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Conserved domains on  [gi|27477136|ref|NP_064504|]
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zinc finger CCCH-type antiviral protein 1 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 784-893 1.62e-49

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


:

Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 170.58  E-value: 1.62e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136 784 LLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFAKDAIYSHKNC---PYDAKNVVMFVAQVLVGKFTEGNITYTSP 860
Cdd:cd01439   1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSkksPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 27477136 861 PP--------QFDSCVDTRSNPSVFVIFQKDQVYPQYVIEY 893
Cdd:cd01439  81 PLkpsgveldRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
 5-66 1.51e-35

Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. This domain is a helix turn helix domain found at the N-terminal region constituting the top cockpit layer of the protein.


:

Pssm-ID: 465819  Cd Length: 62  Bit Score: 128.67  E-value: 1.51e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477136     5 EVCCFITKILCAHGGRMALDALLQEIALSEPQLCEVLQVAGPDRFVVLETGGEAGITRSVVA 66
Cdd:pfam18606   1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 607-689 1.39e-15

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


:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 71.99  E-value: 1.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136    607 WIWYWKNESGTWIQYgeekDKRKNSNVDSSYL--ESLYQSCPRGvvpfqagsRNYELSFQGMIQTNIASKTQKdVIRRPT 684
Cdd:smart00678   1 YVWEYEGRNGKWWPY----DPRVSEDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTR-KVRRVT 67


                   ....*
gi 27477136    685 FVPQW 689
Cdd:smart00678  68 YSPYS 72
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
 143-170 1.71e-13

Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. N-terminal domain of ZAP is the major functional domain which contains four zinc-finger motifs. This entry represents the third zinc finger type CCCH.


:

Pssm-ID: 436636  Cd Length: 28  Bit Score: 64.80  E-value: 1.71e-13
                          10        20
                  ....*....|....*....|....*...
gi 27477136   143 PFFMPEICKSYKGEGRQQICNQQPPCSR 170
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
 
Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 784-893 1.62e-49

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 170.58  E-value: 1.62e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136 784 LLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFAKDAIYSHKNC---PYDAKNVVMFVAQVLVGKFTEGNITYTSP 860
Cdd:cd01439   1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSkksPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 27477136 861 PP--------QFDSCVDTRSNPSVFVIFQKDQVYPQYVIEY 893
Cdd:cd01439  81 PLkpsgveldRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
 5-66 1.51e-35

Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. This domain is a helix turn helix domain found at the N-terminal region constituting the top cockpit layer of the protein.


Pssm-ID: 465819  Cd Length: 62  Bit Score: 128.67  E-value: 1.51e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477136     5 EVCCFITKILCAHGGRMALDALLQEIALSEPQLCEVLQVAGPDRFVVLETGGEAGITRSVVA 66
Cdd:pfam18606   1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 739-893 1.29e-19

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 87.77  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136   739 EYVRVSEHFKASM-----KNFKIEKIKKIENSELLDKFTWKKSQMKEegKLLFYATSRAYVESICSNNFDSFLHET--HE 811
Cdd:pfam00644   3 EYQIIEKYFLSTHdpthgYPLFILEIFRVQRDGEWERFQPKKKLRNR--RLLWHGSRLTNFLGILSQGLRIAPPEApvTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136   812 NKYGKGIYFAKDAIYSHKNCP--YDAKNVVMFVAQVLVGKFTE-GNITY-TSPPPQFDSCV------------------- 868
Cdd:pfam00644  81 YMFGKGIYFADDASKSANYCPpsEAHGNGLMLLSEVALGDMNElKKADYaEKLPPGKHSVKglgktapesfvdldgvplg 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 27477136   869 --------DTRSNPSVFVIFQKDQVYPQYVIEY 893
Cdd:pfam00644 161 klvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 607-689 1.39e-15

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 71.99  E-value: 1.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136    607 WIWYWKNESGTWIQYgeekDKRKNSNVDSSYL--ESLYQSCPRGvvpfqagsRNYELSFQGMIQTNIASKTQKdVIRRPT 684
Cdd:smart00678   1 YVWEYEGRNGKWWPY----DPRVSEDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTR-KVRRVT 67


                   ....*
gi 27477136    685 FVPQW 689
Cdd:smart00678  68 YSPYS 72
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
 143-170 1.71e-13

Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. N-terminal domain of ZAP is the major functional domain which contains four zinc-finger motifs. This entry represents the third zinc finger type CCCH.


Pssm-ID: 436636  Cd Length: 28  Bit Score: 64.80  E-value: 1.71e-13
                          10        20
                  ....*....|....*....|....*...
gi 27477136   143 PFFMPEICKSYKGEGRQQICNQQPPCSR 170
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 608-682 7.04e-13

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


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 64.24  E-value: 7.04e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477136   608 IWYWKNESGTWIQYGEEkdkrknsnvDSSYLESLYQS-CPRGVVPFQAGSRNYELSFQGMIQTNIASKTQKDvIRR 682
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
 
Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 784-893 1.62e-49

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 170.58  E-value: 1.62e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136 784 LLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFAKDAIYSHKNC---PYDAKNVVMFVAQVLVGKFTEGNITYTSP 860
Cdd:cd01439   1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSkksPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 27477136 861 PP--------QFDSCVDTRSNPSVFVIFQKDQVYPQYVIEY 893
Cdd:cd01439  81 PLkpsgveldRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
 5-66 1.51e-35

Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. This domain is a helix turn helix domain found at the N-terminal region constituting the top cockpit layer of the protein.


Pssm-ID: 465819  Cd Length: 62  Bit Score: 128.67  E-value: 1.51e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477136     5 EVCCFITKILCAHGGRMALDALLQEIALSEPQLCEVLQVAGPDRFVVLETGGEAGITRSVVA 66
Cdd:pfam18606   1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 739-893 1.29e-19

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 87.77  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136   739 EYVRVSEHFKASM-----KNFKIEKIKKIENSELLDKFTWKKSQMKEegKLLFYATSRAYVESICSNNFDSFLHET--HE 811
Cdd:pfam00644   3 EYQIIEKYFLSTHdpthgYPLFILEIFRVQRDGEWERFQPKKKLRNR--RLLWHGSRLTNFLGILSQGLRIAPPEApvTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136   812 NKYGKGIYFAKDAIYSHKNCP--YDAKNVVMFVAQVLVGKFTE-GNITY-TSPPPQFDSCV------------------- 868
Cdd:pfam00644  81 YMFGKGIYFADDASKSANYCPpsEAHGNGLMLLSEVALGDMNElKKADYaEKLPPGKHSVKglgktapesfvdldgvplg 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 27477136   869 --------DTRSNPSVFVIFQKDQVYPQYVIEY 893
Cdd:pfam00644 161 klvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 607-689 1.39e-15

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 71.99  E-value: 1.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136    607 WIWYWKNESGTWIQYgeekDKRKNSNVDSSYL--ESLYQSCPRGvvpfqagsRNYELSFQGMIQTNIASKTQKdVIRRPT 684
Cdd:smart00678   1 YVWEYEGRNGKWWPY----DPRVSEDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTR-KVRRVT 67


                   ....*
gi 27477136    685 FVPQW 689
Cdd:smart00678  68 YSPYS 72
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
 143-170 1.71e-13

Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. N-terminal domain of ZAP is the major functional domain which contains four zinc-finger motifs. This entry represents the third zinc finger type CCCH.


Pssm-ID: 436636  Cd Length: 28  Bit Score: 64.80  E-value: 1.71e-13
                          10        20
                  ....*....|....*....|....*...
gi 27477136   143 PFFMPEICKSYKGEGRQQICNQQPPCSR 170
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 608-682 7.04e-13

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


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 64.24  E-value: 7.04e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477136   608 IWYWKNESGTWIQYGEEkdkrknsnvDSSYLESLYQS-CPRGVVPFQAGSRNYELSFQGMIQTNIASKTQKDvIRR 682
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 754-893 5.50e-04

Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis).


Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 42.58  E-value: 5.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136 754 FKIEKIKKIENSELLDKFTWKKSQMKEEG------KLLFYATSraYVESICSNNFDSfLHETHENKYGKGIYFAKDAIYS 827
Cdd:cd01438  55 YNIIRIQKVVNKKLRERYCHRQKEIAEENhnhhneRMLFHGSP--FINAIIHKGFDE-RHAYIGGMFGAGIYFAENSSKS 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136 828 HK---------NCP-YDAKNVVMFVAQVLVGKFTEGN-------ITYTSPPPQFDSCVdtrSNPSV-------FVIFQKD 883
Cdd:cd01438 132 NQyvygigggtGCPtHKDRSCYVCHRQMLFCRVTLGKsflqfsaMKMAHAPPGHHSVI---GRPSVnglayaeYVIYRGE 208

                       170
                ....*....|
gi 27477136 884 QVYPQYVIEY 893
Cdd:cd01438 209 QAYPEYLITY 218
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 738-888 4.15e-03

Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active. Poly(ADP-ribose)-like polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length through interactions with telomere repeat binding factor 1.


Pssm-ID: 238717 [Multi-domain]  Cd Length: 347  Bit Score: 40.33  E-value: 4.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136 738 PEYVRVSE-----HFKASMKNFKIEKIKKIENSELLDKF-TWKKSQMKeegKLLFYATSRAYVESICSNNFDSFLHETHE 811
Cdd:cd01437 148 EEYKIIEKylkntHAPTTEYTVEVQEIFRVEREGETDRFkPFKKLGNR---KLLWHGSRLTNFVGILSQGLRIAPPEAPV 224

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477136 812 NKY--GKGIYFA----KDAIYSHkncPYDAKNV-VMFVAQVLVGK---FTEGNITYTSPPPQFDSCV---DTRSNPSVFV 878
Cdd:cd01437 225 TGYmfGKGIYFAdmfsKSANYCH---ASASDPTgLLLLCEVALGKmneLKKADYMAKELPKGKHSVKglgKTAPDPSEFE 301

                       170
                ....*....|
gi 27477136 879 IFQKDQVYPQ 888
Cdd:cd01437 302 IDLDGVVVPL 311
 
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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