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Conserved domains on  [gi|2462581743|ref|XP_054180078|]
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E3 ubiquitin-protein ligase Itchy homolog isoform X3 [Homo sapiens]

Protein Classification

WW and HECTc domain-containing protein( domain architecture ID 13102327)

protein containing domains C2, WW, and HECTc

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];
249-793 0e+00

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: 557.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 249 PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIYGNQDLFATS-QSKEFD-- 325
Cdd:COG5021   298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFLEAHPeFSELLKnq 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 326 ------PLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQG-------------------QLNEKPLPEGWEMRFTV 380
Cdd:COG5021   378 srgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQlgresdesfyvasnvqqqrASREGPLLSGWKTRLNN 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 381 DGIPYFVDHNRRTTTYIDPRTG-KSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQhIKITVTRKTLFEDSFQQIMSFS 459
Cdd:COG5021   458 LYRFYFVEHRKKTLTKNDSRLGsFISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY-LHIKVRRDRVFEDSYREIMDES 536

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 460 PQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMAL 539
Cdd:COG5021   537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 540 FHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSVDKEILGEIKSHDLKPNGGNILV 619
Cdd:COG5021   617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 620 TEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQE-IDLNDWQRHAIYRHYARTSKQ 698
Cdd:COG5021   697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 699 IMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVG-KENWLPRSHTCFNRLDLPPYKSYEQLK 777
Cdd:COG5021   777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                         570
                  ....*....|....*.
gi 2462581743 778 EKLLFAIEETEGFGQE 793
Cdd:COG5021   857 SKLLTAINEGAGFGLL 872
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 218-247 5.82e-11

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: 57.51  E-value: 5.82e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462581743 218 LPPGWEQRVDQHGRVYYVDHVEKRTTWDRP 247
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 1-30 9.56e-03

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: 36.87  E-value: 9.56e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462581743   1 MKLEEVVVTLQL-GGDKEPTETIGDLSICLD 30
Cdd:cd04021    95 GKLENVKLTLNLsSENKGSSVKVGELTVILD 125
 
Name Accession Description Interval E-value
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
249-793 0e+00

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 557.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 249 PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIYGNQDLFATS-QSKEFD-- 325
Cdd:COG5021   298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFLEAHPeFSELLKnq 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 326 ------PLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQG-------------------QLNEKPLPEGWEMRFTV 380
Cdd:COG5021   378 srgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQlgresdesfyvasnvqqqrASREGPLLSGWKTRLNN 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 381 DGIPYFVDHNRRTTTYIDPRTG-KSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQhIKITVTRKTLFEDSFQQIMSFS 459
Cdd:COG5021   458 LYRFYFVEHRKKTLTKNDSRLGsFISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY-LHIKVRRDRVFEDSYREIMDES 536

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 460 PQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMAL 539
Cdd:COG5021   537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 540 FHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSVDKEILGEIKSHDLKPNGGNILV 619
Cdd:COG5021   617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 620 TEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQE-IDLNDWQRHAIYRHYARTSKQ 698
Cdd:COG5021   697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 699 IMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVG-KENWLPRSHTCFNRLDLPPYKSYEQLK 777
Cdd:COG5021   777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                         570
                  ....*....|....*.
gi 2462581743 778 EKLLFAIEETEGFGQE 793
Cdd:COG5021   857 SKLLTAINEGAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 438-791 8.90e-174

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: 503.64  E-value: 8.90e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 438 IKITVTRKTLFEDSFQQIMSFSPQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPA 517
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 518 SYINPDHLKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSV 597
Cdd:cd00078    81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 598 DKEI-LGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQ 676
Cdd:cd00078   161 ELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 677 EIDLNDWQRHAIYRH-YARTSKQIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMgsngpQKFCIEKVGK-ENW 754
Cdd:cd00078   241 DIDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDR 315

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2462581743 755 LPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 791
Cdd:cd00078   316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 462-790 3.56e-161

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: 470.18  E-value: 3.56e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743  462 DLR-RRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAgKDNYCLQINPASYI-NPDHLKYFRFIGRFIAMAL 539
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743  540 FHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFS-VDKEILGEIKSHDLKPNGGNIL 618
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743  619 VTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRH-YARTSK 697
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743  698 QIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGsngpqKFCIEKVG-KENWLPRSHTCFNRLDLPPYKSYEQL 776
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 2462581743  777 KEKLLFAIEETEGF 790
Cdd:smart00119 315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 488-791 1.54e-126

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 380.42  E-value: 1.54e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 488 FLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDH--LKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLK 565
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 566 DLESIDPEFYNSLIWVKE-NNIEECDLEMYFSVDkeILGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQT 644
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 645 QAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRH-YARTSKQIMWFWQFVKEIDNEKRMRLLQFVTG 723
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 724 TCRLPVGGFADLmgsngpQKFCIEKVG--KENWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 791
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 218-247 5.82e-11

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: 57.51  E-value: 5.82e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462581743 218 LPPGWEQRVDQHGRVYYVDHVEKRTTWDRP 247
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 217-249 1.39e-10

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 56.46  E-value: 1.39e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462581743  217 PLPPGWEQRVDQHGRVYYVDHVEKRTTWDRPEP 249
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 219-249 4.18e-10

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 55.23  E-value: 4.18e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462581743 219 PPGWEQRVDQHGRVYYVDHVEKRTTWDRPEP 249
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 1-30 9.56e-03

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: 36.87  E-value: 9.56e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462581743   1 MKLEEVVVTLQL-GGDKEPTETIGDLSICLD 30
Cdd:cd04021    95 GKLENVKLTLNLsSENKGSSVKVGELTVILD 125
 
Name Accession Description Interval E-value
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
249-793 0e+00

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 557.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 249 PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIYGNQDLFATS-QSKEFD-- 325
Cdd:COG5021   298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFLEAHPeFSELLKnq 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 326 ------PLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQG-------------------QLNEKPLPEGWEMRFTV 380
Cdd:COG5021   378 srgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQlgresdesfyvasnvqqqrASREGPLLSGWKTRLNN 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 381 DGIPYFVDHNRRTTTYIDPRTG-KSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQhIKITVTRKTLFEDSFQQIMSFS 459
Cdd:COG5021   458 LYRFYFVEHRKKTLTKNDSRLGsFISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY-LHIKVRRDRVFEDSYREIMDES 536

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 460 PQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMAL 539
Cdd:COG5021   537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 540 FHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSVDKEILGEIKSHDLKPNGGNILV 619
Cdd:COG5021   617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 620 TEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQE-IDLNDWQRHAIYRHYARTSKQ 698
Cdd:COG5021   697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 699 IMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVG-KENWLPRSHTCFNRLDLPPYKSYEQLK 777
Cdd:COG5021   777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                         570
                  ....*....|....*.
gi 2462581743 778 EKLLFAIEETEGFGQE 793
Cdd:COG5021   857 SKLLTAINEGAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 438-791 8.90e-174

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: 503.64  E-value: 8.90e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 438 IKITVTRKTLFEDSFQQIMSFSPQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPA 517
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 518 SYINPDHLKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSV 597
Cdd:cd00078    81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 598 DKEI-LGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQ 676
Cdd:cd00078   161 ELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 677 EIDLNDWQRHAIYRH-YARTSKQIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMgsngpQKFCIEKVGK-ENW 754
Cdd:cd00078   241 DIDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDR 315

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2462581743 755 LPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 791
Cdd:cd00078   316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 462-790 3.56e-161

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: 470.18  E-value: 3.56e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743  462 DLR-RRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAgKDNYCLQINPASYI-NPDHLKYFRFIGRFIAMAL 539
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743  540 FHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFS-VDKEILGEIKSHDLKPNGGNIL 618
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743  619 VTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRH-YARTSK 697
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743  698 QIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGsngpqKFCIEKVG-KENWLPRSHTCFNRLDLPPYKSYEQL 776
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 2462581743  777 KEKLLFAIEETEGF 790
Cdd:smart00119 315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 488-791 1.54e-126

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 380.42  E-value: 1.54e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 488 FLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDH--LKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLK 565
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 566 DLESIDPEFYNSLIWVKE-NNIEECDLEMYFSVDkeILGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQT 644
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 645 QAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRH-YARTSKQIMWFWQFVKEIDNEKRMRLLQFVTG 723
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 724 TCRLPVGGFADLmgsngpQKFCIEKVG--KENWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 791
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 330-359 1.68e-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: 64.83  E-value: 1.68e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462581743 330 LPPGWEKRTDSNGRVYFVNHNTRITQWEDP 359
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 331-360 3.52e-13

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: 64.09  E-value: 3.52e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462581743 331 PPGWEKRTDSNGRVYFVNHNTRITQWEDPR 360
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 329-361 3.85e-13

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: 63.77  E-value: 3.85e-13
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462581743  329 PLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRS 361
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 218-247 5.82e-11

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: 57.51  E-value: 5.82e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462581743 218 LPPGWEQRVDQHGRVYYVDHVEKRTTWDRP 247
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 250-279 8.03e-11

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: 57.13  E-value: 8.03e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462581743 250 LPPGWERRVDNMGRIYYVDHFTRTTTWQRP 279
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 217-249 1.39e-10

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 56.46  E-value: 1.39e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462581743  217 PLPPGWEQRVDQHGRVYYVDHVEKRTTWDRPEP 249
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 251-281 1.82e-10

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 56.38  E-value: 1.82e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462581743 251 PPGWERRVDNMGRIYYVDHFTRTTTWQRPTL 281
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 249-281 2.50e-10

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: 55.68  E-value: 2.50e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462581743  249 PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTL 281
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 219-249 4.18e-10

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 55.23  E-value: 4.18e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462581743 219 PPGWEQRVDQHGRVYYVDHVEKRTTWDRPEP 249
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 369-400 3.02e-09

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: 52.60  E-value: 3.02e-09
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462581743  369 PLPEGWEMRFTVDGIPYFVDHNRRTTTYIDPR 400
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 371-400 2.24e-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: 50.22  E-value: 2.24e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462581743 371 PEGWEMRFTVDGIPYFVDHNRRTTTYIDPR 400
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 370-399 7.23e-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: 45.96  E-value: 7.23e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462581743 370 LPEGWEMRFTVDGIPYFVDHNRRTTTYIDP 399
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
PRP40 COG5104
Splicing factor [RNA processing and modification];
222-299 9.04e-07

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 52.39  E-value: 9.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462581743 222 WEQRVDQHGRVYYVDHVEKRTTWDRPEPLPPGWERRVDNM---------GRIYYVDHFTRTTTWQRPTLESVRN--YEQW 290
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDpwkecrtadGKVYYYNSITRESRWKIPPERKKVEpiAEQK 96


                  ....*....
gi 2462581743 291 QLQRSQLQG 299
Cdd:COG5104    97 HDERSMIGG 105
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 1-30 9.56e-03

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: 36.87  E-value: 9.56e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462581743   1 MKLEEVVVTLQL-GGDKEPTETIGDLSICLD 30
Cdd:cd04021    95 GKLENVKLTLNLsSENKGSSVKVGELTVILD 125
 
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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