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Conserved domains on  [gi|1407380404|ref|NP_001350420|]
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zinc finger CCCH-type antiviral protein 1 isoform 3 [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 ...
 906-1015 9.70e-50

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: 171.35  E-value: 9.70e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404  906 LLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFAKDAIYSHKNC---PYDAKNVVMFVAQVLVGKFTEGNITYTSP 982
Cdd:cd01439      1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSkksPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1407380404  983 PP--------QFDSCVDTRSNPSVFVIFQKDQVYPQYVIEY 1015
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 1.72e-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: 1.72e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1407380404    5 EVCCFITKILCAHGGRMALDALLQEIALSEPQLCEVLQVAGPDRFVVLETGGEAGITRSVVA 66
Cdd:pfam18606    1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 729-811 9.98e-16

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


:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 72.76  E-value: 9.98e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404   729 WIWYWKNESGTWIQYgeekDKRKNSNVDSSYL--ESLYQSCPRGvvpfqagsRNYELSFQGMIQTNIASKTQKdVIRRPT 806
Cdd:smart00678    1 YVWEYEGRNGKWWPY----DPRVSEDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTR-KVRRVT 67


                    ....*
gi 1407380404   807 FVPQW 811
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 9.13e-14

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: 65.95  E-value: 9.13e-14
                           10        20
                   ....*....|....*....|....*...
gi 1407380404  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 ...
 906-1015 9.70e-50

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: 171.35  E-value: 9.70e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404  906 LLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFAKDAIYSHKNC---PYDAKNVVMFVAQVLVGKFTEGNITYTSP 982
Cdd:cd01439      1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSkksPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1407380404  983 PP--------QFDSCVDTRSNPSVFVIFQKDQVYPQYVIEY 1015
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 1.72e-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: 1.72e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1407380404    5 EVCCFITKILCAHGGRMALDALLQEIALSEPQLCEVLQVAGPDRFVVLETGGEAGITRSVVA 66
Cdd:pfam18606    1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 861-1015 8.63e-20

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: 88.54  E-value: 8.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404  861 EYVRVSEHFKASM-----KNFKIEKIKKIENSELLDKFTWKKSQMKEegKLLFYATSRAYVESICSNNFDSFLHET--HE 933
Cdd:pfam00644    3 EYQIIEKYFLSTHdpthgYPLFILEIFRVQRDGEWERFQPKKKLRNR--RLLWHGSRLTNFLGILSQGLRIAPPEApvTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404  934 NKYGKGIYFAKDAIYSHKNCP--YDAKNVVMFVAQVLVGKFTE-GNITY-TSPPPQFDSCV------------------- 990
Cdd:pfam00644   81 YMFGKGIYFADDASKSANYCPpsEAHGNGLMLLSEVALGDMNElKKADYaEKLPPGKHSVKglgktapesfvdldgvplg 160

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1407380404  991 --------DTRSNPSVFVIFQKDQVYPQYVIEY 1015
Cdd:pfam00644  161 klvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 729-811 9.98e-16

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 72.76  E-value: 9.98e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404   729 WIWYWKNESGTWIQYgeekDKRKNSNVDSSYL--ESLYQSCPRGvvpfqagsRNYELSFQGMIQTNIASKTQKdVIRRPT 806
Cdd:smart00678    1 YVWEYEGRNGKWWPY----DPRVSEDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTR-KVRRVT 67


                    ....*
gi 1407380404   807 FVPQW 811
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 9.13e-14

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: 65.95  E-value: 9.13e-14
                           10        20
                   ....*....|....*....|....*...
gi 1407380404  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 ...
 730-804 5.53e-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: 64.63  E-value: 5.53e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1407380404  730 IWYWKNESGTWIQYGEEkdkrknsnvDSSYLESLYQS-CPRGVVPFQAGSRNYELSFQGMIQTNIASKTQKDvIRR 804
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 ...
 906-1015 9.70e-50

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: 171.35  E-value: 9.70e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404  906 LLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFAKDAIYSHKNC---PYDAKNVVMFVAQVLVGKFTEGNITYTSP 982
Cdd:cd01439      1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSkksPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1407380404  983 PP--------QFDSCVDTRSNPSVFVIFQKDQVYPQYVIEY 1015
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 1.72e-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: 1.72e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1407380404    5 EVCCFITKILCAHGGRMALDALLQEIALSEPQLCEVLQVAGPDRFVVLETGGEAGITRSVVA 66
Cdd:pfam18606    1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 861-1015 8.63e-20

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: 88.54  E-value: 8.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404  861 EYVRVSEHFKASM-----KNFKIEKIKKIENSELLDKFTWKKSQMKEegKLLFYATSRAYVESICSNNFDSFLHET--HE 933
Cdd:pfam00644    3 EYQIIEKYFLSTHdpthgYPLFILEIFRVQRDGEWERFQPKKKLRNR--RLLWHGSRLTNFLGILSQGLRIAPPEApvTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404  934 NKYGKGIYFAKDAIYSHKNCP--YDAKNVVMFVAQVLVGKFTE-GNITY-TSPPPQFDSCV------------------- 990
Cdd:pfam00644   81 YMFGKGIYFADDASKSANYCPpsEAHGNGLMLLSEVALGDMNElKKADYaEKLPPGKHSVKglgktapesfvdldgvplg 160

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1407380404  991 --------DTRSNPSVFVIFQKDQVYPQYVIEY 1015
Cdd:pfam00644  161 klvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 729-811 9.98e-16

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 72.76  E-value: 9.98e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404   729 WIWYWKNESGTWIQYgeekDKRKNSNVDSSYL--ESLYQSCPRGvvpfqagsRNYELSFQGMIQTNIASKTQKdVIRRPT 806
Cdd:smart00678    1 YVWEYEGRNGKWWPY----DPRVSEDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTR-KVRRVT 67


                    ....*
gi 1407380404   807 FVPQW 811
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 9.13e-14

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: 65.95  E-value: 9.13e-14
                           10        20
                   ....*....|....*....|....*...
gi 1407380404  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 ...
 730-804 5.53e-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: 64.63  E-value: 5.53e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1407380404  730 IWYWKNESGTWIQYGEEkdkrknsnvDSSYLESLYQS-CPRGVVPFQAGSRNYELSFQGMIQTNIASKTQKDvIRR 804
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 876-1015 4.97e-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: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404  876 FKIEKIKKIENSELLDKFTWKKSQMKEEG------KLLFYATSraYVESICSNNFDSfLHETHENKYGKGIYFAKDAIYS 949
Cdd:cd01438     55 YNIIRIQKVVNKKLRERYCHRQKEIAEENhnhhneRMLFHGSP--FINAIIHKGFDE-RHAYIGGMFGAGIYFAENSSKS 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404  950 HK---------NCP-YDAKNVVMFVAQVLVGKFTEGN-------ITYTSPPPQFDSCVdtrSNPSV-------FVIFQKD 1005
Cdd:cd01438    132 NQyvygigggtGCPtHKDRSCYVCHRQMLFCRVTLGKsflqfsaMKMAHAPPGHHSVI---GRPSVnglayaeYVIYRGE 208

                          170
                   ....*....|
gi 1407380404 1006 QVYPQYVIEY 1015
Cdd:cd01438    209 QAYPEYLITY 218
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 860-1010 4.82e-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: 4.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404  860 PEYVRVSE-----HFKASMKNFKIEKIKKIENSELLDKF-TWKKSQMKeegKLLFYATSRAYVESICSNNFDSFLHETHE 933
Cdd:cd01437    148 EEYKIIEKylkntHAPTTEYTVEVQEIFRVEREGETDRFkPFKKLGNR---KLLWHGSRLTNFVGILSQGLRIAPPEAPV 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407380404  934 NKY--GKGIYFA----KDAIYSHkncPYDAKNV-VMFVAQVLVGK---FTEGNITYTSPPPQFDSCV---DTRSNPSVFV 1000
Cdd:cd01437    225 TGYmfGKGIYFAdmfsKSANYCH---ASASDPTgLLLLCEVALGKmneLKKADYMAKELPKGKHSVKglgKTAPDPSEFE 301

                          170
                   ....*....|
gi 1407380404 1001 IFQKDQVYPQ 1010
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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