|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
901-1230 |
3.94e-177 |
|
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: 524.49 E-value: 3.94e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 901 DVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFTFIGRVAGLAV 980
Cdd:smart00119 1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 981 FHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLMFCIDEEN-FGQTYQVDLKPNGSEIM 1057
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1058 VTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHP 1137
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1138 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGSP-EKLPRAHTCFNRLDLPPYETFEDL 1216
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 2217316457 1217 REKLLMAVENAQGF 1230
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| C2 super family |
cl14603 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
379-432 |
3.40e-25 |
|
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 cd04033:
Pssm-ID: 472691 [Multi-domain] Cd Length: 133 Bit Score: 102.05 E-value: 3.40e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2217316457 379 TRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYM 432
Cdd:cd04033 80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
646-675 |
1.11e-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: 62.91 E-value: 1.11e-12
10 20 30
....*....|....*....|....*....|
gi 2217316457 646 LPSGWEERKDAKGRTYYVNHNNRTTTWTRP 675
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
759-789 |
5.04e-12 |
|
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: 61.00 E-value: 5.04e-12
10 20 30
....*....|....*....|....*....|.
gi 2217316457 759 PPGWEMRIAPNGRPFFIDHNTKTTTWEDPRL 789
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
808-840 |
3.39e-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: 58.77 E-value: 3.39e-11
10 20 30
....*....|....*....|....*....|...
gi 2217316457 808 PLPPGWEERIHLDGRTFYIDHNSKITQWEDPRL 840
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
477-503 |
9.86e-10 |
|
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: 54.82 E-value: 9.86e-10
10 20
....*....|....*....|....*..
gi 2217316457 477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:pfam00397 4 GWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
79-404 |
1.83e-06 |
|
large tegument protein UL36; Provisional
The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.63 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 79 TSIDARPTCSSSvqiSLQRKATDGATDGCGP-PEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPPR 157
Cdd:PHA03247 2667 ARRLGRAAQASS---PPQRPRRRAARPTVGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 158 AARDPGLQVN-GTCGRRVRCSGPVDCAEEAAPGLRIQHRASSADVRQVRL----LPLGPDGQGGPAAAEPRRWSLQHVPD 232
Cdd:PHA03247 2744 VPAGPATPGGpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSEsresLPSPWDPADPPAAVLAPAAALPPAAS 2823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 233 ASGSSGKRCFVFQLQQPQQGASGPGSDLNFGFTGTKGDRLVRYPRIRLERSTSYPTQPRSERGSptedRGALEASPRAGR 312
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLA----RPAVSRSTESFA 2899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 313 MAP---EIRRTNSAERTPQGQGCTFKIRQDQNAGQqhfrilvTRGPEEAPQNPEEKSAKSPVSTGADTTTRDDFL--GQV 387
Cdd:PHA03247 2900 LPPdqpERPPQPQAPPPPQPQPQPPPPPQPQPPPP-------PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALvpGRV 2972
|
330
....*....|....*..
gi 2217316457 388 DVPLSHLPTEDPTMERP 404
Cdd:PHA03247 2973 AVPRFRVPQPAPSREAP 2989
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
901-1230 |
3.94e-177 |
|
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: 524.49 E-value: 3.94e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 901 DVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFTFIGRVAGLAV 980
Cdd:smart00119 1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 981 FHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLMFCIDEEN-FGQTYQVDLKPNGSEIM 1057
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1058 VTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHP 1137
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1138 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGSP-EKLPRAHTCFNRLDLPPYETFEDL 1216
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 2217316457 1217 REKLLMAVENAQGF 1230
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
646-1230 |
3.98e-173 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 534.73 E-value: 3.98e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 646 LPSGWEERKDAKGRTYYVNHNNRTTTWTRPImqlaedgASGSATNSNNHLIEPQIRRPRSLSSPTVTLSAPLEgaKDSPV 725
Cdd:COG5021 299 LNSLFSTRADSFGRTYYLDHDRILTQYSRPL-------LEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFL--EAHPE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 726 RRAVKDTLSNpqspqpspynspkpQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDP-RLKFPVHMRSKTSLNPN 804
Cdd:COG5021 370 FSELLKNQSR--------------GTTRDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLrREQLGRESDESFYVASN 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 805 -------DLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPA--ITGPAVPYSREFKQKYDYFRKKLKKPADIPn 875
Cdd:COG5021 436 vqqqrasREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY- 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 876 rFEMKLHRNNIFEESYRRIMSvKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQIN 955
Cdd:COG5021 515 -LHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPIN 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 956 PNSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILEN--DPTELDLM 1033
Cdd:COG5021 593 PLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNdiDETILDLT 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1034 FCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCG 1113
Cdd:COG5021 672 FTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGG 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1114 LGD-VDVNDWRQHSIYKnGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSP 1192
Cdd:COG5021 752 IPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTD 830
|
570 580 590
....*....|....*....|....*....|....*....
gi 2217316457 1193 -EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGF 1230
Cdd:COG5021 831 dDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
|
|
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
877-1231 |
4.83e-169 |
|
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: 504.79 E-value: 4.83e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 877 FEMKLHRNNIFEESYRRIMSVKRPDvLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 956
Cdd:cd00078 1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 957 NSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPT--ELDLMF 1034
Cdd:cd00078 80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1035 CIDEEN-FGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCG 1113
Cdd:cd00078 159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1114 LGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTIEQWGSP- 1192
Cdd:cd00078 239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 2217316457 1193 EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 1231
Cdd:cd00078 314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
928-1231 |
1.24e-132 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 407.38 E-value: 1.24e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 928 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLN 1006
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1007 DMESVDSEYYNSLKWIL---ENDPTELDLMFCIDEenFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQM 1083
Cdd:pfam00632 81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1084 NAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTG 1163
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1164 TSRVPMNGFAELygsngpQLFTIEQWGS--PEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 1231
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
|
|
| C2_NEDD4_NEDD4L |
cd04033 |
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ... |
379-432 |
3.40e-25 |
|
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42); Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. 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: 175999 [Multi-domain] Cd Length: 133 Bit Score: 102.05 E-value: 3.40e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2217316457 379 TRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYM 432
Cdd:cd04033 80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
646-675 |
1.11e-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: 62.91 E-value: 1.11e-12
10 20 30
....*....|....*....|....*....|
gi 2217316457 646 LPSGWEERKDAKGRTYYVNHNNRTTTWTRP 675
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
645-675 |
2.90e-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: 61.85 E-value: 2.90e-12
10 20 30
....*....|....*....|....*....|.
gi 2217316457 645 GLPSGWEERKDAKGRTYYVNHNNRTTTWTRP 675
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
759-789 |
5.04e-12 |
|
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: 61.00 E-value: 5.04e-12
10 20 30
....*....|....*....|....*....|.
gi 2217316457 759 PPGWEMRIAPNGRPFFIDHNTKTTTWEDPRL 789
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
647-675 |
6.56e-12 |
|
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: 61.00 E-value: 6.56e-12
10 20
....*....|....*....|....*....
gi 2217316457 647 PSGWEERKDAKGRTYYVNHNNRTTTWTRP 675
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
758-787 |
6.76e-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: 60.60 E-value: 6.76e-12
10 20 30
....*....|....*....|....*....|
gi 2217316457 758 LPPGWEMRIAPNGRPFFIDHNTKTTTWEDP 787
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
758-789 |
7.92e-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: 7.92e-12
10 20 30
....*....|....*....|....*....|..
gi 2217316457 758 LPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRL 789
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
808-840 |
3.39e-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: 58.77 E-value: 3.39e-11
10 20 30
....*....|....*....|....*....|...
gi 2217316457 808 PLPPGWEERIHLDGRTFYIDHNSKITQWEDPRL 840
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
810-840 |
1.00e-10 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.54 E-value: 1.00e-10
10 20 30
....*....|....*....|....*....|.
gi 2217316457 810 PPGWEERIHLDGRTFYIDHNSKITQWEDPRL 840
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
809-838 |
1.93e-10 |
|
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: 56.74 E-value: 1.93e-10
10 20 30
....*....|....*....|....*....|
gi 2217316457 809 LPPGWEERIHLDGRTFYIDHNSKITQWEDP 838
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
477-503 |
9.86e-10 |
|
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: 54.82 E-value: 9.86e-10
10 20
....*....|....*....|....*..
gi 2217316457 477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:pfam00397 4 GWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
477-503 |
2.75e-09 |
|
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: 53.30 E-value: 2.75e-09
10 20
....*....|....*....|....*..
gi 2217316457 477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:cd00201 3 GWEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
477-503 |
1.21e-08 |
|
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: 51.45 E-value: 1.21e-08
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
79-404 |
1.83e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.63 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 79 TSIDARPTCSSSvqiSLQRKATDGATDGCGP-PEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPPR 157
Cdd:PHA03247 2667 ARRLGRAAQASS---PPQRPRRRAARPTVGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 158 AARDPGLQVN-GTCGRRVRCSGPVDCAEEAAPGLRIQHRASSADVRQVRL----LPLGPDGQGGPAAAEPRRWSLQHVPD 232
Cdd:PHA03247 2744 VPAGPATPGGpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSEsresLPSPWDPADPPAAVLAPAAALPPAAS 2823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 233 ASGSSGKRCFVFQLQQPQQGASGPGSDLNFGFTGTKGDRLVRYPRIRLERSTSYPTQPRSERGSptedRGALEASPRAGR 312
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLA----RPAVSRSTESFA 2899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 313 MAP---EIRRTNSAERTPQGQGCTFKIRQDQNAGQqhfrilvTRGPEEAPQNPEEKSAKSPVSTGADTTTRDDFL--GQV 387
Cdd:PHA03247 2900 LPPdqpERPPQPQAPPPPQPQPQPPPPPQPQPPPP-------PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALvpGRV 2972
|
330
....*....|....*..
gi 2217316457 388 DVPLSHLPTEDPTMERP 404
Cdd:PHA03247 2973 AVPRFRVPQPAPSREAP 2989
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
901-1230 |
3.94e-177 |
|
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: 524.49 E-value: 3.94e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 901 DVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFTFIGRVAGLAV 980
Cdd:smart00119 1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 981 FHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLMFCIDEEN-FGQTYQVDLKPNGSEIM 1057
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1058 VTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHP 1137
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1138 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGSP-EKLPRAHTCFNRLDLPPYETFEDL 1216
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 2217316457 1217 REKLLMAVENAQGF 1230
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
646-1230 |
3.98e-173 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 534.73 E-value: 3.98e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 646 LPSGWEERKDAKGRTYYVNHNNRTTTWTRPImqlaedgASGSATNSNNHLIEPQIRRPRSLSSPTVTLSAPLEgaKDSPV 725
Cdd:COG5021 299 LNSLFSTRADSFGRTYYLDHDRILTQYSRPL-------LEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFL--EAHPE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 726 RRAVKDTLSNpqspqpspynspkpQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDP-RLKFPVHMRSKTSLNPN 804
Cdd:COG5021 370 FSELLKNQSR--------------GTTRDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLrREQLGRESDESFYVASN 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 805 -------DLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPA--ITGPAVPYSREFKQKYDYFRKKLKKPADIPn 875
Cdd:COG5021 436 vqqqrasREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY- 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 876 rFEMKLHRNNIFEESYRRIMSvKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQIN 955
Cdd:COG5021 515 -LHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPIN 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 956 PNSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILEN--DPTELDLM 1033
Cdd:COG5021 593 PLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNdiDETILDLT 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1034 FCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCG 1113
Cdd:COG5021 672 FTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGG 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1114 LGD-VDVNDWRQHSIYKnGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSP 1192
Cdd:COG5021 752 IPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTD 830
|
570 580 590
....*....|....*....|....*....|....*....
gi 2217316457 1193 -EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGF 1230
Cdd:COG5021 831 dDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
|
|
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
877-1231 |
4.83e-169 |
|
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: 504.79 E-value: 4.83e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 877 FEMKLHRNNIFEESYRRIMSVKRPDvLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 956
Cdd:cd00078 1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 957 NSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPT--ELDLMF 1034
Cdd:cd00078 80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1035 CIDEEN-FGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCG 1113
Cdd:cd00078 159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1114 LGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTIEQWGSP- 1192
Cdd:cd00078 239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 2217316457 1193 EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 1231
Cdd:cd00078 314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
928-1231 |
1.24e-132 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 407.38 E-value: 1.24e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 928 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLN 1006
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1007 DMESVDSEYYNSLKWIL---ENDPTELDLMFCIDEenFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQM 1083
Cdd:pfam00632 81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1084 NAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTG 1163
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 1164 TSRVPMNGFAELygsngpQLFTIEQWGS--PEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 1231
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
|
|
| C2_NEDD4_NEDD4L |
cd04033 |
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ... |
379-432 |
3.40e-25 |
|
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42); Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. 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: 175999 [Multi-domain] Cd Length: 133 Bit Score: 102.05 E-value: 3.40e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2217316457 379 TRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYM 432
Cdd:cd04033 80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
646-675 |
1.11e-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: 62.91 E-value: 1.11e-12
10 20 30
....*....|....*....|....*....|
gi 2217316457 646 LPSGWEERKDAKGRTYYVNHNNRTTTWTRP 675
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
645-675 |
2.90e-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: 61.85 E-value: 2.90e-12
10 20 30
....*....|....*....|....*....|.
gi 2217316457 645 GLPSGWEERKDAKGRTYYVNHNNRTTTWTRP 675
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
759-789 |
5.04e-12 |
|
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: 61.00 E-value: 5.04e-12
10 20 30
....*....|....*....|....*....|.
gi 2217316457 759 PPGWEMRIAPNGRPFFIDHNTKTTTWEDPRL 789
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
647-675 |
6.56e-12 |
|
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: 61.00 E-value: 6.56e-12
10 20
....*....|....*....|....*....
gi 2217316457 647 PSGWEERKDAKGRTYYVNHNNRTTTWTRP 675
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
758-787 |
6.76e-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: 60.60 E-value: 6.76e-12
10 20 30
....*....|....*....|....*....|
gi 2217316457 758 LPPGWEMRIAPNGRPFFIDHNTKTTTWEDP 787
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
758-789 |
7.92e-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: 7.92e-12
10 20 30
....*....|....*....|....*....|..
gi 2217316457 758 LPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRL 789
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
808-840 |
3.39e-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: 58.77 E-value: 3.39e-11
10 20 30
....*....|....*....|....*....|...
gi 2217316457 808 PLPPGWEERIHLDGRTFYIDHNSKITQWEDPRL 840
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
810-840 |
1.00e-10 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.54 E-value: 1.00e-10
10 20 30
....*....|....*....|....*....|.
gi 2217316457 810 PPGWEERIHLDGRTFYIDHNSKITQWEDPRL 840
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
809-838 |
1.93e-10 |
|
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: 56.74 E-value: 1.93e-10
10 20 30
....*....|....*....|....*....|
gi 2217316457 809 LPPGWEERIHLDGRTFYIDHNSKITQWEDP 838
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
477-503 |
9.86e-10 |
|
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: 54.82 E-value: 9.86e-10
10 20
....*....|....*....|....*..
gi 2217316457 477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:pfam00397 4 GWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
477-503 |
2.75e-09 |
|
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: 53.30 E-value: 2.75e-09
10 20
....*....|....*....|....*..
gi 2217316457 477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:cd00201 3 GWEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
477-503 |
1.21e-08 |
|
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: 51.45 E-value: 1.21e-08
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
79-404 |
1.83e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.63 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 79 TSIDARPTCSSSvqiSLQRKATDGATDGCGP-PEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPPR 157
Cdd:PHA03247 2667 ARRLGRAAQASS---PPQRPRRRAARPTVGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 158 AARDPGLQVN-GTCGRRVRCSGPVDCAEEAAPGLRIQHRASSADVRQVRL----LPLGPDGQGGPAAAEPRRWSLQHVPD 232
Cdd:PHA03247 2744 VPAGPATPGGpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSEsresLPSPWDPADPPAAVLAPAAALPPAAS 2823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 233 ASGSSGKRCFVFQLQQPQQGASGPGSDLNFGFTGTKGDRLVRYPRIRLERSTSYPTQPRSERGSptedRGALEASPRAGR 312
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLA----RPAVSRSTESFA 2899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 313 MAP---EIRRTNSAERTPQGQGCTFKIRQDQNAGQqhfrilvTRGPEEAPQNPEEKSAKSPVSTGADTTTRDDFL--GQV 387
Cdd:PHA03247 2900 LPPdqpERPPQPQAPPPPQPQPQPPPPPQPQPPPP-------PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALvpGRV 2972
|
330
....*....|....*..
gi 2217316457 388 DVPLSHLPTEDPTMERP 404
Cdd:PHA03247 2973 AVPRFRVPQPAPSREAP 2989
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
99-327 |
8.12e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.09 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 99 ATDGATDGCGPPEGADDGPPCATPDPRDQASA-----TATTRASPQSGSREPSPRDtPGSSPPRAAR--------DPGLQ 165
Cdd:PHA03307 57 AGAAACDRFEPPTGPPPGPGTEAPANESRSTPtwslsTLAPASPAREGSPTPPGPS-SPDPPPPTPPpaspppspAPDLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 166 VNgtcGRRVRCSGPVDCAEEAAPGLriQHRASSADVRQVR----LLPLGPDGQGGPAAAEPRRWSLQHVPDASGSSGKRC 241
Cdd:PHA03307 136 EM---LRPVGSPGPPPAASPPAAGA--SPAAVASDAASSRqaalPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 242 FVFQLQQPQQGASGPGSD-----------LNFGFTGTKGDRLVRYPRIRLERSTSyPTQPRSERGSPTEDRGALEASPRA 310
Cdd:PHA03307 211 SPISASASSPAPAPGRSAaddagasssdsSSSESSGCGWGPENECPLPRPAPITL-PTRIWEASGWNGPSSRPGPASSSS 289
|
250
....*....|....*..
gi 2217316457 311 GRMAPEIRRTNSAERTP 327
Cdd:PHA03307 290 SPRERSPSPSPSSPGSG 306
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
102-328 |
6.06e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 102 GATDGCGPPEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPPRAARDPGLQVNGTCGRRVRCSGPVD 181
Cdd:PRK07764 593 GAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAK 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 182 cAEEAAPglriqhraSSADVRQVRLLPLGPDGQGGPAAAEPRRWSLQHVPDASGSSgkrcfvfQLQQPQQGASGPGSDln 261
Cdd:PRK07764 673 -AGGAAP--------AAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAA-------QPPQAAQGASAPSPA-- 734
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217316457 262 fgftgtkGDRLVRYPRIRLERSTSYPTQPRSERGSPTEDRGALEASPRAGRMAPEIRRTNSAERTPQ 328
Cdd:PRK07764 735 -------ADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMD 794
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
65-222 |
1.06e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 65 ALKRSSSMFIPQLLTSIDARPTCSSSVQISLQRKATDGATDGCGPP-----EGADDGPPCATPDPRDQASATATTRASPQ 139
Cdd:PHA03307 744 ARARASAWDITDALFSNPSLVPAKLAEALALLEPAEPQRGAGSSPPvraeaAFRRPGRLRRSGPAADAASRTASKRKSRS 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 140 SGSREPSPRDTPGSSPPRAARDPGLQVNGTCGRRVRCSGPVDCAEEAAPGLRIQHRASSADVRQVRLLPLGPDGQGGPAA 219
Cdd:PHA03307 824 HTPDGGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAP 903
|
...
gi 2217316457 220 AEP 222
Cdd:PHA03307 904 RPR 906
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
83-331 |
2.40e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 83 ARPTCSSSVQISLQRKATDGATDGCGPPegaDDGPPcATPDPRDQASATATTRASPQSGSREPSPRD-----------TP 151
Cdd:PHA03307 86 STPTWSLSTLAPASPAREGSPTPPGPSS---PDPPP-PTPPPASPPPSPAPDLSEMLRPVGSPGPPPaasppaagaspAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 152 GSSPPRAARDPGLQVNGTcGRRVRCSG------PVDCAEEAAPGlRIQHRASSADVRQVRLLPLGPDGQGGPAAAEPrrw 225
Cdd:PHA03307 162 VASDAASSRQAALPLSSP-EETARAPSsppaepPPSTPPAAASP-RPPRRSSPISASASSPAPAPGRSAADDAGASS--- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 226 slqhvPDASGSSGKRCFVFQLQQPQQGASGPGSDLNFGFTGTKGDRlvRYPRIRLERSTSYPTQPRSERGSPTEDRGALE 305
Cdd:PHA03307 237 -----SDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNG--PSSRPGPASSSSSPRERSPSPSPSSPGSGPAP 309
|
250 260
....*....|....*....|....*.
gi 2217316457 306 ASPRAGRMAPEIRRTNSAERTPQGQG 331
Cdd:PHA03307 310 SSPRASSSSSSSRESSSSSTSSSSES 335
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
109-319 |
3.93e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.59 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 109 PPEGADDGPPCATPDPRDQASATATTRASPQSGS------------REPSPRDTPGSS-PPRAARDPGLQVNGTCGRRVR 175
Cdd:PHA03378 697 PPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAApgrarppaaapgRARPPAAAPGRArPPAAAPGRARPPAAAPGAPTP 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 176 CSGPvdcaeEAAPGLRIQHRASSADVRQ-------VRLLPLGPDGQGGPAAAEPRRWSLQHVpdasgSSGKRCFVFQLQQ 248
Cdd:PHA03378 777 QPPP-----QAPPAPQQRPRGAPTPQPPpqagptsMQLMPRAAPGQQGPTKQILRQLLTGGV-----KRGRPSLKKPAAL 846
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217316457 249 PQQGASGPGSDLNFGftgtKGDRLVRYPRIRLERSTsyPTQPRSERGSPTEdrGALEASPRAGRMAPEIRR 319
Cdd:PHA03378 847 ERQAAAGPTPSPGSG----TSDKIVQAPVFYPPVLQ--PIQVMRQLGSVRA--AAASTVTQAPTEYTGERR 909
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
77-324 |
4.06e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 77 LLTSIDARPTCSSSVQISLQRKATDGATDGCGPPEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPP 156
Cdd:PHA03307 175 PLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 157 RAARDPGLQVNGTCGRRvrcsGPVDCAEEAAPGlriqhRASSADVRQVRLLPLGPDGQGGPAAAEPRRWSLQHVPDASGS 236
Cdd:PHA03307 255 CPLPRPAPITLPTRIWE----ASGWNGPSSRPG-----PASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESS 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 237 SGKRcfvfqlqqpqqGASGPGSDlnfgftgtkgDRLVRYPRiRLERSTSYPTQPRSERGSPTEDRGALEASPRAGRMA-- 314
Cdd:PHA03307 326 SSST-----------SSSSESSR----------GAAVSPGP-SPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASag 383
|
250
....*....|.
gi 2217316457 315 -PEIRRTNSAE 324
Cdd:PHA03307 384 rPTRRRARAAV 394
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
95-236 |
9.26e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316457 95 LQRKATDgatDGCGPPEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPPRAARDPGLQVNGTC---- 170
Cdd:PHA03247 2540 LEELASD---DAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAppsp 2616
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217316457 171 -------------GRRVRCSGPVDCAEEAAPGlRIQHRASSADVRQVRLLPLGPDGQGGPAAAEPRRWSLQHVPDASGS 236
Cdd:PHA03247 2617 lppdthapdppppSPSPAANEPDPHPPPTVPP-PERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGS 2694
|
|
| |
