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Conserved domains on  [gi|1034654642|ref|XP_016867373|]
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E3 ubiquitin-protein ligase HECW1 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
1282-1636 2.26e-160

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: 490.54  E-value: 2.26e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1282 IKLIIRRDHLLEGTFNQVMAYSRKELqRNKLYVTFVGEEGLDYSGPSREFFFLLSQELFNPYYGLFEYSANDTYTVQISP 1361
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDL-KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1362 MSAFVENHLEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRLPCDLSDLEYLDEEFHQSLQWMKDNNI-TDILDLTFT 1440
Cdd:cd00078     80 SSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGdEDDLELTFT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1441 VNEEV-FGQVTERELKSGGANTQVTEKNKKEYIERMVKWRVERGVVQQTEALVRGFYEVVDSRLVSVFDARELELVIAGT 1519
Cdd:cd00078    160 IELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1520 AEIDLNDWRNNTEYRGGYHDGHLVIRWFWAAVERFNNEQRLRLLQFVTGTSSVPYEGFAALRgsnglRRFCIEKWGK-IT 1598
Cdd:cd00078    240 EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDD 314
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1034654642 1599 SLPRAHTCFNRLDLPPYPSYSMLYEKLLTAVEETSTFG 1636
Cdd:cd00078    315 RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
C2_NEDL1-like cd08691
C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 ...
237-373 4.36e-87

C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1)) is a newly identified HECT-type E3 ubiquitin protein ligase highly expressed in favorable neuroblastomas. In vertebrates it is found primarily in neuronal tissues, including the spinal cord. NEDL1 is thought to normally function in the quality control of cellular proteins by eliminating misfolded proteins. This is thought to be accomplished via a mechanism analogous to that of ER-associated degradation by forming tight complexes and aggregating misfolded proteins that have escaped ubiquitin-mediated degradation. NEDL1, is composed of a C2 domain, two WW domains, and a ubiquitin ligase Hect 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: 176073 [Multi-domain]  Cd Length: 137  Bit Score: 279.67  E-value: 4.36e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  237 ISFSLSDFQAMGLKKGMFFNPDPYLKISIQPGKHSIFPALPHHGQERRSKIIGNTVNPIWQAEQFSFVSLPTDVLEIEVK 316
Cdd:cd08691      1 LSFSLSGLQARNLKKGMFFNPDPYVKISIQPGKRHIFPALPHHGQECRTSIVENTINPVWHREQFVFVGLPTDVLEIEVK 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654642  317 DKFAKSRPIIKRFLGKLSMPVQRLLERHAIGDRVVSYTLGRRLPTDHVSGQLQFRFE 373
Cdd:cd08691     81 DKFAKSRPIIRRFLGKLSIPVQRLLERHAIGDQELSYTLGRRTPTDHVSGQLTFRFE 137
HECW_N pfam16562
N-terminal domain of E3 ubiquitin-protein ligase HECW1 and 2; HECW_N is a domain on E3 ...
97-214 8.49e-69

N-terminal domain of E3 ubiquitin-protein ligase HECW1 and 2; HECW_N is a domain on E3 ubiquitin-protein ligases that lies upstream of the C2 domain; its function is not clearly understood, except perhaps to determine the substrate spectrum of the ligase.


:

Pssm-ID: 465177  Cd Length: 118  Bit Score: 226.58  E-value: 8.49e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642   97 RSTSDTDLVTSDSRSTLMVSSSYYSIGHSQDLVIHWDIKEEVDAGDWIGMYLIDEVLSENFLDYKNRGVNGSHRGQIIWK 176
Cdd:pfam16562    1 RANSDTDLVTSQSRSSLTVSTYEYTLGQGQSLIISWDIKEEVDANDWIGLYHIDENSPANFWDYKNRGVNGTQKGQIVWR 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034654642  177 IDASSYFVEPETKICFKYYHGVSGALRATTPSVTVKNS 214
Cdd:pfam16562   81 IDPSPYFMEAETKICFKYYHGTSGALRATTPSITVKNP 118
HECW1_helix pfam18436
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids ...
980-1046 6.53e-37

Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids found in HECW1 proteins in Eukaryotes.Polymorphisms in the same region in the C.elegans homolog affects C. elegans behavioural avoidance of a lawn of Pseudomonas aeruginosa.


:

Pssm-ID: 465766  Cd Length: 67  Bit Score: 133.39  E-value: 6.53e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654642  980 LLLQSPAVKFITNPEFFTVLHANYSAYRVFTSSTCLKHMILKVRRDARNFERYQHNRDLVNFINMFA 1046
Cdd:pfam18436    1 ALLNSPAVKFITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
863-892 1.58e-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: 57.13  E-value: 1.58e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034654642  863 LPPNWEARIDSHGRVFYVDHVNRTTTWQRP 892
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
1052-1083 6.68e-06

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: 44.13  E-value: 6.68e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1034654642  1052 LPRGWEIKTDQQGKSFFVDHNSRATTFIDPRI 1083
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03169 super family cl27451
hypothetical protein; Provisional
406-530 2.16e-03

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  406 ESGSGEPRSEAPESSESWKPEQLGEGSVPDGPGNQSIElsRPAEEAAVITEAGDQGMVSVGPEGAGELLAQVQKDIQPAP 485
Cdd:PHA03169    92 PSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPE--SPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034654642  486 SAEELAEQldlGEEASALLLEDGEAPASTKE--------EPLEEEATTQSRAG 530
Cdd:PHA03169   170 SHEDSPEE---PEPPTSEPEPDSPGPPQSETptsspppqSPPDEPGEPQSPTP 219
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
1282-1636 2.26e-160

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: 490.54  E-value: 2.26e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1282 IKLIIRRDHLLEGTFNQVMAYSRKELqRNKLYVTFVGEEGLDYSGPSREFFFLLSQELFNPYYGLFEYSANDTYTVQISP 1361
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDL-KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1362 MSAFVENHLEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRLPCDLSDLEYLDEEFHQSLQWMKDNNI-TDILDLTFT 1440
Cdd:cd00078     80 SSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGdEDDLELTFT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1441 VNEEV-FGQVTERELKSGGANTQVTEKNKKEYIERMVKWRVERGVVQQTEALVRGFYEVVDSRLVSVFDARELELVIAGT 1519
Cdd:cd00078    160 IELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1520 AEIDLNDWRNNTEYRGGYHDGHLVIRWFWAAVERFNNEQRLRLLQFVTGTSSVPYEGFAALRgsnglRRFCIEKWGK-IT 1598
Cdd:cd00078    240 EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDD 314
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1034654642 1599 SLPRAHTCFNRLDLPPYPSYSMLYEKLLTAVEETSTFG 1636
Cdd:cd00078    315 RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1306-1635 2.08e-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: 487.13  E-value: 2.08e-159
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  1306 ELQRNKLYVTFVGEEGLDYSGPSREFFFLLSQELFNPYYGLFEYSANDtYTVQISPMSAF-VENHLEWFRFSGRILGLAL 1384
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  1385 IHQYLLDAFFTRPFYKALLRLPCDLSDLEYLDEEFHQSLQWMK-DNNITDILDLTFTVNE-EVFGQVTERELKSGGANTQ 1462
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLlNNDTSEELDLTFSIVLtSEFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  1463 VTEKNKKEYIERMVKWRVERGVVQQTEALVRGFYEVVDSRLVSVFDARELELVIAGTAEIDLNDWRNNTEYRGGYHDGHL 1542
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  1543 VIRWFWAAVERFNNEQRLRLLQFVTGTSSVPYEGFAALRGSnglrrFCIEKWG-KITSLPRAHTCFNRLDLPPYPSYSML 1621
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 1034654642  1622 YEKLLTAVEETSTF 1635
Cdd:smart00119  315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1041-1638 4.97e-130

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 427.65  E-value: 4.97e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1041 FINMFADTRLELPRGWEIKTDQQGKSFFVDHNSRATTFI--DPRIPLQNGRLPNHL-THRQHLQRLR---------SYSA 1108
Cdd:COG5021    288 SHSSFEDSLLRLNSLFSTRADSFGRTYYLDHDRILTQYSrpLLEETLGESTSFLVVnNDDSSSIKDLphqvgsnpfLEAH 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1109 GEASEVSRNRGaSLLARPGHSLVAAIRSQHQHESLPLayndKIVAFLRQpnifemlqerqpSLARNhTLREkiHYIRTEG 1188
Cdd:COG5021    368 PEFSELLKNQS-RGTTRDFRNKPTGWSSSIEDLGQFL----FSDFLTSS------------STYED-LRRE--QLGRESD 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1189 NHGLEKLSCDADLVILLSLFEEEIMSYVPLQAAFHPGYSFSPRCSPCSSPQNSPGLQRASarapsPYRRDFEAKLRNFYR 1268
Cdd:COG5021    428 ESFYVASNVQQQRASREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFISLNKL-----DIRRIKEDKRRKLFY 502
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1269 KLEAKGfGQGPGKIKLIIRRDHLLEGTFNQVMAYSrKELQRNKLYVTFVGEEGLDYSGPSREFFFLLSQELFNPYYGLFE 1348
Cdd:COG5021    503 SLKQKA-KIFDPYLHIKVRRDRVFEDSYREIMDES-GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFE 580
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1349 YSANDTYTVQISPMSAFVENHLEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRLPCDLSDLEYLDEEFHQSLQWMKD 1428
Cdd:COG5021    581 YITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLN 660
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1429 NNITD-ILDLTFTVNEEVFGQVTERELKSGGANTQVTEKNKKEYIERMVKWRVERGVVQQTEALVRGFYEVVDSRLVSVF 1507
Cdd:COG5021    661 NDIDEtILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIF 740
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1508 DARELELVIAGTAE-IDLNDWRNNTEYRgGYHDGHLVIRWFWAAVERFNNEQRLRLLQFVTGTSSVPYEGFAALRGSNGL 1586
Cdd:COG5021    741 DESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGV 819
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034654642 1587 RRFCIEKWG-KITSLPRAHTCFNRLDLPPYPSYSMLYEKLLTAVEETSTFGLE 1638
Cdd:COG5021    820 RKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1333-1637 7.40e-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: 395.44  E-value: 7.40e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1333 FLLSQELFNPYYGLFEYSANDTYTVQISPMSAFVENH--LEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRLPCDLS 1410
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1411 DLEYLDEEFHQSLQWMK--DNNITDILDLTFTVneEVFGQVTERELKSGGANTQVTEKNKKEYIERMVKWRVERGVVQQT 1488
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1489 EALVRGFYEVVDSRLVSVFDARELELVIAGTAEIDLNDWRNNTEYRGGYHDGHLVIRWFWAAVERFNNEQRLRLLQFVTG 1568
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654642 1569 TSSVPYEGFAalrgsnGLRRFCIEKWG--KITSLPRAHTCFNRLDLPPYPSYSMLYEKLLTAVEETSTFGL 1637
Cdd:pfam00632  239 SSRLPVGGFK------SLPKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
C2_NEDL1-like cd08691
C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 ...
237-373 4.36e-87

C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1)) is a newly identified HECT-type E3 ubiquitin protein ligase highly expressed in favorable neuroblastomas. In vertebrates it is found primarily in neuronal tissues, including the spinal cord. NEDL1 is thought to normally function in the quality control of cellular proteins by eliminating misfolded proteins. This is thought to be accomplished via a mechanism analogous to that of ER-associated degradation by forming tight complexes and aggregating misfolded proteins that have escaped ubiquitin-mediated degradation. NEDL1, is composed of a C2 domain, two WW domains, and a ubiquitin ligase Hect 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: 176073 [Multi-domain]  Cd Length: 137  Bit Score: 279.67  E-value: 4.36e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  237 ISFSLSDFQAMGLKKGMFFNPDPYLKISIQPGKHSIFPALPHHGQERRSKIIGNTVNPIWQAEQFSFVSLPTDVLEIEVK 316
Cdd:cd08691      1 LSFSLSGLQARNLKKGMFFNPDPYVKISIQPGKRHIFPALPHHGQECRTSIVENTINPVWHREQFVFVGLPTDVLEIEVK 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654642  317 DKFAKSRPIIKRFLGKLSMPVQRLLERHAIGDRVVSYTLGRRLPTDHVSGQLQFRFE 373
Cdd:cd08691     81 DKFAKSRPIIRRFLGKLSIPVQRLLERHAIGDQELSYTLGRRTPTDHVSGQLTFRFE 137
HECW_N pfam16562
N-terminal domain of E3 ubiquitin-protein ligase HECW1 and 2; HECW_N is a domain on E3 ...
97-214 8.49e-69

N-terminal domain of E3 ubiquitin-protein ligase HECW1 and 2; HECW_N is a domain on E3 ubiquitin-protein ligases that lies upstream of the C2 domain; its function is not clearly understood, except perhaps to determine the substrate spectrum of the ligase.


Pssm-ID: 465177  Cd Length: 118  Bit Score: 226.58  E-value: 8.49e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642   97 RSTSDTDLVTSDSRSTLMVSSSYYSIGHSQDLVIHWDIKEEVDAGDWIGMYLIDEVLSENFLDYKNRGVNGSHRGQIIWK 176
Cdd:pfam16562    1 RANSDTDLVTSQSRSSLTVSTYEYTLGQGQSLIISWDIKEEVDANDWIGLYHIDENSPANFWDYKNRGVNGTQKGQIVWR 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034654642  177 IDASSYFVEPETKICFKYYHGVSGALRATTPSVTVKNS 214
Cdd:pfam16562   81 IDPSPYFMEAETKICFKYYHGTSGALRATTPSITVKNP 118
HECW1_helix pfam18436
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids ...
980-1046 6.53e-37

Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids found in HECW1 proteins in Eukaryotes.Polymorphisms in the same region in the C.elegans homolog affects C. elegans behavioural avoidance of a lawn of Pseudomonas aeruginosa.


Pssm-ID: 465766  Cd Length: 67  Bit Score: 133.39  E-value: 6.53e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654642  980 LLLQSPAVKFITNPEFFTVLHANYSAYRVFTSSTCLKHMILKVRRDARNFERYQHNRDLVNFINMFA 1046
Cdd:pfam18436    1 ALLNSPAVKFITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
244-344 1.40e-12

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: 65.20  E-value: 1.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642   244 FQAMGLKKGMFFN-PDPYLKISIQPGKHSIFpalphhgqerRSKIIGNTVNPIWQaEQFSF--VSLPTDVLEIEVKDKFA 320
Cdd:smart00239    7 ISARNLPPKDKGGkSDPYVKVSLDGDPKEKK----------KTKVVKNTLNPVWN-ETFEFevPPPELAELEIEVYDKDR 75
                            90       100
                    ....*....|....*....|....
gi 1034654642   321 KSRpiiKRFLGKLSMPVQRLLERH 344
Cdd:smart00239   76 FGR---DDFIGQVTIPLSDLLLGG 96
C2 pfam00168
C2 domain;
250-346 3.31e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 61.57  E-value: 3.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  250 KKGMFFNPDPYLKISIQPGKhsifpalphhgQERRSKIIGNTVNPIWQaEQFSFV--SLPTDVLEIEVKDkfaKSRPIIK 327
Cdd:pfam00168   15 PKDGNGTSDPYVKVYLLDGK-----------QKKKTKVVKNTLNPVWN-ETFTFSvpDPENAVLEIEVYD---YDRFGRD 79
                           90
                   ....*....|....*....
gi 1034654642  328 RFLGKLSMPVQRLLERHAI 346
Cdd:pfam00168   80 DFIGEVRIPLSELDSGEGL 98
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
863-892 1.58e-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: 57.13  E-value: 1.58e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034654642  863 LPPNWEARIDSHGRVFYVDHVNRTTTWQRP 892
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
862-893 2.44e-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: 56.84  E-value: 2.44e-10
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1034654642   862 PLPPNWEARIDSHGRVFYVDHVNRTTTWQRPT 893
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
864-893 5.63e-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: 5.63e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034654642  864 PPNWEARIDSHGRVFYVDHVNRTTTWQRPT 893
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
1052-1083 6.68e-06

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: 44.13  E-value: 6.68e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1034654642  1052 LPRGWEIKTDQQGKSFFVDHNSRATTFIDPRI 1083
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
1052-1081 1.43e-05

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: 43.26  E-value: 1.43e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034654642 1052 LPRGWEIKTDQQGKSFFVDHNSRATTFIDP 1081
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
1053-1083 2.52e-05

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: 42.52  E-value: 2.52e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1034654642 1053 PRGWEIKTDQQGKSFFVDHNSRATTFIDPRI 1083
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
PHA03169 PHA03169
hypothetical protein; Provisional
406-530 2.16e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  406 ESGSGEPRSEAPESSESWKPEQLGEGSVPDGPGNQSIElsRPAEEAAVITEAGDQGMVSVGPEGAGELLAQVQKDIQPAP 485
Cdd:PHA03169    92 PSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPE--SPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034654642  486 SAEELAEQldlGEEASALLLEDGEAPASTKE--------EPLEEEATTQSRAG 530
Cdd:PHA03169   170 SHEDSPEE---PEPPTSEPEPDSPGPPQSETptsspppqSPPDEPGEPQSPTP 219
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
1282-1636 2.26e-160

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: 490.54  E-value: 2.26e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1282 IKLIIRRDHLLEGTFNQVMAYSRKELqRNKLYVTFVGEEGLDYSGPSREFFFLLSQELFNPYYGLFEYSANDTYTVQISP 1361
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDL-KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1362 MSAFVENHLEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRLPCDLSDLEYLDEEFHQSLQWMKDNNI-TDILDLTFT 1440
Cdd:cd00078     80 SSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGdEDDLELTFT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1441 VNEEV-FGQVTERELKSGGANTQVTEKNKKEYIERMVKWRVERGVVQQTEALVRGFYEVVDSRLVSVFDARELELVIAGT 1519
Cdd:cd00078    160 IELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1520 AEIDLNDWRNNTEYRGGYHDGHLVIRWFWAAVERFNNEQRLRLLQFVTGTSSVPYEGFAALRgsnglRRFCIEKWGK-IT 1598
Cdd:cd00078    240 EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDD 314
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1034654642 1599 SLPRAHTCFNRLDLPPYPSYSMLYEKLLTAVEETSTFG 1636
Cdd:cd00078    315 RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1306-1635 2.08e-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: 487.13  E-value: 2.08e-159
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  1306 ELQRNKLYVTFVGEEGLDYSGPSREFFFLLSQELFNPYYGLFEYSANDtYTVQISPMSAF-VENHLEWFRFSGRILGLAL 1384
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  1385 IHQYLLDAFFTRPFYKALLRLPCDLSDLEYLDEEFHQSLQWMK-DNNITDILDLTFTVNE-EVFGQVTERELKSGGANTQ 1462
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLlNNDTSEELDLTFSIVLtSEFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  1463 VTEKNKKEYIERMVKWRVERGVVQQTEALVRGFYEVVDSRLVSVFDARELELVIAGTAEIDLNDWRNNTEYRGGYHDGHL 1542
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  1543 VIRWFWAAVERFNNEQRLRLLQFVTGTSSVPYEGFAALRGSnglrrFCIEKWG-KITSLPRAHTCFNRLDLPPYPSYSML 1621
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 1034654642  1622 YEKLLTAVEETSTF 1635
Cdd:smart00119  315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1041-1638 4.97e-130

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 427.65  E-value: 4.97e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1041 FINMFADTRLELPRGWEIKTDQQGKSFFVDHNSRATTFI--DPRIPLQNGRLPNHL-THRQHLQRLR---------SYSA 1108
Cdd:COG5021    288 SHSSFEDSLLRLNSLFSTRADSFGRTYYLDHDRILTQYSrpLLEETLGESTSFLVVnNDDSSSIKDLphqvgsnpfLEAH 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1109 GEASEVSRNRGaSLLARPGHSLVAAIRSQHQHESLPLayndKIVAFLRQpnifemlqerqpSLARNhTLREkiHYIRTEG 1188
Cdd:COG5021    368 PEFSELLKNQS-RGTTRDFRNKPTGWSSSIEDLGQFL----FSDFLTSS------------STYED-LRRE--QLGRESD 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1189 NHGLEKLSCDADLVILLSLFEEEIMSYVPLQAAFHPGYSFSPRCSPCSSPQNSPGLQRASarapsPYRRDFEAKLRNFYR 1268
Cdd:COG5021    428 ESFYVASNVQQQRASREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFISLNKL-----DIRRIKEDKRRKLFY 502
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1269 KLEAKGfGQGPGKIKLIIRRDHLLEGTFNQVMAYSrKELQRNKLYVTFVGEEGLDYSGPSREFFFLLSQELFNPYYGLFE 1348
Cdd:COG5021    503 SLKQKA-KIFDPYLHIKVRRDRVFEDSYREIMDES-GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFE 580
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1349 YSANDTYTVQISPMSAFVENHLEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRLPCDLSDLEYLDEEFHQSLQWMKD 1428
Cdd:COG5021    581 YITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLN 660
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1429 NNITD-ILDLTFTVNEEVFGQVTERELKSGGANTQVTEKNKKEYIERMVKWRVERGVVQQTEALVRGFYEVVDSRLVSVF 1507
Cdd:COG5021    661 NDIDEtILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIF 740
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1508 DARELELVIAGTAE-IDLNDWRNNTEYRgGYHDGHLVIRWFWAAVERFNNEQRLRLLQFVTGTSSVPYEGFAALRGSNGL 1586
Cdd:COG5021    741 DESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGV 819
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034654642 1587 RRFCIEKWG-KITSLPRAHTCFNRLDLPPYPSYSMLYEKLLTAVEETSTFGLE 1638
Cdd:COG5021    820 RKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1333-1637 7.40e-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: 395.44  E-value: 7.40e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1333 FLLSQELFNPYYGLFEYSANDTYTVQISPMSAFVENH--LEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRLPCDLS 1410
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1411 DLEYLDEEFHQSLQWMK--DNNITDILDLTFTVneEVFGQVTERELKSGGANTQVTEKNKKEYIERMVKWRVERGVVQQT 1488
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642 1489 EALVRGFYEVVDSRLVSVFDARELELVIAGTAEIDLNDWRNNTEYRGGYHDGHLVIRWFWAAVERFNNEQRLRLLQFVTG 1568
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654642 1569 TSSVPYEGFAalrgsnGLRRFCIEKWG--KITSLPRAHTCFNRLDLPPYPSYSMLYEKLLTAVEETSTFGL 1637
Cdd:pfam00632  239 SSRLPVGGFK------SLPKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
C2_NEDL1-like cd08691
C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 ...
237-373 4.36e-87

C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1)) is a newly identified HECT-type E3 ubiquitin protein ligase highly expressed in favorable neuroblastomas. In vertebrates it is found primarily in neuronal tissues, including the spinal cord. NEDL1 is thought to normally function in the quality control of cellular proteins by eliminating misfolded proteins. This is thought to be accomplished via a mechanism analogous to that of ER-associated degradation by forming tight complexes and aggregating misfolded proteins that have escaped ubiquitin-mediated degradation. NEDL1, is composed of a C2 domain, two WW domains, and a ubiquitin ligase Hect 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: 176073 [Multi-domain]  Cd Length: 137  Bit Score: 279.67  E-value: 4.36e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  237 ISFSLSDFQAMGLKKGMFFNPDPYLKISIQPGKHSIFPALPHHGQERRSKIIGNTVNPIWQAEQFSFVSLPTDVLEIEVK 316
Cdd:cd08691      1 LSFSLSGLQARNLKKGMFFNPDPYVKISIQPGKRHIFPALPHHGQECRTSIVENTINPVWHREQFVFVGLPTDVLEIEVK 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654642  317 DKFAKSRPIIKRFLGKLSMPVQRLLERHAIGDRVVSYTLGRRLPTDHVSGQLQFRFE 373
Cdd:cd08691     81 DKFAKSRPIIRRFLGKLSIPVQRLLERHAIGDQELSYTLGRRTPTDHVSGQLTFRFE 137
HECW_N pfam16562
N-terminal domain of E3 ubiquitin-protein ligase HECW1 and 2; HECW_N is a domain on E3 ...
97-214 8.49e-69

N-terminal domain of E3 ubiquitin-protein ligase HECW1 and 2; HECW_N is a domain on E3 ubiquitin-protein ligases that lies upstream of the C2 domain; its function is not clearly understood, except perhaps to determine the substrate spectrum of the ligase.


Pssm-ID: 465177  Cd Length: 118  Bit Score: 226.58  E-value: 8.49e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642   97 RSTSDTDLVTSDSRSTLMVSSSYYSIGHSQDLVIHWDIKEEVDAGDWIGMYLIDEVLSENFLDYKNRGVNGSHRGQIIWK 176
Cdd:pfam16562    1 RANSDTDLVTSQSRSSLTVSTYEYTLGQGQSLIISWDIKEEVDANDWIGLYHIDENSPANFWDYKNRGVNGTQKGQIVWR 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034654642  177 IDASSYFVEPETKICFKYYHGVSGALRATTPSVTVKNS 214
Cdd:pfam16562   81 IDPSPYFMEAETKICFKYYHGTSGALRATTPSITVKNP 118
HECW1_helix pfam18436
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids ...
980-1046 6.53e-37

Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids found in HECW1 proteins in Eukaryotes.Polymorphisms in the same region in the C.elegans homolog affects C. elegans behavioural avoidance of a lawn of Pseudomonas aeruginosa.


Pssm-ID: 465766  Cd Length: 67  Bit Score: 133.39  E-value: 6.53e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654642  980 LLLQSPAVKFITNPEFFTVLHANYSAYRVFTSSTCLKHMILKVRRDARNFERYQHNRDLVNFINMFA 1046
Cdd:pfam18436    1 ALLNSPAVKFITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
244-344 1.40e-12

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: 65.20  E-value: 1.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642   244 FQAMGLKKGMFFN-PDPYLKISIQPGKHSIFpalphhgqerRSKIIGNTVNPIWQaEQFSF--VSLPTDVLEIEVKDKFA 320
Cdd:smart00239    7 ISARNLPPKDKGGkSDPYVKVSLDGDPKEKK----------KTKVVKNTLNPVWN-ETFEFevPPPELAELEIEVYDKDR 75
                            90       100
                    ....*....|....*....|....
gi 1034654642   321 KSRpiiKRFLGKLSMPVQRLLERH 344
Cdd:smart00239   76 FGR---DDFIGQVTIPLSDLLLGG 96
C2 pfam00168
C2 domain;
250-346 3.31e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 61.57  E-value: 3.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  250 KKGMFFNPDPYLKISIQPGKhsifpalphhgQERRSKIIGNTVNPIWQaEQFSFV--SLPTDVLEIEVKDkfaKSRPIIK 327
Cdd:pfam00168   15 PKDGNGTSDPYVKVYLLDGK-----------QKKKTKVVKNTLNPVWN-ETFTFSvpDPENAVLEIEVYD---YDRFGRD 79
                           90
                   ....*....|....*....
gi 1034654642  328 RFLGKLSMPVQRLLERHAI 346
Cdd:pfam00168   80 DFIGEVRIPLSELDSGEGL 98
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
863-892 1.58e-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: 57.13  E-value: 1.58e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034654642  863 LPPNWEARIDSHGRVFYVDHVNRTTTWQRP 892
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
862-893 2.44e-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: 56.84  E-value: 2.44e-10
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1034654642   862 PLPPNWEARIDSHGRVFYVDHVNRTTTWQRPT 893
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
864-893 5.63e-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: 5.63e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034654642  864 PPNWEARIDSHGRVFYVDHVNRTTTWQRPT 893
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
245-349 9.02e-09

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: 54.38  E-value: 9.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  245 QAMGLK-KGMFFNPDPYLKISIQPGkhsifpalphhgQERRSKIIGNTVNPIWQaEQFSF--VSLPTDVLEIEVKDKFAK 321
Cdd:cd00030      7 EARNLPaKDLNGKSDPYVKVSLGGK------------QKFKTKVVKNTLNPVWN-ETFEFpvLDPESDTLTVEVWDKDRF 73
                           90       100
                   ....*....|....*....|....*...
gi 1034654642  322 SRpiiKRFLGKLSMPVQRLLERHAIGDR 349
Cdd:cd00030     74 SK---DDFLGEVEIPLSELLDSGKEGEL 98
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
256-342 2.57e-08

C2 domain second repeat present 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 the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176015 [Multi-domain]  Cd Length: 105  Bit Score: 53.34  E-value: 2.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  256 NPDPYLKISIQpgkhsifpalphhGQERRSKIIGNTVNPIWQaEQFSF-VSLP-TDVLEIEVKDKFAKSRpiikrfLGKL 333
Cdd:cd04050     20 EPSPYVELTVG-------------KTTQKSKVKERTNNPVWE-EGFTFlVRNPeNQELEIEVKDDKTGKS------LGSL 79

                   ....*....
gi 1034654642  334 SMPVQRLLE 342
Cdd:cd04050     80 TLPLSELLK 88
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
257-355 4.33e-06

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: 47.63  E-value: 4.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  257 PDPYLKISIQpgkhsifpalphhGQERRSKIIGNTVNPIWQaEQFSF----VSLPTDVLEIEVKDkfaKSRPIIKRFLGK 332
Cdd:cd08373     15 GDRIAKVTFR-------------GVKKKTRVLENELNPVWN-ETFEWplagSPDPDESLEIVVKD---YEKVGRNRLIGS 77
                           90       100
                   ....*....|....*....|...
gi 1034654642  333 LSMPVQRLLERHAIgdrVVSYTL 355
Cdd:cd08373     78 ATVSLQDLVSEGLL---EVTEPL 97
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
1052-1083 6.68e-06

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: 44.13  E-value: 6.68e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1034654642  1052 LPRGWEIKTDQQGKSFFVDHNSRATTFIDPRI 1083
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
1052-1081 1.43e-05

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: 43.26  E-value: 1.43e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034654642 1052 LPRGWEIKTDQQGKSFFVDHNSRATTFIDP 1081
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
268-376 1.66e-05

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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: 175989 [Multi-domain]  Cd Length: 127  Bit Score: 45.79  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  268 GKHSIFPALPHHGQERRSKIIGNTVNPIWQaEQFSF-----VSLPTDVLEIEVKDKFAKSRPiiKRFLGKLSMPVQRLLE 342
Cdd:cd04022     19 GSSSAYVELDFDGQKKRTRTKPKDLNPVWN-EKLVFnvsdpSRLSNLVLEVYVYNDRRSGRR--RSFLGRVRISGTSFVP 95
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034654642  343 RhaiGDRVV-SYTLGRRLPTDHVSGQLQFRFEITS 376
Cdd:cd04022     96 P---SEAVVqRYPLEKRGLFSRVRGEIGLKVYITD 127
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
1053-1083 2.52e-05

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: 42.52  E-value: 2.52e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1034654642 1053 PRGWEIKTDQQGKSFFVDHNSRATTFIDPRI 1083
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
247-373 1.22e-04

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: 43.43  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  247 MGLKKGMffnPDPYLKISIQpgkhsifpalphhGQERRSKIIGNTVNPIWQaEQFSFV--SLPTDVLEIEVKDK-FAKSr 323
Cdd:cd08391     21 GGLVKGK---SDPYVIVRVG-------------AQTFKSKVIKENLNPKWN-EVYEAVvdEVPGQELEIELFDEdPDKD- 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034654642  324 piikRFLGKLSMPvqrllerhaIGDRVVSYTLGRRLPTDHV-SGQLQFRFE 373
Cdd:cd08391     83 ----DFLGRLSID---------LGSVEKKGFIDEWLPLEDVkSGRLHLKLE 120
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
257-374 1.27e-04

C2 domain first repeat present 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 the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 175990 [Multi-domain]  Cd Length: 128  Bit Score: 43.57  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  257 PDPYLKISIQpgkhsifpalphhGQERRSKIIGNTVNPIWQA-EQFSFVSLPTDVLEIEVKDK--FAKsrpiiKRFLGKL 333
Cdd:cd04024     24 SDPYAILSVG-------------AQRFKTQTIPNTLNPKWNYwCEFPIFSAQNQLLKLILWDKdrFAG-----KDYLGEF 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1034654642  334 SMPVQRLLERHAIGDRVVSYTL--GRRLPTDHVSGQLQFRFEI 374
Cdd:cd04024     86 DIALEEVFADGKTGQSDKWITLksTRPGKTSVVSGEIHLQFSW 128
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
258-343 1.79e-04

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. 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 a type-I topology.


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 43.02  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  258 DPYLKISIQPGkhsifpalPHHGQERRSKIIGNTVNPIWQaEQFSFVSLPTDV---LEIEVKDKFAKSRpiiKRFLGKLS 334
Cdd:cd04026     35 DPYVKLKLIPD--------PKNETKQKTKTIKKTLNPVWN-ETFTFDLKPADKdrrLSIEVWDWDRTTR---NDFMGSLS 102

                   ....*....
gi 1034654642  335 MPVQRLLER 343
Cdd:cd04026    103 FGVSELIKM 111
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
246-342 2.55e-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: 42.29  E-value: 2.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  246 AMGL-KKGMFFNPDPYLKISIQPgkhsifpalphhGQERRSKIIGNTVNPIWQaEQFSFVSLPTDVLEIEVKDKfaksRP 324
Cdd:cd08382      9 ADGLaKRDLFRLPDPFAVITVDG------------GQTHSTDVAKKTLDPKWN-EHFDLTVGPSSIITIQVFDQ----KK 71
                           90       100
                   ....*....|....*....|.
gi 1034654642  325 IIKR---FLGKLSMPVQRLLE 342
Cdd:cd08382     72 FKKKdqgFLGCVRIRANAVLP 92
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
246-348 2.98e-04

C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. 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: 176009 [Multi-domain]  Cd Length: 124  Bit Score: 42.16  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  246 AMGLKKGMFFN--PDPYLKISIQPGKhsifpalphhgQERRSKIIGNTVNPIWQAEQFSFVSLPTDVLEIEVKDKfaksR 323
Cdd:cd04044     11 ARGLKGSDIIGgtVDPYVTFSISNRR-----------ELARTKVKKDTSNPVWNETKYILVNSLTEPLNLTVYDF----N 75
                           90       100
                   ....*....|....*....|....*.
gi 1034654642  324 PIIK-RFLGKLSMPVQRLLERHAIGD 348
Cdd:cd04044     76 DKRKdKLIGTAEFDLSSLLQNPEQEN 101
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
245-332 3.30e-04

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. 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 the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 42.19  E-value: 3.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  245 QAMGLKK-GMFFNPDPYLKISIQPGKHSIFpalphhgqERRSKIIGNTVNPIWQaEQFSF----VSLPTDVLEIEVKDKF 319
Cdd:cd00276     22 KARNLPPsDGKGLSDPYVKVSLLQGGKKLK--------KKKTSVKKGTLNPVFN-EAFSFdvpaEQLEEVSLVITVVDKD 92
                           90
                   ....*....|...
gi 1034654642  320 AKSRPIIkrfLGK 332
Cdd:cd00276     93 SVGRNEV---IGQ 102
C2A_Synaptotagmin-8 cd08387
C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking ...
258-325 1.69e-03

C2A domain first repeat present in Synaptotagmin 8; 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 the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176033 [Multi-domain]  Cd Length: 124  Bit Score: 40.08  E-value: 1.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034654642  258 DPYLKISIQPGKHSifpalphhgqERRSKIIGNTVNPIWQaEQFSFvSLPTDVLE---IEVK----DKFAKSRPI 325
Cdd:cd08387     38 DPYCKVRLLPDRSN----------TKQSKIHKKTLNPEFD-ESFVF-EVPPQELPkrtLEVLlydfDQFSRDECI 100
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
257-333 1.75e-03

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 39.95  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  257 PDPYLKISIQPGKHSifpalphhGQERRSKIIGNTVNPIWQaEQFSFVSLPTDV----LEIEVK-DKFAKSRPiiKRFLG 331
Cdd:cd04030     37 PDPYVRLYLLPDKSK--------STRRKTSVKKDNLNPVFD-ETFEFPVSLEELkrrtLDVAVKnSKSFLSRE--KKLLG 105

                   ..
gi 1034654642  332 KL 333
Cdd:cd04030    106 QV 107
PHA03169 PHA03169
hypothetical protein; Provisional
406-530 2.16e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  406 ESGSGEPRSEAPESSESWKPEQLGEGSVPDGPGNQSIElsRPAEEAAVITEAGDQGMVSVGPEGAGELLAQVQKDIQPAP 485
Cdd:PHA03169    92 PSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPE--SPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034654642  486 SAEELAEQldlGEEASALLLEDGEAPASTKE--------EPLEEEATTQSRAG 530
Cdd:PHA03169   170 SHEDSPEE---PEPPTSEPEPDSPGPPQSETptsspppqSPPDEPGEPQSPTP 219
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
250-343 2.45e-03

C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. 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 second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176012 [Multi-domain]  Cd Length: 110  Bit Score: 39.09  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  250 KKGMFFNPDPYLKISIQPGKHSifpALPHHgqerRSKIIGNTVNPIWQAEQFSFVSL----PTDVLEIEVKDKFAKSRPi 325
Cdd:cd04047     14 KKDFFGKSDPFLEISRQSEDGT---WVLVY----RTEVIKNTLNPVWKPFTIPLQKLcngdYDRPIKIEVYDYDSSGKH- 85
                           90
                   ....*....|....*...
gi 1034654642  326 ikRFLGKLSMPVQRLLER 343
Cdd:cd04047     86 --DLIGEFETTLDELLKS 101
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
257-338 4.79e-03

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). 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 a type-I topology and do not bind Ca2+.


Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 38.77  E-value: 4.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  257 PDPYLKISIQPGkhsifpalPHHGQERRSKIIGNTVNPIWQaEQFSFVSLPTD-----VLEIEVKDkFAKSRPIIkrFLG 331
Cdd:cd04031     37 RNPYVKVYLLPD--------RSEKSKRRTKTVKKTLNPEWN-QTFEYSNVRREtlkerTLEVTVWD-YDRDGEND--FLG 104

                   ....*..
gi 1034654642  332 KLSMPVQ 338
Cdd:cd04031    105 EVVIDLA 111
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
256-344 8.89e-03

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 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. Members here have a type-II topology.


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 37.91  E-value: 8.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654642  256 NPDPYLKISIqpgkhsiFPALPHHGQERRSKII-GNTVNPIWQaEQFSF-VSLPT-DVLEIEVKDkfakSRPIIKRFLGK 332
Cdd:cd00275     24 IVDPYVEVEI-------HGLPADDSAKFKTKVVkNNGFNPVWN-ETFEFdVTVPElAFLRFVVYD----EDSGDDDFLGQ 91
                           90
                   ....*....|....
gi 1034654642  333 LSMPVQRLLE--RH 344
Cdd:cd00275     92 ACLPLDSLRQgyRH 105
 
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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