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Conserved domains on  [gi|112734836|ref|NP_796301|]
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NEDD4-like E3 ubiquitin-protein ligase WWP1 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HUL4 super family cl34867
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
377-918 1.41e-176

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: 533.96  E-value: 1.41e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 377 QPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQF------NQRYLYSASMLAAEND- 449
Cdd:COG5021  297 LRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDlphqvgSNPFLEAHPEFSELLKn 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 450 -------PYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL-------------------PNEEPLPEGWEIRYT 503
Cdd:COG5021  377 qsrgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLgresdesfyvasnvqqqraSREGPLLSGWKTRLN 456
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 504 REGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNaLPSHVKINVSRQTLFEDSFQQIMAL 583
Cdd:COG5021  457 NLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDE 535
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 584 KPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMA 663
Cdd:COG5021  536 SGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKA 615
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 664 LFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNIL 743
Cdd:COG5021  616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 744 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE-VDLADWQRNTVYRHYTRNSK 822
Cdd:COG5021  696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSP 775
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 823 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 901
Cdd:COG5021  776 IIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKL 855
                        570
                 ....*....|....*..
gi 112734836 902 KEKLLFAIEETEGFGQE 918
Cdd:COG5021  856 RSKLLTAINEGAGFGLL 872
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
17-140 6.42e-56

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: 188.64  E-value: 6.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  17 RLQLKVTVSSAKLKRKKNWFGTAIYTEVIVDGE-VKKTAKSSSSSNPKWDEQLIVNVTPQTTLEFRVWSHHTLKADALLG 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQpPKKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKADVLLG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 112734836  96 KATVDLKQVLLTHNRKLEKVKEQLKLSLENKNGIVQTGELTVVLD 140
Cdd:cd04021   81 EASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
347-376 5.25e-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: 5.25e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 112734836  347 LPSGWEQRKDPHGRTYYVDHNTRTTTWERP 376
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
148-381 9.50e-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: 9.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  148 PVTNRSSSPPIEIQqNGDALHeNGDPATRT----------TPRLPVEGTIGIDNHVSTntVVPNSCCSHVVNGENTPSSP 217
Cdd:pfam17823 150 CRANASAAPRAAIA-AASAPH-AASPAPRTaassttaassTTAASSAPTTAASSAPAT--LTPARGISTAATATGHPAAG 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  218 SQVAARPKNAPAPKPVTSAptsdtVNGESSSVLADNTSTMGTLLPSEDTTSTSNctstttqepPVQEPPASSEHSECIPS 297
Cdd:pfam17823 226 TALAAVGNSSPAAGTVTAA-----VGTVTPAALATLAAAAGTVASAAGTINMGD---------PHARRLSPAKHMPSDTM 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  298 AS---AEVGPEAR---SLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQS-GNTNTEALPSGWEQRKDPHGRTYYVDHNTR- 369
Cdd:pfam17823 292 ARnpaAPMGAQAQgpiIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSvASTNLAVVTTTKAQAKEPSASPVPVLHTSMi 371
                         250
                  ....*....|....*..
gi 112734836  370 -----TTTWERPQPLPP 381
Cdd:pfam17823 372 peveaTSPTTQPSPLLP 388
 
Name Accession Description Interval E-value
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
377-918 1.41e-176

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 533.96  E-value: 1.41e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 377 QPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQF------NQRYLYSASMLAAEND- 449
Cdd:COG5021  297 LRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDlphqvgSNPFLEAHPEFSELLKn 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 450 -------PYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL-------------------PNEEPLPEGWEIRYT 503
Cdd:COG5021  377 qsrgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLgresdesfyvasnvqqqraSREGPLLSGWKTRLN 456
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 504 REGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNaLPSHVKINVSRQTLFEDSFQQIMAL 583
Cdd:COG5021  457 NLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDE 535
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 584 KPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMA 663
Cdd:COG5021  536 SGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKA 615
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 664 LFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNIL 743
Cdd:COG5021  616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 744 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE-VDLADWQRNTVYRHYTRNSK 822
Cdd:COG5021  696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSP 775
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 823 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 901
Cdd:COG5021  776 IIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKL 855
                        570
                 ....*....|....*..
gi 112734836 902 KEKLLFAIEETEGFGQE 918
Cdd:COG5021  856 RSKLLTAINEGAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
564-916 2.09e-169

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: 496.32  E-value: 2.09e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 564 KINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 643
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 644 TINPDHLSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVD 723
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 724 MEI-LGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE 802
Cdd:cd00078  162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 803 VDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMgsngpQKFCIEKVGK-DTWL 880
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDRL 316
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 112734836 881 PRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 916
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
587-915 7.35e-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: 468.25  E-value: 7.35e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836   587 DLR-RRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINP-ASTINPDHLSYFCFIGRFIAMAL 664
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPrSGFANEEHLSYFRFIGRVLGKAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836   665 FHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFS-VDMEILGKVTSHDLKLGGSNIL 743
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836   744 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSK 822
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836   823 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGsngpqKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 901
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
                          330
                   ....*....|....
gi 112734836   902 KEKLLFAIEETEGF 915
Cdd:smart00119 315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
613-916 7.65e-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: 366.55  E-value: 7.65e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  613 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDH--LSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIK 690
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  691 DLESIDTEFYNSLIWIR--DNNIEECgLEMYFSVDmeILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQ 768
Cdd:pfam00632  81 DLESIDPELYKSLKSLLnmDNDDDED-LGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  769 TKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVT 847
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112734836  848 GTCRLPLGGFAELmgsngpQKFCIEKVG--KDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 916
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 ...
17-140 6.42e-56

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: 188.64  E-value: 6.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  17 RLQLKVTVSSAKLKRKKNWFGTAIYTEVIVDGE-VKKTAKSSSSSNPKWDEQLIVNVTPQTTLEFRVWSHHTLKADALLG 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQpPKKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKADVLLG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 112734836  96 KATVDLKQVLLTHNRKLEKVKEQLKLSLENKNGIVQTGELTVVLD 140
Cdd:cd04021   81 EASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
347-376 5.25e-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: 5.25e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 112734836  347 LPSGWEQRKDPHGRTYYVDHNTRTTTWERP 376
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
347-378 2.50e-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: 2.50e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 112734836   347 LPSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 378
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
348-378 2.76e-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: 61.39  E-value: 2.76e-12
                         10        20        30
                 ....*....|....*....|....*....|.
gi 112734836 348 PSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 378
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
C2 pfam00168
C2 domain;
19-108 4.74e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 60.41  E-value: 4.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836   19 QLKVTVSSAKLKRKKNWFGTA-IYTEVIV--DGEVKKTAKSSSSSNPKWDEQLIVNVTP--QTTLEFRVWSHHTLKADAL 93
Cdd:pfam00168   2 RLTVTVIEAKNLPPKDGNGTSdPYVKVYLldGKQKKKTKVVKNTLNPVWNETFTFSVPDpeNAVLEIEVYDYDRFGRDDF 81
                          90
                  ....*....|....*
gi 112734836   94 LGKATVDLKQVLLTH 108
Cdd:pfam00168  82 IGEVRIPLSELDSGE 96
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
19-111 2.90e-10

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 57.88  E-value: 2.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836    19 QLKVTVSSAKLKRKKNWFGTA-IYTEVIVDG---EVKKTAKSSSSSNPKWDEQLIVNVTPQTT--LEFRVWSHHTLKADA 92
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSdPYVKVSLDGdpkEKKKTKVVKNTLNPVWNETFEFEVPPPELaeLEIEVYDKDRFGRDD 80
                           90
                   ....*....|....*....
gi 112734836    93 LLGKATVDLKQVLLTHNRK 111
Cdd:smart00239  81 FIGQVTIPLSDLLLGGRHE 99
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
148-381 9.50e-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: 9.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  148 PVTNRSSSPPIEIQqNGDALHeNGDPATRT----------TPRLPVEGTIGIDNHVSTntVVPNSCCSHVVNGENTPSSP 217
Cdd:pfam17823 150 CRANASAAPRAAIA-AASAPH-AASPAPRTaassttaassTTAASSAPTTAASSAPAT--LTPARGISTAATATGHPAAG 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  218 SQVAARPKNAPAPKPVTSAptsdtVNGESSSVLADNTSTMGTLLPSEDTTSTSNctstttqepPVQEPPASSEHSECIPS 297
Cdd:pfam17823 226 TALAAVGNSSPAAGTVTAA-----VGTVTPAALATLAAAAGTVASAAGTINMGD---------PHARRLSPAKHMPSDTM 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  298 AS---AEVGPEAR---SLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQS-GNTNTEALPSGWEQRKDPHGRTYYVDHNTR- 369
Cdd:pfam17823 292 ARnpaAPMGAQAQgpiIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSvASTNLAVVTTTKAQAKEPSASPVPVLHTSMi 371
                         250
                  ....*....|....*..
gi 112734836  370 -----TTTWERPQPLPP 381
Cdd:pfam17823 372 peveaTSPTTQPSPLLP 388
 
Name Accession Description Interval E-value
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
377-918 1.41e-176

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 533.96  E-value: 1.41e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 377 QPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQF------NQRYLYSASMLAAEND- 449
Cdd:COG5021  297 LRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDlphqvgSNPFLEAHPEFSELLKn 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 450 -------PYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL-------------------PNEEPLPEGWEIRYT 503
Cdd:COG5021  377 qsrgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLgresdesfyvasnvqqqraSREGPLLSGWKTRLN 456
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 504 REGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNaLPSHVKINVSRQTLFEDSFQQIMAL 583
Cdd:COG5021  457 NLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDE 535
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 584 KPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMA 663
Cdd:COG5021  536 SGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKA 615
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 664 LFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNIL 743
Cdd:COG5021  616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 744 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE-VDLADWQRNTVYRHYTRNSK 822
Cdd:COG5021  696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSP 775
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 823 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 901
Cdd:COG5021  776 IIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKL 855
                        570
                 ....*....|....*..
gi 112734836 902 KEKLLFAIEETEGFGQE 918
Cdd:COG5021  856 RSKLLTAINEGAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
564-916 2.09e-169

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: 496.32  E-value: 2.09e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 564 KINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 643
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 644 TINPDHLSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVD 723
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 724 MEI-LGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE 802
Cdd:cd00078  162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836 803 VDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMgsngpQKFCIEKVGK-DTWL 880
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDRL 316
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 112734836 881 PRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 916
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
587-915 7.35e-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: 468.25  E-value: 7.35e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836   587 DLR-RRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINP-ASTINPDHLSYFCFIGRFIAMAL 664
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPrSGFANEEHLSYFRFIGRVLGKAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836   665 FHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFS-VDMEILGKVTSHDLKLGGSNIL 743
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836   744 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSK 822
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836   823 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGsngpqKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 901
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
                          330
                   ....*....|....
gi 112734836   902 KEKLLFAIEETEGF 915
Cdd:smart00119 315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
613-916 7.65e-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: 366.55  E-value: 7.65e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  613 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDH--LSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIK 690
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  691 DLESIDTEFYNSLIWIR--DNNIEECgLEMYFSVDmeILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQ 768
Cdd:pfam00632  81 DLESIDPELYKSLKSLLnmDNDDDED-LGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  769 TKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVT 847
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112734836  848 GTCRLPLGGFAELmgsngpQKFCIEKVG--KDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 916
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 ...
17-140 6.42e-56

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: 188.64  E-value: 6.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  17 RLQLKVTVSSAKLKRKKNWFGTAIYTEVIVDGE-VKKTAKSSSSSNPKWDEQLIVNVTPQTTLEFRVWSHHTLKADALLG 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQpPKKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKADVLLG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 112734836  96 KATVDLKQVLLTHNRKLEKVKEQLKLSLENKNGIVQTGELTVVLD 140
Cdd:cd04021   81 EASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
347-376 5.25e-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: 5.25e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 112734836  347 LPSGWEQRKDPHGRTYYVDHNTRTTTWERP 376
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
379-408 1.80e-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: 1.80e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 112734836  379 LPPGWERRVDDRGRVYYVDHNTRTTTWQRP 408
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
347-378 2.50e-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: 2.50e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 112734836   347 LPSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 378
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
348-378 2.76e-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: 61.39  E-value: 2.76e-12
                         10        20        30
                 ....*....|....*....|....*....|.
gi 112734836 348 PSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 378
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
454-483 3.84e-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: 60.98  E-value: 3.84e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 112734836  454 LPPGWEKRVDSTDRVYFVNHNTKTTQWEDP 483
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
455-484 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 112734836 455 PPGWEKRVDSTDRVYFVNHNTKTTQWEDPR 484
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
453-484 1.82e-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: 59.15  E-value: 1.82e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 112734836   453 PLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPR 484
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
380-410 1.98e-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: 59.08  E-value: 1.98e-11
                         10        20        30
                 ....*....|....*....|....*....|.
gi 112734836 380 PPGWERRVDDRGRVYYVDHNTRTTTWQRPTM 410
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
20-116 2.12e-11

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.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 61.31  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  20 LKVTVSSAKLKRKKNWFGTA-IYTEVIVDGE-VKKTAKSSSSSNPKWDEQLIVNVTP--QTTLEFRVWSHHTLKADALLG 95
Cdd:cd00030    1 LRVTVIEARNLPAKDLNGKSdPYVKVSLGGKqKFKTKVVKNTLNPVWNETFEFPVLDpeSDTLTVEVWDKDRFSKDDFLG 80
                         90       100
                 ....*....|....*....|.
gi 112734836  96 KATVDLKQVLLTHNRKLEKVK 116
Cdd:cd00030   81 EVEIPLSELLDSGKEGELWLP 101
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
378-410 3.71e-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: 3.71e-11
                           10        20        30
                   ....*....|....*....|....*....|...
gi 112734836   378 PLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTM 410
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
C2 pfam00168
C2 domain;
19-108 4.74e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 60.41  E-value: 4.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836   19 QLKVTVSSAKLKRKKNWFGTA-IYTEVIV--DGEVKKTAKSSSSSNPKWDEQLIVNVTP--QTTLEFRVWSHHTLKADAL 93
Cdd:pfam00168   2 RLTVTVIEAKNLPPKDGNGTSdPYVKVYLldGKQKKKTKVVKNTLNPVWNETFTFSVPDpeNAVLEIEVYDYDRFGRDDF 81
                          90
                  ....*....|....*
gi 112734836   94 LGKATVDLKQVLLTH 108
Cdd:pfam00168  82 IGEVRIPLSELDSGE 96
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
19-111 2.90e-10

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 57.88  E-value: 2.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836    19 QLKVTVSSAKLKRKKNWFGTA-IYTEVIVDG---EVKKTAKSSSSSNPKWDEQLIVNVTPQTT--LEFRVWSHHTLKADA 92
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSdPYVKVSLDGdpkEKKKTKVVKNTLNPVWNETFEFEVPPPELaeLEIEVYDKDRFGRDD 80
                           90
                   ....*....|....*....
gi 112734836    93 LLGKATVDLKQVLLTHNRK 111
Cdd:smart00239  81 FIGQVTIPLSDLLLGGRHE 99
PRP40 COG5104
Splicing factor [RNA processing and modification];
346-408 2.36e-09

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 60.86  E-value: 2.36e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112734836 346 ALPSG-----WEQRKDPHGRTYYVDHNTRTTTWERPQPLPPGWERRVDD---------RGRVYYVDHNTRTTTWQRP 408
Cdd:COG5104    7 GMASGearseWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVdpwkecrtaDGKVYYYNSITRESRWKIP 83
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
495-524 2.19e-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: 2.19e-08
                         10        20        30
                 ....*....|....*....|....*....|
gi 112734836 495 PEGWEIRYTREGVRYFVDHNTRTTTFKDPR 524
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
493-525 3.15e-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: 49.91  E-value: 3.15e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 112734836   493 PLPEGWEIRYTREGVRYFVDHNTRTTTFKDPRN 525
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
494-523 1.71e-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: 1.71e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 112734836  494 LPEGWEIRYTREGVRYFVDHNTRTTTFKDP 523
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
148-381 9.50e-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: 9.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  148 PVTNRSSSPPIEIQqNGDALHeNGDPATRT----------TPRLPVEGTIGIDNHVSTntVVPNSCCSHVVNGENTPSSP 217
Cdd:pfam17823 150 CRANASAAPRAAIA-AASAPH-AASPAPRTaassttaassTTAASSAPTTAASSAPAT--LTPARGISTAATATGHPAAG 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  218 SQVAARPKNAPAPKPVTSAptsdtVNGESSSVLADNTSTMGTLLPSEDTTSTSNctstttqepPVQEPPASSEHSECIPS 297
Cdd:pfam17823 226 TALAAVGNSSPAAGTVTAA-----VGTVTPAALATLAAAAGTVASAAGTINMGD---------PHARRLSPAKHMPSDTM 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  298 AS---AEVGPEAR---SLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQS-GNTNTEALPSGWEQRKDPHGRTYYVDHNTR- 369
Cdd:pfam17823 292 ARnpaAPMGAQAQgpiIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSvASTNLAVVTTTKAQAKEPSASPVPVLHTSMi 371
                         250
                  ....*....|....*..
gi 112734836  370 -----TTTWERPQPLPP 381
Cdd:pfam17823 372 peveaTSPTTQPSPLLP 388
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
20-105 4.60e-05

C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. 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: 176016 [Multi-domain]  Cd Length: 125  Bit Score: 43.76  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  20 LKVTVSSAKLKRKKNWFG-TAIYTEVIVDGEVKKTAKSSSS--SNPKWDEQLIVNVTPQT------TLEFRVWSHHTLKA 90
Cdd:cd04051    2 LEITIISAEDLKNVNLFGkMKVYAVVWIDPSHKQSTPVDRDggTNPTWNETLRFPLDERLlqqgrlALTIEVYCERPSLG 81
                         90
                 ....*....|....*
gi 112734836  91 DALLGKATVDLKQVL 105
Cdd:cd04051   82 DKLIGEVRVPLKDLL 96
C2_fungal_Inn1p-like cd08681
C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 ...
41-105 3.08e-04

C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. The C2 domain of Inn1, located at the N-terminus, is required for ingression of the plasma membrane. The C-terminus is relatively unstructured and contains eight PXXP motifs that are thought to mediate interaction of Inn1 with other proteins with SH3 domains in the cytokinesis proteins Hof1 (an F-BAR protein) and Cyk3 (whose overexpression can restore primary septum formation in Inn1Delta cells) as well as recruiting Inn1 to the bud-neck by binding to Cyk3. Inn1 and Cyk3 appear to cooperate in activating chitin synthase Chs2 for primary septum formation, which allows coordination of actomyosin ring contraction with ingression of the cleavage furrow. It is thought that the C2 domain of Inn1 helps to preserve the link between the actomyosin ring and the plasma membrane, contributing both to membrane ingression, as well as to stability of the contracting ring. Additionally, Inn1 might induce curvature of the plasma membrane adjacent to the contracting ring, thereby promoting ingression of the membrane. It has been shown that the C2 domain of human synaptotagmin induces curvature in target membranes and thereby contributes to fusion of these membranes with synaptic vesicles. 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 synaptotagmin1. 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: 176063 [Multi-domain]  Cd Length: 118  Bit Score: 41.47  E-value: 3.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112734836  41 YTEVIVDGEVKKT-AKSSSSSNPKWDEQLIVNVTP--QTTLEFRVWsHHTLKADALLGKATVDLKQVL 105
Cdd:cd08681   25 YCVLRIGGVTKKTkTDFRGGQHPEWDEELRFEITEdkKPILKVAVF-DDDKRKPDLIGDTEVDLSPAL 91
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
52-137 3.92e-04

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. 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.


Pssm-ID: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 41.20  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  52 KTAKSSSSSNPKWDEQLIVNVTPQT-TLEFRVWSHHTLKADALLGKATVDLKqvLLTHNRKLEKVkeqLKLSLENKNGIV 130
Cdd:cd08678   34 QSSTQKNTSNPFWDEHFLFELSPNSkELLFEVYDNGKKSDSKFLGLAIVPFD--ELRKNPSGRQI---FPLQGRPYEGDS 108

                 ....*..
gi 112734836 131 QTGELTV 137
Cdd:cd08678  109 VSGSITV 115
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
20-85 4.37e-04

C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 domain is found in Smurf proteins, C2-WW-HECT-domain E3s, which play an important role in the downregulation of the TGF-beta signaling pathway. Smurf proteins also regulate cell shape, motility, and polarity by degrading small guanosine triphosphatases (GTPases). 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. Members here have type-II topology.


Pssm-ID: 176028 [Multi-domain]  Cd Length: 123  Bit Score: 41.14  E-value: 4.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112734836  20 LKVTVSSAKLKRKKNWFGTA-IYTEVIVDGE-VKKTAKSSSSSNPKWDEQLIVNVTPQTTLEFRVWSH 85
Cdd:cd08382    2 VRLTVLCADGLAKRDLFRLPdPFAVITVDGGqTHSTDVAKKTLDPKWNEHFDLTVGPSSIITIQVFDQ 69
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
20-105 1.27e-03

C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. 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. This cd contains either the first or third repeat in Synaptotagmin-like proteins with a type-I topology.


Pssm-ID: 176037 [Multi-domain]  Cd Length: 121  Bit Score: 39.58  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  20 LKVTVSSAK-LKRKKNWFGTAI------YTEVIVDGEVKKTAKSSSSSNPKWDE--QLIVNVTPQTTLEFRVWSHHTLKA 90
Cdd:cd08391    3 LRIHVIEAQdLVAKDKFVGGLVkgksdpYVIVRVGAQTFKSKVIKENLNPKWNEvyEAVVDEVPGQELEIELFDEDPDKD 82
                         90
                 ....*....|....*
gi 112734836  91 DAlLGKATVDLKQVL 105
Cdd:cd08391   83 DF-LGRLSIDLGSVE 96
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
20-117 2.20e-03

C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (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.


Pssm-ID: 176003 [Multi-domain]  Cd Length: 145  Bit Score: 39.62  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734836  20 LKVTVSSAKLKRKKNWFGTAIYTEVIVDGEVKKTAKSSSSSNPKWDEQLIVNVT-PQTTLEFRVWSHHTLKADALLGKAT 98
Cdd:cd04038    4 LKVRVVRGTNLAVRDFTSSDPYVVLTLGNQKVKTRVIKKNLNPVWNEELTLSVPnPMAPLKLEVFDKDTFSKDDSMGEAE 83
                         90       100
                 ....*....|....*....|...
gi 112734836  99 VDLKQVL----LTHNRKLEKVKE 117
Cdd:cd04038   84 IDLEPLVeaakLDHLRDTPGGTQ 106
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
61-105 4.05e-03

C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive proteins are triggered in response to specific elicitor molecules such as glycolproteins, peptides, carbohydrates and lipids. A host of defensive responses are also triggered resulting in localized cell death. Antimicrobial secondary metabolites, such as phytoalexins, or defense-related proteins, including pathogenesis-related (PR) proteins are also produced. There is a single C2 domain present here. 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. Members have a type-II topology.


Pssm-ID: 176014 [Multi-domain]  Cd Length: 124  Bit Score: 38.08  E-value: 4.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 112734836  61 NPKWDEQLIVNV-----TPQTTLEFRVWSHHTLKADALLGKATVDLKQVL 105
Cdd:cd04049   46 NPEWNEKFKFTVeypgwGGDTKLILRIMDKDNFSDDDFIGEATIHLKGLF 95
C2_KIAA0528-like cd08688
C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the ...
41-106 4.11e-03

C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the Human KIAA0528 cDNA clone. All members here contain a single C2 repeat. No other information on this protein is currently known. 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.


Pssm-ID: 176070 [Multi-domain]  Cd Length: 110  Bit Score: 37.67  E-value: 4.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 112734836  41 YTEVIVDGEVKKTAKSSSSSNPKW----------DEQLIVNVtpqttLEFRVWSHHTLKADALLGKATVDLKQVLL 106
Cdd:cd08688   24 FVEVKFGSTTYKTDVVKKSLNPVWnsewfrfevdDEELQDEP-----LQIRVMDHDTYSANDAIGKVYIDLNPLLL 94
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
43-105 5.21e-03

C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176019 [Multi-domain]  Cd Length: 127  Bit Score: 38.00  E-value: 5.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112734836  43 EVIVDGEVKKTAKSSSSSNPKWDEQLIVNVT----PQTTLEFRVWSHHTLKADALLGKATVDLKQVL 105
Cdd:cd08373   20 KVTFRGVKKKTRVLENELNPVWNETFEWPLAgspdPDESLEIVVKDYEKVGRNRLIGSATVSLQDLV 86
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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