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Conserved domains on  [gi|578824428|ref|XP_006719745|]
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ubiquitin-protein ligase E3B isoform X4 [Homo sapiens]

Protein Classification

HECT domain-containing protein( domain architecture ID 10050984)

HECT domain-containing protein may function as an E3 ubiquitin-protein ligase that catalyzes the attachment of ubiquitin chains to target proteins

CATH:  3.30.2410.10
EC:  2.3.2.26
Gene Ontology:  GO:0004842
PubMed:  22389392|29016349
SCOP:  4002196

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
682-1004 5.98e-130

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: 398.09  E-value: 5.98e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  682 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 760
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  761 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 840
Cdd:cd00078    77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  841 TDLGLTLSYDEDV-MGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 919
Cdd:cd00078   152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  920 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 999
Cdd:cd00078   232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309

                  ....*
gi 578824428 1000 EVSDD 1004
Cdd:cd00078   310 GSPDD 314
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
682-1004 5.98e-130

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: 398.09  E-value: 5.98e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  682 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 760
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  761 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 840
Cdd:cd00078    77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  841 TDLGLTLSYDEDV-MGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 919
Cdd:cd00078   152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  920 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 999
Cdd:cd00078   232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309

                  ....*
gi 578824428 1000 EVSDD 1004
Cdd:cd00078   310 GSPDD 314
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
737-1005 5.67e-92

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 295.67  E-value: 5.67e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428   737 EIIKRVFDPALNLFKTTSGDERLY-PSPTSYI--HENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfy 813
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYwFNPSSSEspDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428   814 SSVDELPSLDSEFYKNLTSIKRYDGDIT-DLGLTLSYDedVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQI 892
Cdd:pfam00632   77 LTLEDLESIDPELYKSLKSLLNMDNDDDeDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428   893 KNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDNaEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMF 972
Cdd:pfam00632  155 EPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGYTKNSPTIQWFWEIL-EEFSPEQRRLF 232
                          250       260       270
                   ....*....|....*....|....*....|...
gi 578824428   973 LKFVTSCSRPPLLGFAYLkPPFSIRCVEVSDDQ 1005
Cdd:pfam00632  233 LKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDD 264
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
707-1004 1.91e-87

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: 284.51  E-value: 1.91e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428    707 KGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDERLYPSPTSYI-HENYLQLFEFVGKMLGKA 785
Cdd:smart00119    4 KRVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKA 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428    786 VYEGIVVDVPFASFFLSQLLGHhhSVfysSVDELPSLDSEFYKNLTSIKRYDGDITDLGLTLSYDED-VMGQLVCHELIP 864
Cdd:smart00119   79 LYDNRLLDLFFARPFYKKLLGK--PV---TLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLTsEFGQVKVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428    865 GGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDnAEIDLEDLKKHTVYYG 944
Cdd:smart00119  154 GGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGS-PEIDVDDLKSNTEYKG 232
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428    945 GFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCVEVSDD 1004
Cdd:smart00119  233 GYSANSQTIKWFWEVVES-FTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDE 291
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
682-1004 9.88e-76

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 267.79  E-value: 9.88e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  682 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 760
Cdd:COG5021   516 HIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLP 590
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  761 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfySSVDELPSLDSEFYKNLTSIKRYDGDI 840
Cdd:COG5021   591 INPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKP-----VSLVDLESLDPELYRSLVWLLNNDIDE 665
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  841 TDLGLTLSYDEDVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPEL 920
Cdd:COG5021   666 TILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESEL 745
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  921 QRLISGDNAEIDLEDLKKHTVYYgGFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFAYLKPP-----FS 995
Cdd:COG5021   746 ELLIGGIPEDIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISE-FDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkFT 823

                  ....*....
gi 578824428  996 IRCVEVSDD 1004
Cdd:COG5021   824 IEKGGTDDD 832
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
682-1004 5.98e-130

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: 398.09  E-value: 5.98e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  682 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 760
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  761 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 840
Cdd:cd00078    77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  841 TDLGLTLSYDEDV-MGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 919
Cdd:cd00078   152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  920 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 999
Cdd:cd00078   232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309

                  ....*
gi 578824428 1000 EVSDD 1004
Cdd:cd00078   310 GSPDD 314
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
737-1005 5.67e-92

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 295.67  E-value: 5.67e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428   737 EIIKRVFDPALNLFKTTSGDERLY-PSPTSYI--HENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfy 813
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYwFNPSSSEspDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428   814 SSVDELPSLDSEFYKNLTSIKRYDGDIT-DLGLTLSYDedVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQI 892
Cdd:pfam00632   77 LTLEDLESIDPELYKSLKSLLNMDNDDDeDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428   893 KNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDNaEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMF 972
Cdd:pfam00632  155 EPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGYTKNSPTIQWFWEIL-EEFSPEQRRLF 232
                          250       260       270
                   ....*....|....*....|....*....|...
gi 578824428   973 LKFVTSCSRPPLLGFAYLkPPFSIRCVEVSDDQ 1005
Cdd:pfam00632  233 LKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDD 264
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
707-1004 1.91e-87

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: 284.51  E-value: 1.91e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428    707 KGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDERLYPSPTSYI-HENYLQLFEFVGKMLGKA 785
Cdd:smart00119    4 KRVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKA 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428    786 VYEGIVVDVPFASFFLSQLLGHhhSVfysSVDELPSLDSEFYKNLTSIKRYDGDITDLGLTLSYDED-VMGQLVCHELIP 864
Cdd:smart00119   79 LYDNRLLDLFFARPFYKKLLGK--PV---TLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLTsEFGQVKVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428    865 GGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDnAEIDLEDLKKHTVYYG 944
Cdd:smart00119  154 GGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGS-PEIDVDDLKSNTEYKG 232
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428    945 GFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCVEVSDD 1004
Cdd:smart00119  233 GYSANSQTIKWFWEVVES-FTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDE 291
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
682-1004 9.88e-76

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 267.79  E-value: 9.88e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  682 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 760
Cdd:COG5021   516 HIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLP 590
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  761 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfySSVDELPSLDSEFYKNLTSIKRYDGDI 840
Cdd:COG5021   591 INPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKP-----VSLVDLESLDPELYRSLVWLLNNDIDE 665
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  841 TDLGLTLSYDEDVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPEL 920
Cdd:COG5021   666 TILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESEL 745
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824428  921 QRLISGDNAEIDLEDLKKHTVYYgGFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFAYLKPP-----FS 995
Cdd:COG5021   746 ELLIGGIPEDIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISE-FDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkFT 823

                  ....*....
gi 578824428  996 IRCVEVSDD 1004
Cdd:COG5021   824 IEKGGTDDD 832
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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