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Conserved domains on  [gi|380420338|ref|NP_001244067|]
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E3 ubiquitin-protein ligase Itchy homolog isoform 3 [Homo sapiens]

Protein Classification

synaptotagmin family protein; RIM/PCLO family C2 domain-containing protein( domain architecture ID 13102327)

synaptotagmin family protein is a membrane-trafficking protein characterized by an N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains; similar to synaptotagmins 4 and 11, which do not bind calcium| RIM (Rab-3-interacting molecule)/PCLO (protein piccolo) family C2 domain-containing protein

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];
208-752 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: 555.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 208 PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIYGNQDLFATS-QSKEFD-- 284
Cdd:COG5021  298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFLEAHPeFSELLKnq 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 285 ------PLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQG-------------------QLNEKPLPEGWEMRFTV 339
Cdd:COG5021  378 srgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQlgresdesfyvasnvqqqrASREGPLLSGWKTRLNN 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 340 DGIPYFVDHNRRTTTYIDPRTG-KSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQhIKITVTRKTLFEDSFQQIMSFS 418
Cdd:COG5021  458 LYRFYFVEHRKKTLTKNDSRLGsFISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY-LHIKVRRDRVFEDSYREIMDES 536

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 419 PQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMAL 498
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 499 FHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSVDKEILGEIKSHDLKPNGGNILV 578
Cdd:COG5021  617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 579 TEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQE-IDLNDWQRHAIYRHYARTSKQ 657
Cdd:COG5021  697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 658 IMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVG-KENWLPRSHTCFNRLDLPPYKSYEQLK 736
Cdd:COG5021  777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                        570
                 ....*....|....*.
gi 380420338 737 EKLLFAIEETEGFGQE 752
Cdd:COG5021  857 SKLLTAINEGAGFGLL 872
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 177-206 9.27e-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: 9.27e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 380420338  177 LPPGWEQRVDQHGRVYYVDHVEKRTTWDRP 206
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 9.02e-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: 9.02e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 380420338   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];
208-752 0e+00

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 555.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 208 PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIYGNQDLFATS-QSKEFD-- 284
Cdd:COG5021  298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFLEAHPeFSELLKnq 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 285 ------PLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQG-------------------QLNEKPLPEGWEMRFTV 339
Cdd:COG5021  378 srgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQlgresdesfyvasnvqqqrASREGPLLSGWKTRLNN 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 340 DGIPYFVDHNRRTTTYIDPRTG-KSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQhIKITVTRKTLFEDSFQQIMSFS 418
Cdd:COG5021  458 LYRFYFVEHRKKTLTKNDSRLGsFISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY-LHIKVRRDRVFEDSYREIMDES 536

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 419 PQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMAL 498
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 499 FHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSVDKEILGEIKSHDLKPNGGNILV 578
Cdd:COG5021  617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 579 TEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQE-IDLNDWQRHAIYRHYARTSKQ 657
Cdd:COG5021  697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 658 IMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVG-KENWLPRSHTCFNRLDLPPYKSYEQLK 736
Cdd:COG5021  777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                        570
                 ....*....|....*.
gi 380420338 737 EKLLFAIEETEGFGQE 752
Cdd:COG5021  857 SKLLTAINEGAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 397-750 1.14e-173

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 501.71  E-value: 1.14e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 397 IKITVTRKTLFEDSFQQIMSFSPQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPA 476
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 477 SYINPDHLKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSV 556
Cdd:cd00078   81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 557 DKEI-LGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQ 635
Cdd:cd00078  161 ELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 636 EIDLNDWQRHAIYRH-YARTSKQIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMgsngpQKFCIEKVGK-ENW 713
Cdd:cd00078  241 DIDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDR 315

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 380420338 714 LPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 750
Cdd:cd00078  316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 421-749 6.49e-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: 468.25  E-value: 6.49e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338   421 DLR-RRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAgKDNYCLQINPASYI-NPDHLKYFRFIGRFIAMAL 498
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338   499 FHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFS-VDKEILGEIKSHDLKPNGGNIL 577
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338   578 VTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRH-YARTSK 656
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338   657 QIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGsngpqKFCIEKVG-KENWLPRSHTCFNRLDLPPYKSYEQL 735
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 380420338   736 KEKLLFAIEETEGF 749
Cdd:smart00119 315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 447-750 1.33e-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: 379.26  E-value: 1.33e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338  447 FLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDH--LKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLK 524
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338  525 DLESIDPEFYNSLIWVKE-NNIEECDLEMYFSVDkeILGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQT 603
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338  604 QAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRH-YARTSKQIMWFWQFVKEIDNEKRMRLLQFVTG 682
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338  683 TCRLPVGGFADLmgsngpQKFCIEKVG--KENWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 750
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 177-206 9.27e-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: 9.27e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 380420338  177 LPPGWEQRVDQHGRVYYVDHVEKRTTWDRP 206
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 176-208 2.17e-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: 56.07  E-value: 2.17e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 380420338   176 PLPPGWEQRVDQHGRVYYVDHVEKRTTWDRPEP 208
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 178-208 6.73e-10

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 54.46  E-value: 6.73e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 380420338 178 PPGWEQRVDQHGRVYYVDHVEKRTTWDRPEP 208
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 9.02e-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: 9.02e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 380420338   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];
208-752 0e+00

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 555.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 208 PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIYGNQDLFATS-QSKEFD-- 284
Cdd:COG5021  298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFLEAHPeFSELLKnq 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 285 ------PLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQG-------------------QLNEKPLPEGWEMRFTV 339
Cdd:COG5021  378 srgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQlgresdesfyvasnvqqqrASREGPLLSGWKTRLNN 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 340 DGIPYFVDHNRRTTTYIDPRTG-KSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQhIKITVTRKTLFEDSFQQIMSFS 418
Cdd:COG5021  458 LYRFYFVEHRKKTLTKNDSRLGsFISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY-LHIKVRRDRVFEDSYREIMDES 536

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 419 PQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMAL 498
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 499 FHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSVDKEILGEIKSHDLKPNGGNILV 578
Cdd:COG5021  617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 579 TEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQE-IDLNDWQRHAIYRHYARTSKQ 657
Cdd:COG5021  697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 658 IMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVG-KENWLPRSHTCFNRLDLPPYKSYEQLK 736
Cdd:COG5021  777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                        570
                 ....*....|....*.
gi 380420338 737 EKLLFAIEETEGFGQE 752
Cdd:COG5021  857 SKLLTAINEGAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 397-750 1.14e-173

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 501.71  E-value: 1.14e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 397 IKITVTRKTLFEDSFQQIMSFSPQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPA 476
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 477 SYINPDHLKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSV 556
Cdd:cd00078   81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 557 DKEI-LGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQ 635
Cdd:cd00078  161 ELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 636 EIDLNDWQRHAIYRH-YARTSKQIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMgsngpQKFCIEKVGK-ENW 713
Cdd:cd00078  241 DIDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDR 315

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 380420338 714 LPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 750
Cdd:cd00078  316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 421-749 6.49e-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: 468.25  E-value: 6.49e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338   421 DLR-RRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAgKDNYCLQINPASYI-NPDHLKYFRFIGRFIAMAL 498
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338   499 FHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFS-VDKEILGEIKSHDLKPNGGNIL 577
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338   578 VTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRH-YARTSK 656
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338   657 QIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGsngpqKFCIEKVG-KENWLPRSHTCFNRLDLPPYKSYEQL 735
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 380420338   736 KEKLLFAIEETEGF 749
Cdd:smart00119 315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 447-750 1.33e-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: 379.26  E-value: 1.33e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338  447 FLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDH--LKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLK 524
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338  525 DLESIDPEFYNSLIWVKE-NNIEECDLEMYFSVDkeILGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQT 603
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338  604 QAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRH-YARTSKQIMWFWQFVKEIDNEKRMRLLQFVTG 682
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338  683 TCRLPVGGFADLmgsngpQKFCIEKVG--KENWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 750
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 289-318 2.87e-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: 64.06  E-value: 2.87e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 380420338  289 LPPGWEKRTDSNGRVYFVNHNTRITQWEDP 318
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 290-319 6.37e-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: 62.93  E-value: 6.37e-13
                         10        20        30
                 ....*....|....*....|....*....|
gi 380420338 290 PPGWEKRTDSNGRVYFVNHNTRITQWEDPR 319
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 288-320 6.43e-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: 63.00  E-value: 6.43e-13
                           10        20        30
                   ....*....|....*....|....*....|...
gi 380420338   288 PLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRS 320
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 177-206 9.27e-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: 9.27e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 380420338  177 LPPGWEQRVDQHGRVYYVDHVEKRTTWDRP 206
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 209-238 1.28e-10

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: 56.36  E-value: 1.28e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 380420338  209 LPPGWERRVDNMGRIYYVDHFTRTTTWQRP 238
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 176-208 2.17e-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: 56.07  E-value: 2.17e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 380420338   176 PLPPGWEQRVDQHGRVYYVDHVEKRTTWDRPEP 208
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 210-240 3.08e-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: 55.61  E-value: 3.08e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 380420338 210 PPGWERRVDNMGRIYYVDHFTRTTTWQRPTL 240
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 208-240 3.94e-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: 55.30  E-value: 3.94e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 380420338   208 PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTL 240
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 178-208 6.73e-10

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 54.46  E-value: 6.73e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 380420338 178 PPGWEQRVDQHGRVYYVDHVEKRTTWDRPEP 208
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 328-359 4.67e-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: 52.22  E-value: 4.67e-09
                           10        20        30
                   ....*....|....*....|....*....|..
gi 380420338   328 PLPEGWEMRFTVDGIPYFVDHNRRTTTYIDPR 359
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 330-359 3.60e-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: 49.45  E-value: 3.60e-08
                         10        20        30
                 ....*....|....*....|....*....|
gi 380420338 330 PEGWEMRFTVDGIPYFVDHNRRTTTYIDPR 359
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 329-358 1.04e-06

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: 45.57  E-value: 1.04e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 380420338  329 LPEGWEMRFTVDGIPYFVDHNRRTTTYIDP 358
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
PRP40 COG5104
Splicing factor [RNA processing and modification];
181-258 1.50e-06

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 51.62  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380420338 181 WEQRVDQHGRVYYVDHVEKRTTWDRPEPLPPGWERRVDNM---------GRIYYVDHFTRTTTWQRPTLESVRN--YEQW 249
Cdd:COG5104   17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDpwkecrtadGKVYYYNSITRESRWKIPPERKKVEpiAEQK 96


                 ....*....
gi 380420338 250 QLQRSQLQG 258
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 9.02e-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: 9.02e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 380420338   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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