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Conserved domains on  [gi|358386240|gb|EHK23836|]
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hypothetical protein TRIVIDRAFT_83144 [Trichoderma virens Gv29-8]

Protein Classification

HECT-type E3 ubiquitin-protein ligase( domain architecture ID 10050984)

HECT-type E3 ubiquitin-protein ligase catalyzes the attachment of ubiquitin chains to target proteins

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 ...
751-1143 1.18e-111

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: 351.87  E-value: 1.18e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  751 KIRRGQLFEDAFEQFYQLGEG-LKDPIQITFVDqfdtpEAGIDGGGVTKEFLTSVTSEAFgNGAGGLGMFTSSGKELLYP 829
Cdd:cd00078     4 TVRRDRILEDALRQLSKVSSSdLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELF-NPSYGLFRYTPDDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  830 NPTAMDVLREslrkqgltesdpewreamsglLRRYEFLGRIVGKCMYEGILVDLAFAGFFLLKWPspnrkeenNYKGSVN 909
Cdd:cd00078    78 NPSSFADEDH---------------------LKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL--------GKPLSLE 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  910 DLQDMDEELYRGLLNLKNYSGDVSALGLDFTITDQISAPGepveIVTRKLVPGGDEMPVTNDNRLLYISYAARHRLVVQP 989
Cdd:cd00078   129 DLEELDPELYKSLKELLDNDGDEDDLELTFTIELDSSFGG----AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGI 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  990 APQTTSFLRGLREIIRPSWLSMFNQSELQRLVGGDSmAIDVENLRQNTVYSGLYAigddgEEHPTIKMFWNVMNSLTDAQ 1069
Cdd:cd00078   205 EEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSE-DIDLEDLKKNTEYKGGYS-----SDSPTIQWFWEVLESFTNEE 278
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358386240 1070 RRDVLKYVTSTPRAPLLGFAQLNPKFAIRDGSSDQERLPSASTCVNLLKLPIYKSESTLRKKLLYAITAGAGFD 1143
Cdd:cd00078   279 RKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
50-79 1.01e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 37.52  E-value: 1.01e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 358386240   50 EKRQaERRRLKAASQIQRTWRGYRSRSTLR 79
Cdd:cd23767     1 EEEE-LQRMNRAATLIQALWRGYKVRKELK 29
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
751-1143 1.18e-111

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: 351.87  E-value: 1.18e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  751 KIRRGQLFEDAFEQFYQLGEG-LKDPIQITFVDqfdtpEAGIDGGGVTKEFLTSVTSEAFgNGAGGLGMFTSSGKELLYP 829
Cdd:cd00078     4 TVRRDRILEDALRQLSKVSSSdLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELF-NPSYGLFRYTPDDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  830 NPTAMDVLREslrkqgltesdpewreamsglLRRYEFLGRIVGKCMYEGILVDLAFAGFFLLKWPspnrkeenNYKGSVN 909
Cdd:cd00078    78 NPSSFADEDH---------------------LKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL--------GKPLSLE 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  910 DLQDMDEELYRGLLNLKNYSGDVSALGLDFTITDQISAPGepveIVTRKLVPGGDEMPVTNDNRLLYISYAARHRLVVQP 989
Cdd:cd00078   129 DLEELDPELYKSLKELLDNDGDEDDLELTFTIELDSSFGG----AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGI 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  990 APQTTSFLRGLREIIRPSWLSMFNQSELQRLVGGDSmAIDVENLRQNTVYSGLYAigddgEEHPTIKMFWNVMNSLTDAQ 1069
Cdd:cd00078   205 EEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSE-DIDLEDLKKNTEYKGGYS-----SDSPTIQWFWEVLESFTNEE 278
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358386240 1070 RRDVLKYVTSTPRAPLLGFAQLNPKFAIRDGSSDQERLPSASTCVNLLKLPIYKSESTLRKKLLYAITAGAGFD 1143
Cdd:cd00078   279 RKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
773-1142 2.30e-94

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: 304.54  E-value: 2.30e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240    773 KDPIQITFVDqfdtpEAGIDGGGVTKEFLTSVTSEAFGngaGGLGMFT-SSGKELLYPNPTAMDVLRESLRKqgltesdp 851
Cdd:smart00119    4 KRVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFN---PDYGLFRySPNDYLLYPNPRSGFANEEHLSY-------- 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240    852 ewreamsgllrrYEFLGRIVGKCMYEGILVDLAFAGFFLLKWpspnrkeeNNYKGSVNDLQDMDEELYRGLLNLKNYSGD 931
Cdd:smart00119   68 ------------FRFIGRVLGKALYDNRLLDLFFARPFYKKL--------LGKPVTLHDLESLDPELYKSLKWLLLNNDT 127
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240    932 VSALGLDFTITDQISAPgepvEIVTRKLVPGGDEMPVTNDNRLLYISYAARHRLVVQPAPQTTSFLRGLREIIRPSWLSM 1011
Cdd:smart00119  128 SEELDLTFSIVLTSEFG----QVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKL 203
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240   1012 FNQSELQRLVGGDSmAIDVENLRQNTVYSGLYAigddgEEHPTIKMFWNVMNSLTDAQRRDVLKYVTSTPRAPLLGFAQL 1091
Cdd:smart00119  204 FDPEELELLICGSP-EIDVDDLKSNTEYKGGYS-----ANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL 277
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|.
gi 358386240   1092 NPKFAIRDGSSDQERLPSASTCVNLLKLPIYKSESTLRKKLLYAITAGAGF 1142
Cdd:smart00119  278 SPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
816-1145 1.78e-93

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 301.07  E-value: 1.78e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240   816 LGMF--TSSGKELLYPNPTAMDVLRESLRKQgltesdpewreamsgllrrYEFLGRIVGKCMYEGILVDLAFAGFFLLKW 893
Cdd:pfam00632   12 YGLFeyETEDDRTYWFNPSSSESPDLELLDY-------------------FKFLGKLLGKAIYNGILLDLPFPPFFYKKL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240   894 pspnrkeeNNYKGSVNDLQDMDEELYRGLLNLKNYSGDVSA-LGLDFTITDQisapGEPVEIvtrKLVPGGDEMPVTNDN 972
Cdd:pfam00632   73 --------LGEPLTLEDLESIDPELYKSLKSLLNMDNDDDEdLGLTFTIPVF----GESKTI---ELIPNGRNIPVTNEN 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240   973 RLLYISYAARHRLVVQPAPQTTSFLRGLREIIRPSWLSMFNQSELQRLVGGDSmAIDVENLRQNTVYSGLYaigddGEEH 1052
Cdd:pfam00632  138 KEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGY-----TKNS 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  1053 PTIKMFWNVMNSLTDAQRRDVLKYVTSTPRAPLLGFAQLnPKFAI-RDGSSDQERLPSASTCVNLLKLPIYKSESTLRKK 1131
Cdd:pfam00632  212 PTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIvRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEK 290
                          330
                   ....*....|....
gi 358386240  1132 LLYAITAGAGFDLS 1145
Cdd:pfam00632  291 LLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
749-1145 2.61e-87

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 302.07  E-value: 2.61e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  749 HAKIRRGQLFEDAFEQFY-QLGEGLKDPIQITFVDqfdtpEAGIDGGGVTKEFLTSVTSEAFgNGAGGLGMFTSSGKELL 827
Cdd:COG5021   516 HIKVRRDRVFEDSYREIMdESGDDLKKTLEIEFVG-----EEGIDAGGLTREWLFLLSKEMF-NPDYGLFEYITEDLYTL 589
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  828 YPNPTAmdvlreslrkqgltESDPEwreamsgLLRRYEFLGRIVGKCMYEGILVDLAFAGFFLLKWpspnrkeeNNYKGS 907
Cdd:COG5021   590 PINPLS--------------SINPE-------HLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKL--------LGKPVS 640
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  908 VNDLQDMDEELYRGLLNLKNYSGDVSALGLDFTITDqiSAPGEPVEIvtrKLVPGGDEMPVTNDNRLLYISYAARHRLVV 987
Cdd:COG5021   641 LVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED--DSFGESRTV---ELIPNGRNISVTNENKKEYVKKVVDYKLNK 715
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  988 QPAPQTTSFLRGLREIIRPSWLSMFNQSELQRLVGGDSMAIDVENLRQNTVYSGlYAigddgEEHPTIKMFWNVMNSLTD 1067
Cdd:COG5021   716 RVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAYHG-YT-----EDSPIIVWFWEIISEFDF 789
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240 1068 AQRRDVLKYVTSTPRAPLLGFAQLNP-----KFAIRDGSSDQERLPSASTCVNLLKLPIYKSESTLRKKLLYAITAGAGF 1142
Cdd:COG5021   790 EERAKLLQFVTGTSRIPINGFKDLQGsdgvrKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869

                  ...
gi 358386240 1143 DLS 1145
Cdd:COG5021   870 GLL 872
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
50-79 1.01e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 37.52  E-value: 1.01e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 358386240   50 EKRQaERRRLKAASQIQRTWRGYRSRSTLR 79
Cdd:cd23767     1 EEEE-LQRMNRAATLIQALWRGYKVRKELK 29
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
751-1143 1.18e-111

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: 351.87  E-value: 1.18e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  751 KIRRGQLFEDAFEQFYQLGEG-LKDPIQITFVDqfdtpEAGIDGGGVTKEFLTSVTSEAFgNGAGGLGMFTSSGKELLYP 829
Cdd:cd00078     4 TVRRDRILEDALRQLSKVSSSdLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELF-NPSYGLFRYTPDDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  830 NPTAMDVLREslrkqgltesdpewreamsglLRRYEFLGRIVGKCMYEGILVDLAFAGFFLLKWPspnrkeenNYKGSVN 909
Cdd:cd00078    78 NPSSFADEDH---------------------LKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLL--------GKPLSLE 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  910 DLQDMDEELYRGLLNLKNYSGDVSALGLDFTITDQISAPGepveIVTRKLVPGGDEMPVTNDNRLLYISYAARHRLVVQP 989
Cdd:cd00078   129 DLEELDPELYKSLKELLDNDGDEDDLELTFTIELDSSFGG----AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGI 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  990 APQTTSFLRGLREIIRPSWLSMFNQSELQRLVGGDSmAIDVENLRQNTVYSGLYAigddgEEHPTIKMFWNVMNSLTDAQ 1069
Cdd:cd00078   205 EEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSE-DIDLEDLKKNTEYKGGYS-----SDSPTIQWFWEVLESFTNEE 278
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358386240 1070 RRDVLKYVTSTPRAPLLGFAQLNPKFAIRDGSSDQERLPSASTCVNLLKLPIYKSESTLRKKLLYAITAGAGFD 1143
Cdd:cd00078   279 RKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
773-1142 2.30e-94

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: 304.54  E-value: 2.30e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240    773 KDPIQITFVDqfdtpEAGIDGGGVTKEFLTSVTSEAFGngaGGLGMFT-SSGKELLYPNPTAMDVLRESLRKqgltesdp 851
Cdd:smart00119    4 KRVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFN---PDYGLFRySPNDYLLYPNPRSGFANEEHLSY-------- 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240    852 ewreamsgllrrYEFLGRIVGKCMYEGILVDLAFAGFFLLKWpspnrkeeNNYKGSVNDLQDMDEELYRGLLNLKNYSGD 931
Cdd:smart00119   68 ------------FRFIGRVLGKALYDNRLLDLFFARPFYKKL--------LGKPVTLHDLESLDPELYKSLKWLLLNNDT 127
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240    932 VSALGLDFTITDQISAPgepvEIVTRKLVPGGDEMPVTNDNRLLYISYAARHRLVVQPAPQTTSFLRGLREIIRPSWLSM 1011
Cdd:smart00119  128 SEELDLTFSIVLTSEFG----QVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKL 203
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240   1012 FNQSELQRLVGGDSmAIDVENLRQNTVYSGLYAigddgEEHPTIKMFWNVMNSLTDAQRRDVLKYVTSTPRAPLLGFAQL 1091
Cdd:smart00119  204 FDPEELELLICGSP-EIDVDDLKSNTEYKGGYS-----ANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAAL 277
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|.
gi 358386240   1092 NPKFAIRDGSSDQERLPSASTCVNLLKLPIYKSESTLRKKLLYAITAGAGF 1142
Cdd:smart00119  278 SPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
816-1145 1.78e-93

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 301.07  E-value: 1.78e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240   816 LGMF--TSSGKELLYPNPTAMDVLRESLRKQgltesdpewreamsgllrrYEFLGRIVGKCMYEGILVDLAFAGFFLLKW 893
Cdd:pfam00632   12 YGLFeyETEDDRTYWFNPSSSESPDLELLDY-------------------FKFLGKLLGKAIYNGILLDLPFPPFFYKKL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240   894 pspnrkeeNNYKGSVNDLQDMDEELYRGLLNLKNYSGDVSA-LGLDFTITDQisapGEPVEIvtrKLVPGGDEMPVTNDN 972
Cdd:pfam00632   73 --------LGEPLTLEDLESIDPELYKSLKSLLNMDNDDDEdLGLTFTIPVF----GESKTI---ELIPNGRNIPVTNEN 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240   973 RLLYISYAARHRLVVQPAPQTTSFLRGLREIIRPSWLSMFNQSELQRLVGGDSmAIDVENLRQNTVYSGLYaigddGEEH 1052
Cdd:pfam00632  138 KEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGY-----TKNS 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  1053 PTIKMFWNVMNSLTDAQRRDVLKYVTSTPRAPLLGFAQLnPKFAI-RDGSSDQERLPSASTCVNLLKLPIYKSESTLRKK 1131
Cdd:pfam00632  212 PTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIvRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEK 290
                          330
                   ....*....|....
gi 358386240  1132 LLYAITAGAGFDLS 1145
Cdd:pfam00632  291 LLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
749-1145 2.61e-87

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 302.07  E-value: 2.61e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  749 HAKIRRGQLFEDAFEQFY-QLGEGLKDPIQITFVDqfdtpEAGIDGGGVTKEFLTSVTSEAFgNGAGGLGMFTSSGKELL 827
Cdd:COG5021   516 HIKVRRDRVFEDSYREIMdESGDDLKKTLEIEFVG-----EEGIDAGGLTREWLFLLSKEMF-NPDYGLFEYITEDLYTL 589
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  828 YPNPTAmdvlreslrkqgltESDPEwreamsgLLRRYEFLGRIVGKCMYEGILVDLAFAGFFLLKWpspnrkeeNNYKGS 907
Cdd:COG5021   590 PINPLS--------------SINPE-------HLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKL--------LGKPVS 640
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  908 VNDLQDMDEELYRGLLNLKNYSGDVSALGLDFTITDqiSAPGEPVEIvtrKLVPGGDEMPVTNDNRLLYISYAARHRLVV 987
Cdd:COG5021   641 LVDLESLDPELYRSLVWLLNNDIDETILDLTFTVED--DSFGESRTV---ELIPNGRNISVTNENKKEYVKKVVDYKLNK 715
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240  988 QPAPQTTSFLRGLREIIRPSWLSMFNQSELQRLVGGDSMAIDVENLRQNTVYSGlYAigddgEEHPTIKMFWNVMNSLTD 1067
Cdd:COG5021   716 RVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAYHG-YT-----EDSPIIVWFWEIISEFDF 789
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358386240 1068 AQRRDVLKYVTSTPRAPLLGFAQLNP-----KFAIRDGSSDQERLPSASTCVNLLKLPIYKSESTLRKKLLYAITAGAGF 1142
Cdd:COG5021   790 EERAKLLQFVTGTSRIPINGFKDLQGsdgvrKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869

                  ...
gi 358386240 1143 DLS 1145
Cdd:COG5021   870 GLL 872
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
50-79 1.01e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 37.52  E-value: 1.01e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 358386240   50 EKRQaERRRLKAASQIQRTWRGYRSRSTLR 79
Cdd:cd23767     1 EEEE-LQRMNRAATLIQALWRGYKVRKELK 29
 
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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