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Conserved domains on  [gi|60097906|ref|NP_080268|]
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E3 ISG15--protein ligase Herc6 [Mus musculus]

Protein Classification

E3 ubiquitin-protein ligase HERC family protein( domain architecture ID 18804227)

E3 ubiquitin-protein ligase HERC (HECT and RCC1 domain) family protein similar to human E3 ISG15--protein ligase HERC5, the major E3 ligase for ISG15 conjugation, that functions as part of the ISGylation machinery that recognizes target proteins in a broad and relatively non-specific manner

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 ...
 658-999 2.42e-120

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: 371.90  E-value: 2.42e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  658 LILKVRRSHLVEDTLRQLRQVEDFDLRKQLSVGFINEIRPEAGGVSSEFFHCIFEEMTDPKYEMFIYPEKGSS-MWFPVN 736
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLYPNPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  737 PKF---EKSSYFLFGILCGLSLHNLKVINLPFPLALYKKLLNQKPSLEDLKELSLPLGRNLQEVLNCEaGDIEELHMYFS 813
Cdd:cd00078   81 SFAdedHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDND-GDEDDLELTFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  814 I-----YWDQKDVDLIPDGISVPVNETNKRDYVSKYVDYIFNISIKTIYEEFHRGFYKVCNWDIIRQFQPEELMTAIIGN 888
Cdd:cd00078  160 IeldssFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  889 ATCDWKQFENNSKYKDGYDKSHPTILLFWKAFHDLTLDEKKKFLLFLTGCDRLHVKGLQNEGIVFRCSETFSEEDN-PRS 967
Cdd:cd00078  240 EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSPDDRlPTA 319

                        330       340       350
                 ....*....|....*....|....*....|..
gi 60097906  968 LTCHRMLDLPKYSSMRRMKEALQVAINNSTGF 999
Cdd:cd00078  320 HTCFNLLKLPPYSSKEILREKLLYAINEGAGF 351
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 26-314 1.60e-64

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


:

Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 221.39  E-value: 1.60e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906   26 QAASGEHHSLLLFSNHRVYSCGDNSWGQLGqrRDQSTERPEPIQALNDLHVDLVSCGKEHSVAVCHKGKVFAWGAGSEGQ 105
Cdd:COG5184    2 QVAAGGSHSCALKSDGTVWCWGDNSYGQLG--DGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  106 LGIGEfKEISFMPTKIKALAGIKiiQVSCGHYHSLALSEDGHVFSWGRNSEGQLGLGKNSrSQAIPQKV-KSLEGIplAQ 184
Cdd:COG5184   80 LGDGT-TTDRTTPVKVPGLTGVV--AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTT-NRLTPVQVdAGLSGV--VA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  185 VAAGGTHSFALSLTGTSFGWGSNRSGQLalsGNKVKEQIYKPHSIGALKNlsVIYISCGYEHTAVLTEEGQVFTFGGNSS 264
Cdd:COG5184  154 IAAGGYHTCALKSDGTVWCWGANSYGQL---GDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSS 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 60097906  265 GQLQPSPRSGQRGPQLIEGIGGrVSQIECASYHTIAyVYTTGQVVSLGRG 314
Cdd:COG5184  229 GQLGDGTTTDRATPVQVAGLTG-VVAIAAGGSHTCA-LKSDGTVWCWGDN 276
PTZ00212 super family cl28960
T-complex protein 1 subunit beta; Provisional
 570-652 6.10e-03

T-complex protein 1 subunit beta; Provisional


The actual alignment was detected with superfamily member PTZ00212:

Pssm-ID: 185514  Cd Length: 533  Bit Score: 40.40  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906   570 HKANCqlpesaFIINELsgIFNFD----AEAGRMFIRHNDLDCTESSDMVVFSDFLFVFDLPSKIKLMKCdsfvKLMSEV 645
Cdd:PTZ00212  287 HGCNV------FINRQL--IYNYPeqlfAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHC----DLIEEI 354


                  ....*..
gi 60097906   646 MAFPEKM 652
Cdd:PTZ00212  355 MIGEDKL 361
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 658-999 2.42e-120

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: 371.90  E-value: 2.42e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  658 LILKVRRSHLVEDTLRQLRQVEDFDLRKQLSVGFINEIRPEAGGVSSEFFHCIFEEMTDPKYEMFIYPEKGSS-MWFPVN 736
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLYPNPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  737 PKF---EKSSYFLFGILCGLSLHNLKVINLPFPLALYKKLLNQKPSLEDLKELSLPLGRNLQEVLNCEaGDIEELHMYFS 813
Cdd:cd00078   81 SFAdedHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDND-GDEDDLELTFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  814 I-----YWDQKDVDLIPDGISVPVNETNKRDYVSKYVDYIFNISIKTIYEEFHRGFYKVCNWDIIRQFQPEELMTAIIGN 888
Cdd:cd00078  160 IeldssFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  889 ATCDWKQFENNSKYKDGYDKSHPTILLFWKAFHDLTLDEKKKFLLFLTGCDRLHVKGLQNEGIVFRCSETFSEEDN-PRS 967
Cdd:cd00078  240 EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSPDDRlPTA 319

                        330       340       350
                 ....*....|....*....|....*....|..
gi 60097906  968 LTCHRMLDLPKYSSMRRMKEALQVAINNSTGF 999
Cdd:cd00078  320 HTCFNLLKLPPYSSKEILREKLLYAINEGAGF 351
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 710-999 1.29e-80

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 264.47  E-value: 1.29e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906    710 IFEEMTDPKYEMFIYP-EKGSSMWF----PVNPKFEKSSYF-LFGILCGLSLHNLKVINLPFPLALYKKLLNQKPSLEDL 783
Cdd:pfam00632    3 LSKELFDPNYGLFEYEtEDDRTYWFnpssSESPDLELLDYFkFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906    784 KELSLPLGRNLQEVLNCEAGDIEELHMYFSI--YWDQKDVDLIPDGISVPVNETNKRDYVSKYVDYIFNISIKTIYEEFH 861
Cdd:pfam00632   83 ESIDPELYKSLKSLLNMDNDDDEDLGLTFTIpvFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906    862 RGFYKVCNWDIIRQFQPEELMTAIIGNATCDWKQFENNSKYKDGYDKSHPTILLFWKAFHDLTLDEKKKFLLFLTGCDRL 941
Cdd:pfam00632  163 KGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRL 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 60097906    942 HVKGLQNEGIVFRCSETFSEEDN-PRSLTCHRMLDLPKYSSMRRMKEALQVAINNSTGF 999
Cdd:pfam00632  243 PVGGFKSLPKFTIVRKGGDDDDRlPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGF 301
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 682-999 7.95e-77

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: 254.85  E-value: 7.95e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906     682 DLRKQ-LSVGFINEIRPEAGGVSSEFFHCIFEEMTDPKYEMFIYPEKGSSMWFPVNP---KFEKSSYFLF-GILCGLSLH 756
Cdd:smart00119    1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSgfaNEEHLSYFRFiGRVLGKALY 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906     757 NLKVINLPFPLALYKKLLNQKPSLEDLKELSLPLGRNLQEvLNCEAGDIEELHMYFSI-----YWDQKDVDLIPDGISVP 831
Cdd:smart00119   81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKW-LLLNNDTSEELDLTFSIvltseFGQVKVVELKPGGSNIP 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906     832 VNETNKRDYVSKYVDYIFNISIKTIYEEFHRGFYKVCNWDIIRQFQPEELMTAIIGNATCDWKQFENNSKYKDGYDKSHP 911
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906     912 TILLFWKAFHDLTLDEKKKFLLFLTGCDRLHVKGLQNEGIVFRCSETFSEEDN-PRSLTCHRMLDLPKYSSMRRMKEALQ 990
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDERlPTAHTCFNRLKLPPYSSKEILREKLL 319


                    ....*....
gi 60097906     991 VAINNSTGF 999
Cdd:smart00119  320 LAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
618-999 3.76e-65

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 236.59  E-value: 3.76e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  618 SDFLFVFDLPSKIKLMKCDS-----------FVKLMSE-------VMAFPEKMSSPPYLILKVRRSHLVEDTLRQLRQVE 679
Cdd:COG5021  457 NLYRFYFVEHRKKTLTKNDSrlgsfislnklDIRRIKEdkrrklfYSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDES 536

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  680 DFDLRKQLSVGFINEIRPEAGGVSSEFFHCIFEEMTDPKYEMFIYPEKGSSMWFP-----VNPKfEKSSYFLFGILCGLS 754
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPInplssINPE-HLSYFKFLGRVIGKA 615

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  755 LHNLKVINLPFPLALYKKLLNQKPSLEDLKELSLPLGRNLQEVLNCE-AGDIEELHMYF--SIYWDQKDVDLIPDGISVP 831
Cdd:COG5021  616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDiDETILDLTFTVedDSFGESRTVELIPNGRNIS 695

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  832 VNETNKRDYVSKYVDYIFNISIKTIYEEFHRGFYKVCNWDIIRQFQPEELMTAIIGNATC-DWKQFENNSKYkDGYDKSH 910
Cdd:COG5021  696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDiDIDDWKSNTAY-HGYTEDS 774

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  911 PTILLFWKAFHDLTLDEKKKFLLFLTGCDRLHV---KGLQ-NEGIVFRCSETFSEEDN--PRSLTCHRMLDLPKYSSMRR 984
Cdd:COG5021  775 PIIVWFWEIISEFDFEERAKLLQFVTGTSRIPIngfKDLQgSDGVRKFTIEKGGTDDDrlPSAHTCFNRLKLPEYSSKEK 854

                        410
                 ....*....|....*
gi 60097906  985 MKEALQVAINNSTGF 999
Cdd:COG5021  855 LRSKLLTAINEGAGF 869
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 26-314 1.60e-64

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 221.39  E-value: 1.60e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906   26 QAASGEHHSLLLFSNHRVYSCGDNSWGQLGqrRDQSTERPEPIQALNDLHVDLVSCGKEHSVAVCHKGKVFAWGAGSEGQ 105
Cdd:COG5184    2 QVAAGGSHSCALKSDGTVWCWGDNSYGQLG--DGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  106 LGIGEfKEISFMPTKIKALAGIKiiQVSCGHYHSLALSEDGHVFSWGRNSEGQLGLGKNSrSQAIPQKV-KSLEGIplAQ 184
Cdd:COG5184   80 LGDGT-TTDRTTPVKVPGLTGVV--AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTT-NRLTPVQVdAGLSGV--VA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  185 VAAGGTHSFALSLTGTSFGWGSNRSGQLalsGNKVKEQIYKPHSIGALKNlsVIYISCGYEHTAVLTEEGQVFTFGGNSS 264
Cdd:COG5184  154 IAAGGYHTCALKSDGTVWCWGANSYGQL---GDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSS 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 60097906  265 GQLQPSPRSGQRGPQLIEGIGGrVSQIECASYHTIAyVYTTGQVVSLGRG 314
Cdd:COG5184  229 GQLGDGTTTDRATPVQVAGLTG-VVAIAAGGSHTCA-LKSDGTVWCWGDN 276
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
145-195 3.20e-17

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 76.02  E-value: 3.20e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 60097906    145 DGHVFSWGRNSEGQLGLGkNSRSQAIPQKVKSLEGIPLAQVAAGGTHSFAL 195
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLG-TTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
 570-652 6.10e-03

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 40.40  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906   570 HKANCqlpesaFIINELsgIFNFD----AEAGRMFIRHNDLDCTESSDMVVFSDFLFVFDLPSKIKLMKCdsfvKLMSEV 645
Cdd:PTZ00212  287 HGCNV------FINRQL--IYNYPeqlfAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHC----DLIEEI 354


                  ....*..
gi 60097906   646 MAFPEKM 652
Cdd:PTZ00212  355 MIGEDKL 361
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
 570-652 7.96e-03

TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239452 [Multi-domain]  Cd Length: 517  Bit Score: 40.01  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  570 HKANCqlpesaFIINELsgIFNFD----AEAGRMFIRHNDLDCTESSDMVVFSDFLFVFDLPSKIKLMKCdsfvKLMSEV 645
Cdd:cd03336  275 HGINC------FINRQL--IYNYPeqlfADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELVKLGTC----KLIEEI 342


                 ....*..
gi 60097906  646 MAFPEKM 652
Cdd:cd03336  343 MIGEDKL 349
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 658-999 2.42e-120

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: 371.90  E-value: 2.42e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  658 LILKVRRSHLVEDTLRQLRQVEDFDLRKQLSVGFINEIRPEAGGVSSEFFHCIFEEMTDPKYEMFIYPEKGSS-MWFPVN 736
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLYPNPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  737 PKF---EKSSYFLFGILCGLSLHNLKVINLPFPLALYKKLLNQKPSLEDLKELSLPLGRNLQEVLNCEaGDIEELHMYFS 813
Cdd:cd00078   81 SFAdedHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDND-GDEDDLELTFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  814 I-----YWDQKDVDLIPDGISVPVNETNKRDYVSKYVDYIFNISIKTIYEEFHRGFYKVCNWDIIRQFQPEELMTAIIGN 888
Cdd:cd00078  160 IeldssFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  889 ATCDWKQFENNSKYKDGYDKSHPTILLFWKAFHDLTLDEKKKFLLFLTGCDRLHVKGLQNEGIVFRCSETFSEEDN-PRS 967
Cdd:cd00078  240 EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSPDDRlPTA 319

                        330       340       350
                 ....*....|....*....|....*....|..
gi 60097906  968 LTCHRMLDLPKYSSMRRMKEALQVAINNSTGF 999
Cdd:cd00078  320 HTCFNLLKLPPYSSKEILREKLLYAINEGAGF 351
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 710-999 1.29e-80

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 264.47  E-value: 1.29e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906    710 IFEEMTDPKYEMFIYP-EKGSSMWF----PVNPKFEKSSYF-LFGILCGLSLHNLKVINLPFPLALYKKLLNQKPSLEDL 783
Cdd:pfam00632    3 LSKELFDPNYGLFEYEtEDDRTYWFnpssSESPDLELLDYFkFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906    784 KELSLPLGRNLQEVLNCEAGDIEELHMYFSI--YWDQKDVDLIPDGISVPVNETNKRDYVSKYVDYIFNISIKTIYEEFH 861
Cdd:pfam00632   83 ESIDPELYKSLKSLLNMDNDDDEDLGLTFTIpvFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906    862 RGFYKVCNWDIIRQFQPEELMTAIIGNATCDWKQFENNSKYKDGYDKSHPTILLFWKAFHDLTLDEKKKFLLFLTGCDRL 941
Cdd:pfam00632  163 KGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRL 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 60097906    942 HVKGLQNEGIVFRCSETFSEEDN-PRSLTCHRMLDLPKYSSMRRMKEALQVAINNSTGF 999
Cdd:pfam00632  243 PVGGFKSLPKFTIVRKGGDDDDRlPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGF 301
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 682-999 7.95e-77

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: 254.85  E-value: 7.95e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906     682 DLRKQ-LSVGFINEIRPEAGGVSSEFFHCIFEEMTDPKYEMFIYPEKGSSMWFPVNP---KFEKSSYFLF-GILCGLSLH 756
Cdd:smart00119    1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSgfaNEEHLSYFRFiGRVLGKALY 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906     757 NLKVINLPFPLALYKKLLNQKPSLEDLKELSLPLGRNLQEvLNCEAGDIEELHMYFSI-----YWDQKDVDLIPDGISVP 831
Cdd:smart00119   81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKW-LLLNNDTSEELDLTFSIvltseFGQVKVVELKPGGSNIP 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906     832 VNETNKRDYVSKYVDYIFNISIKTIYEEFHRGFYKVCNWDIIRQFQPEELMTAIIGNATCDWKQFENNSKYKDGYDKSHP 911
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906     912 TILLFWKAFHDLTLDEKKKFLLFLTGCDRLHVKGLQNEGIVFRCSETFSEEDN-PRSLTCHRMLDLPKYSSMRRMKEALQ 990
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDERlPTAHTCFNRLKLPPYSSKEILREKLL 319


                    ....*....
gi 60097906     991 VAINNSTGF 999
Cdd:smart00119  320 LAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
618-999 3.76e-65

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 236.59  E-value: 3.76e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  618 SDFLFVFDLPSKIKLMKCDS-----------FVKLMSE-------VMAFPEKMSSPPYLILKVRRSHLVEDTLRQLRQVE 679
Cdd:COG5021  457 NLYRFYFVEHRKKTLTKNDSrlgsfislnklDIRRIKEdkrrklfYSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDES 536

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  680 DFDLRKQLSVGFINEIRPEAGGVSSEFFHCIFEEMTDPKYEMFIYPEKGSSMWFP-----VNPKfEKSSYFLFGILCGLS 754
Cdd:COG5021  537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPInplssINPE-HLSYFKFLGRVIGKA 615

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  755 LHNLKVINLPFPLALYKKLLNQKPSLEDLKELSLPLGRNLQEVLNCE-AGDIEELHMYF--SIYWDQKDVDLIPDGISVP 831
Cdd:COG5021  616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDiDETILDLTFTVedDSFGESRTVELIPNGRNIS 695

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  832 VNETNKRDYVSKYVDYIFNISIKTIYEEFHRGFYKVCNWDIIRQFQPEELMTAIIGNATC-DWKQFENNSKYkDGYDKSH 910
Cdd:COG5021  696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDiDIDDWKSNTAY-HGYTEDS 774

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  911 PTILLFWKAFHDLTLDEKKKFLLFLTGCDRLHV---KGLQ-NEGIVFRCSETFSEEDN--PRSLTCHRMLDLPKYSSMRR 984
Cdd:COG5021  775 PIIVWFWEIISEFDFEERAKLLQFVTGTSRIPIngfKDLQgSDGVRKFTIEKGGTDDDrlPSAHTCFNRLKLPEYSSKEK 854

                        410
                 ....*....|....*
gi 60097906  985 MKEALQVAINNSTGF 999
Cdd:COG5021  855 LRSKLLTAINEGAGF 869
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 26-314 1.60e-64

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 221.39  E-value: 1.60e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906   26 QAASGEHHSLLLFSNHRVYSCGDNSWGQLGqrRDQSTERPEPIQALNDLHVDLVSCGKEHSVAVCHKGKVFAWGAGSEGQ 105
Cdd:COG5184    2 QVAAGGSHSCALKSDGTVWCWGDNSYGQLG--DGTTTDRSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNNSYGQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  106 LGIGEfKEISFMPTKIKALAGIKiiQVSCGHYHSLALSEDGHVFSWGRNSEGQLGLGKNSrSQAIPQKV-KSLEGIplAQ 184
Cdd:COG5184   80 LGDGT-TTDRTTPVKVPGLTGVV--AVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTT-NRLTPVQVdAGLSGV--VA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  185 VAAGGTHSFALSLTGTSFGWGSNRSGQLalsGNKVKEQIYKPHSIGALKNlsVIYISCGYEHTAVLTEEGQVFTFGGNSS 264
Cdd:COG5184  154 IAAGGYHTCALKSDGTVWCWGANSYGQL---GDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSS 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 60097906  265 GQLQPSPRSGQRGPQLIEGIGGrVSQIECASYHTIAyVYTTGQVVSLGRG 314
Cdd:COG5184  229 GQLGDGTTTDRATPVQVAGLTG-VVAIAAGGSHTCA-LKSDGTVWCWGDN 276
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 6-314 4.90e-61

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 211.76  E-value: 4.90e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906    6 AAGSRKPRRLkAGTSGIEllQAASGEHHSLLLFSNHRVYSCGDNSWGQLGQrrDQSTERPEPIQALNDLHVDLVSCGKEH 85
Cdd:COG5184   35 TTDRSTPVRV-PGLSNVV--AVAAGGDHTCALKADGTVWCWGNNSYGQLGD--GTTTDRTTPVKVPGLTGVVAVAAGYYH 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906   86 SVAVCHKGKVFAWGAGSEGQLGIGEFKEiSFMPTKIkALAGIKIIQVSCGHYHSLALSEDGHVFSWGRNSEGQLGLGkNS 165
Cdd:COG5184  110 SCALKSDGTVWCWGDNSSGQLGDGTTTN-RLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDG-TT 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  166 RSQAIPQKVKSLEGIplAQVAAGGTHSFALSLTGTSFGWGSNRSGQLalsGNKVKEQIYKPHSIGALKNlsVIYISCGYE 245
Cdd:COG5184  187 TDRPTPVQVGGLSGV--VAVAAGGDHSCALKSDGTVWCWGSNSSGQL---GDGTTTDRATPVQVAGLTG--VVAIAAGGS 259

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60097906  246 HTAVLTEEGQVFTFGGNSSGQLQPSPRSGQRGPQLIEGIGGrVSQIECASYHTIAYVyTTGQVV--------SLGRG 314
Cdd:COG5184  260 HTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG-VVAVAAGSSHTCALL-TDGTVWcwgdnaygQLGDG 334
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 130-316 6.70e-37

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 142.42  E-value: 6.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  130 IQVSCGHYHSLALSEDGHVFSWGRNSEGQLGLGKNSRSqAIPQKVKSLEGIplAQVAAGGTHSFALSLTGTSFGWGSNRS 209
Cdd:COG5184    1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDR-STPVRVPGLSNV--VAVAAGGDHTCALKADGTVWCWGNNSY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  210 GQLalsGNKVKEQIYKPHSIGALKNlsVIYISCGYEHTAVLTEEGQVFTFGGNSSGQLQPSPRSGQRGPQLIEGIGGRVS 289
Cdd:COG5184   78 GQL---GDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQVDAGLSGVV 152

                        170       180
                 ....*....|....*....|....*..
gi 60097906  290 QIECASYHTIAyVYTTGQVVSLGRGPS 316
Cdd:COG5184  153 AIAAGGYHTCA-LKSDGTVWCWGANSY 178
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 28-172 8.02e-30

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 121.62  E-value: 8.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906   28 ASGEHHSLLLFSNHRVYSCGDNSWGQLGQrrDQSTERPEPIQALNDLHVDLVSCGKEHSVAVCHKGKVFAWGAGSEGQLG 107
Cdd:COG5184  205 AAGGDHSCALKSDGTVWCWGSNSSGQLGD--GTTTDRATPVQVAGLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLG 282

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60097906  108 IGEfKEISFMPTKIKALAGIkiIQVSCGHYHSLALSEDGHVFSWGRNSEGQLGLGkNSRSQAIPQ 172
Cdd:COG5184  283 DGT-TTDRSTPVKVPGLSGV--VAVAAGSSHTCALLTDGTVWCWGDNAYGQLGDG-TTTDRSTPV 343
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
145-195 3.20e-17

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 76.02  E-value: 3.20e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 60097906    145 DGHVFSWGRNSEGQLGLGkNSRSQAIPQKVKSLEGIPLAQVAAGGTHSFAL 195
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLG-TTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
92-142 8.14e-16

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 72.16  E-value: 8.14e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 60097906     92 KGKVFAWGAGSEGQLGIGEFKEISFmPTKIKALAGIKIIQVSCGHYHSLAL 142
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLV-PQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
129-158 4.62e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 58.20  E-value: 4.62e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 60097906    129 IIQVSCGHYHSLALSEDGHVFSWGRNSEGQ 158
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
40-89 1.94e-10

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 56.76  E-value: 1.94e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 60097906     40 NHRVYSCGDNSWGQLGQRRDQSTERPEPIQALNDLHVDLVSCGKEHSVAV 89
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
253-300 6.20e-08

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 49.82  E-value: 6.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 60097906    253 EGQVFTFGGNSSGQL-QPSPRSgQRGPQLIEGIGG-RVSQIECASYHTIA 300
Cdd:pfam00415    1 DGRVYTWGRNDYGQLgLGTTEN-VLVPQKVEGLSGnKVVQVACGGDHTVA 49
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
237-266 6.34e-08

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 49.34  E-value: 6.34e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 60097906    237 VIYISCGYEHTAVLTEEGQVFTFGGNSSGQ 266
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
183-211 4.19e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 43.95  E-value: 4.19e-06
                           10        20
                   ....*....|....*....|....*....
gi 60097906    183 AQVAAGGTHSFALSLTGTSFGWGSNRSGQ 211
Cdd:pfam13540    2 VSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
76-105 1.87e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 39.33  E-value: 1.87e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 60097906     76 VDLVSCGKEHSVAVCHKGKVFAWGAGSEGQ 105
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
26-53 3.23e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 38.94  E-value: 3.23e-04
                           10        20
                   ....*....|....*....|....*...
gi 60097906     26 QAASGEHHSLLLFSNHRVYSCGDNSWGQ 53
Cdd:pfam13540    3 SVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
 570-652 6.10e-03

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 40.40  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906   570 HKANCqlpesaFIINELsgIFNFD----AEAGRMFIRHNDLDCTESSDMVVFSDFLFVFDLPSKIKLMKCdsfvKLMSEV 645
Cdd:PTZ00212  287 HGCNV------FINRQL--IYNYPeqlfAEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHC----DLIEEI 354


                  ....*..
gi 60097906   646 MAFPEKM 652
Cdd:PTZ00212  355 MIGEDKL 361
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
 570-652 7.96e-03

TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239452 [Multi-domain]  Cd Length: 517  Bit Score: 40.01  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60097906  570 HKANCqlpesaFIINELsgIFNFD----AEAGRMFIRHNDLDCTESSDMVVFSDFLFVFDLPSKIKLMKCdsfvKLMSEV 645
Cdd:cd03336  275 HGINC------FINRQL--IYNYPeqlfADAGIMAIEHADFDGVERLALVTGGEIASTFDHPELVKLGTC----KLIEEI 342


                 ....*..
gi 60097906  646 MAFPEKM 652
Cdd:cd03336  343 MIGEDKL 349
 
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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