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Conserved domains on  [gi|157818573|ref|NP_001099654|]
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NEDD4-like E3 ubiquitin-protein ligase WWP2 [Rattus norvegicus]

Protein Classification

C2_E3_ubiquitin_ligase and HECTc domain-containing protein( domain architecture ID 10134116)

protein containing domains C2_E3_ubiquitin_ligase, PHA03247, WW, and HECTc

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 ...
 516-868 0e+00

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: 529.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLELFF-IQ 674
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 675 DMEILGKVTTHELKEGGENIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 755 IDMSDWQKNAIYRH-YTKSSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDRVGK-ETWL 832
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 157818573 833 PRSHTCFNRLDLPPYKSYEQLKEKLLYAIEETEGFG 868
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 17-142 4.03e-52

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 177.85  E-value: 4.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  17 KSQLTLRVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEVIVLNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157818573  96 LGTASVNLSNVLKNNGGKMENTQLTLNLQTENKGSVVSGGELTIFLD 142
Cdd:cd04021   79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 332-361 1.51e-12

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 62.14  E-value: 1.51e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 157818573  332 LPPGWEKRTDPRGRFYYVDHNTRTTTWQRP 361
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 407-435 3.37e-12

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 61.37  E-value: 3.37e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 157818573  407 LPPGWEKRQD-NGRVYYVNHNTRTTQWEDP 435
Cdd:pfam00397   1 LPPGWEERWDpDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 302-331 1.96e-11

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 59.06  E-value: 1.96e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 157818573  302 LPAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 447-477 1.17e-08

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


:

Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 51.37  E-value: 1.17e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 157818573 447 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 163-312 4.30e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 4.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  163 PPSRESSGTAL-----APETRHQPPSTNCFGGRSRTHRHSGGSARTATATgeqSPgaRNRHRQPVKNPSSSGLANGT--V 235
Cdd:PHA03247 2628 PPSPSPAANEPdphppPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS---SP--PQRPRRRAARPTVGSLTSLAdpP 2702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  236 SEEPTTASDPEEL-SVVGVTSPPAAASSVSPNPNTTSLP--APSTPAEGEEPSTSGTQQLPAA--AQAPDALPAGWEQRQ 310
Cdd:PHA03247 2703 PPPPTPEPAPHALvSATPLPPGPAAARQASPALPAAPAPpaVPAGPATPGGPARPARPPTTAGppAPAPPAAPAAGPPRR 2782


                  ..
gi 157818573  311 LP 312
Cdd:PHA03247 2783 LT 2784
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 516-868 0e+00

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: 529.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLELFF-IQ 674
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 675 DMEILGKVTTHELKEGGENIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 755 IDMSDWQKNAIYRH-YTKSSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDRVGK-ETWL 832
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 157818573 833 PRSHTCFNRLDLPPYKSYEQLKEKLLYAIEETEGFG 868
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 539-867 1.14e-175

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: 509.85  E-value: 1.14e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   539 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 616
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   617 YHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLEL-FFIQDMEILGKVTTHELKEGGENIR 695
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLtFSIVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   696 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKNAIYRH-YTKSSK 774
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   775 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDRVG-KETWLPRSHTCFNRLDLPPYKSYEQL 853
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 157818573   854 KEKLLYAIEETEGF 867
Cdd:smart00119 315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
331-870 5.35e-175

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 528.18  E-value: 5.35e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 402
Cdd:COG5021  298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 403 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 456
Cdd:COG5021  378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 457 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYERSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 536
Cdd:COG5021  458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 537 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 616
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 617 YHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLELFFIQDMEILGKVTTHELKEGGENIRV 696
Cdd:COG5021  617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 697 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKNAIYRHYTKSSKQ 775
Cdd:COG5021  697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 776 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDRVG-KETWLPRSHTCFNRLDLPPYKSYEQLK 854
Cdd:COG5021  777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                        570
                 ....*....|....*.
gi 157818573 855 EKLLYAIEETEGFGQE 870
Cdd:COG5021  857 SKLLTAINEGAGFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 565-868 3.04e-129

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 389.66  E-value: 3.04e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  565 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLR 642
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  643 DLESIDPEFYNSIIWIKENNLD-ECGLELFFIqdMEILGKVTTHELKEGGENIRVTEENKEEYIMLLTDWRFTRGVEEQT 721
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDdDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  722 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKNAIYRH-YTKSSKQIQWFWQVVKEMDNEKRIRLLQFVTG 800
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  801 TCRLPVGGFAELigsngpQKFCIDRVG--KETWLPRSHTCFNRLDLPPYKSYEQLKEKLLYAIEETEGFG 868
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 17-142 4.03e-52

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 177.85  E-value: 4.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  17 KSQLTLRVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEVIVLNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157818573  96 LGTASVNLSNVLKNNGGKMENTQLTLNLQTENKGSVVSGGELTIFLD 142
Cdd:cd04021   79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 332-361 1.51e-12

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 62.14  E-value: 1.51e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 157818573  332 LPPGWEKRTDPRGRFYYVDHNTRTTTWQRP 361
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 407-435 3.37e-12

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 61.37  E-value: 3.37e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 157818573  407 LPPGWEKRQD-NGRVYYVNHNTRTTQWEDP 435
Cdd:pfam00397   1 LPPGWEERWDpDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 406-436 5.18e-12

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 60.69  E-value: 5.18e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 157818573   406 PLPPGWEKRQD-NGRVYYVNHNTRTTQWEDPR 436
Cdd:smart00456   1 PLPPGWEERKDpDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 408-436 1.11e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 59.85  E-value: 1.11e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 157818573 408 PPGWEKRQDN-GRVYYVNHNTRTTQWEDPR 436
Cdd:cd00201    1 PPGWEERWDPdGRVYYYNHNTKETQWEDPR 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 302-331 1.96e-11

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 59.06  E-value: 1.96e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 157818573  302 LPAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 331-362 3.69e-11

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 58.38  E-value: 3.69e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 157818573   331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 362
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 333-362 7.23e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 57.54  E-value: 7.23e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 157818573 333 PPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 362
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 302-331 8.06e-11

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 57.23  E-value: 8.06e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 157818573   302 LPAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 303-331 9.79e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 57.15  E-value: 9.79e-11
                         10        20
                 ....*....|....*....|....*....
gi 157818573 303 PAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 19-115 4.57e-09

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: 54.42  E-value: 4.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573    19 QLTLRVVSAKPKVHNRQPR-INSYVEVAVDGLPSETKKTGKRIGSSELLWNEVIVLNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80

                           90       100
                   ....*....|....*....|.
gi 157818573    95 LLGTASVNLSNVLKNNGGKME 115
Cdd:smart00239  81 FIGQVTIPLSDLLLGGRHEKL 101
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 447-477 1.17e-08

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 51.37  E-value: 1.17e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 157818573 447 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 446-475 7.48e-08

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: 49.04  E-value: 7.48e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 157818573  446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDP 475
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 446-477 1.45e-07

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: 47.98  E-value: 1.45e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 157818573   446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03247 PHA03247
large tegument protein UL36; Provisional
 163-312 4.30e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 4.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  163 PPSRESSGTAL-----APETRHQPPSTNCFGGRSRTHRHSGGSARTATATgeqSPgaRNRHRQPVKNPSSSGLANGT--V 235
Cdd:PHA03247 2628 PPSPSPAANEPdphppPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS---SP--PQRPRRRAARPTVGSLTSLAdpP 2702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  236 SEEPTTASDPEEL-SVVGVTSPPAAASSVSPNPNTTSLP--APSTPAEGEEPSTSGTQQLPAA--AQAPDALPAGWEQRQ 310
Cdd:PHA03247 2703 PPPPTPEPAPHALvSATPLPPGPAAARQASPALPAAPAPpaVPAGPATPGGPARPARPPTTAGppAPAPPAAPAAGPPRR 2782


                  ..
gi 157818573  311 LP 312
Cdd:PHA03247 2783 LT 2784
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 104-310 6.51e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.36  E-value: 6.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   104 SNVLKNNGGKMENTQLTLNLQTENKGSVVSGGelTIFLDGPTVDLGSVPNGSAVTDGSQPPSRESSGTALApETRhqpPS 183
Cdd:TIGR00927  268 TDLLTSPRSVVEKNTLTTPRRVESNSSTNHWG--LVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSSPA-ETK---AS 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   184 TNCFGGRSRTHRHSGGSARTATATgeqspgarnrHRQPVKNPSS--SGLANGTVSEEPTTASDPeelsvvGVTSPPAAAS 261
Cdd:TIGR00927  342 TAAWKIRNPLSRTSAPAVRIASAT----------FRGLEKNPSTapSTPATPRVRAVLTTQVHH------CVVVKPAPAV 405

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 157818573   262 SVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRQ 310
Cdd:TIGR00927  406 PTTPSPSLTTALFPEAPSPSPSALPPGQPDLHPKAEYPPDLFSVEERRQ 454
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 516-868 0e+00

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: 529.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLELFF-IQ 674
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 675 DMEILGKVTTHELKEGGENIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 755 IDMSDWQKNAIYRH-YTKSSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDRVGK-ETWL 832
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 157818573 833 PRSHTCFNRLDLPPYKSYEQLKEKLLYAIEETEGFG 868
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 539-867 1.14e-175

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: 509.85  E-value: 1.14e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   539 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 616
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   617 YHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLEL-FFIQDMEILGKVTTHELKEGGENIR 695
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLtFSIVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   696 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKNAIYRH-YTKSSK 774
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   775 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDRVG-KETWLPRSHTCFNRLDLPPYKSYEQL 853
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 157818573   854 KEKLLYAIEETEGF 867
Cdd:smart00119 315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
331-870 5.35e-175

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 528.18  E-value: 5.35e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 402
Cdd:COG5021  298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 403 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 456
Cdd:COG5021  378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 457 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYERSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 536
Cdd:COG5021  458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 537 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 616
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 617 YHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLELFFIQDMEILGKVTTHELKEGGENIRV 696
Cdd:COG5021  617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 697 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKNAIYRHYTKSSKQ 775
Cdd:COG5021  697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 776 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDRVG-KETWLPRSHTCFNRLDLPPYKSYEQLK 854
Cdd:COG5021  777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                        570
                 ....*....|....*.
gi 157818573 855 EKLLYAIEETEGFGQE 870
Cdd:COG5021  857 SKLLTAINEGAGFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 565-868 3.04e-129

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 389.66  E-value: 3.04e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  565 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLR 642
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  643 DLESIDPEFYNSIIWIKENNLD-ECGLELFFIqdMEILGKVTTHELKEGGENIRVTEENKEEYIMLLTDWRFTRGVEEQT 721
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDdDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  722 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKNAIYRH-YTKSSKQIQWFWQVVKEMDNEKRIRLLQFVTG 800
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  801 TCRLPVGGFAELigsngpQKFCIDRVG--KETWLPRSHTCFNRLDLPPYKSYEQLKEKLLYAIEETEGFG 868
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 17-142 4.03e-52

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 177.85  E-value: 4.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  17 KSQLTLRVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEVIVLNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157818573  96 LGTASVNLSNVLKNNGGKMENTQLTLNLQTENKGSVVSGGELTIFLD 142
Cdd:cd04021   79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 332-361 1.51e-12

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 62.14  E-value: 1.51e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 157818573  332 LPPGWEKRTDPRGRFYYVDHNTRTTTWQRP 361
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 407-435 3.37e-12

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 61.37  E-value: 3.37e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 157818573  407 LPPGWEKRQD-NGRVYYVNHNTRTTQWEDP 435
Cdd:pfam00397   1 LPPGWEERWDpDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 406-436 5.18e-12

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 60.69  E-value: 5.18e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 157818573   406 PLPPGWEKRQD-NGRVYYVNHNTRTTQWEDPR 436
Cdd:smart00456   1 PLPPGWEERKDpDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 408-436 1.11e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 59.85  E-value: 1.11e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 157818573 408 PPGWEKRQDN-GRVYYVNHNTRTTQWEDPR 436
Cdd:cd00201    1 PPGWEERWDPdGRVYYYNHNTKETQWEDPR 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 302-331 1.96e-11

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 59.06  E-value: 1.96e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 157818573  302 LPAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 331-362 3.69e-11

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 58.38  E-value: 3.69e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 157818573   331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 362
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 333-362 7.23e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 57.54  E-value: 7.23e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 157818573 333 PPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 362
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 302-331 8.06e-11

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 57.23  E-value: 8.06e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 157818573   302 LPAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 303-331 9.79e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 57.15  E-value: 9.79e-11
                         10        20
                 ....*....|....*....|....*....
gi 157818573 303 PAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 19-115 4.57e-09

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: 54.42  E-value: 4.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573    19 QLTLRVVSAKPKVHNRQPR-INSYVEVAVDGLPSETKKTGKRIGSSELLWNEVIVLNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80

                           90       100
                   ....*....|....*....|.
gi 157818573    95 LLGTASVNLSNVLKNNGGKME 115
Cdd:smart00239  81 FIGQVTIPLSDLLLGGRHEKL 101
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 447-477 1.17e-08

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 51.37  E-value: 1.17e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 157818573 447 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 446-475 7.48e-08

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: 49.04  E-value: 7.48e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 157818573  446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDP 475
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
PRP40 COG5104
Splicing factor [RNA processing and modification];
297-381 7.98e-08

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 55.86  E-value: 7.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 297 QAPDALPAG-----WEQRQLPNGRVYYVDHNTKTTTWERPLP-----------PGWEKRTDPRGRFYYVDHNTRTTTWQR 360
Cdd:COG5104    3 AALLGMASGearseWEELKAPDGRIYYYNKRTGKSSWEKPKEllkgseedldvDPWKECRTADGKVYYYNSITRESRWKI 82

                         90       100
                 ....*....|....*....|....
gi 157818573 361 PtAEYVR---NYEQWQSQRNQLQG 381
Cdd:COG5104   83 P-PERKKvepIAEQKHDERSMIGG 105
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 446-477 1.45e-07

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: 47.98  E-value: 1.45e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 157818573   446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03247 PHA03247
large tegument protein UL36; Provisional
 163-312 4.30e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 4.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  163 PPSRESSGTAL-----APETRHQPPSTNCFGGRSRTHRHSGGSARTATATgeqSPgaRNRHRQPVKNPSSSGLANGT--V 235
Cdd:PHA03247 2628 PPSPSPAANEPdphppPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS---SP--PQRPRRRAARPTVGSLTSLAdpP 2702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  236 SEEPTTASDPEEL-SVVGVTSPPAAASSVSPNPNTTSLP--APSTPAEGEEPSTSGTQQLPAA--AQAPDALPAGWEQRQ 310
Cdd:PHA03247 2703 PPPPTPEPAPHALvSATPLPPGPAAARQASPALPAAPAPpaVPAGPATPGGPARPARPPTTAGppAPAPPAAPAAGPPRR 2782


                  ..
gi 157818573  311 LP 312
Cdd:PHA03247 2783 LT 2784
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 20-112 9.73e-06

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: 45.14  E-value: 9.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  20 LTLRVVSAK-PKVHNRQPRINSYVEVAVDGlpSETKKTGKRIGSSELLWNEVIVLNVT--AQSHLDLKVWSCHTL-RNEL 95
Cdd:cd00030    1 LRVTVIEARnLPAKDLNGKSDPYVKVSLGG--KQKFKTKVVKNTLNPVWNETFEFPVLdpESDTLTVEVWDKDRFsKDDF 78

                         90
                 ....*....|....*..
gi 157818573  96 LGTASVNLSNVLKNNGG 112
Cdd:cd00030   79 LGEVEIPLSELLDSGKE 95
PHA03247 PHA03247
large tegument protein UL36; Provisional
 162-345 1.14e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  162 QPPSRESSGTALAPETrhqPPSTNCFGGRSRTHRHSGGSARTATATGEQSPGARNRHRQP--VKNPSSSGLANGTVSEEP 239
Cdd:PHA03247 2704 PPPTPEPAPHALVSAT---PLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPptTAGPPAPAPPAAPAAGPP 2780

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  240 TTASDPEELSVVGVT----SPPAAASSVSP-NPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRQLPNG 314
Cdd:PHA03247 2781 RRLTRPAVASLSESReslpSPWDPADPPAAvLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGG 2860

                         170       180       190
                  ....*....|....*....|....*....|.
gi 157818573  315 rvyyvDHNTKTTTweRPLPPGWEKRTDPRGR 345
Cdd:PHA03247 2861 -----DVRRRPPS--RSPAAKPAAPARPPVR 2884
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
149-299 4.40e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 47.15  E-value: 4.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 149 GSVPNGSAVTDGSQPPSRESSGTALAPETRHQPPSTNCFGGRSRTHRHSGGSARTATATGEQSPGARNRhrQPVKNPSSS 228
Cdd:PRK07003 400 TAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDA--QPPADSGSA 477

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157818573 229 GLANGTVseEPTTASDPEELSVVgvtSPPAAASSVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAP 299
Cdd:PRK07003 478 SAPASDA--PPDAAFEPAPRAAA---PSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 151-310 4.67e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.47  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  151 VPNGSAVTDGSQPPSRESsGTALAPETRHQPPSTNCFGGRSRTHRHSGGSARTATATGEQSPGARNRHRQPVKNPSSSGL 230
Cdd:PHA03307  230 DDAGASSSDSSSSESSGC-GWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPA 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  231 ANGTVSEEPTTASDPEELSVVGVTSPPAAASSVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRQ 310
Cdd:PHA03307  309 PSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRR 388
PHA03247 PHA03247
large tegument protein UL36; Provisional
 159-345 5.90e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 5.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  159 DGSQPPSRESSGTALAPETrhQPPSTNCFGGRSRTHRHSGGSARTATATGEQ----SPGARNRHRQpVKNPSSSGLANGT 234
Cdd:PHA03247 2603 DDRGDPRGPAPPSPLPPDT--HAPDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSP 2679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  235 VSEEPTTASDPEELSVVGVTSPPAaassvsPNPNTTSLPAPSTPAegeEPSTSGTQQLPAAAQAPDALPAgweQRQLPNG 314
Cdd:PHA03247 2680 PQRPRRRAARPTVGSLTSLADPPP------PPPTPEPAPHALVSA---TPLPPGPAAARQASPALPAAPA---PPAVPAG 2747

                         170       180       190
                  ....*....|....*....|....*....|.
gi 157818573  315 RVYYVDHNTKTTtweRPLPPGWEKRTDPRGR 345
Cdd:PHA03247 2748 PATPGGPARPAR---PPTTAGPPAPAPPAAP 2775
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
144-300 2.20e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.84  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 144 PTVDLGSVPNG--SAVTDGSQPPSRESSGTALAPETR-HQPPSTNCFGGRSRTHrhsggSARTATATGEQSPGARNrhrq 220
Cdd:PRK07003 360 PAVTGGGAPGGgvPARVAGAVPAPGARAAAAVGASAVpAVTAVTGAAGAALAPK-----AAAAAAATRAEAPPAAP---- 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 221 pvkNPSSSGLANGTVSEEPTTASDPEELSVVGVTSPPAAASSVSPNPNTTSLPAPSTPAEG-EEPSTSGTQQLPAAAQAP 299
Cdd:PRK07003 431 ---APPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAaFEPAPRAAAPSAATPAAV 507


                 .
gi 157818573 300 D 300
Cdd:PRK07003 508 P 508
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 154-308 5.61e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 154 GSAVTDGSQPPSRESSGTALAPETRHQPPStncfggrsrthrhSGGSARTATATGEQSPGARNRHRQPVKNPSSSGLANG 233
Cdd:PRK07764 390 GAGAPAAAAPSAAAAAPAAAPAPAAAAPAA-------------AAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSP 456

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157818573 234 TVSEEPTTASDPeelsvvgvtsPPAAASSVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALpagWEQ 308
Cdd:PRK07764 457 PPAAAPSAQPAP----------APAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRER---WPE 518
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 143-300 6.21e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 6.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 143 GPTVDLGSVPNGSAVTDGSQPPSRESSGTALAPETRHQPPSTNCFGGRSRTHrhsggSARTATATGEQSPGARNRHRQPV 222
Cdd:PRK07764 651 EHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA-----PAPAATPPAGQADDPAAQPPQAA 725

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818573 223 KNPSSSGLANGTVSEEPTTASDPEELSVVGVTSPPAAASSVSPNPNTTslPAPSTPAEGEEPstsgtqqLPAAAQAPD 300
Cdd:PRK07764 726 QGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAA--PPPSPPSEEEEM-------AEDDAPSMD 794
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 141-334 1.09e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  141 LDGPTVDLGSVPNGSAVTDGSQPPSRESSGTALAPETRHQPPSTNCFGGRSRTHRHSGGSARTAT----ATGEQSPGARN 216
Cdd:PHA03307  259 RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSREssssSTSSSSESSRG 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  217 RHRQPVKNPSSSglangtvseePTTASDPEELSvvgvTSPPAAASSVSPNPNTTSLPAPSTP-------AEGEEPSTSGT 289
Cdd:PHA03307  339 AAVSPGPSPSRS----------PSPSRPPPPAD----PSSPRKRPRPSRAPSSPAASAGRPTrrraraaVAGRARRRDAT 404

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157818573  290 QQLPAAAQAPDALPA-GWEQRQLPNGRVYYVDhntKTTTWERPLPP 334
Cdd:PHA03307  405 GRFPAGRPRPSPLDAgAASGAFYARYPLLTPS---GEPWPGSPPPP 447
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
156-301 1.14e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 156 AVTDGSQPPsressGTALAPETRHQPpstncfGGRSRTHRHSGGSARTATATGEQSPGARNRhrqpvknPSSSGLANGTV 235
Cdd:PRK07003 361 AVTGGGAPG-----GGVPARVAGAVP------APGARAAAAVGASAVPAVTAVTGAAGAALA-------PKAAAAAAATR 422

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157818573 236 SEEPTTASDPEELSVVGVTSPPAAASSVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDA 301
Cdd:PRK07003 423 AEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDA 488
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 144-315 2.00e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  144 PTVDLGSVPNGSAVTDGSQPPSRESSGTALAPETRHQPPSTNCFGGRSRTHrhsgGSARTATATGEQSPGARNRHRQPvK 223
Cdd:PHA03307   80 PANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSP----APDLSEMLRPVGSPGPPPAASPP-A 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  224 NPSSSGlangtvsEEPTTASDPEELSVVGVTSPPAAASSVSPNPNttslPAPSTPAEGEEPSTSGTQQlPAAAQAPDALP 303
Cdd:PHA03307  155 AGASPA-------AVASDAASSRQAALPLSSPEETARAPSSPPAE----PPPSTPPAAASPRPPRRSS-PISASASSPAP 222

                         170
                  ....*....|..
gi 157818573  304 AGWEQRQLPNGR 315
Cdd:PHA03307  223 APGRSAADDAGA 234
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
 20-131 2.53e-03

C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176016 [Multi-domain]  Cd Length: 125  Bit Score: 38.75  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573  20 LTLRVVSAKP-KVHNRQPRINSYVEVAVDGlpsETKKTGK--RIGSSELLWNEVIVLNVTAQ------SHLDLKVWsCHT 90
Cdd:cd04051    2 LEITIISAEDlKNVNLFGKMKVYAVVWIDP---SHKQSTPvdRDGGTNPTWNETLRFPLDERllqqgrLALTIEVY-CER 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157818573  91 --LRNELLGTASVNLSNVLKNNGGKMENTQLTLNLQTEN---KGSV 131
Cdd:cd04051   78 psLGDKLIGEVRVPLKDLLDGASPAGELRFLSYQLRRPSgkpQGVL 123
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 160-371 4.29e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 160 GSQPPSRESSGTALAPETRHQPPSTncfggrsrthRHSGGSARTATAtGEQSPGARNRHRQPVKNPSSSGLANGTVSEEP 239
Cdd:PRK07764 594 AAGGEGPPAPASSGPPEEAARPAAP----------AAPAAPAAPAPA-GAAAAPAEASAAPAPGVAAPEHHPKHVAVPDA 662

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 240 TTASDPEelsvvGVTSPPAAASSVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRQLPNGRVyyv 319
Cdd:PRK07764 663 SDGGDGW-----PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPA--- 734

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157818573 320 dhntktTTWERPLPPGWEKRTDPRGRFYYVDHNTRT---TTWQRPTAEYVRNYEQ 371
Cdd:PRK07764 735 ------ADDPVPLPPEPDDPPDPAGAPAQPPPPPAPapaAAPAAAPPPSPPSEEE 783
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 104-310 6.51e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.36  E-value: 6.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   104 SNVLKNNGGKMENTQLTLNLQTENKGSVVSGGelTIFLDGPTVDLGSVPNGSAVTDGSQPPSRESSGTALApETRhqpPS 183
Cdd:TIGR00927  268 TDLLTSPRSVVEKNTLTTPRRVESNSSTNHWG--LVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSSPA-ETK---AS 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573   184 TNCFGGRSRTHRHSGGSARTATATgeqspgarnrHRQPVKNPSS--SGLANGTVSEEPTTASDPeelsvvGVTSPPAAAS 261
Cdd:TIGR00927  342 TAAWKIRNPLSRTSAPAVRIASAT----------FRGLEKNPSTapSTPATPRVRAVLTTQVHH------CVVVKPAPAV 405

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 157818573   262 SVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRQ 310
Cdd:TIGR00927  406 PTTPSPSLTTALFPEAPSPSPSALPPGQPDLHPKAEYPPDLFSVEERRQ 454
 
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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