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Conserved domains on  [gi|767989305|ref|XP_011521128|]
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NEDD4-like E3 ubiquitin-protein ligase WWP2 isoform X2 [Homo sapiens]

Protein Classification

WW domain-containing protein( domain architecture ID 11093557)

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 ...
 400-752 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: 527.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 400 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 479
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 480 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQ 558
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 559 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 638
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 639 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVGK-ETWL 716
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 767989305 717 PRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFG 752
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 216-245 3.17e-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: 3.17e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 767989305  216 LPPGWEKRTDPRGRFYYVDHNTRTTTWQRP 245
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 291-319 7.26e-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: 60.21  E-value: 7.26e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 767989305  291 LPPGWEKRQD-NGRVYYVNHNTRTTQWEDP 319
Cdd:pfam00397   1 LPPGWEERWDpDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 186-215 4.30e-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: 57.90  E-value: 4.30e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 767989305  186 LPAGWEQRELPNGRVYYVDHNTKTTTWERP 215
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 331-361 2.21e-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: 50.22  E-value: 2.21e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767989305 331 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 361
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 48-227 4.82e-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: 47.24  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   48 PSRDSSGTAVAPENRHqPPSTNCFGGRSRTHRHSGASARTTPATGEQ----SPGARSRHRQpVKNSGHSGLANGTVNDEP 123
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTH-APDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSPPQRPR 2684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  124 TTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATP----AEGEEPSTSGTQQLPAAAQAPdALPAGWEQRELPngr 199
Cdd:PHA03247 2685 RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGP-ATPGGPARPARP--- 2760

                         170       180
                  ....*....|....*....|....*...
gi 767989305  200 vyyvdhnTKTTTWERPLPPGWEKRTDPR 227
Cdd:PHA03247 2761 -------PTTAGPPAPAPPAAPAAGPPR 2781
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 1-26 6.87e-05

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


The actual alignment was detected with superfamily member cd04021:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 125  Bit Score: 43.03  E-value: 6.87e-05
                         10        20
                 ....*....|....*....|....*.
gi 767989305   1 MQLTLNLQTENKGSVVSGGELTIFLD 26
Cdd:cd04021  100 VKLTLNLSSENKGSSVKVGELTVILD 125
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 400-752 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: 527.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 400 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 479
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 480 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQ 558
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 559 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 638
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 639 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVGK-ETWL 716
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 767989305 717 PRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFG 752
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 423-751 3.84e-179

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: 514.86  E-value: 3.84e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   423 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 500
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   501 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQDMEILGKVTTHELKEGGESIR 579
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFsIVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   580 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSK 658
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   659 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQL 737
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 767989305   738 REKLLYAIEETEGF 751
Cdd:smart00119 315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
215-754 1.86e-177

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 530.49  E-value: 1.86e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 215 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 286
Cdd:COG5021  298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 287 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 340
Cdd:COG5021  378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 341 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 420
Cdd:COG5021  458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 421 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 500
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 501 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRV 580
Cdd:COG5021  617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 581 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKSTIYRHYTKNSKQ 659
Cdd:COG5021  697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 660 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQLR 738
Cdd:COG5021  777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                        570
                 ....*....|....*.
gi 767989305 739 EKLLYAIEETEGFGQE 754
Cdd:COG5021  857 SKLLTAINEGAGFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 449-752 1.73e-129

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 386.97  E-value: 1.73e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  449 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLK 526
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  527 DLESIDPEFYNSIVWIKE-NNLEECGLELYFIqdMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQT 605
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  606 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTG 684
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  685 TCRLPVGGFAELigsngpQKFCIDKVG--KETWLPRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFG 752
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 216-245 3.17e-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: 3.17e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 767989305  216 LPPGWEKRTDPRGRFYYVDHNTRTTTWQRP 245
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 291-319 7.26e-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: 60.21  E-value: 7.26e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 767989305  291 LPPGWEKRQD-NGRVYYVNHNTRTTQWEDP 319
Cdd:pfam00397   1 LPPGWEERWDpDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 290-320 1.16e-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: 59.54  E-value: 1.16e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767989305   290 PLPPGWEKRQD-NGRVYYVNHNTRTTQWEDPR 320
Cdd:smart00456   1 PLPPGWEERKDpDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 292-320 2.63e-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: 58.69  E-value: 2.63e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 767989305 292 PPGWEKRQDN-GRVYYVNHNTRTTQWEDPR 320
Cdd:cd00201    1 PPGWEERWDPdGRVYYYNHNTKETQWEDPR 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 186-215 4.30e-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: 57.90  E-value: 4.30e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 767989305  186 LPAGWEQRELPNGRVYYVDHNTKTTTWERP 215
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 215-246 7.43e-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: 7.43e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767989305   215 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 246
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 217-246 1.48e-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: 56.38  E-value: 1.48e-10
                         10        20        30
                 ....*....|....*....|....*....|
gi 767989305 217 PPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 246
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 186-215 1.75e-10

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 56.07  E-value: 1.75e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 767989305   186 LPAGWEQRELPNGRVYYVDHNTKTTTWERP 215
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 187-215 2.15e-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: 56.00  E-value: 2.15e-10
                         10        20
                 ....*....|....*....|....*....
gi 767989305 187 PAGWEQRELPNGRVYYVDHNTKTTTWERP 215
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 331-361 2.21e-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: 50.22  E-value: 2.21e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767989305 331 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 361
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 330-359 1.30e-07

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: 47.88  E-value: 1.30e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 767989305  330 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDP 359
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 330-361 2.57e-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: 47.21  E-value: 2.57e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767989305   330 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 361
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03247 PHA03247
large tegument protein UL36; Provisional
 48-227 4.82e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   48 PSRDSSGTAVAPENRHqPPSTNCFGGRSRTHRHSGASARTTPATGEQ----SPGARSRHRQpVKNSGHSGLANGTVNDEP 123
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTH-APDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSPPQRPR 2684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  124 TTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATP----AEGEEPSTSGTQQLPAAAQAPdALPAGWEQRELPngr 199
Cdd:PHA03247 2685 RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGP-ATPGGPARPARP--- 2760

                         170       180
                  ....*....|....*....|....*...
gi 767989305  200 vyyvdhnTKTTTWERPLPPGWEKRTDPR 227
Cdd:PHA03247 2761 -------PTTAGPPAPAPPAAPAAGPPR 2781
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 1-26 6.87e-05

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: 43.03  E-value: 6.87e-05
                         10        20
                 ....*....|....*....|....*.
gi 767989305   1 MQLTLNLQTENKGSVVSGGELTIFLD 26
Cdd:cd04021  100 VKLTLNLSSENKGSSVKVGELTVILD 125
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 400-752 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: 527.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 400 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 479
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 480 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQ 558
Cdd:cd00078   82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 559 DMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 638
Cdd:cd00078  162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 639 IDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVGK-ETWL 716
Cdd:cd00078  242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 767989305 717 PRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFG 752
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 423-751 3.84e-179

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: 514.86  E-value: 3.84e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   423 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 500
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   501 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYF-IQDMEILGKVTTHELKEGGESIR 579
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFsIVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   580 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSK 658
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   659 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQL 737
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 767989305   738 REKLLYAIEETEGF 751
Cdd:smart00119 315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
215-754 1.86e-177

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 530.49  E-value: 1.86e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 215 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 286
Cdd:COG5021  298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 287 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 340
Cdd:COG5021  378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 341 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 420
Cdd:COG5021  458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 421 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 500
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 501 YHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRV 580
Cdd:COG5021  617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 581 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKSTIYRHYTKNSKQ 659
Cdd:COG5021  697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 660 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVG-KETWLPRSHTCFNRLDLPPYKSYEQLR 738
Cdd:COG5021  777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856

                        570
                 ....*....|....*.
gi 767989305 739 EKLLYAIEETEGFGQE 754
Cdd:COG5021  857 SKLLTAINEGAGFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 449-752 1.73e-129

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 386.97  E-value: 1.73e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  449 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLK 526
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  527 DLESIDPEFYNSIVWIKE-NNLEECGLELYFIqdMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQT 605
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  606 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRH-YTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTG 684
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  685 TCRLPVGGFAELigsngpQKFCIDKVG--KETWLPRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFG 752
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 216-245 3.17e-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: 3.17e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 767989305  216 LPPGWEKRTDPRGRFYYVDHNTRTTTWQRP 245
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 291-319 7.26e-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: 60.21  E-value: 7.26e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 767989305  291 LPPGWEKRQD-NGRVYYVNHNTRTTQWEDP 319
Cdd:pfam00397   1 LPPGWEERWDpDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 290-320 1.16e-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: 59.54  E-value: 1.16e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767989305   290 PLPPGWEKRQD-NGRVYYVNHNTRTTQWEDPR 320
Cdd:smart00456   1 PLPPGWEERKDpDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 292-320 2.63e-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: 58.69  E-value: 2.63e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 767989305 292 PPGWEKRQDN-GRVYYVNHNTRTTQWEDPR 320
Cdd:cd00201    1 PPGWEERWDPdGRVYYYNHNTKETQWEDPR 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 186-215 4.30e-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: 57.90  E-value: 4.30e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 767989305  186 LPAGWEQRELPNGRVYYVDHNTKTTTWERP 215
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 215-246 7.43e-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: 7.43e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767989305   215 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 246
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 217-246 1.48e-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: 56.38  E-value: 1.48e-10
                         10        20        30
                 ....*....|....*....|....*....|
gi 767989305 217 PPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 246
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 186-215 1.75e-10

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 56.07  E-value: 1.75e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 767989305   186 LPAGWEQRELPNGRVYYVDHNTKTTTWERP 215
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 187-215 2.15e-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: 56.00  E-value: 2.15e-10
                         10        20
                 ....*....|....*....|....*....
gi 767989305 187 PAGWEQRELPNGRVYYVDHNTKTTTWERP 215
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 331-361 2.21e-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: 50.22  E-value: 2.21e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767989305 331 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 361
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
PRP40 COG5104
Splicing factor [RNA processing and modification];
181-265 8.14e-08

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 55.86  E-value: 8.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 181 QAPDALPAG-----WEQRELPNGRVYYVDHNTKTTTWERPLP-----------PGWEKRTDPRGRFYYVDHNTRTTTWQR 244
Cdd:COG5104    3 AALLGMASGearseWEELKAPDGRIYYYNKRTGKSSWEKPKEllkgseedldvDPWKECRTADGKVYYYNSITRESRWKI 82

                         90       100
                 ....*....|....*....|....
gi 767989305 245 PtAEYVR---NYEQWQSQRNQLQG 265
Cdd:COG5104   83 P-PERKKvepIAEQKHDERSMIGG 105
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 330-359 1.30e-07

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: 47.88  E-value: 1.30e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 767989305  330 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDP 359
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 330-361 2.57e-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: 47.21  E-value: 2.57e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767989305   330 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 361
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03247 PHA03247
large tegument protein UL36; Provisional
 48-227 4.82e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   48 PSRDSSGTAVAPENRHqPPSTNCFGGRSRTHRHSGASARTTPATGEQ----SPGARSRHRQpVKNSGHSGLANGTVNDEP 123
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTH-APDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSPPQRPR 2684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  124 TTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATP----AEGEEPSTSGTQQLPAAAQAPdALPAGWEQRELPngr 199
Cdd:PHA03247 2685 RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGP-ATPGGPARPARP--- 2760

                         170       180
                  ....*....|....*....|....*...
gi 767989305  200 vyyvdhnTKTTTWERPLPPGWEKRTDPR 227
Cdd:PHA03247 2761 -------PTTAGPPAPAPPAAPAAGPPR 2781
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 1-26 6.87e-05

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: 43.03  E-value: 6.87e-05
                         10        20
                 ....*....|....*....|....*.
gi 767989305   1 MQLTLNLQTENKGSVVSGGELTIFLD 26
Cdd:cd04021  100 VKLTLNLSSENKGSSVKVGELTVILD 125
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
56-183 1.02e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.00  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  56 AVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRhrQPVKNSGHSGLANGTVndEPTTATDPEEPSVV 135
Cdd:PRK07003 423 AEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDA--QPPADSGSASAPASDA--PPDAAFEPAPRAAA 498

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767989305 136 gvtSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAP 183
Cdd:PRK07003 499 ---PSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
PHA03247 PHA03247
large tegument protein UL36; Provisional
 19-229 1.33e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   19 GELTIFLDGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQP--PSTncfggrsrthrhsgASARTTPAtGEQSP 96
Cdd:PHA03247 2693 GSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPapPAV--------------PAGPATPG-GPARP 2757

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305   97 GARSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSP--PAAPLSVTPNPNTTsLPAPATPAEGEEPSTSGTQ 174
Cdd:PHA03247 2758 ARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwdPADPPAAVLAPAAA-LPPAASPAGPLPPPTSAQP 2836

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767989305  175 QLPAAAQAPDALPAGWEQRELPNGrvyyvDHNTKTTTweRPLPPGWEKRTDPRGR 229
Cdd:PHA03247 2837 TAPPPPPGPPPPSLPLGGSVAPGG-----DVRRRPPS--RSPAAKPAAPARPPVR 2884
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 33-203 2.65e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  33 GNVPNGSALTDGSQLPS-RDSSGTAVAPENRHQPPSTncfGGRSRTHRHSGASArttPATGEQSPGARSRHRQPVKNSgh 111
Cdd:PRK07764 384 RLGVAGGAGAPAAAAPSaAAAAPAAAPAPAAAAPAAA---AAPAPAAAPQPAPA---PAPAPAPPSPAGNAPAGGAPS-- 455

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 112 sglangtvndePTTATDPEEPSVVGVTSPPAAplsvTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALpagWE 191
Cdd:PRK07764 456 -----------PPPAAAPSAQPAPAPAAAPEP----TAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRER---WP 517

                        170
                 ....*....|...
gi 767989305 192 Q-RELPNGRVYYV 203
Cdd:PRK07764 518 EiLAAVPKRSRKT 530
PRK10905 PRK10905
cell division protein DamX; Validated
 82-185 4.17e-04

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 43.39  E-value: 4.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  82 GASARTTP--ATGEQSPGARSRHRQPVKNSGHSglangtvndEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAP 159
Cdd:PRK10905 136 GNASRQTAktQTAERPATTRPARKQAVIEPKKP---------QATAKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAP 206

                         90       100
                 ....*....|....*....|....*.
gi 767989305 160 ATPAEGEEPSTSGtqqlPAAAQAPDA 185
Cdd:PRK10905 207 KETATTAPVQTAS----PAQTTATPA 228
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 35-184 5.95e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 5.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  35 VPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNcfGGRSRTHRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGL 114
Cdd:PRK07764 659 VPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAP--AGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAAD 736

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 115 ANGTVNDEPTTATDPEEPSvvgvtSPPAAPLSVTPNPNTTSLPAPATPAEGEEPstsgtqqLPAAAQAPD 184
Cdd:PRK07764 737 DPVPLPPEPDDPPDPAGAP-----AQPPPPPAPAPAAAPAAAPPPSPPSEEEEM-------AEDDAPSMD 794
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 47-189 6.05e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  47 LPSRDSSGTAVA-----PENRHQPPSTNCFGGRSRThRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTvnd 121
Cdd:PRK07764 364 LPSASDDERGLLarlerLERRLGVAGGAGAPAAAAP-SAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAP--- 439

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767989305 122 EPTTATDPEEPSVVGVTSPPAAPlSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAG 189
Cdd:PRK07764 440 APPSPAGNAPAGGAPSPPPAAAP-SAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGA 506
PRK10118 PRK10118
flagellar hook length control protein FliK;
83-192 7.69e-04

flagellar hook length control protein FliK;


Pssm-ID: 236652 [Multi-domain]  Cd Length: 408  Bit Score: 42.55  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  83 ASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTVND--EPTTATDPEEPSVVGVTSPPAAPLSV-----TPNPNTTS 155
Cdd:PRK10118 156 TTPVADAPSTVLPAEKPTLLTKDMPSAPQDETHTLSSDEheKGLTSAQLTTAQPDDAPGTPAQPLTPlaaeaQAKAEVIS 235

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767989305 156 LPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAG---WEQ 192
Cdd:PRK10118 236 TPSPVTAAASPTITPHQTQPLPTAAAPVLSAPLGsheWQQ 275
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
44-227 1.02e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.56  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  44 GSQLPSRDSSGT--AVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGeQSPGARSRHRQPVKNSGHSGLANGTVND 121
Cdd:PRK12323 370 GGAGPATAAAAPvaQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVA-AAPARRSPAPEALAAARQASARGPGGAP 448

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 122 EPTTAtdpeePSVVGVTSPPAAPLSVTPNPNT-TSLPAPATPAEGEEPSTSGT---QQLPAAAQAP-----DALPAGWEQ 192
Cdd:PRK12323 449 APAPA-----PAAAPAAAARPAAAGPRPVAAAaAAAPARAAPAAAPAPADDDPppwEELPPEFASPapaqpDAAPAGWVA 523

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767989305 193 RELPNGRVYYVDHNTKTTTWERPLPPGWEKRTDPR 227
Cdd:PRK12323 524 ESIPDPATADPDDAFETLAPAPAAAPAPRAAAATE 558
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 105-306 1.10e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  105 PVKNsGHSGLANGTVNDEPTTATD----PEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAA 180
Cdd:PRK10263  309 PLLN-GAPITEPVAVAAAATTATQswaaPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYA 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  181 QAPDALPAGWEQRELPNGRVYYVDHNTktttwERPLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQWQSQR 260
Cdd:PRK10263  388 QPAVQYNEPLQQPVQPQQPYYAPAAEQ-----PAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTY 462

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 767989305  261 NQLQGAMQHFSQRFLYQSSSASTDHDPLGPLPPGWEKRQDNGRVYY 306
Cdd:PRK10263  463 QTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYY 508
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 26-192 1.17e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305  26 DGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRHRQP 105
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989305 106 VKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDA 185
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPD 750


                 ....*..
gi 767989305 186 LPAGWEQ 192
Cdd:PRK07764 751 PAGAPAQ 757
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 123-188 1.76e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 41.48  E-value: 1.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767989305 123 PTTATDPEEPSVVGVTSPPAAPLSVTpNPNTTSLPAPATPAEGEEPSTSGTQ-------QLPAAAQAPDALPA 188
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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