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Conserved domains on  [gi|55741473|ref|NP_065811|]
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E3 ubiquitin-protein ligase HECW2 isoform 1 [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 ...
 1216-1570 8.34e-162

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: 493.24  E-value: 8.34e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1216 LKLIIRRDHLLEDAFNQIMGYSRKDLqRNKLYVTFVGEEGLDYSGPSREFFFLVSRELFNPYYGLFEYSANDTYTVQISP 1295
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDL-KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1296 MSAFVDNHHEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRILCDLSDLEYLDEEFHQSLQWMKDNDIH-DILDLTFT 1374
Cdd:cd00078   80 SSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDeDDLELTFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1375 VNEEV-FGQITERELKPGGANIPVTEKNKKEYIERMVKWRIERGVVQQTESLVRGFYEVVDARLVSVFDARELELVIAGT 1453
Cdd:cd00078  160 IELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1454 AEIDLSDWRNNTEYRGGYHDNHIVIRWFWAAVERFNNEQRLRLLQFVTGTSSIPYEGFASLRgsngpRRFCVEKWGK-IT 1532
Cdd:cd00078  240 EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDD 314

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 55741473 1533 ALPRAHTCFNRLDLPPYPSFSMLYEKLLTAVEETSTFG 1570
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 ...
 185-321 1.17e-80

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: 261.18  E-value: 1.17e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  185 VSFTLSDLRAVGLKKGMFFNPDPYLKMSIQPGKKSSFPTCAHHGQERRSTIISNTTNPIWHREKYSFFALLTDVLEIEIK 264
Cdd:cd08691    1 LSFSLSGLQARNLKKGMFFNPDPYVKISIQPGKRHIFPALPHHGQECRTSIVENTINPVWHREQFVFVGLPTDVLEIEVK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55741473  265 DKFAKSRPIIKRFLGKLTIPVQRLLERQAIGDQMLSYNLGRRLPADHVSGYLQFKVE 321
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 ...
 45-162 1.18e-79

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: 257.40  E-value: 1.18e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473     45 RANSDTDLVTSESRSSLTASMYEYTLGQAQNLIIFWDIKEEVDPSDWIGLYHIDENSPANFWDSKNRGVTGTQKGQIVWR 124
Cdd:pfam16562    1 RANSDTDLVTSQSRSSLTVSTYEYTLGQGQSLIISWDIKEEVDANDWIGLYHIDENSPANFWDYKNRGVNGTQKGQIVWR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 55741473    125 IEPGPYFMEPEIKICFKYYHGISGALRATTPCITVKNP 162
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 ...
 915-981 7.46e-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: 7.46e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55741473    915 LLLQSPPVKFLISPEFFTVLHSNPSAYRMFTNNTCLKHMITKVRRDTHHFERYQHNRDLVGFLNMFA 981
Cdd:pfam18436    1 ALLNSPAVKFITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 809-838 2.47e-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: 56.74  E-value: 2.47e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 55741473    809 LPPNWEARIDSHGRIFYVDHVNRTTTWQRP 838
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 987-1016 6.07e-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: 44.03  E-value: 6.07e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 55741473    987 LPRGWEMKHDHQGKAFFVDHNSRTTTFIDP 1016
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
PHA03169 super family cl27451
hypothetical protein; Provisional
 584-794 9.05e-06

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.97  E-value: 9.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   584 TSDASGGSRRAVSETESLDQGSEpsqvSSETEPSDPARTESVSEASTRPEGESDLECADSSCNESVTTQLSSVDTRCSSL 663
Cdd:PHA03169   50 APTTSGPQVRAVAEQGHRQTESD----TETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   664 ESarfPETPAFSSQEEEDGA-----CAAEPTSSGPAEGSQESVCTAgslpvvqvPSGEDEGPGAESATVPDQEELGEVWQ 738
Cdd:PHA03169  126 SS---PESPASHSPPPSPPShpgphEPAPPESHNPSPNQQPSSFLQ--------PSHEDSPEEPEPPTSEPEPDSPGPPQ 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   739 ----RRGSLEGAAAAAESPPQEEGSAGEAQGTCEGATAQEEGATGGSQANGHQPLRSLPS 794
Cdd:PHA03169  195 setpTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSHS 254
DMP1 super family cl25845
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 345-700 1.90e-04

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


The actual alignment was detected with superfamily member pfam07263:

Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 46.07  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    345 NGDLGSPSDDEDMPGSHHDSqvcsnGPVSEDSAADgTPKHSFRTSSTLEIDTEELTSTSSRTSPPR-----GRQDSLNDY 419
Cdd:pfam07263  130 NSRLGSDEDSADTTQSREDS-----ASQGEDSAQD-TTSESRDLDNEDEVSSRPESGDSTQDSESEehwvgGGSEGDSSH 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    420 LDAIEHNGHSRPGTATCSERSMGASPKLRSSfptdtrlnamlHIDSDE----EDHEFQQDLGYPSSLEEEGGLIMF-SRA 494
Cdd:pfam07263  204 GDGSEFDDEGMQSDDPDSIRSERGNSRMSSA-----------SVKSKEskgdSEQASTQDSGDSQSVEYPSRKFFRkSRI 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    495 SRADDGSltsqtKLEDN--PVENEEASTHEAASFEDKPENLPELAESslpagPAPEEGEGGPEPQPSADQGSAELCGSQE 572
Cdd:pfam07263  273 SEEDDRG-----ELDDSntMEEVKSDSTESTSSKEAGLSQSREDSKS-----ESQEDSEESQSQEDSQNSQDPSSESSQE 342

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    573 VDQPTSgadtgtsDASGGSRRAVSETESLDQGSEPSQVSSETEPSDPARTESVSEASTRpEGESDLECADSSCNESVT-- 650
Cdd:pfam07263  343 ADLPSQ-------ESSSESQEEVVSESRGDNPDNTSSSEEDQEDSDSSEEDSLSTFSSS-ESESREEQADSESNESLRss 414

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 55741473    651 --TQLSSVDTRCSSLESARFPETPAfSSQEEEDGACAAEPTSSGPAEGSQES 700
Cdd:pfam07263  415 eeSPESSEDENSSSQEGLQSHSAST-ESQSEESQSEQDSQSEEDDESDSQDS 465
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 1216-1570 8.34e-162

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: 493.24  E-value: 8.34e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1216 LKLIIRRDHLLEDAFNQIMGYSRKDLqRNKLYVTFVGEEGLDYSGPSREFFFLVSRELFNPYYGLFEYSANDTYTVQISP 1295
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDL-KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1296 MSAFVDNHHEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRILCDLSDLEYLDEEFHQSLQWMKDNDIH-DILDLTFT 1374
Cdd:cd00078   80 SSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDeDDLELTFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1375 VNEEV-FGQITERELKPGGANIPVTEKNKKEYIERMVKWRIERGVVQQTESLVRGFYEVVDARLVSVFDARELELVIAGT 1453
Cdd:cd00078  160 IELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1454 AEIDLSDWRNNTEYRGGYHDNHIVIRWFWAAVERFNNEQRLRLLQFVTGTSSIPYEGFASLRgsngpRRFCVEKWGK-IT 1532
Cdd:cd00078  240 EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDD 314

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 55741473 1533 ALPRAHTCFNRLDLPPYPSFSMLYEKLLTAVEETSTFG 1570
Cdd:cd00078  315 RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 1240-1569 4.22e-157

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: 479.81  E-value: 4.22e-157
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    1240 DLQRNKLYVTFVGEEGLDYSGPSREFFFLVSRELFNPYYGLFEYSANDtYTVQISPMSAFVDNHH-EWFRFSGRILGLAL 1318
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHlSYFRFIGRVLGKAL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    1319 IHQYLLDAFFTRPFYKALLRILCDLSDLEYLDEEFHQSLQWMK-DNDIHDILDLTFTVNE-EVFGQITERELKPGGANIP 1396
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLlNNDTSEELDLTFSIVLtSEFGQVKVVELKPGGSNIP 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    1397 VTEKNKKEYIERMVKWRIERGVVQQTESLVRGFYEVVDARLVSVFDARELELVIAGTAEIDLSDWRNNTEYRGGYHDNHI 1476
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    1477 VIRWFWAAVERFNNEQRLRLLQFVTGTSSIPYEGFASLRGSngprrFCVEKWG-KITALPRAHTCFNRLDLPPYPSFSML 1555
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                           330
                    ....*....|....
gi 55741473    1556 YEKLLTAVEETSTF 1569
Cdd:smart00119  315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
907-1572 2.36e-132

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 433.04  E-value: 2.36e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  907 STSRSRITLLLQSPPVKFLISPEfftvlhsnpSAYRMFTNnTCLKHMITKVRRDTHHFeryqhnrdlvgFLNMFANKQLE 986
Cdd:COG5021  240 ALLARYISIKLVIKKLYLGPGPD---------ASSRISTL-IIRLSNTNLNRRLSYIL-----------SHSSFEDSLLR 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  987 LPRGWEMKHDHQGKAFFVDHNSRTTTFIDPRLPLQSSRPTSALVHRQHLTRQRSHSAGEVGEDSRHagpPVLPRPSSTFN 1066
Cdd:COG5021  299 LNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFL---EAHPEFSELLK 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1067 TVSRPQYQD-MVPVAYNDKIVAFLRQpniFEILQERQPDLTRNHSLREkiQFIRTEGTPGLVRLSSDADLVM----LLSL 1141
Cdd:COG5021  376 NQSRGTTRDfRNKPTGWSSSIEDLGQ---FLFSDFLTSSSTYEDLRRE--QLGRESDESFYVASNVQQQRASregpLLSG 450

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1142 FEEEIMS----YVPPHALLHPSYCQSPRGSPVSSPQNSpgTQRanarapapYKRDFEAKLRNFYrkleTKGYGQGPGKLK 1217
Cdd:COG5021  451 WKTRLNNlyrfYFVEHRKKTLTKNDSRLGSFISLNKLD--IRR--------IKEDKRRKLFYSL----KQKAKIFDPYLH 516

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1218 LIIRRDHLLEDAFNQIMGYSrKDLQRNKLYVTFVGEEGLDYSGPSREFFFLVSRELFNPYYGLFEYSANDTYTVQISPMS 1297
Cdd:COG5021  517 IKVRRDRVFEDSYREIMDES-GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLS 595

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1298 AFVDNHHEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRILCDLSDLEYLDEEFHQSLQWMKDNDIHD-ILDLTFTVN 1376
Cdd:COG5021  596 SINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDEtILDLTFTVE 675

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1377 EEVFGQITERELKPGGANIPVTEKNKKEYIERMVKWRIERGVVQQTESLVRGFYEVVDARLVSVFDARELELVIAGTAE- 1455
Cdd:COG5021  676 DDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEd 755

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1456 IDLSDWRNNTEYRgGYHDNHIVIRWFWAAVERFNNEQRLRLLQFVTGTSSIPYEGFASLRGSNGPRRFCVEKWG-KITAL 1534
Cdd:COG5021  756 IDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRL 834

                        650       660       670
                 ....*....|....*....|....*....|....*...
gi 55741473 1535 PRAHTCFNRLDLPPYPSFSMLYEKLLTAVEETSTFGLE 1572
Cdd:COG5021  835 PSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 1267-1571 2.28e-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: 396.21  E-value: 2.28e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   1267 FLVSRELFNPYYGLFEYSANDTYTVQISPMSAFVDNHH--EWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRILCDLS 1344
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLEllDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   1345 DLEYLDEEFHQSLQWMK--DNDIHDILDLTFTVneEVFGQITERELKPGGANIPVTEKNKKEYIERMVKWRIERGVVQQT 1422
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   1423 ESLVRGFYEVVDARLVSVFDARELELVIAGTAEIDLSDWRNNTEYRGGYHDNHIVIRWFWAAVERFNNEQRLRLLQFVTG 1502
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55741473   1503 TSSIPYEGFASLrgsngpRRFCVEKWG--KITALPRAHTCFNRLDLPPYPSFSMLYEKLLTAVEETSTFGL 1571
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
C2_NEDL1-like cd08691
C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 ...
 185-321 1.17e-80

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: 261.18  E-value: 1.17e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  185 VSFTLSDLRAVGLKKGMFFNPDPYLKMSIQPGKKSSFPTCAHHGQERRSTIISNTTNPIWHREKYSFFALLTDVLEIEIK 264
Cdd:cd08691    1 LSFSLSGLQARNLKKGMFFNPDPYVKISIQPGKRHIFPALPHHGQECRTSIVENTINPVWHREQFVFVGLPTDVLEIEVK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55741473  265 DKFAKSRPIIKRFLGKLTIPVQRLLERQAIGDQMLSYNLGRRLPADHVSGYLQFKVE 321
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 ...
 45-162 1.18e-79

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: 257.40  E-value: 1.18e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473     45 RANSDTDLVTSESRSSLTASMYEYTLGQAQNLIIFWDIKEEVDPSDWIGLYHIDENSPANFWDSKNRGVTGTQKGQIVWR 124
Cdd:pfam16562    1 RANSDTDLVTSQSRSSLTVSTYEYTLGQGQSLIISWDIKEEVDANDWIGLYHIDENSPANFWDYKNRGVNGTQKGQIVWR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 55741473    125 IEPGPYFMEPEIKICFKYYHGISGALRATTPCITVKNP 162
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 ...
 915-981 7.46e-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: 7.46e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55741473    915 LLLQSPPVKFLISPEFFTVLHSNPSAYRMFTNNTCLKHMITKVRRDTHHFERYQHNRDLVGFLNMFA 981
Cdd:pfam18436    1 ALLNSPAVKFITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 186-292 1.37e-11

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: 62.50  E-value: 1.37e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473     186 SFTLSDLRAVGLKKGMFFN-PDPYLKMSIQPGKKSSFptcahhgqerRSTIISNTTNPIWHrEKYSF--FALLTDVLEIE 262
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKK----------KTKVVKNTLNPVWN-ETFEFevPPPELAELEIE 69

                            90       100       110
                    ....*....|....*....|....*....|
gi 55741473     263 IKDKFAKSRpiiKRFLGKLTIPVQRLLERQ 292
Cdd:smart00239   70 VYDKDRFGR---DDFIGQVTIPLSDLLLGG 96
C2 pfam00168
C2 domain;
192-294 7.40e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 60.41  E-value: 7.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    192 LRAVGL-KKGMFFNPDPYLKMSIQPGKkssfptcahhgQERRSTIISNTTNPIWHrEKYSF--FALLTDVLEIEIKDkfa 268
Cdd:pfam00168    8 IEAKNLpPKDGNGTSDPYVKVYLLDGK-----------QKKKTKVVKNTLNPVWN-ETFTFsvPDPENAVLEIEVYD--- 72

                           90       100
                   ....*....|....*....|....*.
gi 55741473    269 KSRPIIKRFLGKLTIPVQRLLERQAI 294
Cdd:pfam00168   73 YDRFGRDDFIGEVRIPLSELDSGEGL 98
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 809-838 2.47e-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: 56.74  E-value: 2.47e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 55741473    809 LPPNWEARIDSHGRIFYVDHVNRTTTWQRP 838
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 810-839 1.41e-09

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: 1.41e-09
                         10        20        30
                 ....*....|....*....|....*....|
gi 55741473  810 PPNWEARIDSHGRIFYVDHVNRTTTWQRPT 839
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 809-839 2.24e-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: 54.14  E-value: 2.24e-09
                            10        20        30
                    ....*....|....*....|....*....|.
gi 55741473     809 LPPNWEARIDSHGRIFYVDHVNRTTTWQRPT 839
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 987-1016 6.07e-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: 44.03  E-value: 6.07e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 55741473    987 LPRGWEMKHDHQGKAFFVDHNSRTTTFIDP 1016
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 987-1018 6.35e-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: 6.35e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 55741473     987 LPRGWEMKHDHQGKAFFVDHNSRTTTFIDPRL 1018
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03169 PHA03169
hypothetical protein; Provisional
 584-794 9.05e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.97  E-value: 9.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   584 TSDASGGSRRAVSETESLDQGSEpsqvSSETEPSDPARTESVSEASTRPEGESDLECADSSCNESVTTQLSSVDTRCSSL 663
Cdd:PHA03169   50 APTTSGPQVRAVAEQGHRQTESD----TETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   664 ESarfPETPAFSSQEEEDGA-----CAAEPTSSGPAEGSQESVCTAgslpvvqvPSGEDEGPGAESATVPDQEELGEVWQ 738
Cdd:PHA03169  126 SS---PESPASHSPPPSPPShpgphEPAPPESHNPSPNQQPSSFLQ--------PSHEDSPEEPEPPTSEPEPDSPGPPQ 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   739 ----RRGSLEGAAAAAESPPQEEGSAGEAQGTCEGATAQEEGATGGSQANGHQPLRSLPS 794
Cdd:PHA03169  195 setpTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSHS 254
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 988-1018 9.35e-06

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: 43.67  E-value: 9.35e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 55741473  988 PRGWEMKHDHQGKAFFVDHNSRTTTFIDPRL 1018
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 345-700 1.90e-04

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 46.07  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    345 NGDLGSPSDDEDMPGSHHDSqvcsnGPVSEDSAADgTPKHSFRTSSTLEIDTEELTSTSSRTSPPR-----GRQDSLNDY 419
Cdd:pfam07263  130 NSRLGSDEDSADTTQSREDS-----ASQGEDSAQD-TTSESRDLDNEDEVSSRPESGDSTQDSESEehwvgGGSEGDSSH 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    420 LDAIEHNGHSRPGTATCSERSMGASPKLRSSfptdtrlnamlHIDSDE----EDHEFQQDLGYPSSLEEEGGLIMF-SRA 494
Cdd:pfam07263  204 GDGSEFDDEGMQSDDPDSIRSERGNSRMSSA-----------SVKSKEskgdSEQASTQDSGDSQSVEYPSRKFFRkSRI 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    495 SRADDGSltsqtKLEDN--PVENEEASTHEAASFEDKPENLPELAESslpagPAPEEGEGGPEPQPSADQGSAELCGSQE 572
Cdd:pfam07263  273 SEEDDRG-----ELDDSntMEEVKSDSTESTSSKEAGLSQSREDSKS-----ESQEDSEESQSQEDSQNSQDPSSESSQE 342

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    573 VDQPTSgadtgtsDASGGSRRAVSETESLDQGSEPSQVSSETEPSDPARTESVSEASTRpEGESDLECADSSCNESVT-- 650
Cdd:pfam07263  343 ADLPSQ-------ESSSESQEEVVSESRGDNPDNTSSSEEDQEDSDSSEEDSLSTFSSS-ESESREEQADSESNESLRss 414

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 55741473    651 --TQLSSVDTRCSSLESARFPETPAfSSQEEEDGACAAEPTSSGPAEGSQES 700
Cdd:pfam07263  415 eeSPESSEDENSSSQEGLQSHSAST-ESQSEESQSEQDSQSEEDDESDSQDS 465
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 319-737 8.62e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 8.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   319 KVEVTSSVHEdaSPEAVGTILGVNSvNGDLGSPSDDEDMPGSHHDSQVCSNGP-VSEDSAADGTPKHSFRTSSTLEidte 397
Cdd:PHA03307   83 ESRSTPTWSL--STLAPASPAREGS-PTPPGPSSPDPPPPTPPPASPPPSPAPdLSEMLRPVGSPGPPPAASPPAA---- 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   398 ELTSTSSRTSPPRGRQDSLNdyLDAIEHngHSRPGTATCSERSMGASPKLRSsfPTDTRLNAMLHIDSDEEDhefqqdlg 477
Cdd:PHA03307  156 GASPAAVASDAASSRQAALP--LSSPEE--TARAPSSPPAEPPPSTPPAAAS--PRPPRRSSPISASASSPA-------- 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   478 yPSSLEEEGglimfSRASRADDGSLTSQTKLEDNPVENEEASTHEAASFEDKPENLPELAESSlpagpapeegeGGPEPQ 557
Cdd:PHA03307  222 -PAPGRSAA-----DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGP-----------SSRPGP 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   558 PSADQGSAELCGSQEVDQPTSGADTGTSDASGGSrraVSETESLDQGSEPSQVSSETEPSDPARTESVSEASTRPEGESD 637
Cdd:PHA03307  285 ASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSS---SSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAD 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   638 lecadsscnesvttqLSSVDTRCSSLESARFPETPAFSSQEEedgacAAEPTSSGPAEGSQESVCTAGSLPVVqVPSGED 717
Cdd:PHA03307  362 ---------------PSSPRKRPRPSRAPSSPAASAGRPTRR-----RARAAVAGRARRRDATGRFPAGRPRP-SPLDAG 420

                         410       420
                  ....*....|....*....|
gi 55741473   718 EGPGAESATVPDQEELGEVW 737
Cdd:PHA03307  421 AASGAFYARYPLLTPSGEPW 440
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 1216-1570 8.34e-162

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: 493.24  E-value: 8.34e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1216 LKLIIRRDHLLEDAFNQIMGYSRKDLqRNKLYVTFVGEEGLDYSGPSREFFFLVSRELFNPYYGLFEYSANDTYTVQISP 1295
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDL-KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1296 MSAFVDNHHEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRILCDLSDLEYLDEEFHQSLQWMKDNDIH-DILDLTFT 1374
Cdd:cd00078   80 SSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDeDDLELTFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1375 VNEEV-FGQITERELKPGGANIPVTEKNKKEYIERMVKWRIERGVVQQTESLVRGFYEVVDARLVSVFDARELELVIAGT 1453
Cdd:cd00078  160 IELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1454 AEIDLSDWRNNTEYRGGYHDNHIVIRWFWAAVERFNNEQRLRLLQFVTGTSSIPYEGFASLRgsngpRRFCVEKWGK-IT 1532
Cdd:cd00078  240 EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDD 314

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 55741473 1533 ALPRAHTCFNRLDLPPYPSFSMLYEKLLTAVEETSTFG 1570
Cdd:cd00078  315 RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 1240-1569 4.22e-157

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: 479.81  E-value: 4.22e-157
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    1240 DLQRNKLYVTFVGEEGLDYSGPSREFFFLVSRELFNPYYGLFEYSANDtYTVQISPMSAFVDNHH-EWFRFSGRILGLAL 1318
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHlSYFRFIGRVLGKAL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    1319 IHQYLLDAFFTRPFYKALLRILCDLSDLEYLDEEFHQSLQWMK-DNDIHDILDLTFTVNE-EVFGQITERELKPGGANIP 1396
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLlNNDTSEELDLTFSIVLtSEFGQVKVVELKPGGSNIP 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    1397 VTEKNKKEYIERMVKWRIERGVVQQTESLVRGFYEVVDARLVSVFDARELELVIAGTAEIDLSDWRNNTEYRGGYHDNHI 1476
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    1477 VIRWFWAAVERFNNEQRLRLLQFVTGTSSIPYEGFASLRGSngprrFCVEKWG-KITALPRAHTCFNRLDLPPYPSFSML 1555
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                           330
                    ....*....|....
gi 55741473    1556 YEKLLTAVEETSTF 1569
Cdd:smart00119  315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
907-1572 2.36e-132

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 433.04  E-value: 2.36e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  907 STSRSRITLLLQSPPVKFLISPEfftvlhsnpSAYRMFTNnTCLKHMITKVRRDTHHFeryqhnrdlvgFLNMFANKQLE 986
Cdd:COG5021  240 ALLARYISIKLVIKKLYLGPGPD---------ASSRISTL-IIRLSNTNLNRRLSYIL-----------SHSSFEDSLLR 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  987 LPRGWEMKHDHQGKAFFVDHNSRTTTFIDPRLPLQSSRPTSALVHRQHLTRQRSHSAGEVGEDSRHagpPVLPRPSSTFN 1066
Cdd:COG5021  299 LNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFL---EAHPEFSELLK 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1067 TVSRPQYQD-MVPVAYNDKIVAFLRQpniFEILQERQPDLTRNHSLREkiQFIRTEGTPGLVRLSSDADLVM----LLSL 1141
Cdd:COG5021  376 NQSRGTTRDfRNKPTGWSSSIEDLGQ---FLFSDFLTSSSTYEDLRRE--QLGRESDESFYVASNVQQQRASregpLLSG 450

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1142 FEEEIMS----YVPPHALLHPSYCQSPRGSPVSSPQNSpgTQRanarapapYKRDFEAKLRNFYrkleTKGYGQGPGKLK 1217
Cdd:COG5021  451 WKTRLNNlyrfYFVEHRKKTLTKNDSRLGSFISLNKLD--IRR--------IKEDKRRKLFYSL----KQKAKIFDPYLH 516

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1218 LIIRRDHLLEDAFNQIMGYSrKDLQRNKLYVTFVGEEGLDYSGPSREFFFLVSRELFNPYYGLFEYSANDTYTVQISPMS 1297
Cdd:COG5021  517 IKVRRDRVFEDSYREIMDES-GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLS 595

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1298 AFVDNHHEWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRILCDLSDLEYLDEEFHQSLQWMKDNDIHD-ILDLTFTVN 1376
Cdd:COG5021  596 SINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDEtILDLTFTVE 675

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1377 EEVFGQITERELKPGGANIPVTEKNKKEYIERMVKWRIERGVVQQTESLVRGFYEVVDARLVSVFDARELELVIAGTAE- 1455
Cdd:COG5021  676 DDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEd 755

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473 1456 IDLSDWRNNTEYRgGYHDNHIVIRWFWAAVERFNNEQRLRLLQFVTGTSSIPYEGFASLRGSNGPRRFCVEKWG-KITAL 1534
Cdd:COG5021  756 IDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRL 834

                        650       660       670
                 ....*....|....*....|....*....|....*...
gi 55741473 1535 PRAHTCFNRLDLPPYPSFSMLYEKLLTAVEETSTFGLE 1572
Cdd:COG5021  835 PSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 1267-1571 2.28e-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: 396.21  E-value: 2.28e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   1267 FLVSRELFNPYYGLFEYSANDTYTVQISPMSAFVDNHH--EWFRFSGRILGLALIHQYLLDAFFTRPFYKALLRILCDLS 1344
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLEllDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   1345 DLEYLDEEFHQSLQWMK--DNDIHDILDLTFTVneEVFGQITERELKPGGANIPVTEKNKKEYIERMVKWRIERGVVQQT 1422
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   1423 ESLVRGFYEVVDARLVSVFDARELELVIAGTAEIDLSDWRNNTEYRGGYHDNHIVIRWFWAAVERFNNEQRLRLLQFVTG 1502
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55741473   1503 TSSIPYEGFASLrgsngpRRFCVEKWG--KITALPRAHTCFNRLDLPPYPSFSMLYEKLLTAVEETSTFGL 1571
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
C2_NEDL1-like cd08691
C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 ...
 185-321 1.17e-80

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: 261.18  E-value: 1.17e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  185 VSFTLSDLRAVGLKKGMFFNPDPYLKMSIQPGKKSSFPTCAHHGQERRSTIISNTTNPIWHREKYSFFALLTDVLEIEIK 264
Cdd:cd08691    1 LSFSLSGLQARNLKKGMFFNPDPYVKISIQPGKRHIFPALPHHGQECRTSIVENTINPVWHREQFVFVGLPTDVLEIEVK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55741473  265 DKFAKSRPIIKRFLGKLTIPVQRLLERQAIGDQMLSYNLGRRLPADHVSGYLQFKVE 321
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 ...
 45-162 1.18e-79

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: 257.40  E-value: 1.18e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473     45 RANSDTDLVTSESRSSLTASMYEYTLGQAQNLIIFWDIKEEVDPSDWIGLYHIDENSPANFWDSKNRGVTGTQKGQIVWR 124
Cdd:pfam16562    1 RANSDTDLVTSQSRSSLTVSTYEYTLGQGQSLIISWDIKEEVDANDWIGLYHIDENSPANFWDYKNRGVNGTQKGQIVWR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 55741473    125 IEPGPYFMEPEIKICFKYYHGISGALRATTPCITVKNP 162
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 ...
 915-981 7.46e-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: 7.46e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55741473    915 LLLQSPPVKFLISPEFFTVLHSNPSAYRMFTNNTCLKHMITKVRRDTHHFERYQHNRDLVGFLNMFA 981
Cdd:pfam18436    1 ALLNSPAVKFITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 186-292 1.37e-11

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: 62.50  E-value: 1.37e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473     186 SFTLSDLRAVGLKKGMFFN-PDPYLKMSIQPGKKSSFptcahhgqerRSTIISNTTNPIWHrEKYSF--FALLTDVLEIE 262
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKK----------KTKVVKNTLNPVWN-ETFEFevPPPELAELEIE 69

                            90       100       110
                    ....*....|....*....|....*....|
gi 55741473     263 IKDKFAKSRpiiKRFLGKLTIPVQRLLERQ 292
Cdd:smart00239   70 VYDKDRFGR---DDFIGQVTIPLSDLLLGG 96
C2 pfam00168
C2 domain;
192-294 7.40e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 60.41  E-value: 7.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    192 LRAVGL-KKGMFFNPDPYLKMSIQPGKkssfptcahhgQERRSTIISNTTNPIWHrEKYSF--FALLTDVLEIEIKDkfa 268
Cdd:pfam00168    8 IEAKNLpPKDGNGTSDPYVKVYLLDGK-----------QKKKTKVVKNTLNPVWN-ETFTFsvPDPENAVLEIEVYD--- 72

                           90       100
                   ....*....|....*....|....*.
gi 55741473    269 KSRPIIKRFLGKLTIPVQRLLERQAI 294
Cdd:pfam00168   73 YDRFGRDDFIGEVRIPLSELDSGEGL 98
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 809-838 2.47e-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: 56.74  E-value: 2.47e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 55741473    809 LPPNWEARIDSHGRIFYVDHVNRTTTWQRP 838
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 810-839 1.41e-09

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: 1.41e-09
                         10        20        30
                 ....*....|....*....|....*....|
gi 55741473  810 PPNWEARIDSHGRIFYVDHVNRTTTWQRPT 839
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 809-839 2.24e-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: 54.14  E-value: 2.24e-09
                            10        20        30
                    ....*....|....*....|....*....|.
gi 55741473     809 LPPNWEARIDSHGRIFYVDHVNRTTTWQRPT 839
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 192-297 1.02e-08

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: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  192 LRAVGLK-KGMFFNPDPYLKMSIQPGKKssfptcahhgqeRRSTIISNTTNPIWhREKYSFFAL--LTDVLEIEIKDKFA 268
Cdd:cd00030    6 IEARNLPaKDLNGKSDPYVKVSLGGKQK------------FKTKVVKNTLNPVW-NETFEFPVLdpESDTLTVEVWDKDR 72

                         90       100
                 ....*....|....*....|....*....
gi 55741473  269 KSRpiiKRFLGKLTIPVQRLLERQAIGDQ 297
Cdd:cd00030   73 FSK---DDFLGEVEIPLSELLDSGKEGEL 98
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 204-302 1.50e-07

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: 51.03  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  204 NPDPYLKMSIqpGKKSsfptcahhgqeRRSTIISNTTNPIWHrEKYSFFA--LLTDVLEIEIKDKFAKSRpiikrfLGKL 281
Cdd:cd04050   20 EPSPYVELTV--GKTT-----------QKSKVKERTNNPVWE-EGFTFLVrnPENQELEIEVKDDKTGKS------LGSL 79

                         90       100
                 ....*....|....*....|.
gi 55741473  282 TIPVQRLLErqaigDQMLSYN 302
Cdd:cd04050   80 TLPLSELLK-----EPDLTLD 95
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 193-296 9.38e-07

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: 49.48  E-value: 9.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  193 RAVGLKKGMFFN--PDPYLKMSIqpgkkSSFPTCAhhgqerRSTIISNTTNPIWHREKYSFFALLTDVLEIEIKDKfaks 270
Cdd:cd04044   10 SARGLKGSDIIGgtVDPYVTFSI-----SNRRELA------RTKVKKDTSNPVWNETKYILVNSLTEPLNLTVYDF---- 74

                         90       100
                 ....*....|....*....|....*..
gi 55741473  271 RPIIK-RFLGKLTIPVQRLLERQAIGD 296
Cdd:cd04044   75 NDKRKdKLIGTAEFDLSSLLQNPEQEN 101
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 987-1016 6.07e-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: 44.03  E-value: 6.07e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 55741473    987 LPRGWEMKHDHQGKAFFVDHNSRTTTFIDP 1016
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 987-1018 6.35e-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: 6.35e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 55741473     987 LPRGWEMKHDHQGKAFFVDHNSRTTTFIDPRL 1018
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03169 PHA03169
hypothetical protein; Provisional
 584-794 9.05e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.97  E-value: 9.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   584 TSDASGGSRRAVSETESLDQGSEpsqvSSETEPSDPARTESVSEASTRPEGESDLECADSSCNESVTTQLSSVDTRCSSL 663
Cdd:PHA03169   50 APTTSGPQVRAVAEQGHRQTESD----TETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   664 ESarfPETPAFSSQEEEDGA-----CAAEPTSSGPAEGSQESVCTAgslpvvqvPSGEDEGPGAESATVPDQEELGEVWQ 738
Cdd:PHA03169  126 SS---PESPASHSPPPSPPShpgphEPAPPESHNPSPNQQPSSFLQ--------PSHEDSPEEPEPPTSEPEPDSPGPPQ 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   739 ----RRGSLEGAAAAAESPPQEEGSAGEAQGTCEGATAQEEGATGGSQANGHQPLRSLPS 794
Cdd:PHA03169  195 setpTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSHS 254
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 988-1018 9.35e-06

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: 43.67  E-value: 9.35e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 55741473  988 PRGWEMKHDHQGKAFFVDHNSRTTTFIDPRL 1018
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
PHA03169 PHA03169
hypothetical protein; Provisional
 562-816 1.31e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.12  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   562 QGSAELCGSQEVDQPTSG-ADTGTSDASGGSRRAVSEtesldqGSEPSQVSSETEPSDPARTESVSEASTRPEGESDLEC 640
Cdd:PHA03169   89 QGGPSGSGSESVGSPTPSpSGSAEELASGLSPENTSG------SSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQ 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   641 ADSscnesvttqlssvdtrcsslesarfpetpaFSSQEEEDGACAAEPTSSGPAEGSQESVctagslpvvQVPSGEDEGP 720
Cdd:PHA03169  163 PSS------------------------------FLQPSHEDSPEEPEPPTSEPEPDSPGPP---------QSETPTSSPP 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   721 GAESATVPDQEELGEVWQRRGSLEGAAAAAESPPQEEGSAGEAQGTCEGATAQEEGATGGSQANGHQPLR----SLPSVR 796
Cdd:PHA03169  204 PQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPGGVPKLClrctSHPSHR 283

                         250       260
                  ....*....|....*....|
gi 55741473   797 QDVSRYQRVDEALPPNWEAR 816
Cdd:PHA03169  284 SRLPEGQQSEDKVPRKYQAR 303
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 345-700 1.90e-04

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 46.07  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    345 NGDLGSPSDDEDMPGSHHDSqvcsnGPVSEDSAADgTPKHSFRTSSTLEIDTEELTSTSSRTSPPR-----GRQDSLNDY 419
Cdd:pfam07263  130 NSRLGSDEDSADTTQSREDS-----ASQGEDSAQD-TTSESRDLDNEDEVSSRPESGDSTQDSESEehwvgGGSEGDSSH 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    420 LDAIEHNGHSRPGTATCSERSMGASPKLRSSfptdtrlnamlHIDSDE----EDHEFQQDLGYPSSLEEEGGLIMF-SRA 494
Cdd:pfam07263  204 GDGSEFDDEGMQSDDPDSIRSERGNSRMSSA-----------SVKSKEskgdSEQASTQDSGDSQSVEYPSRKFFRkSRI 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    495 SRADDGSltsqtKLEDN--PVENEEASTHEAASFEDKPENLPELAESslpagPAPEEGEGGPEPQPSADQGSAELCGSQE 572
Cdd:pfam07263  273 SEEDDRG-----ELDDSntMEEVKSDSTESTSSKEAGLSQSREDSKS-----ESQEDSEESQSQEDSQNSQDPSSESSQE 342

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    573 VDQPTSgadtgtsDASGGSRRAVSETESLDQGSEPSQVSSETEPSDPARTESVSEASTRpEGESDLECADSSCNESVT-- 650
Cdd:pfam07263  343 ADLPSQ-------ESSSESQEEVVSESRGDNPDNTSSSEEDQEDSDSSEEDSLSTFSSS-ESESREEQADSESNESLRss 414

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 55741473    651 --TQLSSVDTRCSSLESARFPETPAfSSQEEEDGACAAEPTSSGPAEGSQES 700
Cdd:pfam07263  415 eeSPESSEDENSSSQEGLQSHSAST-ESQSEESQSEQDSQSEEDDESDSQDS 465
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 464-631 3.31e-04

Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian neuroendocrine-specific golgi protein P55 (NESP55) sequences. NESP55 is a novel member of the chromogranin family and is a soluble, acidic, heat-stable secretory protein that is expressed exclusively in endocrine and nervous tissues, although less widely than chromogranins.


Pssm-ID: 115071 [Multi-domain]  Cd Length: 261  Bit Score: 44.47  E-value: 3.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    464 DSDEEDHEFQQDLGYPSSLEeegglimfsrasrADDGSLTSQTKLEDNPVENEEASTHeaasFEDKPENLPELAESSlpa 543
Cdd:pfam06390   87 ESDHEDEDFEPELARPECLE-------------YDEDDFDTETDSETEPESDIESETE----FETEPETEPDTAPTT--- 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473    544 gpapeegegGPEPQPSADQGSAELCGS---QEVDQPTSGADTGTSDASggSRRA---VSETESLDQGSEPSQVSSETEPS 617
Cdd:pfam06390  147 ---------EPETEPEDEPGPVVPKGAtfhQSLTERLHALKLQSADAS--PRRAppsTQEPESAREGEEPERGPLDKDPR 215

                          170
                   ....*....|....
gi 55741473    618 DPARTESVSEASTR 631
Cdd:pfam06390  216 DPEEEEEEKEEEKQ 229
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 192-292 2.26e-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: 39.47  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  192 LRAVGL-KKGMFFNPDPYLKMSIQPGkkSSFPTCAHhgqerRSTIISNTTNPIWHREKYSFFAL----LTDVLEIEIKDK 266
Cdd:cd04047    7 FSGKKLdKKDFFGKSDPFLEISRQSE--DGTWVLVY-----RTEVIKNTLNPVWKPFTIPLQKLcngdYDRPIKIEVYDY 79

                         90       100
                 ....*....|....*....|....*.
gi 55741473  267 FAKSRPiikRFLGKLTIPVQRLLERQ 292
Cdd:cd04047   80 DSSGKH---DLIGEFETTLDELLKSS 102
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 489-716 2.49e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 42.27  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   489 IMFSRASRADDGSLTSQTKLEDNPVENEEASTheAASFEDKPENlpelaesslpagpapeegeggpePQPSADQGSAelc 568
Cdd:PRK13108  272 IILAPKGREAPGALRGSEYVVDEALEREPAEL--AAAAVASAAS-----------------------AVGPVGPGEP--- 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   569 gsqevdqptSGADTGTSDASGgsrrAVSETESLDQGSEPSQVSSETEPSDPARTESVSEASTRPEGEsDLECADSSCNES 648
Cdd:PRK13108  324 ---------NQPDDVAEAVKA----EVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPG-DLAGQAPAAHQV 389

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55741473   649 VTTQLSSVDTRCSSLESA----RFPETPAfSSQEEEDGACAAEPTSSGPAEGSQESvctAGSLPVVQVPSGE 716
Cdd:PRK13108  390 DAEAASAAPEEPAALASEahdeTEPEVPE-KAAPIPDPAKPDELAVAGPGDDPAEP---DGIRRQDDFSSRR 457
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
 185-299 2.52e-03

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: 39.60  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  185 VSFTLsdLRAVGL-KKGMFFNPDPYLKMSIQPgkkssfptcahhGQERRSTIISNTTNPIWHrEKYSFFALLTDVLEIEI 263
Cdd:cd08382    2 VRLTV--LCADGLaKRDLFRLPDPFAVITVDG------------GQTHSTDVAKKTLDPKWN-EHFDLTVGPSSIITIQV 66

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 55741473  264 KDKfaksRPIIKR---FLGKLTIPVQRLLERQAIGDQML 299
Cdd:cd08382   67 FDQ----KKFKKKdqgFLGCVRIRANAVLPLKDTGYQRL 101
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 228-324 2.99e-03

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: 39.24  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  228 GQERRSTIISNTTNPIWHrEKYSFF-----ALLTDVLEIEIKDKFAKSRPiiKRFLGKLTIPVQRLLERQAIGdqMLSYN 302
Cdd:cd04022   31 GQKKRTRTKPKDLNPVWN-EKLVFNvsdpsRLSNLVLEVYVYNDRRSGRR--RSFLGRVRISGTSFVPPSEAV--VQRYP 105

                         90       100
                 ....*....|....*....|..
gi 55741473  303 LGRRLPADHVSGYLQFKVEVTS 324
Cdd:cd04022  106 LEKRGLFSRVRGEIGLKVYITD 127
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 229-314 3.29e-03

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 39.27  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  229 QERRSTIISNTTNPIWhrEKYSFFAL--LTDVLEIEIKDKFAKSRPiikRFLGKLTIPVQrLLERQAIGDQMLSYNlGRR 306
Cdd:cd08678   31 QKYQSSTQKNTSNPFW--DEHFLFELspNSKELLFEVYDNGKKSDS---KFLGLAIVPFD-ELRKNPSGRQIFPLQ-GRP 103


                 ....*...
gi 55741473  307 LPADHVSG 314
Cdd:cd08678  104 YEGDSVSG 111
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 192-283 8.28e-03

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: 38.33  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473  192 LRAVGLKK-GMFFNPDPYLKMSI-QPGKKSSfptcahhgqERRSTIISNTTNPIWhREKYSF----FALLTDVLEIEIKD 265
Cdd:cd00276   21 LKARNLPPsDGKGLSDPYVKVSLlQGGKKLK---------KKKTSVKKGTLNPVF-NEAFSFdvpaEQLEEVSLVITVVD 90

                         90
                 ....*....|....*...
gi 55741473  266 KFAKSRPIIkrfLGKLTI 283
Cdd:cd00276   91 KDSVGRNEV---IGQVVL 105
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 319-737 8.62e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 8.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   319 KVEVTSSVHEdaSPEAVGTILGVNSvNGDLGSPSDDEDMPGSHHDSQVCSNGP-VSEDSAADGTPKHSFRTSSTLEidte 397
Cdd:PHA03307   83 ESRSTPTWSL--STLAPASPAREGS-PTPPGPSSPDPPPPTPPPASPPPSPAPdLSEMLRPVGSPGPPPAASPPAA---- 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   398 ELTSTSSRTSPPRGRQDSLNdyLDAIEHngHSRPGTATCSERSMGASPKLRSsfPTDTRLNAMLHIDSDEEDhefqqdlg 477
Cdd:PHA03307  156 GASPAAVASDAASSRQAALP--LSSPEE--TARAPSSPPAEPPPSTPPAAAS--PRPPRRSSPISASASSPA-------- 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   478 yPSSLEEEGglimfSRASRADDGSLTSQTKLEDNPVENEEASTHEAASFEDKPENLPELAESSlpagpapeegeGGPEPQ 557
Cdd:PHA03307  222 -PAPGRSAA-----DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGP-----------SSRPGP 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   558 PSADQGSAELCGSQEVDQPTSGADTGTSDASGGSrraVSETESLDQGSEPSQVSSETEPSDPARTESVSEASTRPEGESD 637
Cdd:PHA03307  285 ASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSS---SSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAD 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741473   638 lecadsscnesvttqLSSVDTRCSSLESARFPETPAFSSQEEedgacAAEPTSSGPAEGSQESVCTAGSLPVVqVPSGED 717
Cdd:PHA03307  362 ---------------PSSPRKRPRPSRAPSSPAASAGRPTRR-----RARAAVAGRARRRDATGRFPAGRPRP-SPLDAG 420

                         410       420
                  ....*....|....*....|
gi 55741473   718 EGPGAESATVPDQEELGEVW 737
Cdd:PHA03307  421 AASGAFYARYPLLTPSGEPW 440
 
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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