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Conserved domains on  [gi|1622950938|ref|XP_028706261|]
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ubiquitin-protein ligase E3A isoform X5 [Macaca mulatta]

Protein Classification

AZUL and HECTc domain-containing protein( domain architecture ID 11243968)

AZUL and HECTc domain-containing protein

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 ...
500-765 1.52e-110

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: 343.01  E-value: 1.52e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 500 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-STKLFWF 578
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 579 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNvEDDMMI 655
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 656 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 735
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 1622950938 736 ICGSRNLDFQALEETTEYDGGYTRDSVLIR 765
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQ 265
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 1.79e-21

Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal zinc-binding domain of ubiquitin E3a ligase is found in eukaryotes, and is an unusual zinc-finger domain. The final cysteine is usually mutated in Angelman syndrome patients. It is likely that AZUL plays a role in Ube3A substrate-recognition.


:

Pssm-ID: 465173  Cd Length: 59  Bit Score: 88.51  E-value: 1.79e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622950938   6 AKHLIERYYHQLTEGCGNEACTNEFCASCPTF--LRMDNNAAAIKALELYK--INAKLC 60
Cdd:pfam16558   1 FKLLVERYFYQLTYGCGSPNCTNPTCASCRDFpvRRLSPNSAAALALYLASqdPEAGLC 59
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
500-765 1.52e-110

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: 343.01  E-value: 1.52e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 500 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-STKLFWF 578
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 579 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNvEDDMMI 655
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 656 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 735
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 1622950938 736 ICGSRNLDFQALEETTEYDGGYTRDSVLIR 765
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQ 265
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
527-765 4.34e-100

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: 314.94  E-value: 4.34e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938  527 DLKKQ-LYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEG----QFTLIGIVLGLAIY 601
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938  602 NNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDL-LEYEGNVEDDmmITFQISQTDLFGNPMMYDLKENGDKI 680
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSIVLTSEFGQVKVVELKPGGSNI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938  681 PITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRD 760
Cdd:smart00119 159 PVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSAN 237

                   ....*
gi 1622950938  761 SVLIR 765
Cdd:smart00119 238 SQTIK 242
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
553-765 9.10e-77

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 252.15  E-value: 9.10e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 553 QLVVEEIFNPDIGMFTY-DESTKLFWFNPSSFETEG-----QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFR 626
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPDlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 627 DLGDSHPVLYQSLKDLLEYEGNVEDDMMITFQISQtdlFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQ 706
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV---FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622950938 707 FKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIR 765
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQ 215
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
436-764 1.65e-67

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 241.59  E-value: 1.65e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 436 EMDKDYTFFKVETENKfSFMTCPFILNAvtKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALv 515
Cdd:COG5021   454 RLNNLYRFYFVEHRKK-TLTKNDSRLGS--FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSY- 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 516 rlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKL-FWFNPSSFETEGQ---FTL 591
Cdd:COG5021   530 --REIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLPINPLSSINPEHlsyFKF 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 592 IGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNVEDdMMITFQIsQTDLFGNPMMY 671
Cdd:COG5021   608 LGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETI-LDLTFTV-EDDSFGESRTV 685
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 672 DLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYlFRPEEIELLICGSR-NLDFQALEET 750
Cdd:COG5021   686 ELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI-FDESELELLIGGIPeDIDIDDWKSN 764
                         330
                  ....*....|....
gi 1622950938 751 TEYDgGYTRDSVLI 764
Cdd:COG5021   765 TAYH-GYTEDSPII 777
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 1.79e-21

Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal zinc-binding domain of ubiquitin E3a ligase is found in eukaryotes, and is an unusual zinc-finger domain. The final cysteine is usually mutated in Angelman syndrome patients. It is likely that AZUL plays a role in Ube3A substrate-recognition.


Pssm-ID: 465173  Cd Length: 59  Bit Score: 88.51  E-value: 1.79e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622950938   6 AKHLIERYYHQLTEGCGNEACTNEFCASCPTF--LRMDNNAAAIKALELYK--INAKLC 60
Cdd:pfam16558   1 FKLLVERYFYQLTYGCGSPNCTNPTCASCRDFpvRRLSPNSAAALALYLASqdPEAGLC 59
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
500-765 1.52e-110

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: 343.01  E-value: 1.52e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 500 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-STKLFWF 578
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 579 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNvEDDMMI 655
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 656 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 735
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 1622950938 736 ICGSRNLDFQALEETTEYDGGYTRDSVLIR 765
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQ 265
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
527-765 4.34e-100

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: 314.94  E-value: 4.34e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938  527 DLKKQ-LYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEG----QFTLIGIVLGLAIY 601
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938  602 NNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDL-LEYEGNVEDDmmITFQISQTDLFGNPMMYDLKENGDKI 680
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSIVLTSEFGQVKVVELKPGGSNI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938  681 PITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRD 760
Cdd:smart00119 159 PVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSAN 237

                   ....*
gi 1622950938  761 SVLIR 765
Cdd:smart00119 238 SQTIK 242
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
553-765 9.10e-77

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 252.15  E-value: 9.10e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 553 QLVVEEIFNPDIGMFTY-DESTKLFWFNPSSFETEG-----QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFR 626
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPDlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 627 DLGDSHPVLYQSLKDLLEYEGNVEDDMMITFQISQtdlFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQ 706
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV---FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622950938 707 FKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIR 765
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQ 215
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
436-764 1.65e-67

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 241.59  E-value: 1.65e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 436 EMDKDYTFFKVETENKfSFMTCPFILNAvtKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALv 515
Cdd:COG5021   454 RLNNLYRFYFVEHRKK-TLTKNDSRLGS--FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSY- 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 516 rlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKL-FWFNPSSFETEGQ---FTL 591
Cdd:COG5021   530 --REIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLPINPLSSINPEHlsyFKF 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 592 IGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNVEDdMMITFQIsQTDLFGNPMMY 671
Cdd:COG5021   608 LGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETI-LDLTFTV-EDDSFGESRTV 685
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950938 672 DLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYlFRPEEIELLICGSR-NLDFQALEET 750
Cdd:COG5021   686 ELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI-FDESELELLIGGIPeDIDIDDWKSN 764
                         330
                  ....*....|....
gi 1622950938 751 TEYDgGYTRDSVLI 764
Cdd:COG5021   765 TAYH-GYTEDSPII 777
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 1.79e-21

Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal zinc-binding domain of ubiquitin E3a ligase is found in eukaryotes, and is an unusual zinc-finger domain. The final cysteine is usually mutated in Angelman syndrome patients. It is likely that AZUL plays a role in Ube3A substrate-recognition.


Pssm-ID: 465173  Cd Length: 59  Bit Score: 88.51  E-value: 1.79e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622950938   6 AKHLIERYYHQLTEGCGNEACTNEFCASCPTF--LRMDNNAAAIKALELYK--INAKLC 60
Cdd:pfam16558   1 FKLLVERYFYQLTYGCGSPNCTNPTCASCRDFpvRRLSPNSAAALALYLASqdPEAGLC 59
 
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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