NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|929653749|dbj|BAA05837|]
View 

KIAA0045 [Homo sapiens]

Protein Classification

E3 ubiquitin-protein ligase TRIP12 family protein( domain architecture ID 13359941)

E3 ubiquitin-protein ligase TRIP12 (thyroid hormone receptor interactor 12) family protein is involved in a broad range of physiological processes such as mouse embryogenesis; TRIP12 displays a HECT domain, a WW (tryptophan-tryptophan) protein-protein interaction motif and an ARM domain (armadillo/beta-catenin-like repeats)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
1590-1990 1.76e-128

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: 407.34  E-value: 1.76e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1590 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqeg 1666
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1667 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1746
Cdd:cd00078    67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1747 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1826
Cdd:cd00078   139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1827 FWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1906
Cdd:cd00078   197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1907 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGq 1986
Cdd:cd00078   275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                  ....
gi 929653749 1987 QSFH 1990
Cdd:cd00078   349 AGFG 352
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
762-798 9.51e-09

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


:

Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 53.45  E-value: 9.51e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 929653749   762 IWQWRDDRGLWHPYNRIDSRIIE-----------------------------QINEDTGTARAIQR 798
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEeayqkgkpsvdlsittagfpytidfksmtQTNKDTGTTRPVRR 66
SRP1 super family cl34886
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
441-666 2.41e-05

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


The actual alignment was detected with superfamily member COG5064:

Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 49.12  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  441 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 519
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  520 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 592
Cdd:COG5064   154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929653749  593 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 666
Cdd:COG5064   233 NPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTPALRSVG 310
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
2-420 7.40e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749    2 SNRPNNNPGGSLRrSQRNTAGAQPQDDSIGGRSCSSSSAVIVPQPEDPDRANtSERQKTGQVPKKDNSRGVKRSASPDYN 81
Cdd:PHA03307   81 ANESRSTPTWSLS-TLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPA-PDLSEMLRPVGSPGPPPAASPPAAGAS 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   82 RTNSPSSAKKPK----ALQHTESPSETNKPHSKSKKRHLDQEQQLKSAQSPSTSKAHTRKSGATGGSRSQKRKRTESSCV 157
Cdd:PHA03307  159 PAAVASDAASSRqaalPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSD 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  158 KSGSGSESTGAEERSAKPTKLASKSATSakagcSTITDSSSAASTSSSSSAVASASSTVPPGARVKQGKDqNKARRSRSA 237
Cdd:PHA03307  239 SSSSESSGCGWGPENECPLPRPAPITLP-----TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSP-GSGPAPSSP 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  238 SSPSPRRSSREKEQSKTGGSSKFDWAARFSPKvslpktklSLPGSSKSETSKPGPSGlqaklaslRKSTKKR---SESPP 314
Cdd:PHA03307  313 RASSSSSSSRESSSSSTSSSSESSRGAAVSPG--------PSPSRSPSPSRPPPPAD--------PSSPRKRprpSRAPS 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  315 AELPSLRRSTRQKTTGSCASTSRRGSGLGKRGAAEARRQEKMADpesnqeaVNSSAARTDEAPqgaagavgMTTSGES-- 392
Cdd:PHA03307  377 SPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAG-------AASGAFYARYPL--------LTPSGEPwp 441
                         410       420
                  ....*....|....*....|....*...
gi 929653749  393 ESDDSEMGRLqallearglpphLFGPLG 420
Cdd:PHA03307  442 GSPPPPPGRV------------RYGGLG 457
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
1590-1990 1.76e-128

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: 407.34  E-value: 1.76e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1590 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqeg 1666
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1667 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1746
Cdd:cd00078    67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1747 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1826
Cdd:cd00078   139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1827 FWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1906
Cdd:cd00078   197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1907 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGq 1986
Cdd:cd00078   275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                  ....
gi 929653749 1987 QSFH 1990
Cdd:cd00078   349 AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1608-1986 3.30e-126

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: 399.69  E-value: 3.30e-126
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   1608 DLGSSRamLEIQYENEVG-TGLGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqegtkYIQNLQGLFALPFGRTAK 1686
Cdd:smart00119    1 DLKKRV--LEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFR-----------------YSPNDYLLYPNPRSGFAN 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   1687 PAHIakvkMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRqeTSLTSHDLFDIDPVVARSVYHLedivrqkkRLEQDK 1766
Cdd:smart00119   62 EEHL----SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL--------LLNNDT 127
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   1767 SqtkeslqYALETltmngcsVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFE 1846
Cdd:smart00119  128 S-------EELDL-------TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFS 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   1847 SVFPLSHLQYFYPEELDQLLCGSKadTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPV 1926
Cdd:smart00119  194 EVIPENLLKLFDPEELELLICGSP--EIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV 271
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   1927 GGFRSLNPPLTIVRKTFEstenpDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGQ 1986
Cdd:smart00119  272 GGFAALSPKFTIRKAGSD-----DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGK 326
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1637-1992 1.24e-103

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 334.58  E-value: 1.24e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  1637 LVSQELQRADLGLWRGEevtlsnpkgsQEGTKYIqnlqglfalPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDL 1716
Cdd:pfam00632    2 LLSKELFDPNYGLFEYE----------TEDDRTY---------WFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDL 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  1717 PLGLPFYKWMLRQEtsLTSHDLFDIDPVVARSVYHLedivrqkkrleqdksqtkeslqyaletLTMNGCSVEDLGLDFTL 1796
Cdd:pfam00632   63 PFPPFFYKKLLGEP--LTLEDLESIDPELYKSLKSL---------------------------LNMDNDDDEDLGLTFTI 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  1797 PGF---PNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDT 1873
Cdd:pfam00632  114 PVFgesKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PE 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  1874 WDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLnPPLTIVRKTFesteNPDDFL 1953
Cdd:pfam00632  192 IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGG----DDDDRL 266
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 929653749  1954 PSVMTCVNYLKLPDYSSIEIMREKLLIAAREGqQSFHLS 1992
Cdd:pfam00632  267 PTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1500-1991 3.52e-80

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 285.12  E-value: 3.52e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1500 TSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGktcPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPeinqSDSQD 1579
Cdd:COG5021   410 SSSTYEDLRREQLGRESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSR----LGSFI 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1580 SRVAPRLDRKKRTVNREELLKQAESVM-----QDLGSSRAM----LEIQYENEVGTGLGPTLEFYALVSQELQRADLGLW 1650
Cdd:COG5021   483 SLNKLDIRRIKEDKRRKLFYSLKQKAKifdpyLHIKVRRDRvfedSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTRE 562
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1651 RgeEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTA--KPAHIAKvkmkFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLR 1728
Cdd:COG5021   563 W--LFLLSKEMFNPDYGLFEYITEDLYTLPINPLSsiNPEHLSY----FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG 636
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1729 QetSLTSHDLFDIDPVVARSVyhledivrqKKRLEQDKsqTKESLqyaleTLTMngcSVEDLGLDFTLPgfpnIELKKGG 1808
Cdd:COG5021   637 K--PVSLVDLESLDPELYRSL---------VWLLNNDI--DETIL-----DLTF---TVEDDSFGESRT----VELIPNG 691
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1809 KDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkADTWDAKTLMECCRpDHG 1888
Cdd:COG5021   692 RNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGI-PEDIDIDDWKSNTA-YHG 769
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1889 YTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDY 1968
Cdd:COG5021   770 YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEY 849
                         490       500
                  ....*....|....*....|...
gi 929653749 1969 SSIEIMREKLLIAAREGQQSFHL 1991
Cdd:COG5021   850 SSKEKLRSKLLTAINEGAGFGLL 872
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
762-798 9.51e-09

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 53.45  E-value: 9.51e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 929653749   762 IWQWRDDRGLWHPYNRIDSRIIE-----------------------------QINEDTGTARAIQR 798
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEeayqkgkpsvdlsittagfpytidfksmtQTNKDTGTTRPVRR 66
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
441-666 2.41e-05

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 49.12  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  441 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 519
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  520 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 592
Cdd:COG5064   154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929653749  593 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 666
Cdd:COG5064   233 NPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTPALRSVG 310
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
762-802 2.87e-05

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 43.87  E-value: 2.87e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 929653749    762 IWQWRDDRGLWHPYNRIDSRIIE---------------------------QINEDTGTARAIQRKPNP 802
Cdd:smart00678    2 VWEYEGRNGKWWPYDPRVSEDIEeayaagkklcelsicgfpytidfnamtQYNQATGTTRKVRRVTYS 69
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2-420 7.40e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749    2 SNRPNNNPGGSLRrSQRNTAGAQPQDDSIGGRSCSSSSAVIVPQPEDPDRANtSERQKTGQVPKKDNSRGVKRSASPDYN 81
Cdd:PHA03307   81 ANESRSTPTWSLS-TLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPA-PDLSEMLRPVGSPGPPPAASPPAAGAS 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   82 RTNSPSSAKKPK----ALQHTESPSETNKPHSKSKKRHLDQEQQLKSAQSPSTSKAHTRKSGATGGSRSQKRKRTESSCV 157
Cdd:PHA03307  159 PAAVASDAASSRqaalPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSD 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  158 KSGSGSESTGAEERSAKPTKLASKSATSakagcSTITDSSSAASTSSSSSAVASASSTVPPGARVKQGKDqNKARRSRSA 237
Cdd:PHA03307  239 SSSSESSGCGWGPENECPLPRPAPITLP-----TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSP-GSGPAPSSP 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  238 SSPSPRRSSREKEQSKTGGSSKFDWAARFSPKvslpktklSLPGSSKSETSKPGPSGlqaklaslRKSTKKR---SESPP 314
Cdd:PHA03307  313 RASSSSSSSRESSSSSTSSSSESSRGAAVSPG--------PSPSRSPSPSRPPPPAD--------PSSPRKRprpSRAPS 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  315 AELPSLRRSTRQKTTGSCASTSRRGSGLGKRGAAEARRQEKMADpesnqeaVNSSAARTDEAPqgaagavgMTTSGES-- 392
Cdd:PHA03307  377 SPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAG-------AASGAFYARYPL--------LTPSGEPwp 441
                         410       420
                  ....*....|....*....|....*...
gi 929653749  393 ESDDSEMGRLqallearglpphLFGPLG 420
Cdd:PHA03307  442 GSPPPPPGRV------------RYGGLG 457
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
1590-1990 1.76e-128

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: 407.34  E-value: 1.76e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1590 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqeg 1666
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1667 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1746
Cdd:cd00078    67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1747 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1826
Cdd:cd00078   139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1827 FWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1906
Cdd:cd00078   197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1907 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGq 1986
Cdd:cd00078   275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                  ....
gi 929653749 1987 QSFH 1990
Cdd:cd00078   349 AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1608-1986 3.30e-126

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: 399.69  E-value: 3.30e-126
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   1608 DLGSSRamLEIQYENEVG-TGLGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqegtkYIQNLQGLFALPFGRTAK 1686
Cdd:smart00119    1 DLKKRV--LEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFR-----------------YSPNDYLLYPNPRSGFAN 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   1687 PAHIakvkMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRqeTSLTSHDLFDIDPVVARSVYHLedivrqkkRLEQDK 1766
Cdd:smart00119   62 EEHL----SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL--------LLNNDT 127
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   1767 SqtkeslqYALETltmngcsVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFE 1846
Cdd:smart00119  128 S-------EELDL-------TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFS 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   1847 SVFPLSHLQYFYPEELDQLLCGSKadTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPV 1926
Cdd:smart00119  194 EVIPENLLKLFDPEELELLICGSP--EIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV 271
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   1927 GGFRSLNPPLTIVRKTFEstenpDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGQ 1986
Cdd:smart00119  272 GGFAALSPKFTIRKAGSD-----DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGK 326
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1637-1992 1.24e-103

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 334.58  E-value: 1.24e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  1637 LVSQELQRADLGLWRGEevtlsnpkgsQEGTKYIqnlqglfalPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDL 1716
Cdd:pfam00632    2 LLSKELFDPNYGLFEYE----------TEDDRTY---------WFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDL 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  1717 PLGLPFYKWMLRQEtsLTSHDLFDIDPVVARSVYHLedivrqkkrleqdksqtkeslqyaletLTMNGCSVEDLGLDFTL 1796
Cdd:pfam00632   63 PFPPFFYKKLLGEP--LTLEDLESIDPELYKSLKSL---------------------------LNMDNDDDEDLGLTFTI 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  1797 PGF---PNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDT 1873
Cdd:pfam00632  114 PVFgesKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PE 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  1874 WDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLnPPLTIVRKTFesteNPDDFL 1953
Cdd:pfam00632  192 IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGG----DDDDRL 266
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 929653749  1954 PSVMTCVNYLKLPDYSSIEIMREKLLIAAREGqQSFHLS 1992
Cdd:pfam00632  267 PTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1500-1991 3.52e-80

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 285.12  E-value: 3.52e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1500 TSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGktcPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPeinqSDSQD 1579
Cdd:COG5021   410 SSSTYEDLRREQLGRESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSR----LGSFI 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1580 SRVAPRLDRKKRTVNREELLKQAESVM-----QDLGSSRAM----LEIQYENEVGTGLGPTLEFYALVSQELQRADLGLW 1650
Cdd:COG5021   483 SLNKLDIRRIKEDKRRKLFYSLKQKAKifdpyLHIKVRRDRvfedSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTRE 562
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1651 RgeEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTA--KPAHIAKvkmkFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLR 1728
Cdd:COG5021   563 W--LFLLSKEMFNPDYGLFEYITEDLYTLPINPLSsiNPEHLSY----FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG 636
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1729 QetSLTSHDLFDIDPVVARSVyhledivrqKKRLEQDKsqTKESLqyaleTLTMngcSVEDLGLDFTLPgfpnIELKKGG 1808
Cdd:COG5021   637 K--PVSLVDLESLDPELYRSL---------VWLLNNDI--DETIL-----DLTF---TVEDDSFGESRT----VELIPNG 691
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1809 KDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkADTWDAKTLMECCRpDHG 1888
Cdd:COG5021   692 RNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGI-PEDIDIDDWKSNTA-YHG 769
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749 1889 YTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDY 1968
Cdd:COG5021   770 YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEY 849
                         490       500
                  ....*....|....*....|...
gi 929653749 1969 SSIEIMREKLLIAAREGQQSFHL 1991
Cdd:COG5021   850 SSKEKLRSKLLTAINEGAGFGLL 872
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
762-798 9.51e-09

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 53.45  E-value: 9.51e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 929653749   762 IWQWRDDRGLWHPYNRIDSRIIE-----------------------------QINEDTGTARAIQR 798
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEeayqkgkpsvdlsittagfpytidfksmtQTNKDTGTTRPVRR 66
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
441-666 2.41e-05

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 49.12  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  441 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 519
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  520 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 592
Cdd:COG5064   154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929653749  593 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 666
Cdd:COG5064   233 NPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTPALRSVG 310
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
762-802 2.87e-05

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 43.87  E-value: 2.87e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 929653749    762 IWQWRDDRGLWHPYNRIDSRIIE---------------------------QINEDTGTARAIQRKPNP 802
Cdd:smart00678    2 VWEYEGRNGKWWPYDPRVSEDIEeayaagkklcelsicgfpytidfnamtQYNQATGTTRKVRRVTYS 69
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2-420 7.40e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749    2 SNRPNNNPGGSLRrSQRNTAGAQPQDDSIGGRSCSSSSAVIVPQPEDPDRANtSERQKTGQVPKKDNSRGVKRSASPDYN 81
Cdd:PHA03307   81 ANESRSTPTWSLS-TLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPA-PDLSEMLRPVGSPGPPPAASPPAAGAS 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749   82 RTNSPSSAKKPK----ALQHTESPSETNKPHSKSKKRHLDQEQQLKSAQSPSTSKAHTRKSGATGGSRSQKRKRTESSCV 157
Cdd:PHA03307  159 PAAVASDAASSRqaalPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSD 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  158 KSGSGSESTGAEERSAKPTKLASKSATSakagcSTITDSSSAASTSSSSSAVASASSTVPPGARVKQGKDqNKARRSRSA 237
Cdd:PHA03307  239 SSSSESSGCGWGPENECPLPRPAPITLP-----TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSP-GSGPAPSSP 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  238 SSPSPRRSSREKEQSKTGGSSKFDWAARFSPKvslpktklSLPGSSKSETSKPGPSGlqaklaslRKSTKKR---SESPP 314
Cdd:PHA03307  313 RASSSSSSSRESSSSSTSSSSESSRGAAVSPG--------PSPSRSPSPSRPPPPAD--------PSSPRKRprpSRAPS 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929653749  315 AELPSLRRSTRQKTTGSCASTSRRGSGLGKRGAAEARRQEKMADpesnqeaVNSSAARTDEAPqgaagavgMTTSGES-- 392
Cdd:PHA03307  377 SPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAG-------AASGAFYARYPL--------LTPSGEPwp 441
                         410       420
                  ....*....|....*....|....*...
gi 929653749  393 ESDDSEMGRLqallearglpphLFGPLG 420
Cdd:PHA03307  442 GSPPPPPGRV------------RYGGLG 457
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH