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Conserved domains on  [gi|2217304378|ref|XP_047289479|]
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NEDD4-like E3 ubiquitin-protein ligase WWP2 isoform X1 [Homo sapiens]

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: 529.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQ 674
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 675 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078   162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 755 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVGK-ETWL 832
Cdd:cd00078   242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2217304378 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 3.93e-54

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: 183.25  E-value: 3.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021     1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2217304378  96 LGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLD 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 1.72e-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: 1.72e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217304378 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 3.75e-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 2217304378 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 2217304378 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 2217304378 447 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
PHA03247 super family cl33720
large tegument protein UL36; Provisional
164-343 3.58e-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: 48.01  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  164 PSRDSSGTAVAPENRHqPPSTNCFGGRSRTHRHSGASARTTPATGEQ----SPGARSRHRQpVKNSGHSGLANGTVNDEP 239
Cdd:PHA03247  2607 DPRGPAPPSPLPPDTH-APDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSPPQRPR 2684
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  240 TTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATP----AEGEEPSTSGTQQLPAAAQAPdALPAGWEQRELPngr 315
Cdd:PHA03247  2685 RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGP-ATPGGPARPARP--- 2760
                          170       180
                   ....*....|....*....|....*...
gi 2217304378  316 vyyvdhnTKTTTWERPLPPGWEKRTDPR 343
Cdd:PHA03247  2761 -------PTTAGPPAPAPPAAPAAGPPR 2781
 
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: 529.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQ 674
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 675 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078   162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 755 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVGK-ETWL 832
Cdd:cd00078   242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2217304378 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 5.83e-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: 516.02  E-value: 5.83e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  539 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 616
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQDMEILGKVTTHELKEGGESIR 695
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFsIVLTSEFGQVKVVELKPGGSNIP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  696 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSK 774
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  775 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQL 853
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
                          330
                   ....*....|....
gi 2217304378  854 REKLLYAIEETEGF 867
Cdd:smart00119 315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
331-870 3.16e-175

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 528.95  E-value: 3.16e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 402
Cdd:COG5021   298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 403 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 456
Cdd:COG5021   378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 457 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 536
Cdd:COG5021   458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 537 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 616
Cdd:COG5021   537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRV 696
Cdd:COG5021   617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 697 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKSTIYRHYTKNSKQ 775
Cdd:COG5021   697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 776 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQLR 854
Cdd:COG5021   777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856
                         570
                  ....*....|....*.
gi 2217304378 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 3.65e-128

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 386.97  E-value: 3.65e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 565 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLK 642
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 643 DLESIDPEFYNSIVWIKE-NNLEECGLELYFIqdMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQT 721
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 722 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTG 800
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 801 TCRLPVGGFAELigsngpQKFCIDKVG--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 3.93e-54

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: 183.25  E-value: 3.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021     1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2217304378  96 LGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLD 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 1.72e-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: 1.72e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217304378 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 3.75e-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 2217304378 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 5.88e-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: 5.88e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2217304378  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 2217304378 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 2217304378 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 4.19e-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: 58.00  E-value: 4.19e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2217304378  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 7.82e-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: 7.82e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217304378 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 9.80e-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: 9.80e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217304378  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; ...
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 2217304378 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 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 2217304378   19 QLTLKVVSAKPKVHNRQPR-INSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80
                           90       100
                   ....*....|....*....|.
gi 2217304378   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 2217304378 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 2217304378 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 1.61e-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: 1.61e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2217304378  446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03247 PHA03247
large tegument protein UL36; Provisional
164-343 3.58e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  164 PSRDSSGTAVAPENRHqPPSTNCFGGRSRTHRHSGASARTTPATGEQ----SPGARSRHRQpVKNSGHSGLANGTVNDEP 239
Cdd:PHA03247  2607 DPRGPAPPSPLPPDTH-APDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSPPQRPR 2684
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  240 TTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATP----AEGEEPSTSGTQQLPAAAQAPdALPAGWEQRELPngr 315
Cdd:PHA03247  2685 RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGP-ATPGGPARPARP--- 2760
                          170       180
                   ....*....|....*....|....*...
gi 2217304378  316 vyyvdhnTKTTTWERPLPPGWEKRTDPR 343
Cdd:PHA03247  2761 -------PTTAGPPAPAPPAAPAAGPPR 2781
 
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: 529.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQ 674
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 675 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078   162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 755 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVGK-ETWL 832
Cdd:cd00078   242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2217304378 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 5.83e-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: 516.02  E-value: 5.83e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  539 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 616
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQDMEILGKVTTHELKEGGESIR 695
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFsIVLTSEFGQVKVVELKPGGSNIP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  696 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSK 774
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  775 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQL 853
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
                          330
                   ....*....|....
gi 2217304378  854 REKLLYAIEETEGF 867
Cdd:smart00119 315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
331-870 3.16e-175

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 528.95  E-value: 3.16e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 402
Cdd:COG5021   298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 403 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 456
Cdd:COG5021   378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 457 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 536
Cdd:COG5021   458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 537 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 616
Cdd:COG5021   537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRV 696
Cdd:COG5021   617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 697 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKSTIYRHYTKNSKQ 775
Cdd:COG5021   697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 776 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQLR 854
Cdd:COG5021   777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856
                         570
                  ....*....|....*.
gi 2217304378 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 3.65e-128

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 386.97  E-value: 3.65e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 565 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLK 642
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 643 DLESIDPEFYNSIVWIKE-NNLEECGLELYFIqdMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQT 721
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 722 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTG 800
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 801 TCRLPVGGFAELigsngpQKFCIDKVG--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 3.93e-54

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: 183.25  E-value: 3.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021     1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2217304378  96 LGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLD 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 1.72e-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: 1.72e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217304378 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 3.75e-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 2217304378 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 5.88e-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: 5.88e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2217304378  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 2217304378 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 2217304378 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 4.19e-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: 58.00  E-value: 4.19e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2217304378  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 7.82e-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: 7.82e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217304378 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 9.80e-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: 9.80e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217304378  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; ...
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 2217304378 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 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 2217304378   19 QLTLKVVSAKPKVHNRQPR-INSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80
                           90       100
                   ....*....|....*....|.
gi 2217304378   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 2217304378 447 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
PRP40 COG5104
Splicing factor [RNA processing and modification];
297-381 8.26e-08

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 55.86  E-value: 8.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 297 QAPDALPAG-----WEQRELPNGRVYYVDHNTKTTTWERPLP-----------PGWEKRTDPRGRFYYVDHNTRTTTWQR 360
Cdd:COG5104     3 AALLGMASGearseWEELKAPDGRIYYYNKRTGKSSWEKPKEllkgseedldvDPWKECRTADGKVYYYNSITRESRWKI 82
                          90       100
                  ....*....|....*....|....
gi 2217304378 361 PtAEYVR---NYEQWQSQRNQLQG 381
Cdd:COG5104    83 P-PERKKvepIAEQKHDERSMIGG 105
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 2217304378 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 1.61e-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: 1.61e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2217304378  446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03247 PHA03247
large tegument protein UL36; Provisional
164-343 3.58e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  164 PSRDSSGTAVAPENRHqPPSTNCFGGRSRTHRHSGASARTTPATGEQ----SPGARSRHRQpVKNSGHSGLANGTVNDEP 239
Cdd:PHA03247  2607 DPRGPAPPSPLPPDTH-APDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSPPQRPR 2684
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  240 TTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATP----AEGEEPSTSGTQQLPAAAQAPdALPAGWEQRELPngr 315
Cdd:PHA03247  2685 RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGP-ATPGGPARPARP--- 2760
                          170       180
                   ....*....|....*....|....*...
gi 2217304378  316 vyyvdhnTKTTTWERPLPPGWEKRTDPR 343
Cdd:PHA03247  2761 -------PTTAGPPAPAPPAAPAAGPPR 2781
PHA03247 PHA03247
large tegument protein UL36; Provisional
135-345 9.71e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 9.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  135 GELTIFLDGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQP--PSTncfggrsrthrhsgASARTTPAtGEQSP 212
Cdd:PHA03247  2693 GSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPapPAV--------------PAGPATPG-GPARP 2757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378  213 GARSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSP--PAAPLSVTPNPNTTsLPAPATPAEGEEPSTSGTQ 290
Cdd:PHA03247  2758 ARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwdPADPPAAVLAPAAA-LPPAASPAGPLPPPTSAQP 2836
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217304378  291 QLPAAAQAPDALPAGWEQRELPNGrvyyvDHNTKTTTweRPLPPGWEKRTDPRGR 345
Cdd:PHA03247  2837 TAPPPPPGPPPPSLPLGGSVAPGG-----DVRRRPPS--RSPAAKPAAPARPPVR 2884
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
172-299 1.22e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.00  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 172 AVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRhrQPVKNSGHSGLANGTVndEPTTATDPEEPSVV 251
Cdd:PRK07003  423 AEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDA--QPPADSGSASAPASDA--PPDAAFEPAPRAAA 498
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2217304378 252 gvtSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAP 299
Cdd:PRK07003  499 ---PSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
149-319 3.04e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 149 GNVPNGSALTDGSQLPS-RDSSGTAVAPENRHQPPSTncfGGRSRTHRHSGASArttPATGEQSPGARSRHRQPVKNSgh 227
Cdd:PRK07764  384 RLGVAGGAGAPAAAAPSaAAAAPAAAPAPAAAAPAAA---AAPAPAAAPQPAPA---PAPAPAPPSPAGNAPAGGAPS-- 455
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 228 sglangtvndePTTATDPEEPSVVGVTSPPAAplsvTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALpagWE 307
Cdd:PRK07764  456 -----------PPPAAAPSAQPAPAPAAAPEP----TAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRER---WP 517
                         170
                  ....*....|...
gi 2217304378 308 Q-RELPNGRVYYV 319
Cdd:PRK07764  518 EiLAAVPKRSRKT 530
PRK10905 PRK10905
cell division protein DamX; Validated
198-301 5.61e-04

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 43.00  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 198 GASARTTP--ATGEQSPGARSRHRQPVKNSGHSglangtvndEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAP 275
Cdd:PRK10905  136 GNASRQTAktQTAERPATTRPARKQAVIEPKKP---------QATAKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAP 206
                          90       100
                  ....*....|....*....|....*.
gi 2217304378 276 ATPAEGEEPSTSGtqqlPAAAQAPDA 301
Cdd:PRK10905  207 KETATTAPVQTAS----PAQTTATPA 228
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
163-305 6.54e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 6.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 163 LPSRDSSGTAVA-----PENRHQPPSTNCFGGRSRThRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTvnd 237
Cdd:PRK07764  364 LPSASDDERGLLarlerLERRLGVAGGAGAPAAAAP-SAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAP--- 439
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217304378 238 EPTTATDPEEPSVVGVTSPPAAPlSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAG 305
Cdd:PRK07764  440 APPSPAGNAPAGGAPSPPPAAAP-SAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGA 506
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
151-300 6.71e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 6.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 151 VPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNcfGGRSRTHRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGL 230
Cdd:PRK07764  659 VPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAP--AGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAAD 736
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 231 ANGTVNDEPTTATDPEEPSvvgvtSPPAAPLSVTPNPNTTSLPAPATPAEGEEPstsgtqqLPAAAQAPD 300
Cdd:PRK07764  737 DPVPLPPEPDDPPDPAGAP-----AQPPPPPAPAPAAAPAAAPPPSPPSEEEEM-------AEDDAPSMD 794
PRK10118 PRK10118
flagellar hook length control protein FliK;
199-308 9.17e-04

flagellar hook length control protein FliK;


Pssm-ID: 236652 [Multi-domain]  Cd Length: 408  Bit Score: 42.55  E-value: 9.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 199 ASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTVND--EPTTATDPEEPSVVGVTSPPAAPLSV-----TPNPNTTS 271
Cdd:PRK10118  156 TTPVADAPSTVLPAEKPTLLTKDMPSAPQDETHTLSSDEheKGLTSAQLTTAQPDDAPGTPAQPLTPlaaeaQAKAEVIS 235
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217304378 272 LPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAG---WEQ 308
Cdd:PRK10118  236 TPSPVTAAASPTITPHQTQPLPTAAAPVLSAPLGsheWQQ 275
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
142-308 1.34e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 142 DGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRHRQP 221
Cdd:PRK07764  591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217304378 222 VKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDA 301
Cdd:PRK07764  671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPD 750

                  ....*..
gi 2217304378 302 LPAGWEQ 308
Cdd:PRK07764  751 PAGAPAQ 757
PHA03291 PHA03291
envelope glycoprotein I; Provisional
239-304 1.60e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 41.86  E-value: 1.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217304378 239 PTTATDPEEPSVVGVTSPPAAPLSVTpNPNTTSLPAPATPAEGEEPSTSGTQ-------QLPAAAQAPDALPA 304
Cdd:PHA03291  224 PSTTTSPPSTTIPAPSTTIAAPQAGT-TPEAEGTPAPPTPGGGEAPPANATPapeasryELTVTQIIQIAIPA 295
 
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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