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Conserved domains on  [gi|380786207|gb|AFE64979|]
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NEDD4-like E3 ubiquitin-protein ligase WWP2 isoform 1 [Macaca mulatta]

Protein Classification

WW domain-containing protein( domain architecture ID 10134116)

WW domain-containing protein; the WW domain mediates protein-protein interaction via proline-rich motifs, such as PPxY; similar to mammalian Yes-associated protein 1 (YAP1) which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis

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: 531.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESVDPEFYNSIVWIKENNLEECGLELYF-IQ 674
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 675 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 755 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPIGGFAELigsngPQKFCIDKVGK-ETWL 832
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 380786207 833 PRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFG 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 1.51e-53

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: 181.71  E-value: 1.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLasETKKTAKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQ--PPKKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 380786207  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 2.49e-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: 61.75  E-value: 2.49e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 380786207  332 LPPGWEKRTDPRGRFYYVDHNTRTTTWQPP 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 3.75e-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: 60.98  E-value: 3.75e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 380786207  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 2.40e-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: 58.67  E-value: 2.40e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 380786207  302 LPAGWEQRELPNGRVYYVDHNTKTTTWERP 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 1.26e-08

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


:

Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 50.99  E-value: 1.26e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 380786207 447 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 163-312 1.28e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  163 PPSRDSSGTAV-----APENRHQLPSTNCFGGRSRTHRHSGAAARttpATGEQSPGARSqhRQPVKNSGHSGLANgtVND 237
Cdd:PHA03247 2628 PPSPSPAANEPdphppPTVPPPERPRDDPAPGRVSRPRRARRLGR---AAQASSPPQRP--RRRAARPTVGSLTS--LAD 2700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  238 EPTTATDPE---EPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGE----EPSTSGTQQLPAA--AQAPDALPAGWEQ 308
Cdd:PHA03247 2701 PPPPPPTPEpapHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPatpgGPARPARPPTTAGppAPAPPAAPAAGPP 2780


                  ....
gi 380786207  309 RELP 312
Cdd:PHA03247 2781 RRLT 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: 531.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESVDPEFYNSIVWIKENNLEECGLELYF-IQ 674
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 675 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 755 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPIGGFAELigsngPQKFCIDKVGK-ETWL 832
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 380786207 833 PRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFG 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 3.54e-178

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: 516.40  E-value: 3.54e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207   539 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 616
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207   617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESVDPEFYNSIVWIKENNLEECGLELYF-IQDMEILGKVTTHELKEGGESIR 695
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFsIVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207   696 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSK 774
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207   775 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPIGGFAELigsngPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQL 853
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 380786207   854 REKLLYAIEETEGF 867
Cdd:smart00119 315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
331-870 1.46e-174

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 527.03  E-value: 1.46e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQPPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 402
Cdd:COG5021  298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 403 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 456
Cdd:COG5021  378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 457 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 536
Cdd:COG5021  458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 537 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 616
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESVDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRV 696
Cdd:COG5021  617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 697 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKSTIYRHYTKNSKQ 775
Cdd:COG5021  697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 776 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPIGGFAELIGSNGPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQLR 854
Cdd:COG5021  777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                        570
                 ....*....|....*.
gi 380786207 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 1.09e-127

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 385.81  E-value: 1.09e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  565 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLK 642
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  643 DLESVDPEFYNSIVWIKE-NNLEECGLELYFIqdMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQT 721
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  722 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTG 800
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  801 TCRLPIGGFAELigsngpQKFCIDKVG--KETWLPRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFG 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 1.51e-53

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: 181.71  E-value: 1.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLasETKKTAKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQ--PPKKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 380786207  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 2.49e-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: 61.75  E-value: 2.49e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 380786207  332 LPPGWEKRTDPRGRFYYVDHNTRTTTWQPP 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 3.75e-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: 60.98  E-value: 3.75e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 380786207  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 6.00e-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: 6.00e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 380786207   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 1.26e-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: 59.46  E-value: 1.26e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 380786207 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 2.40e-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: 58.67  E-value: 2.40e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 380786207  302 LPAGWEQRELPNGRVYYVDHNTKTTTWERP 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 5.84e-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: 57.61  E-value: 5.84e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 380786207   331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQPPT 362
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 302-331 1.00e-10

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 57.23  E-value: 1.00e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 380786207   302 LPAGWEQRELPNGRVYYVDHNTKTTTWERP 331
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 333-362 1.03e-10

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 57.15  E-value: 1.03e-10
                         10        20        30
                 ....*....|....*....|....*....|
gi 380786207 333 PPGWEKRTDPRGRFYYVDHNTRTTTWQPPT 362
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 303-331 1.14e-10

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 56.77  E-value: 1.14e-10
                         10        20
                 ....*....|....*....|....*....
gi 380786207 303 PAGWEQRELPNGRVYYVDHNTKTTTWERP 331
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 19-115 1.22e-08

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: 53.26  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207    19 QLTLKVVSAKPKVHNRQPR-INSYVEVAVDGLASETKKTAKRIGSSELLWNEIIILNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80

                           90       100
                   ....*....|....*....|.
gi 380786207    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 1.26e-08

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 50.99  E-value: 1.26e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 380786207 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 8.42e-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: 48.66  E-value: 8.42e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 380786207  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 1.64e-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: 1.64e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 380786207   446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03247 PHA03247
large tegument protein UL36; Provisional
 163-312 1.28e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  163 PPSRDSSGTAV-----APENRHQLPSTNCFGGRSRTHRHSGAAARttpATGEQSPGARSqhRQPVKNSGHSGLANgtVND 237
Cdd:PHA03247 2628 PPSPSPAANEPdphppPTVPPPERPRDDPAPGRVSRPRRARRLGR---AAQASSPPQRP--RRRAARPTVGSLTS--LAD 2700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  238 EPTTATDPE---EPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGE----EPSTSGTQQLPAA--AQAPDALPAGWEQ 308
Cdd:PHA03247 2701 PPPPPPTPEpapHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPatpgGPARPARPPTTAGppAPAPPAAPAAGPP 2780


                  ....
gi 380786207  309 RELP 312
Cdd:PHA03247 2781 RRLT 2784
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 221-422 2.98e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.69  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  221 PVKNsGHSGLANGTVNDEPTTATD----PEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAA 296
Cdd:PRK10263  309 PLLN-GAPITEPVAVAAAATTATQswaaPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYA 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  297 QAPDALPAGWEQRELPNGRVYYVDHNTktttwERPLPPGWEKRTDPRGRFYYVDHNTRTTT---WQPPTAEYVrnYEQwQ 373
Cdd:PRK10263  388 QPAVQYNEPLQQPVQPQQPYYAPAAEQ-----PAQQPYYAPAPEQPAQQPYYAPAPEQPVAgnaWQAEEQQST--FAP-Q 459

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 380786207  374 SQRNQLQGAMQHFSQRFLYQSSSASTDHDPLGPLPPGWEKRQDNGRVYY 422
Cdd:PRK10263  460 STYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYY 508
 
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: 531.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESVDPEFYNSIVWIKENNLEECGLELYF-IQ 674
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 675 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 755 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPIGGFAELigsngPQKFCIDKVGK-ETWL 832
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 380786207 833 PRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFG 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 3.54e-178

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: 516.40  E-value: 3.54e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207   539 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 616
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207   617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESVDPEFYNSIVWIKENNLEECGLELYF-IQDMEILGKVTTHELKEGGESIR 695
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFsIVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207   696 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSK 774
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207   775 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPIGGFAELigsngPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQL 853
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 380786207   854 REKLLYAIEETEGF 867
Cdd:smart00119 315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
331-870 1.46e-174

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 527.03  E-value: 1.46e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQPPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 402
Cdd:COG5021  298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 403 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 456
Cdd:COG5021  378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 457 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 536
Cdd:COG5021  458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 537 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 616
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESVDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRV 696
Cdd:COG5021  617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 697 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKSTIYRHYTKNSKQ 775
Cdd:COG5021  697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 776 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPIGGFAELIGSNGPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQLR 854
Cdd:COG5021  777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                        570
                 ....*....|....*.
gi 380786207 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 1.09e-127

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 385.81  E-value: 1.09e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  565 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLK 642
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  643 DLESVDPEFYNSIVWIKE-NNLEECGLELYFIqdMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQT 721
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  722 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTG 800
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  801 TCRLPIGGFAELigsngpQKFCIDKVG--KETWLPRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFG 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 1.51e-53

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: 181.71  E-value: 1.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLasETKKTAKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQ--PPKKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 380786207  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 2.49e-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: 61.75  E-value: 2.49e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 380786207  332 LPPGWEKRTDPRGRFYYVDHNTRTTTWQPP 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 3.75e-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: 60.98  E-value: 3.75e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 380786207  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 6.00e-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: 6.00e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 380786207   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 1.26e-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: 59.46  E-value: 1.26e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 380786207 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 2.40e-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: 58.67  E-value: 2.40e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 380786207  302 LPAGWEQRELPNGRVYYVDHNTKTTTWERP 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 5.84e-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: 57.61  E-value: 5.84e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 380786207   331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQPPT 362
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 302-331 1.00e-10

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 57.23  E-value: 1.00e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 380786207   302 LPAGWEQRELPNGRVYYVDHNTKTTTWERP 331
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 333-362 1.03e-10

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 57.15  E-value: 1.03e-10
                         10        20        30
                 ....*....|....*....|....*....|
gi 380786207 333 PPGWEKRTDPRGRFYYVDHNTRTTTWQPPT 362
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 303-331 1.14e-10

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 56.77  E-value: 1.14e-10
                         10        20
                 ....*....|....*....|....*....
gi 380786207 303 PAGWEQRELPNGRVYYVDHNTKTTTWERP 331
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 19-115 1.22e-08

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: 53.26  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207    19 QLTLKVVSAKPKVHNRQPR-INSYVEVAVDGLASETKKTAKRIGSSELLWNEIIILNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80

                           90       100
                   ....*....|....*....|.
gi 380786207    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 1.26e-08

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 50.99  E-value: 1.26e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 380786207 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 8.42e-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: 48.66  E-value: 8.42e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 380786207  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 1.64e-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: 1.64e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 380786207   446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PRP40 COG5104
Splicing factor [RNA processing and modification];
297-381 5.90e-07

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 53.16  E-value: 5.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 297 QAPDALPAG-----WEQRELPNGRVYYVDHNTKTTTWERPLP-----------PGWEKRTDPRGRFYYVDHNTRTTTWQP 360
Cdd:COG5104    3 AALLGMASGearseWEELKAPDGRIYYYNKRTGKSSWEKPKEllkgseedldvDPWKECRTADGKVYYYNSITRESRWKI 82

                         90       100
                 ....*....|....*....|....
gi 380786207 361 PtAEYVR---NYEQWQSQRNQLQG 381
Cdd:COG5104   83 P-PERKKvepIAEQKHDERSMIGG 105
PHA03247 PHA03247
large tegument protein UL36; Provisional
 163-312 1.28e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  163 PPSRDSSGTAV-----APENRHQLPSTNCFGGRSRTHRHSGAAARttpATGEQSPGARSqhRQPVKNSGHSGLANgtVND 237
Cdd:PHA03247 2628 PPSPSPAANEPdphppPTVPPPERPRDDPAPGRVSRPRRARRLGR---AAQASSPPQRP--RRRAARPTVGSLTS--LAD 2700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  238 EPTTATDPE---EPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGE----EPSTSGTQQLPAA--AQAPDALPAGWEQ 308
Cdd:PHA03247 2701 PPPPPPTPEpapHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPatpgGPARPARPPTTAGppAPAPPAAPAAGPP 2780


                  ....
gi 380786207  309 RELP 312
Cdd:PHA03247 2781 RRLT 2784
PHA03247 PHA03247
large tegument protein UL36; Provisional
 150-409 4.10e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  150 SVPNGSAVTDGSQPPSrDSSGTAVAPenrhqlpstncfGGRSRTHRHSGAAArTTPATGEQSPgARSQHRQPVKNSGHSg 229
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPS-LPLGGSVAP------------GGDVRRRPPSRSPA-AKPAAPARPP-VRRLARPAVSRSTES- 2897

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  230 langtvndEPTTATDPEEPSvvgvTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPD-ALPAGWEQ 308
Cdd:PHA03247 2898 --------FALPPDQPERPP----QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSgAVPQPWLG 2965

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  309 RELPnGRVYYVDHNTKTTTWERPLPpgwEKRTDPRgrfyyVDHNT-RTTTWQPPTAEYVRNYEQWQSQRNQLQGA--MQH 385
Cdd:PHA03247 2966 ALVP-GRVAVPRFRVPQPAPSREAP---ASSTPPL-----TGHSLsRVSSWASSLALHEETDPPPVSLKQTLWPPddTED 3036

                         250       260
                  ....*....|....*....|....
gi 380786207  386 FSQRFLYQSSSASTDHDPLGPLPP 409
Cdd:PHA03247 3037 SDADSLFDSDSERSDLEALDPLPP 3060
PHA03247 PHA03247
large tegument protein UL36; Provisional
 143-448 9.39e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 9.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  143 GPTVDLGSVPNGSAVTDGSQPPSRDSSGTAVAPENRHQLPSTNCFGGRSRThRHSGAAARTTPATGEQSPGARSQHRQPV 222
Cdd:PHA03247 2724 GPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPW 2802

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  223 KNSGHSGLANGTVNDEPTTATdPEEPSVVGVTSPPAAPlSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDAL 302
Cdd:PHA03247 2803 DPADPPAAVLAPAAALPPAAS-PAGPLPPPTSAQPTAP-PPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPAR 2880

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  303 PagwEQRELPNGRVyyvdhntKTTTWERPLPPGWEKRtdPRgrfyyvdhntrtttwQPPTAEYVRNYEQWQSQ-RNQLQG 381
Cdd:PHA03247 2881 P---PVRRLARPAV-------SRSTESFALPPDQPER--PP---------------QPQAPPPPQPQPQPPPPpQPQPPP 2933

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380786207  382 AMQHFSQRFLYQSSSASTDHDPLGPLPPGWEKRQDNGRVYYVnhNTRTTQWEDPRTqgmIQEPALPP 448
Cdd:PHA03247 2934 PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVP--RFRVPQPAPSRE---APASSTPP 2995
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 154-319 9.46e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 9.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 154 GSAVTDGSQPPSRDSSGTAVAPENRHQLPSTncfGGRSRTHRHSGAAArttPATGEQSPGARSQHRQPVKNSghsglang 233
Cdd:PRK07764 390 GAGAPAAAAPSAAAAAPAAAPAPAAAAPAAA---AAPAPAAAPQPAPA---PAPAPAPPSPAGNAPAGGAPS-------- 455

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 234 tvndePTTATDPEEPSVVGVTSPPAAplsvTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALpagWEQ-RELP 312
Cdd:PRK07764 456 -----PPPAAAPSAQPAPAPAAAPEP----TAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRER---WPEiLAAV 523


                 ....*..
gi 380786207 313 NGRVYYV 319
Cdd:PRK07764 524 PKRSRKT 530
PRK10905 PRK10905
cell division protein DamX; Validated
 198-301 1.26e-04

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 44.93  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 198 GAAARTTP--ATGEQSPGARSQHRQPVKNSGHSglangtvndEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAP 275
Cdd:PRK10905 136 GNASRQTAktQTAERPATTRPARKQAVIEPKKP---------QATAKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAP 206

                         90       100
                 ....*....|....*....|....*.
gi 380786207 276 ATPAEGEEPSTSGtqqlPAAAQAPDA 301
Cdd:PRK10905 207 KETATTAPVQTAS----PAQTTATPA 228
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 221-422 2.98e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.69  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  221 PVKNsGHSGLANGTVNDEPTTATD----PEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAA 296
Cdd:PRK10263  309 PLLN-GAPITEPVAVAAAATTATQswaaPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYA 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  297 QAPDALPAGWEQRELPNGRVYYVDHNTktttwERPLPPGWEKRTDPRGRFYYVDHNTRTTT---WQPPTAEYVrnYEQwQ 373
Cdd:PRK10263  388 QPAVQYNEPLQQPVQPQQPYYAPAAEQ-----PAQQPYYAPAPEQPAQQPYYAPAPEQPVAgnaWQAEEQQST--FAP-Q 459

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 380786207  374 SQRNQLQGAMQHFSQRFLYQSSSASTDHDPLGPLPPGWEKRQDNGRVYY 422
Cdd:PRK10263  460 STYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYY 508
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
149-299 3.31e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.46  E-value: 3.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 149 GSVPNGSAVTDGSQPPSRDSSGTAVAPENRHQLPSTNCFGGRSRTHRHSGAAARTTPATGEQSPGARSQhrQPVKNSGHS 228
Cdd:PRK07003 400 TAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDA--QPPADSGSA 477

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380786207 229 GLANGTVndEPTTATDPEEPSVVgvtSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAP 299
Cdd:PRK07003 478 SAPASDA--PPDAAFEPAPRAAA---PSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 144-315 3.86e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  144 PTVDLGSVPNGSAVT-----DGSQPPSRDSSGTAVAPENRHQLPSTncfGGRSRThrhSGAAARTTPATGEQSPGARSQH 218
Cdd:PHA03307   63 DRFEPPTGPPPGPGTeapanESRSTPTWSLSTLAPASPAREGSPTP---PGPSSP---DPPPPTPPPASPPPSPAPDLSE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  219 RQPvknSGHSGLANGTVNDEPTTATDPEEPSVvGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGT-----QQLP 293
Cdd:PHA03307  137 MLR---PVGSPGPPPAASPPAAGASPAAVASD-AASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASprpprRSSP 212

                         170       180
                  ....*....|....*....|..
gi 380786207  294 AAAQAPDALPAGWEQRELPNGR 315
Cdd:PHA03307  213 ISASASSPAPAPGRSAADDAGA 234
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 196-422 4.09e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 196 HSGAAARTTPATGEQSPGARSQHRQPvknsghsglangtvnDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAP 275
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARP---------------AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHP 654

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 276 ATPAEGEEPSTSGtqqlPAAAQAPDALPAGWEQRELPNGRVyyvdhntktttWERPLPPGwekRTDPRGRfyyvdhntrt 355
Cdd:PRK07764 655 KHVAVPDASDGGD----GWPAKAGGAAPAAPPPAPAPAAPA-----------APAGAAPA---QPAPAPA---------- 706

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380786207 356 ttWQPPTAeyvrnyeQWQSQRNQLQGAMQhfsqrflyQSSSASTDHDPLGPLPPGWEKRQDNGRVYY 422
Cdd:PRK07764 707 --ATPPAG-------QADDPAAQPPQAAQ--------GASAPSPAADDPVPLPPEPDDPPDPAGAPA 756
PRK10118 PRK10118
flagellar hook length control protein FliK;
199-308 5.79e-04

flagellar hook length control protein FliK;


Pssm-ID: 236652 [Multi-domain]  Cd Length: 408  Bit Score: 43.32  E-value: 5.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 199 AAARTTPATGEQSPGARSQHRQPVKNSGHSGLANGTVND--EPTTATDPEEPSVVGVTSPPAAPLSV-----TPNPNTTS 271
Cdd:PRK10118 156 TTPVADAPSTVLPAEKPTLLTKDMPSAPQDETHTLSSDEheKGLTSAQLTTAQPDDAPGTPAQPLTPlaaeaQAKAEVIS 235

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 380786207 272 LPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAG---WEQ 308
Cdd:PRK10118 236 TPSPVTAAASPTITPHQTQPLPTAAAPVLSAPLGsheWQQ 275
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
144-304 1.16e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 144 PTVDLGSVPNG--SAVTDGSQPPSRDSSGTAVAPENRHqlPSTNCFGGRSRTHRHSGAAARttPATGEQSPGARSQHRQP 221
Cdd:PRK07003 360 PAVTGGGAPGGgvPARVAGAVPAPGARAAAAVGASAVP--AVTAVTGAAGAALAPKAAAAA--AATRAEAPPAAPAPPAT 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 222 VKNSGHSGLANGTV-NDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPA--PATPAEGEEPSTSGTQ---QLPAA 295
Cdd:PRK07003 436 ADRGDDAADGDAPVpAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAfePAPRAAAPSAATPAAVpdaRAPAA 515


                 ....*....
gi 380786207 296 AQAPDALPA 304
Cdd:PRK07003 516 ASREDAPAA 524
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
 20-131 1.64e-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: 39.14  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207  20 LTLKVVSAKP-KVHNRQPRINSYVEVAVDGLASETKKTAkRIGSSELLWNEIIILNVTAQ------SHLDLKVWsCHT-- 90
Cdd:cd04051    2 LEITIISAEDlKNVNLFGKMKVYAVVWIDPSHKQSTPVD-RDGGTNPTWNETLRFPLDERllqqgrLALTIEVY-CERps 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 380786207  91 LRNELLGTASVNLSNVLKNNGGKMENTQLTLNLQTEN---KGSV 131
Cdd:cd04051   80 LGDKLIGEVRVPLKDLLDGASPAGELRFLSYQLRRPSgkpQGVL 123
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 239-304 1.80e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 41.48  E-value: 1.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380786207 239 PTTATDPEEPSVVGVTSPPAAPLSVTpNPNTTSLPAPATPAEGEEPSTSGTQ-------QLPAAAQAPDALPA 304
Cdd:PHA03291 224 PSTTTSPPSTTIPAPSTTIAAPQAGT-TPEAEGTPAPPTPGGGEAPPANATPapeasryELTVTQIIQIAIPA 295
PRK10856 PRK10856
cytoskeleton protein RodZ;
206-304 3.70e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.39  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 206 ATGEQSPgarsQHRQPVKNSGHSGLANGTVND----EPTTATDPEEPSVVGVTSPPAAPLSVTP-NPNTTSLPAPATPAE 280
Cdd:PRK10856 150 SSAELSQ----NSGQSVPLDTSTTTDPATTPApaapVDTTPTNSQTPAVATAPAPAVDPQQNAVvAPSQANVDTAATPAP 225

                         90       100
                 ....*....|....*....|....
gi 380786207 281 GEEPSTSGTQQLPAAaQAPDALPA 304
Cdd:PRK10856 226 AAPATPDGAAPLPTD-QAGVSTPA 248
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 142-308 7.66e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 7.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 142 DGPTVDLGSVPNGSAVTDGSQPPSRDSSGTAVAPENRHQLPSTNCFGGRSRTHRHSGAAARTTPATGEQSPGARSQHRQP 221
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380786207 222 VKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDA 301
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPD 750


                 ....*..
gi 380786207 302 LPAGWEQ 308
Cdd:PRK07764 751 PAGAPAQ 757
 
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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