|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
516-868 |
0e+00 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains. :
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 529.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078 2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLELFF-IQ 674
Cdd:cd00078 82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 675 DMEILGKVTTHELKEGGENIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078 162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 755 IDMSDWQKNAIYRH-YTKSSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDRVGK-ETWL 832
Cdd:cd00078 242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 157818573 833 PRSHTCFNRLDLPPYKSYEQLKEKLLYAIEETEGFG 868
Cdd:cd00078 317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| C2_E3_ubiquitin_ligase |
cd04021 |
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ... |
17-142 |
4.03e-52 |
|
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: 177.85 E-value: 4.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 17 KSQLTLRVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEVIVLNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021 1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 157818573 96 LGTASVNLSNVLKNNGGKMENTQLTLNLQTENKGSVVSGGELTIFLD 142
Cdd:cd04021 79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
332-361 |
1.51e-12 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. :
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 62.14 E-value: 1.51e-12
10 20 30
....*....|....*....|....*....|
gi 157818573 332 LPPGWEKRTDPRGRFYYVDHNTRTTTWQRP 361
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
407-435 |
3.37e-12 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. :
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 61.37 E-value: 3.37e-12
10 20 30
....*....|....*....|....*....|
gi 157818573 407 LPPGWEKRQD-NGRVYYVNHNTRTTQWEDP 435
Cdd:pfam00397 1 LPPGWEERWDpDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
302-331 |
1.96e-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: 59.06 E-value: 1.96e-11
10 20 30
....*....|....*....|....*....|
gi 157818573 302 LPAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
447-477 |
1.17e-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: 51.37 E-value: 1.17e-08
10 20 30
....*....|....*....|....*....|.
gi 157818573 447 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
163-312 |
4.30e-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: 50.71 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 163 PPSRESSGTAL-----APETRHQPPSTNCFGGRSRTHRHSGGSARTATATgeqSPgaRNRHRQPVKNPSSSGLANGT--V 235
Cdd:PHA03247 2628 PPSPSPAANEPdphppPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS---SP--PQRPRRRAARPTVGSLTSLAdpP 2702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 236 SEEPTTASDPEEL-SVVGVTSPPAAASSVSPNPNTTSLP--APSTPAEGEEPSTSGTQQLPAA--AQAPDALPAGWEQRQ 310
Cdd:PHA03247 2703 PPPPTPEPAPHALvSATPLPPGPAAARQASPALPAAPAPpaVPAGPATPGGPARPARPPTTAGppAPAPPAAPAAGPPRR 2782
|
..
gi 157818573 311 LP 312
Cdd:PHA03247 2783 LT 2784
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
516-868 |
0e+00 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 529.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078 2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLELFF-IQ 674
Cdd:cd00078 82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 675 DMEILGKVTTHELKEGGENIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078 162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 755 IDMSDWQKNAIYRH-YTKSSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDRVGK-ETWL 832
Cdd:cd00078 242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 157818573 833 PRSHTCFNRLDLPPYKSYEQLKEKLLYAIEETEGFG 868
Cdd:cd00078 317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
539-867 |
1.14e-175 |
|
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: 509.85 E-value: 1.14e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 539 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 616
Cdd:smart00119 1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 617 YHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLEL-FFIQDMEILGKVTTHELKEGGENIR 695
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLtFSIVLTSEFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 696 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKNAIYRH-YTKSSK 774
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 775 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDRVG-KETWLPRSHTCFNRLDLPPYKSYEQL 853
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 157818573 854 KEKLLYAIEETEGF 867
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
331-870 |
5.35e-175 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 528.18 E-value: 5.35e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 402
Cdd:COG5021 298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 403 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 456
Cdd:COG5021 378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 457 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYERSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 536
Cdd:COG5021 458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 537 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 616
Cdd:COG5021 537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 617 YHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLELFFIQDMEILGKVTTHELKEGGENIRV 696
Cdd:COG5021 617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 697 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKNAIYRHYTKSSKQ 775
Cdd:COG5021 697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 776 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDRVG-KETWLPRSHTCFNRLDLPPYKSYEQLK 854
Cdd:COG5021 777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856
|
570
....*....|....*.
gi 157818573 855 EKLLYAIEETEGFGQE 870
Cdd:COG5021 857 SKLLTAINEGAGFGLL 872
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
565-868 |
3.04e-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: 389.66 E-value: 3.04e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 565 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLR 642
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 643 DLESIDPEFYNSIIWIKENNLD-ECGLELFFIqdMEILGKVTTHELKEGGENIRVTEENKEEYIMLLTDWRFTRGVEEQT 721
Cdd:pfam00632 81 DLESIDPELYKSLKSLLNMDNDdDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 722 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKNAIYRH-YTKSSKQIQWFWQVVKEMDNEKRIRLLQFVTG 800
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 801 TCRLPVGGFAELigsngpQKFCIDRVG--KETWLPRSHTCFNRLDLPPYKSYEQLKEKLLYAIEETEGFG 868
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
|
|
| C2_E3_ubiquitin_ligase |
cd04021 |
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ... |
17-142 |
4.03e-52 |
|
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: 177.85 E-value: 4.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 17 KSQLTLRVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEVIVLNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021 1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 157818573 96 LGTASVNLSNVLKNNGGKMENTQLTLNLQTENKGSVVSGGELTIFLD 142
Cdd:cd04021 79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
332-361 |
1.51e-12 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 62.14 E-value: 1.51e-12
10 20 30
....*....|....*....|....*....|
gi 157818573 332 LPPGWEKRTDPRGRFYYVDHNTRTTTWQRP 361
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
407-435 |
3.37e-12 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 61.37 E-value: 3.37e-12
10 20 30
....*....|....*....|....*....|
gi 157818573 407 LPPGWEKRQD-NGRVYYVNHNTRTTQWEDP 435
Cdd:pfam00397 1 LPPGWEERWDpDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
406-436 |
5.18e-12 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 60.69 E-value: 5.18e-12
10 20 30
....*....|....*....|....*....|..
gi 157818573 406 PLPPGWEKRQD-NGRVYYVNHNTRTTQWEDPR 436
Cdd:smart00456 1 PLPPGWEERKDpDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
408-436 |
1.11e-11 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 59.85 E-value: 1.11e-11
10 20 30
....*....|....*....|....*....|
gi 157818573 408 PPGWEKRQDN-GRVYYVNHNTRTTQWEDPR 436
Cdd:cd00201 1 PPGWEERWDPdGRVYYYNHNTKETQWEDPR 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
302-331 |
1.96e-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: 59.06 E-value: 1.96e-11
10 20 30
....*....|....*....|....*....|
gi 157818573 302 LPAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
331-362 |
3.69e-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: 58.38 E-value: 3.69e-11
10 20 30
....*....|....*....|....*....|..
gi 157818573 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 362
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
333-362 |
7.23e-11 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.54 E-value: 7.23e-11
10 20 30
....*....|....*....|....*....|
gi 157818573 333 PPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 362
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
302-331 |
8.06e-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: 8.06e-11
10 20 30
....*....|....*....|....*....|
gi 157818573 302 LPAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
303-331 |
9.79e-11 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.15 E-value: 9.79e-11
10 20
....*....|....*....|....*....
gi 157818573 303 PAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
19-115 |
4.57e-09 |
|
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 54.42 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 19 QLTLRVVSAKPKVHNRQPR-INSYVEVAVDGLPSETKKTGKRIGSSELLWNEVIVLNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239 1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80
|
90 100
....*....|....*....|.
gi 157818573 95 LLGTASVNLSNVLKNNGGKME 115
Cdd:smart00239 81 FIGQVTIPLSDLLLGGRHEKL 101
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
447-477 |
1.17e-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: 51.37 E-value: 1.17e-08
10 20 30
....*....|....*....|....*....|.
gi 157818573 447 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
446-475 |
7.48e-08 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.04 E-value: 7.48e-08
10 20 30
....*....|....*....|....*....|
gi 157818573 446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDP 475
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
446-477 |
1.45e-07 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 47.98 E-value: 1.45e-07
10 20 30
....*....|....*....|....*....|..
gi 157818573 446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
163-312 |
4.30e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.71 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 163 PPSRESSGTAL-----APETRHQPPSTNCFGGRSRTHRHSGGSARTATATgeqSPgaRNRHRQPVKNPSSSGLANGT--V 235
Cdd:PHA03247 2628 PPSPSPAANEPdphppPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS---SP--PQRPRRRAARPTVGSLTSLAdpP 2702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 236 SEEPTTASDPEEL-SVVGVTSPPAAASSVSPNPNTTSLP--APSTPAEGEEPSTSGTQQLPAA--AQAPDALPAGWEQRQ 310
Cdd:PHA03247 2703 PPPPTPEPAPHALvSATPLPPGPAAARQASPALPAAPAPpaVPAGPATPGGPARPARPPTTAGppAPAPPAAPAAGPPRR 2782
|
..
gi 157818573 311 LP 312
Cdd:PHA03247 2783 LT 2784
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
104-310 |
6.51e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 40.36 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 104 SNVLKNNGGKMENTQLTLNLQTENKGSVVSGGelTIFLDGPTVDLGSVPNGSAVTDGSQPPSRESSGTALApETRhqpPS 183
Cdd:TIGR00927 268 TDLLTSPRSVVEKNTLTTPRRVESNSSTNHWG--LVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSSPA-ETK---AS 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 184 TNCFGGRSRTHRHSGGSARTATATgeqspgarnrHRQPVKNPSS--SGLANGTVSEEPTTASDPeelsvvGVTSPPAAAS 261
Cdd:TIGR00927 342 TAAWKIRNPLSRTSAPAVRIASAT----------FRGLEKNPSTapSTPATPRVRAVLTTQVHH------CVVVKPAPAV 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157818573 262 SVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRQ 310
Cdd:TIGR00927 406 PTTPSPSLTTALFPEAPSPSPSALPPGQPDLHPKAEYPPDLFSVEERRQ 454
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
516-868 |
0e+00 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 529.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 516 KISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 595
Cdd:cd00078 2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 596 SINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLELFF-IQ 674
Cdd:cd00078 82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFtIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 675 DMEILGKVTTHELKEGGENIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE 754
Cdd:cd00078 162 LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 755 IDMSDWQKNAIYRH-YTKSSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDRVGK-ETWL 832
Cdd:cd00078 242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSpDDRL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 157818573 833 PRSHTCFNRLDLPPYKSYEQLKEKLLYAIEETEGFG 868
Cdd:cd00078 317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
539-867 |
1.14e-175 |
|
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: 509.85 E-value: 1.14e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 539 DLR-RRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINPASSI-NPDHLTYFRFIGRFIAMAL 616
Cdd:smart00119 1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 617 YHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLEL-FFIQDMEILGKVTTHELKEGGENIR 695
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLtFSIVLTSEFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 696 VTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKNAIYRH-YTKSSK 774
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 775 QIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELigsngPQKFCIDRVG-KETWLPRSHTCFNRLDLPPYKSYEQL 853
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL-----SPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 157818573 854 KEKLLYAIEETEGF 867
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
331-870 |
5.35e-175 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 528.18 E-value: 5.35e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQW----QSQRNQLQGAMQH--FSQRFLYQSSSASTDHD-- 402
Cdd:COG5021 298 RLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSflvvNNDDSSSIKDLPHqvGSNPFLEAHPEFSELLKnq 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 403 ------PLGPLPPGWEKR-QDNGRVYYVNHNTRTTQWEDPRTQGMI-------------------QEPALPPGWEMKYTS 456
Cdd:COG5021 378 srgttrDFRNKPTGWSSSiEDLGQFLFSDFLTSSSTYEDLRREQLGresdesfyvasnvqqqrasREGPLLSGWKTRLNN 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 457 EGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYERSFRWKYHQFRFLCHSNaLPSHVKISVSRQTLFEDSFQQIMNMK 536
Cdd:COG5021 458 LYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDES 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 537 PYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMAL 616
Cdd:COG5021 537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAI 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 617 YHGKFIDTGFTLPFYKRMLNKRPTLRDLESIDPEFYNSIIWIKENNLDECGLELFFIQDMEILGKVTTHELKEGGENIRV 696
Cdd:COG5021 617 YDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISV 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 697 TEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQE-IDMSDWQKNAIYRHYTKSSKQ 775
Cdd:COG5021 697 TNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPI 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 776 IQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDRVG-KETWLPRSHTCFNRLDLPPYKSYEQLK 854
Cdd:COG5021 777 IVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKLR 856
|
570
....*....|....*.
gi 157818573 855 EKLLYAIEETEGFGQE 870
Cdd:COG5021 857 SKLLTAINEGAGFGLL 872
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
565-868 |
3.04e-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: 389.66 E-value: 3.04e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 565 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDH--LTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLR 642
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 643 DLESIDPEFYNSIIWIKENNLD-ECGLELFFIqdMEILGKVTTHELKEGGENIRVTEENKEEYIMLLTDWRFTRGVEEQT 721
Cdd:pfam00632 81 DLESIDPELYKSLKSLLNMDNDdDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 722 KAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKNAIYRH-YTKSSKQIQWFWQVVKEMDNEKRIRLLQFVTG 800
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 801 TCRLPVGGFAELigsngpQKFCIDRVG--KETWLPRSHTCFNRLDLPPYKSYEQLKEKLLYAIEETEGFG 868
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
|
|
| C2_E3_ubiquitin_ligase |
cd04021 |
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ... |
17-142 |
4.03e-52 |
|
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: 177.85 E-value: 4.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 17 KSQLTLRVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEVIVLNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021 1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 157818573 96 LGTASVNLSNVLKNNGGKMENTQLTLNLQTENKGSVVSGGELTIFLD 142
Cdd:cd04021 79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
332-361 |
1.51e-12 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 62.14 E-value: 1.51e-12
10 20 30
....*....|....*....|....*....|
gi 157818573 332 LPPGWEKRTDPRGRFYYVDHNTRTTTWQRP 361
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
407-435 |
3.37e-12 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 61.37 E-value: 3.37e-12
10 20 30
....*....|....*....|....*....|
gi 157818573 407 LPPGWEKRQD-NGRVYYVNHNTRTTQWEDP 435
Cdd:pfam00397 1 LPPGWEERWDpDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
406-436 |
5.18e-12 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 60.69 E-value: 5.18e-12
10 20 30
....*....|....*....|....*....|..
gi 157818573 406 PLPPGWEKRQD-NGRVYYVNHNTRTTQWEDPR 436
Cdd:smart00456 1 PLPPGWEERKDpDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
408-436 |
1.11e-11 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 59.85 E-value: 1.11e-11
10 20 30
....*....|....*....|....*....|
gi 157818573 408 PPGWEKRQDN-GRVYYVNHNTRTTQWEDPR 436
Cdd:cd00201 1 PPGWEERWDPdGRVYYYNHNTKETQWEDPR 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
302-331 |
1.96e-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: 59.06 E-value: 1.96e-11
10 20 30
....*....|....*....|....*....|
gi 157818573 302 LPAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
331-362 |
3.69e-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: 58.38 E-value: 3.69e-11
10 20 30
....*....|....*....|....*....|..
gi 157818573 331 PLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 362
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
333-362 |
7.23e-11 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.54 E-value: 7.23e-11
10 20 30
....*....|....*....|....*....|
gi 157818573 333 PPGWEKRTDPRGRFYYVDHNTRTTTWQRPT 362
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
302-331 |
8.06e-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: 8.06e-11
10 20 30
....*....|....*....|....*....|
gi 157818573 302 LPAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
303-331 |
9.79e-11 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.15 E-value: 9.79e-11
10 20
....*....|....*....|....*....
gi 157818573 303 PAGWEQRQLPNGRVYYVDHNTKTTTWERP 331
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
19-115 |
4.57e-09 |
|
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 54.42 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 19 QLTLRVVSAKPKVHNRQPR-INSYVEVAVDGLPSETKKTGKRIGSSELLWNEVIVLNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239 1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80
|
90 100
....*....|....*....|.
gi 157818573 95 LLGTASVNLSNVLKNNGGKME 115
Cdd:smart00239 81 FIGQVTIPLSDLLLGGRHEKL 101
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
447-477 |
1.17e-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: 51.37 E-value: 1.17e-08
10 20 30
....*....|....*....|....*....|.
gi 157818573 447 PPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
446-475 |
7.48e-08 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.04 E-value: 7.48e-08
10 20 30
....*....|....*....|....*....|
gi 157818573 446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDP 475
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
297-381 |
7.98e-08 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 55.86 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 297 QAPDALPAG-----WEQRQLPNGRVYYVDHNTKTTTWERPLP-----------PGWEKRTDPRGRFYYVDHNTRTTTWQR 360
Cdd:COG5104 3 AALLGMASGearseWEELKAPDGRIYYYNKRTGKSSWEKPKEllkgseedldvDPWKECRTADGKVYYYNSITRESRWKI 82
|
90 100
....*....|....*....|....
gi 157818573 361 PtAEYVR---NYEQWQSQRNQLQG 381
Cdd:COG5104 83 P-PERKKvepIAEQKHDERSMIGG 105
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
446-477 |
1.45e-07 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 47.98 E-value: 1.45e-07
10 20 30
....*....|....*....|....*....|..
gi 157818573 446 LPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRP 477
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
163-312 |
4.30e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.71 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 163 PPSRESSGTAL-----APETRHQPPSTNCFGGRSRTHRHSGGSARTATATgeqSPgaRNRHRQPVKNPSSSGLANGT--V 235
Cdd:PHA03247 2628 PPSPSPAANEPdphppPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS---SP--PQRPRRRAARPTVGSLTSLAdpP 2702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 236 SEEPTTASDPEEL-SVVGVTSPPAAASSVSPNPNTTSLP--APSTPAEGEEPSTSGTQQLPAA--AQAPDALPAGWEQRQ 310
Cdd:PHA03247 2703 PPPPTPEPAPHALvSATPLPPGPAAARQASPALPAAPAPpaVPAGPATPGGPARPARPPTTAGppAPAPPAAPAAGPPRR 2782
|
..
gi 157818573 311 LP 312
Cdd:PHA03247 2783 LT 2784
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
20-112 |
9.73e-06 |
|
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.
Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 45.14 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 20 LTLRVVSAK-PKVHNRQPRINSYVEVAVDGlpSETKKTGKRIGSSELLWNEVIVLNVT--AQSHLDLKVWSCHTL-RNEL 95
Cdd:cd00030 1 LRVTVIEARnLPAKDLNGKSDPYVKVSLGG--KQKFKTKVVKNTLNPVWNETFEFPVLdpESDTLTVEVWDKDRFsKDDF 78
|
90
....*....|....*..
gi 157818573 96 LGTASVNLSNVLKNNGG 112
Cdd:cd00030 79 LGEVEIPLSELLDSGKE 95
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
162-345 |
1.14e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 162 QPPSRESSGTALAPETrhqPPSTNCFGGRSRTHRHSGGSARTATATGEQSPGARNRHRQP--VKNPSSSGLANGTVSEEP 239
Cdd:PHA03247 2704 PPPTPEPAPHALVSAT---PLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPptTAGPPAPAPPAAPAAGPP 2780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 240 TTASDPEELSVVGVT----SPPAAASSVSP-NPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRQLPNG 314
Cdd:PHA03247 2781 RRLTRPAVASLSESReslpSPWDPADPPAAvLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGG 2860
|
170 180 190
....*....|....*....|....*....|.
gi 157818573 315 rvyyvDHNTKTTTweRPLPPGWEKRTDPRGR 345
Cdd:PHA03247 2861 -----DVRRRPPS--RSPAAKPAAPARPPVR 2884
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
149-299 |
4.40e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 47.15 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 149 GSVPNGSAVTDGSQPPSRESSGTALAPETRHQPPSTNCFGGRSRTHRHSGGSARTATATGEQSPGARNRhrQPVKNPSSS 228
Cdd:PRK07003 400 TAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDA--QPPADSGSA 477
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157818573 229 GLANGTVseEPTTASDPEELSVVgvtSPPAAASSVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAP 299
Cdd:PRK07003 478 SAPASDA--PPDAAFEPAPRAAA---PSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
151-310 |
4.67e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.47 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 151 VPNGSAVTDGSQPPSRESsGTALAPETRHQPPSTNCFGGRSRTHRHSGGSARTATATGEQSPGARNRHRQPVKNPSSSGL 230
Cdd:PHA03307 230 DDAGASSSDSSSSESSGC-GWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 231 ANGTVSEEPTTASDPEELSVVGVTSPPAAASSVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRQ 310
Cdd:PHA03307 309 PSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRR 388
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
159-345 |
5.90e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.24 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 159 DGSQPPSRESSGTALAPETrhQPPSTNCFGGRSRTHRHSGGSARTATATGEQ----SPGARNRHRQpVKNPSSSGLANGT 234
Cdd:PHA03247 2603 DDRGDPRGPAPPSPLPPDT--HAPDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSP 2679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 235 VSEEPTTASDPEELSVVGVTSPPAaassvsPNPNTTSLPAPSTPAegeEPSTSGTQQLPAAAQAPDALPAgweQRQLPNG 314
Cdd:PHA03247 2680 PQRPRRRAARPTVGSLTSLADPPP------PPPTPEPAPHALVSA---TPLPPGPAAARQASPALPAAPA---PPAVPAG 2747
|
170 180 190
....*....|....*....|....*....|.
gi 157818573 315 RVYYVDHNTKTTtweRPLPPGWEKRTDPRGR 345
Cdd:PHA03247 2748 PATPGGPARPAR---PPTTAGPPAPAPPAAP 2775
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
144-300 |
2.20e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.84 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 144 PTVDLGSVPNG--SAVTDGSQPPSRESSGTALAPETR-HQPPSTNCFGGRSRTHrhsggSARTATATGEQSPGARNrhrq 220
Cdd:PRK07003 360 PAVTGGGAPGGgvPARVAGAVPAPGARAAAAVGASAVpAVTAVTGAAGAALAPK-----AAAAAAATRAEAPPAAP---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 221 pvkNPSSSGLANGTVSEEPTTASDPEELSVVGVTSPPAAASSVSPNPNTTSLPAPSTPAEG-EEPSTSGTQQLPAAAQAP 299
Cdd:PRK07003 431 ---APPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAaFEPAPRAAAPSAATPAAV 507
|
.
gi 157818573 300 D 300
Cdd:PRK07003 508 P 508
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
154-308 |
5.61e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.82 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 154 GSAVTDGSQPPSRESSGTALAPETRHQPPStncfggrsrthrhSGGSARTATATGEQSPGARNRHRQPVKNPSSSGLANG 233
Cdd:PRK07764 390 GAGAPAAAAPSAAAAAPAAAPAPAAAAPAA-------------AAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSP 456
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157818573 234 TVSEEPTTASDPeelsvvgvtsPPAAASSVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALpagWEQ 308
Cdd:PRK07764 457 PPAAAPSAQPAP----------APAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRER---WPE 518
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
143-300 |
6.21e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.44 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 143 GPTVDLGSVPNGSAVTDGSQPPSRESSGTALAPETRHQPPSTNCFGGRSRTHrhsggSARTATATGEQSPGARNRHRQPV 222
Cdd:PRK07764 651 EHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA-----PAPAATPPAGQADDPAAQPPQAA 725
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818573 223 KNPSSSGLANGTVSEEPTTASDPEELSVVGVTSPPAAASSVSPNPNTTslPAPSTPAEGEEPstsgtqqLPAAAQAPD 300
Cdd:PRK07764 726 QGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAA--PPPSPPSEEEEM-------AEDDAPSMD 794
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
141-334 |
1.09e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 141 LDGPTVDLGSVPNGSAVTDGSQPPSRESSGTALAPETRHQPPSTNCFGGRSRTHRHSGGSARTAT----ATGEQSPGARN 216
Cdd:PHA03307 259 RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSREssssSTSSSSESSRG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 217 RHRQPVKNPSSSglangtvseePTTASDPEELSvvgvTSPPAAASSVSPNPNTTSLPAPSTP-------AEGEEPSTSGT 289
Cdd:PHA03307 339 AAVSPGPSPSRS----------PSPSRPPPPAD----PSSPRKRPRPSRAPSSPAASAGRPTrrraraaVAGRARRRDAT 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157818573 290 QQLPAAAQAPDALPA-GWEQRQLPNGRVYYVDhntKTTTWERPLPP 334
Cdd:PHA03307 405 GRFPAGRPRPSPLDAgAASGAFYARYPLLTPS---GEPWPGSPPPP 447
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
156-301 |
1.14e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.53 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 156 AVTDGSQPPsressGTALAPETRHQPpstncfGGRSRTHRHSGGSARTATATGEQSPGARNRhrqpvknPSSSGLANGTV 235
Cdd:PRK07003 361 AVTGGGAPG-----GGVPARVAGAVP------APGARAAAAVGASAVPAVTAVTGAAGAALA-------PKAAAAAAATR 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157818573 236 SEEPTTASDPEELSVVGVTSPPAAASSVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDA 301
Cdd:PRK07003 423 AEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDA 488
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
144-315 |
2.00e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 144 PTVDLGSVPNGSAVTDGSQPPSRESSGTALAPETRHQPPSTNCFGGRSRTHrhsgGSARTATATGEQSPGARNRHRQPvK 223
Cdd:PHA03307 80 PANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSP----APDLSEMLRPVGSPGPPPAASPP-A 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 224 NPSSSGlangtvsEEPTTASDPEELSVVGVTSPPAAASSVSPNPNttslPAPSTPAEGEEPSTSGTQQlPAAAQAPDALP 303
Cdd:PHA03307 155 AGASPA-------AVASDAASSRQAALPLSSPEETARAPSSPPAE----PPPSTPPAAASPRPPRRSS-PISASASSPAP 222
|
170
....*....|..
gi 157818573 304 AGWEQRQLPNGR 315
Cdd:PHA03307 223 APGRSAADDAGA 234
|
|
| C2_SRC2_like |
cd04051 |
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ... |
20-131 |
2.53e-03 |
|
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 176016 [Multi-domain] Cd Length: 125 Bit Score: 38.75 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 20 LTLRVVSAKP-KVHNRQPRINSYVEVAVDGlpsETKKTGK--RIGSSELLWNEVIVLNVTAQ------SHLDLKVWsCHT 90
Cdd:cd04051 2 LEITIISAEDlKNVNLFGKMKVYAVVWIDP---SHKQSTPvdRDGGTNPTWNETLRFPLDERllqqgrLALTIEVY-CER 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 157818573 91 --LRNELLGTASVNLSNVLKNNGGKMENTQLTLNLQTEN---KGSV 131
Cdd:cd04051 78 psLGDKLIGEVRVPLKDLLDGASPAGELRFLSYQLRRPSgkpQGVL 123
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
160-371 |
4.29e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.74 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 160 GSQPPSRESSGTALAPETRHQPPSTncfggrsrthRHSGGSARTATAtGEQSPGARNRHRQPVKNPSSSGLANGTVSEEP 239
Cdd:PRK07764 594 AAGGEGPPAPASSGPPEEAARPAAP----------AAPAAPAAPAPA-GAAAAPAEASAAPAPGVAAPEHHPKHVAVPDA 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 240 TTASDPEelsvvGVTSPPAAASSVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRQLPNGRVyyv 319
Cdd:PRK07764 663 SDGGDGW-----PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPA--- 734
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157818573 320 dhntktTTWERPLPPGWEKRTDPRGRFYYVDHNTRT---TTWQRPTAEYVRNYEQ 371
Cdd:PRK07764 735 ------ADDPVPLPPEPDDPPDPAGAPAQPPPPPAPapaAAPAAAPPPSPPSEEE 783
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
104-310 |
6.51e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 40.36 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 104 SNVLKNNGGKMENTQLTLNLQTENKGSVVSGGelTIFLDGPTVDLGSVPNGSAVTDGSQPPSRESSGTALApETRhqpPS 183
Cdd:TIGR00927 268 TDLLTSPRSVVEKNTLTTPRRVESNSSTNHWG--LVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSSPA-ETK---AS 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818573 184 TNCFGGRSRTHRHSGGSARTATATgeqspgarnrHRQPVKNPSS--SGLANGTVSEEPTTASDPeelsvvGVTSPPAAAS 261
Cdd:TIGR00927 342 TAAWKIRNPLSRTSAPAVRIASAT----------FRGLEKNPSTapSTPATPRVRAVLTTQVHH------CVVVKPAPAV 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157818573 262 SVSPNPNTTSLPAPSTPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRQ 310
Cdd:TIGR00927 406 PTTPSPSLTTALFPEAPSPSPSALPPGQPDLHPKAEYPPDLFSVEERRQ 454
|
|
|