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Conserved domains on  [gi|767989303|ref|XP_011521127|]
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NEDD4-like E3 ubiquitin-protein ligase WWP2 isoform X1 [Homo sapiens]

Protein Classification

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

protein containing domains C2_E3_ubiquitin_ligase, PHA03247, WW, and HECTc

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 516-868 0e+00

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


:

Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 529.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQ 674
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 675 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 755 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVGK-ETWL 832
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 767989303 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 767989303  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767989303  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 767989303  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 767989303  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 767989303  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 767989303 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 767989303  164 PSRDSSGTAVAPENRHqPPSTNCFGGRSRTHRHSGASARTTPATGEQ----SPGARSRHRQpVKNSGHSGLANGTVNDEP 239
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTH-APDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSPPQRPR 2684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303  240 TTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATP----AEGEEPSTSGTQQLPAAAQAPdALPAGWEQRELPngr 315
Cdd:PHA03247 2685 RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGP-ATPGGPARPARP--- 2760

                         170       180
                  ....*....|....*....|....*...
gi 767989303  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 767989303 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQ 674
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 675 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 755 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVGK-ETWL 832
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 767989303 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 767989303   539 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 616
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303   617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQDMEILGKVTTHELKEGGESIR 695
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFsIVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303   696 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSK 774
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303   775 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQL 853
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 767989303   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 767989303 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 402
Cdd:COG5021  298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 403 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 456
Cdd:COG5021  378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 457 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 536
Cdd:COG5021  458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 537 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 616
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRV 696
Cdd:COG5021  617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 697 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKSTIYRHYTKNSKQ 775
Cdd:COG5021  697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 776 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQLR 854
Cdd:COG5021  777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                        570
                 ....*....|....*.
gi 767989303 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 767989303  565 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLK 642
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303  643 DLESIDPEFYNSIVWIKE-NNLEECGLELYFIqdMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQT 721
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303  722 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTG 800
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303  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 767989303  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767989303  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 767989303  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 767989303  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 767989303   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 767989303 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 767989303  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 767989303   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 767989303 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 767989303   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 767989303 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 767989303    19 QLTLKVVSAKPKVHNRQPR-INSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80

                           90       100
                   ....*....|....*....|.
gi 767989303    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 767989303 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 767989303  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 767989303   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 767989303  164 PSRDSSGTAVAPENRHqPPSTNCFGGRSRTHRHSGASARTTPATGEQ----SPGARSRHRQpVKNSGHSGLANGTVNDEP 239
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTH-APDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSPPQRPR 2684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303  240 TTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATP----AEGEEPSTSGTQQLPAAAQAPdALPAGWEQRELPngr 315
Cdd:PHA03247 2685 RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGP-ATPGGPARPARP--- 2760

                         170       180
                  ....*....|....*....|....*...
gi 767989303  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 767989303 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQ 674
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 675 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 755 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVGK-ETWL 832
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 767989303 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 767989303   539 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 616
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303   617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQDMEILGKVTTHELKEGGESIR 695
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFsIVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303   696 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSK 774
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303   775 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQL 853
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 767989303   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 767989303 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 402
Cdd:COG5021  298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 403 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 456
Cdd:COG5021  378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 457 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 536
Cdd:COG5021  458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 537 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 616
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 617 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRV 696
Cdd:COG5021  617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 697 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKSTIYRHYTKNSKQ 775
Cdd:COG5021  697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 776 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQLR 854
Cdd:COG5021  777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                        570
                 ....*....|....*.
gi 767989303 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 767989303  565 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLK 642
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303  643 DLESIDPEFYNSIVWIKE-NNLEECGLELYFIqdMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQT 721
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303  722 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTG 800
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303  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 767989303  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767989303  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 767989303  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 767989303  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 767989303   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 767989303 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 767989303  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 767989303   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 767989303 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 767989303   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 767989303 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 767989303    19 QLTLKVVSAKPKVHNRQPR-INSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80

                           90       100
                   ....*....|....*....|.
gi 767989303    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 767989303 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 767989303 297 QAPDALPAG-----WEQRELPNGRVYYVDHNTKTTTWERPLP-----------PGWEKRTDPRGRFYYVDHNTRTTTWQR 360
Cdd:COG5104    3 AALLGMASGearseWEELKAPDGRIYYYNKRTGKSSWEKPKEllkgseedldvDPWKECRTADGKVYYYNSITRESRWKI 82

                         90       100
                 ....*....|....*....|....
gi 767989303 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 767989303  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 767989303   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 767989303  164 PSRDSSGTAVAPENRHqPPSTNCFGGRSRTHRHSGASARTTPATGEQ----SPGARSRHRQpVKNSGHSGLANGTVNDEP 239
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTH-APDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSPPQRPR 2684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303  240 TTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATP----AEGEEPSTSGTQQLPAAAQAPdALPAGWEQRELPngr 315
Cdd:PHA03247 2685 RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGP-ATPGGPARPARP--- 2760

                         170       180
                  ....*....|....*....|....*...
gi 767989303  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 767989303  135 GELTIFLDGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQP--PSTncfggrsrthrhsgASARTTPAtGEQSP 212
Cdd:PHA03247 2693 GSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPapPAV--------------PAGPATPG-GPARP 2757

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303  213 GARSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSP--PAAPLSVTPNPNTTsLPAPATPAEGEEPSTSGTQ 290
Cdd:PHA03247 2758 ARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwdPADPPAAVLAPAAA-LPPAASPAGPLPPPTSAQP 2836

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767989303  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 767989303 172 AVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRhrQPVKNSGHSGLANGTVndEPTTATDPEEPSVV 251
Cdd:PRK07003 423 AEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDA--QPPADSGSASAPASDA--PPDAAFEPAPRAAA 498

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767989303 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 767989303 149 GNVPNGSALTDGSQLPS-RDSSGTAVAPENRHQPPSTncfGGRSRTHRHSGASArttPATGEQSPGARSRHRQPVKNSgh 227
Cdd:PRK07764 384 RLGVAGGAGAPAAAAPSaAAAAPAAAPAPAAAAPAAA---AAPAPAAAPQPAPA---PAPAPAPPSPAGNAPAGGAPS-- 455

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 228 sglangtvndePTTATDPEEPSVVGVTSPPAAplsvTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALpagWE 307
Cdd:PRK07764 456 -----------PPPAAAPSAQPAPAPAAAPEP----TAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRER---WP 517

                        170
                 ....*....|...
gi 767989303 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 767989303 198 GASARTTP--ATGEQSPGARSRHRQPVKNSGHSglangtvndEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAP 275
Cdd:PRK10905 136 GNASRQTAktQTAERPATTRPARKQAVIEPKKP---------QATAKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAP 206

                         90       100
                 ....*....|....*....|....*.
gi 767989303 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 767989303 163 LPSRDSSGTAVA-----PENRHQPPSTNCFGGRSRThRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTvnd 237
Cdd:PRK07764 364 LPSASDDERGLLarlerLERRLGVAGGAGAPAAAAP-SAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAP--- 439

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767989303 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 767989303 151 VPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNcfGGRSRTHRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGL 230
Cdd:PRK07764 659 VPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAP--AGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAAD 736

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 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 767989303 199 ASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTVND--EPTTATDPEEPSVVGVTSPPAAPLSV-----TPNPNTTS 271
Cdd:PRK10118 156 TTPVADAPSTVLPAEKPTLLTKDMPSAPQDETHTLSSDEheKGLTSAQLTTAQPDDAPGTPAQPLTPlaaeaQAKAEVIS 235

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767989303 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 767989303 142 DGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRHRQP 221
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989303 222 VKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDA 301
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPD 750


                 ....*..
gi 767989303 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 767989303 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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