKKE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 965 EEKEKLFNEHIEALTKKKREHFRQLldetsaitltstwKEVKKIIKEdprcIKFSSSD--RKKQREFEEYIRdKYIT--- 1039
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEEL-------------AELLKELEE----LGFESVEelEERLKELEPFYN-EYLElkd 609
|
330 340 350
....*....|....*....|....*....|....*.
gi 569004224 1040 AKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKI 1075
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
858-943 |
8.59e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.24 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004224 858 SSMREDLFKQYiekiaknLDSEKEKELERQARIEASlREREREVQKARSEQTKEIDREREQHKREEAIQNFKA--LLSDM 935
Cdd:PLN02316 239 GGMDEHSFEDF-------LLEEKRRELEKLAKEEAE-RERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLqnLLKKA 310
|
....*...
gi 569004224 936 VRSSDVSW 943
Cdd:PLN02316 311 SRSADNVW 318
|
|
| |
