|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
152-504 |
1.83e-173 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
:
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 492.08 E-value: 1.83e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 152 CRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPD 231
Cdd:cd00078 1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 232 SAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDI-TGVLDHTFCV 310
Cdd:cd00078 81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGdEDDLELTFTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 311 EHN-AYGEIIQHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLG 389
Cdd:cd00078 161 ELDsSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 390 KIDVSDWKVNTRLKHC-TPDSNVVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQgaagpRLFTIHQIDACTNN 468
Cdd:cd00078 241 DIDLEDLKKNTEYKGGySSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDR 315
|
330 340 350
....*....|....*....|....*....|....*.
gi 1386635288 469 LPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGF 504
Cdd:cd00078 316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGF 351
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-89 |
7.22e-11 |
|
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: 56.84 E-value: 7.22e-11
10 20 30
....*....|....*....|....*....|...
gi 1386635288 57 PLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRL 89
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
11-42 |
7.93e-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: 48.37 E-value: 7.93e-08
10 20 30
....*....|....*....|....*....|..
gi 1386635288 11 DLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPR 42
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
152-504 |
1.83e-173 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 492.08 E-value: 1.83e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 152 CRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPD 231
Cdd:cd00078 1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 232 SAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDI-TGVLDHTFCV 310
Cdd:cd00078 81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGdEDDLELTFTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 311 EHN-AYGEIIQHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLG 389
Cdd:cd00078 161 ELDsSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 390 KIDVSDWKVNTRLKHC-TPDSNVVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQgaagpRLFTIHQIDACTNN 468
Cdd:cd00078 241 DIDLEDLKKNTEYKGGySSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDR 315
|
330 340 350
....*....|....*....|....*....|....*.
gi 1386635288 469 LPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGF 504
Cdd:cd00078 316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGF 351
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
2-504 |
1.07e-170 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 503.92 E-value: 1.07e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 2 SRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPR----VPRD----LSNINC-----EELGPLPPGWEIRNTA 68
Cdd:COG5021 378 SRGTTRDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRreqlGRESdesfYVASNVqqqraSREGPLLSGWKTRLNN 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 69 TGRVYFVDHNNRTTQFTDPRLSANLHLVLNRqnqlkdqqqqqvvplcpddtecltVPRYKRDLVQKLKILRQElsQQQPQ 148
Cdd:COG5021 458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLD------------------------IRRIKEDKRRKLFYSLKQ--KAKIF 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 149 AGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQI 228
Cdd:COG5021 512 DPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPI 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 229 NPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITG-VLDHT 307
Cdd:COG5021 592 NPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDEtILDLT 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 308 FCVEHNAYGEIIQHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICG 387
Cdd:COG5021 672 FTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGG 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 388 LG-KIDVSDWKVNTRLKHCTPDSNVVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACT 466
Cdd:COG5021 752 IPeDIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDD 831
|
490 500 510
....*....|....*....|....*....|....*...
gi 1386635288 467 NNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGF 504
Cdd:COG5021 832 DRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
179-504 |
1.03e-158 |
|
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.
Pssm-ID: 214523 Cd Length: 328 Bit Score: 454.00 E-value: 1.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 179 KRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDiYTLQINPDS-AVNPEHLSYFHFVGRIMGMAVFHGH 257
Cdd:smart00119 5 RVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSgFANEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 258 YIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWI-LENDITGVLDHTFC-VEHNAYGEIIQHELKPNGKSIPVTEE 335
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIPVTEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 336 NKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVSDWKVNTRLKHC-TPDSNVVKW 414
Cdd:smart00119 164 NKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGySANSQTIKW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 415 FWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAagprlFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKL 494
Cdd:smart00119 244 FWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKL 318
|
330
....*....|
gi 1386635288 495 LTAIEETCGF 504
Cdd:smart00119 319 LLAINEGKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
202-504 |
1.05e-129 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 378.88 E-value: 1.05e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 202 YLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNP--EHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLD 279
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdlELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 280 DMELVDPDLHNSLVWIL--ENDITGVLDHTFCVEHnaYGEIIQHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQF 357
Cdd:pfam00632 81 DLESIDPELYKSLKSLLnmDNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 358 LALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVSDWKVNTRLKH-CTPDSNVVKWFWKAVEFFDEERRARLLQFVTG 436
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386635288 437 SSRVPLQGFKALQgaagprLFTIHQIDAC-TNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGF 504
Cdd:pfam00632 239 SSRLPVGGFKSLP------KFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGF 301
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-89 |
7.22e-11 |
|
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: 56.84 E-value: 7.22e-11
10 20 30
....*....|....*....|....*....|...
gi 1386635288 57 PLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRL 89
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
59-89 |
6.83e-10 |
|
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: 54.07 E-value: 6.83e-10
10 20 30
....*....|....*....|....*....|.
gi 1386635288 59 PPGWEIRNTATGRVYFVDHNNRTTQFTDPRL 89
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
58-87 |
6.41e-09 |
|
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: 51.35 E-value: 6.41e-09
10 20 30
....*....|....*....|....*....|
gi 1386635288 58 LPPGWEIRNTATGRVYFVDHNNRTTQFTDP 87
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
11-42 |
7.93e-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: 48.37 E-value: 7.93e-08
10 20 30
....*....|....*....|....*....|..
gi 1386635288 11 DLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPR 42
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
12-41 |
2.75e-07 |
|
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: 46.73 E-value: 2.75e-07
10 20 30
....*....|....*....|....*....|
gi 1386635288 12 LPEGYEQRTTQQGQVYFLHTQTGVSTWHDP 41
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
13-42 |
3.06e-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: 46.37 E-value: 3.06e-07
10 20 30
....*....|....*....|....*....|
gi 1386635288 13 PEGYEQRTTQQGQVYFLHTQTGVSTWHDPR 42
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| Cas_III-E_gRAMP |
NF041225 |
type III-E CRISPR-associated gRAMP effector Cas7-11; The giant RAMP (gRAMP) effector of type ... |
273-454 |
3.01e-04 |
|
type III-E CRISPR-associated gRAMP effector Cas7-11; The giant RAMP (gRAMP) effector of type III-E CRISPR/Cas systems, named Cas7-11 because of its multiple domains, works together with the caspase-like TPR-CHAT protease (Csx29) in a subset of type III-E systems. The complex of the Cas7-11 and the TPR-CHAT subunits is called craspase (CRISPR-guided caspase).
Pssm-ID: 469128 [Multi-domain] Cd Length: 1629 Bit Score: 43.59 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 273 GKSITLDDMELVDPdlhnslVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVTEENK-----KEYVRLYVNW 347
Cdd:NF041225 1417 GKYVTLPLLERPRP------TWSMPDDESEVPGRKFYVHHNGWREVKKGDHPKNGRATVQTENNRtvealDKGNKFSFEV 1490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 348 RF--LR----GIEAQFLALQKGFNevipqHLL---KTFdekeleliicGLG--KIDVS------DWKVNTRLKHCTPDSN 410
Cdd:NF041225 1491 AFenLRewelGLLLYSLELEPGMA-----HKLgmgKPM----------GFGsvKIRVEslhtrkVNGQWRNEKSSTDLPW 1555
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1386635288 411 VVKWFWKAVEFFDEERRARLLQFVTG--SSRVPLQGFKALQGAAGP 454
Cdd:NF041225 1556 VTKGKLKLSEWFKIEDLRKLLWLPEEddIKLVYPKGLKKKEGEGGD 1601
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
152-504 |
1.83e-173 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 492.08 E-value: 1.83e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 152 CRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPD 231
Cdd:cd00078 1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 232 SAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDI-TGVLDHTFCV 310
Cdd:cd00078 81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGdEDDLELTFTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 311 EHN-AYGEIIQHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLG 389
Cdd:cd00078 161 ELDsSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 390 KIDVSDWKVNTRLKHC-TPDSNVVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQgaagpRLFTIHQIDACTNN 468
Cdd:cd00078 241 DIDLEDLKKNTEYKGGySSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDR 315
|
330 340 350
....*....|....*....|....*....|....*.
gi 1386635288 469 LPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGF 504
Cdd:cd00078 316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGF 351
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
2-504 |
1.07e-170 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 503.92 E-value: 1.07e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 2 SRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPR----VPRD----LSNINC-----EELGPLPPGWEIRNTA 68
Cdd:COG5021 378 SRGTTRDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRreqlGRESdesfYVASNVqqqraSREGPLLSGWKTRLNN 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 69 TGRVYFVDHNNRTTQFTDPRLSANLHLVLNRqnqlkdqqqqqvvplcpddtecltVPRYKRDLVQKLKILRQElsQQQPQ 148
Cdd:COG5021 458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLD------------------------IRRIKEDKRRKLFYSLKQ--KAKIF 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 149 AGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQI 228
Cdd:COG5021 512 DPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPI 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 229 NPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITG-VLDHT 307
Cdd:COG5021 592 NPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDEtILDLT 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 308 FCVEHNAYGEIIQHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICG 387
Cdd:COG5021 672 FTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGG 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 388 LG-KIDVSDWKVNTRLKHCTPDSNVVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACT 466
Cdd:COG5021 752 IPeDIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDD 831
|
490 500 510
....*....|....*....|....*....|....*...
gi 1386635288 467 NNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGF 504
Cdd:COG5021 832 DRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
179-504 |
1.03e-158 |
|
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.
Pssm-ID: 214523 Cd Length: 328 Bit Score: 454.00 E-value: 1.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 179 KRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDiYTLQINPDS-AVNPEHLSYFHFVGRIMGMAVFHGH 257
Cdd:smart00119 5 RVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSgFANEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 258 YIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWI-LENDITGVLDHTFC-VEHNAYGEIIQHELKPNGKSIPVTEE 335
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIPVTEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 336 NKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVSDWKVNTRLKHC-TPDSNVVKW 414
Cdd:smart00119 164 NKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGySANSQTIKW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 415 FWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAagprlFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKL 494
Cdd:smart00119 244 FWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKL 318
|
330
....*....|
gi 1386635288 495 LTAIEETCGF 504
Cdd:smart00119 319 LLAINEGKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
202-504 |
1.05e-129 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 378.88 E-value: 1.05e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 202 YLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNP--EHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLD 279
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdlELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 280 DMELVDPDLHNSLVWIL--ENDITGVLDHTFCVEHnaYGEIIQHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQF 357
Cdd:pfam00632 81 DLESIDPELYKSLKSLLnmDNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 358 LALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVSDWKVNTRLKH-CTPDSNVVKWFWKAVEFFDEERRARLLQFVTG 436
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386635288 437 SSRVPLQGFKALQgaagprLFTIHQIDAC-TNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGF 504
Cdd:pfam00632 239 SSRLPVGGFKSLP------KFTIVRKGGDdDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGF 301
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-89 |
7.22e-11 |
|
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: 56.84 E-value: 7.22e-11
10 20 30
....*....|....*....|....*....|...
gi 1386635288 57 PLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRL 89
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
59-89 |
6.83e-10 |
|
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: 54.07 E-value: 6.83e-10
10 20 30
....*....|....*....|....*....|.
gi 1386635288 59 PPGWEIRNTATGRVYFVDHNNRTTQFTDPRL 89
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
58-87 |
6.41e-09 |
|
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: 51.35 E-value: 6.41e-09
10 20 30
....*....|....*....|....*....|
gi 1386635288 58 LPPGWEIRNTATGRVYFVDHNNRTTQFTDP 87
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
11-42 |
7.93e-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: 48.37 E-value: 7.93e-08
10 20 30
....*....|....*....|....*....|..
gi 1386635288 11 DLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPR 42
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
12-41 |
2.75e-07 |
|
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: 46.73 E-value: 2.75e-07
10 20 30
....*....|....*....|....*....|
gi 1386635288 12 LPEGYEQRTTQQGQVYFLHTQTGVSTWHDP 41
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
13-42 |
3.06e-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: 46.37 E-value: 3.06e-07
10 20 30
....*....|....*....|....*....|
gi 1386635288 13 PEGYEQRTTQQGQVYFLHTQTGVSTWHDPR 42
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| Cas_III-E_gRAMP |
NF041225 |
type III-E CRISPR-associated gRAMP effector Cas7-11; The giant RAMP (gRAMP) effector of type ... |
273-454 |
3.01e-04 |
|
type III-E CRISPR-associated gRAMP effector Cas7-11; The giant RAMP (gRAMP) effector of type III-E CRISPR/Cas systems, named Cas7-11 because of its multiple domains, works together with the caspase-like TPR-CHAT protease (Csx29) in a subset of type III-E systems. The complex of the Cas7-11 and the TPR-CHAT subunits is called craspase (CRISPR-guided caspase).
Pssm-ID: 469128 [Multi-domain] Cd Length: 1629 Bit Score: 43.59 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 273 GKSITLDDMELVDPdlhnslVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVTEENK-----KEYVRLYVNW 347
Cdd:NF041225 1417 GKYVTLPLLERPRP------TWSMPDDESEVPGRKFYVHHNGWREVKKGDHPKNGRATVQTENNRtvealDKGNKFSFEV 1490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386635288 348 RF--LR----GIEAQFLALQKGFNevipqHLL---KTFdekeleliicGLG--KIDVS------DWKVNTRLKHCTPDSN 410
Cdd:NF041225 1491 AFenLRewelGLLLYSLELEPGMA-----HKLgmgKPM----------GFGsvKIRVEslhtrkVNGQWRNEKSSTDLPW 1555
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1386635288 411 VVKWFWKAVEFFDEERRARLLQFVTG--SSRVPLQGFKALQGAAGP 454
Cdd:NF041225 1556 VTKGKLKLSEWFKIEDLRKLLWLPEEddIKLVYPKGLKKKEGEGGD 1601
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
16-87 |
5.72e-04 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 42.37 E-value: 5.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386635288 16 YEQRTTQQGQVYFLHTQTGVSTWHDprvPRDLsnINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDP 87
Cdd:COG5104 17 WEELKAPDGRIYYYNKRTGKSSWEK---PKEL--LKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIP 83
|
|
| |
