|
Name |
Accession |
Description |
Interval |
E-value |
| HUL4 super family |
cl34867 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
309-850 |
1.18e-177 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
The actual alignment was detected with superfamily member COG5021:
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 534.35 E-value: 1.18e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 309 QPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQF------NQRYLYSASMLAAEND- 381
Cdd:COG5021 297 LRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDlphqvgSNPFLEAHPEFSELLKn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 382 -------PYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL-------------------PNEEPLPEGWEIRYT 435
Cdd:COG5021 377 qsrgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLgresdesfyvasnvqqqraSREGPLLSGWKTRLN 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 436 REGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNaLPSHVKINVSRQTLFEDSFQQIMAL 515
Cdd:COG5021 457 NLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 516 KPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMA 595
Cdd:COG5021 536 SGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKA 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 596 LFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNIL 675
Cdd:COG5021 616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 676 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE-VDLADWQRNTVYRHYTRNSK 754
Cdd:COG5021 696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSP 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 755 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 833
Cdd:COG5021 776 IIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKL 855
|
570
....*....|....*..
gi 1243938454 834 KEKLLFAIEETEGFGQE 850
Cdd:COG5021 856 RSKLLTAINEGAGFGLL 872
|
|
| C2 super family |
cl14603 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
8-72 |
3.81e-27 |
|
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
The actual alignment was detected with superfamily member cd04021:
Pssm-ID: 472691 [Multi-domain] Cd Length: 125 Bit Score: 106.98 E-value: 3.81e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243938454 8 TTLEFRVWSHHTLKADALLGKATVDLKQVLLTHNRKLEKVKEQLKLSLENKNGIVQTGELTVVLD 72
Cdd:cd04021 61 STLEFKVWSHHTLKADVLLGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
279-308 |
4.50e-13 |
|
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: 63.68 E-value: 4.50e-13
10 20 30
....*....|....*....|....*....|
gi 1243938454 279 LPSGWEQRKDPHGRTYYVDHNTRTTTWERP 308
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| DUF5585 super family |
cl39316 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
80-313 |
8.85e-06 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
The actual alignment was detected with superfamily member pfam17823:
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 49.19 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 80 PVTNRSSSPPIEIQqNGDALHeNGDPATRT----------TPRLPVEGTIGIDNHVSTntVVPNSCCSHVVNGENTPSSP 149
Cdd:pfam17823 150 CRANASAAPRAAIA-AASAPH-AASPAPRTaassttaassTTAASSAPTTAASSAPAT--LTPARGISTAATATGHPAAG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 150 SQVAARPKNAPAPKPVTSAptsdtVNGESSSVLADNTSTMGTLLPSEDTTSTSNctstttqepPVQEPPASSEHSECIPS 229
Cdd:pfam17823 226 TALAAVGNSSPAAGTVTAA-----VGTVTPAALATLAAAAGTVASAAGTINMGD---------PHARRLSPAKHMPSDTM 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 230 AS---AEVGPEAR---SLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQS-GNTNTEALPSGWEQRKDPHGRTYYVDHNTR- 301
Cdd:pfam17823 292 ARnpaAPMGAQAQgpiIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSvASTNLAVVTTTKAQAKEPSASPVPVLHTSMi 371
|
250
....*....|....*..
gi 1243938454 302 -----TTTWERPQPLPP 313
Cdd:pfam17823 372 peveaTSPTTQPSPLLP 388
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
309-850 |
1.18e-177 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 534.35 E-value: 1.18e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 309 QPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQF------NQRYLYSASMLAAEND- 381
Cdd:COG5021 297 LRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDlphqvgSNPFLEAHPEFSELLKn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 382 -------PYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL-------------------PNEEPLPEGWEIRYT 435
Cdd:COG5021 377 qsrgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLgresdesfyvasnvqqqraSREGPLLSGWKTRLN 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 436 REGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNaLPSHVKINVSRQTLFEDSFQQIMAL 515
Cdd:COG5021 457 NLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 516 KPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMA 595
Cdd:COG5021 536 SGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKA 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 596 LFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNIL 675
Cdd:COG5021 616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 676 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE-VDLADWQRNTVYRHYTRNSK 754
Cdd:COG5021 696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSP 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 755 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 833
Cdd:COG5021 776 IIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKL 855
|
570
....*....|....*..
gi 1243938454 834 KEKLLFAIEETEGFGQE 850
Cdd:COG5021 856 RSKLLTAINEGAGFGLL 872
|
|
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
496-848 |
7.47e-170 |
|
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: 495.55 E-value: 7.47e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 496 KINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 575
Cdd:cd00078 2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 576 TINPDHLSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVD 655
Cdd:cd00078 82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 656 MEI-LGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE 734
Cdd:cd00078 162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 735 VDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMgsngpQKFCIEKVGK-DTWL 812
Cdd:cd00078 242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDRL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 1243938454 813 PRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 848
Cdd:cd00078 317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
519-847 |
2.56e-159 |
|
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: 467.48 E-value: 2.56e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 519 DLR-RRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINP-ASTINPDHLSYFCFIGRFIAMAL 596
Cdd:smart00119 1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPrSGFANEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 597 FHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFS-VDMEILGKVTSHDLKLGGSNIL 675
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 676 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSK 754
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 755 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGsngpqKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 833
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 1243938454 834 KEKLLFAIEETEGF 847
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
545-848 |
2.30e-120 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 366.16 E-value: 2.30e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 545 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDH--LSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIK 622
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 623 DLESIDTEFYNSLIWIR--DNNIEECgLEMYFSVDmeILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQ 700
Cdd:pfam00632 81 DLESIDPELYKSLKSLLnmDNDDDED-LGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 701 TKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVT 779
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243938454 780 GTCRLPLGGFAELmgsngpQKFCIEKVG--KDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 848
Cdd:pfam00632 238 GSSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
|
|
| C2_E3_ubiquitin_ligase |
cd04021 |
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ... |
8-72 |
3.81e-27 |
|
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 175988 [Multi-domain] Cd Length: 125 Bit Score: 106.98 E-value: 3.81e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243938454 8 TTLEFRVWSHHTLKADALLGKATVDLKQVLLTHNRKLEKVKEQLKLSLENKNGIVQTGELTVVLD 72
Cdd:cd04021 61 STLEFKVWSHHTLKADVLLGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
279-308 |
4.50e-13 |
|
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: 63.68 E-value: 4.50e-13
10 20 30
....*....|....*....|....*....|
gi 1243938454 279 LPSGWEQRKDPHGRTYYVDHNTRTTTWERP 308
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
279-310 |
2.04e-12 |
|
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: 61.85 E-value: 2.04e-12
10 20 30
....*....|....*....|....*....|..
gi 1243938454 279 LPSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 310
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
280-310 |
2.14e-12 |
|
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: 61.77 E-value: 2.14e-12
10 20 30
....*....|....*....|....*....|.
gi 1243938454 280 PSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 310
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
80-313 |
8.85e-06 |
|
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: 49.19 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 80 PVTNRSSSPPIEIQqNGDALHeNGDPATRT----------TPRLPVEGTIGIDNHVSTntVVPNSCCSHVVNGENTPSSP 149
Cdd:pfam17823 150 CRANASAAPRAAIA-AASAPH-AASPAPRTaassttaassTTAASSAPTTAASSAPAT--LTPARGISTAATATGHPAAG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 150 SQVAARPKNAPAPKPVTSAptsdtVNGESSSVLADNTSTMGTLLPSEDTTSTSNctstttqepPVQEPPASSEHSECIPS 229
Cdd:pfam17823 226 TALAAVGNSSPAAGTVTAA-----VGTVTPAALATLAAAAGTVASAAGTINMGD---------PHARRLSPAKHMPSDTM 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 230 AS---AEVGPEAR---SLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQS-GNTNTEALPSGWEQRKDPHGRTYYVDHNTR- 301
Cdd:pfam17823 292 ARnpaAPMGAQAQgpiIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSvASTNLAVVTTTKAQAKEPSASPVPVLHTSMi 371
|
250
....*....|....*..
gi 1243938454 302 -----TTTWERPQPLPP 313
Cdd:pfam17823 372 peveaTSPTTQPSPLLP 388
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
309-850 |
1.18e-177 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 534.35 E-value: 1.18e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 309 QPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQF------NQRYLYSASMLAAEND- 381
Cdd:COG5021 297 LRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDlphqvgSNPFLEAHPEFSELLKn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 382 -------PYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL-------------------PNEEPLPEGWEIRYT 435
Cdd:COG5021 377 qsrgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLgresdesfyvasnvqqqraSREGPLLSGWKTRLN 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 436 REGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNaLPSHVKINVSRQTLFEDSFQQIMAL 515
Cdd:COG5021 457 NLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 516 KPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMA 595
Cdd:COG5021 536 SGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKA 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 596 LFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNIL 675
Cdd:COG5021 616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 676 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE-VDLADWQRNTVYRHYTRNSK 754
Cdd:COG5021 696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSP 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 755 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 833
Cdd:COG5021 776 IIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKL 855
|
570
....*....|....*..
gi 1243938454 834 KEKLLFAIEETEGFGQE 850
Cdd:COG5021 856 RSKLLTAINEGAGFGLL 872
|
|
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
496-848 |
7.47e-170 |
|
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: 495.55 E-value: 7.47e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 496 KINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 575
Cdd:cd00078 2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 576 TINPDHLSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVD 655
Cdd:cd00078 82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 656 MEI-LGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE 734
Cdd:cd00078 162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 735 VDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMgsngpQKFCIEKVGK-DTWL 812
Cdd:cd00078 242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDRL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 1243938454 813 PRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 848
Cdd:cd00078 317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
519-847 |
2.56e-159 |
|
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: 467.48 E-value: 2.56e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 519 DLR-RRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINP-ASTINPDHLSYFCFIGRFIAMAL 596
Cdd:smart00119 1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPrSGFANEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 597 FHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFS-VDMEILGKVTSHDLKLGGSNIL 675
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 676 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSK 754
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 755 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGsngpqKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 833
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 1243938454 834 KEKLLFAIEETEGF 847
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
545-848 |
2.30e-120 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 366.16 E-value: 2.30e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 545 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDH--LSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIK 622
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 623 DLESIDTEFYNSLIWIR--DNNIEECgLEMYFSVDmeILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQ 700
Cdd:pfam00632 81 DLESIDPELYKSLKSLLnmDNDDDED-LGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 701 TKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVT 779
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243938454 780 GTCRLPLGGFAELmgsngpQKFCIEKVG--KDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 848
Cdd:pfam00632 238 GSSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
|
|
| C2_E3_ubiquitin_ligase |
cd04021 |
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ... |
8-72 |
3.81e-27 |
|
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 175988 [Multi-domain] Cd Length: 125 Bit Score: 106.98 E-value: 3.81e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243938454 8 TTLEFRVWSHHTLKADALLGKATVDLKQVLLTHNRKLEKVKEQLKLSLENKNGIVQTGELTVVLD 72
Cdd:cd04021 61 STLEFKVWSHHTLKADVLLGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
279-308 |
4.50e-13 |
|
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: 63.68 E-value: 4.50e-13
10 20 30
....*....|....*....|....*....|
gi 1243938454 279 LPSGWEQRKDPHGRTYYVDHNTRTTTWERP 308
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
311-340 |
1.55e-12 |
|
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: 62.14 E-value: 1.55e-12
10 20 30
....*....|....*....|....*....|
gi 1243938454 311 LPPGWERRVDDRGRVYYVDHNTRTTTWQRP 340
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
279-310 |
2.04e-12 |
|
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: 61.85 E-value: 2.04e-12
10 20 30
....*....|....*....|....*....|..
gi 1243938454 279 LPSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 310
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
280-310 |
2.14e-12 |
|
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: 61.77 E-value: 2.14e-12
10 20 30
....*....|....*....|....*....|.
gi 1243938454 280 PSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 310
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
386-415 |
3.23e-12 |
|
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: 61.37 E-value: 3.23e-12
10 20 30
....*....|....*....|....*....|
gi 1243938454 386 LPPGWEKRVDSTDRVYFVNHNTKTTQWEDP 415
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
387-416 |
1.25e-11 |
|
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: 59.46 E-value: 1.25e-11
10 20 30
....*....|....*....|....*....|
gi 1243938454 387 PPGWEKRVDSTDRVYFVNHNTKTTQWEDPR 416
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
385-416 |
1.48e-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: 59.54 E-value: 1.48e-11
10 20 30
....*....|....*....|....*....|..
gi 1243938454 385 PLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPR 416
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
312-342 |
1.57e-11 |
|
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: 59.46 E-value: 1.57e-11
10 20 30
....*....|....*....|....*....|.
gi 1243938454 312 PPGWERRVDDRGRVYYVDHNTRTTTWQRPTM 342
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
310-342 |
2.97e-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: 58.38 E-value: 2.97e-11
10 20 30
....*....|....*....|....*....|...
gi 1243938454 310 PLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTM 342
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
278-340 |
1.64e-09 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 61.25 E-value: 1.64e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243938454 278 ALPSG-----WEQRKDPHGRTYYVDHNTRTTTWERPQPLPPGWERRVDD---------RGRVYYVDHNTRTTTWQRP 340
Cdd:COG5104 7 GMASGearseWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVdpwkecrtaDGKVYYYNSITRESRWKIP 83
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
427-456 |
1.79e-08 |
|
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: 50.60 E-value: 1.79e-08
10 20 30
....*....|....*....|....*....|
gi 1243938454 427 PEGWEIRYTREGVRYFVDHNTRTTTFKDPR 456
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
425-457 |
2.62e-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: 50.29 E-value: 2.62e-08
10 20 30
....*....|....*....|....*....|...
gi 1243938454 425 PLPEGWEIRYTREGVRYFVDHNTRTTTFKDPRN 457
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
426-455 |
1.49e-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: 47.88 E-value: 1.49e-07
10 20 30
....*....|....*....|....*....|
gi 1243938454 426 LPEGWEIRYTREGVRYFVDHNTRTTTFKDP 455
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
80-313 |
8.85e-06 |
|
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: 49.19 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 80 PVTNRSSSPPIEIQqNGDALHeNGDPATRT----------TPRLPVEGTIGIDNHVSTntVVPNSCCSHVVNGENTPSSP 149
Cdd:pfam17823 150 CRANASAAPRAAIA-AASAPH-AASPAPRTaassttaassTTAASSAPTTAASSAPAT--LTPARGISTAATATGHPAAG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 150 SQVAARPKNAPAPKPVTSAptsdtVNGESSSVLADNTSTMGTLLPSEDTTSTSNctstttqepPVQEPPASSEHSECIPS 229
Cdd:pfam17823 226 TALAAVGNSSPAAGTVTAA-----VGTVTPAALATLAAAAGTVASAAGTINMGD---------PHARRLSPAKHMPSDTM 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 230 AS---AEVGPEAR---SLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQS-GNTNTEALPSGWEQRKDPHGRTYYVDHNTR- 301
Cdd:pfam17823 292 ARnpaAPMGAQAQgpiIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSvASTNLAVVTTTKAQAKEPSASPVPVLHTSMi 371
|
250
....*....|....*..
gi 1243938454 302 -----TTTWERPQPLPP 313
Cdd:pfam17823 372 peveaTSPTTQPSPLLP 388
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
390-455 |
5.05e-03 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 40.45 E-value: 5.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243938454 390 WEKRVDSTDRVYFVNHNTKTTQWEDPRTQGLPNEEPLPE-GWEIRYTREGVRYFVDHNTRTTTFKDP 455
Cdd:COG5104 17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVdPWKECRTADGKVYYYNSITRESRWKIP 83
|
|
| |
