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Conserved domains on  [gi|1983961952|gb|KAG3277393|]
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zinc finger CCCH-type containing, antiviral 1 [Ictidomys tridecemlineatus]

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 ...
 752-861 5.99e-39

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: 140.53  E-value: 5.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 752 LLFYATSRTNVDYICSYNFNWSVHGLHEIKYGKGNHFAKEAFSSHKNCQDD---VKSLVMFVARVLVGNVAEGRMTYRMP 828
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSpkaDGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1983961952 829 PP--------RSDSCVDNTVNPSVFVIFHKDQMYPAYVIEY 861
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 6.44e-34

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: 124.05  E-value: 6.44e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1983961952   5 EVCCFITKILCAHGGRMSLEALLDKIALSEVQLCEVLEAAGPDRFVVLETGSRAGVTRSVVA 66
Cdd:pfam18606   1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
 116-143 2.33e-15

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: 70.19  E-value: 2.33e-15
                          10        20
                  ....*....|....*....|....*...
gi 1983961952 116 PFFMPEICKSYKGEGRKQICSQQPPCER 143
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 574-648 1.65e-12

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: 63.08  E-value: 1.65e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983961952 574 VWYWKNESDQWIEYGEEsnnqpgsniDSTYLESMFQS-YPRGVVPFQAGSRNYELNFQGMIQTNIISKTQKDvVRR 648
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
PHA03132 super family cl33716
thymidine kinase; Provisional
 196-394 2.49e-03

thymidine kinase; Provisional


The actual alignment was detected with superfamily member PHA03132:

Pssm-ID: 222997 [Multi-domain]  Cd Length: 580  Bit Score: 41.29  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 196 HARRNPSGPRAPTPHRRAGMTRGRSKSRDRFLPESQEFPPSASAAAQNSRTSSPDVVGQRLFLKDvgvgdltyRFTYLGS 275
Cdd:PHA03132   67 ATSTIYTVPRPPRGPEQTLDKPDSLPASRELPPGPTPVPPGGFRGASSPRLGADSTSPRFLYQVN--------FPVILAP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 276 QDRTPPSSllskapglggpGQVGSSQKFSENGSSDRLFYRNHSDSTPSSSQKGSPTWQNDQGPRRDNvffpgqASGGSPL 355
Cdd:PHA03132  139 IGESNSSS-----------EELSEEEEHSRPPPSESLKVKNGGKVYPKGFSKHKTHKRSEFSGLTKK------AARKRKG 201

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1983961952 356 GLGKTPETVtTRKSTAILSPDLVNVKGQNGTQDTQRHVP 394
Cdd:PHA03132  202 SFVFKPSQL-KELSGSLKNLLHLDDSAETDPATRQVPVP 239
 
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 ...
 752-861 5.99e-39

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: 140.53  E-value: 5.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 752 LLFYATSRTNVDYICSYNFNWSVHGLHEIKYGKGNHFAKEAFSSHKNCQDD---VKSLVMFVARVLVGNVAEGRMTYRMP 828
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSpkaDGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1983961952 829 PP--------RSDSCVDNTVNPSVFVIFHKDQMYPAYVIEY 861
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 6.44e-34

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: 124.05  E-value: 6.44e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1983961952   5 EVCCFITKILCAHGGRMSLEALLDKIALSEVQLCEVLEAAGPDRFVVLETGSRAGVTRSVVA 66
Cdd:pfam18606   1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 705-861 8.59e-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: 85.46  E-value: 8.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 705 SAEYANISDYFKASM-----KNFKIERIKKIHNQELEKNFERKKSEMQteEKLLFYATSRTNVDYICSYNF--NWSVHGL 777
Cdd:pfam00644   1 SEEYQIIEKYFLSTHdpthgYPLFILEIFRVQRDGEWERFQPKKKLRN--RRLLWHGSRLTNFLGILSQGLriAPPEAPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 778 HEIKYGKGNHFAKEAFSSHKNCQDDV--KSLVMFVARVLVGNVAE-GRMTY-RMPPPRSDSCV----------------- 836
Cdd:pfam00644  79 TGYMFGKGIYFADDASKSANYCPPSEahGNGLMLLSEVALGDMNElKKADYaEKLPPGKHSVKglgktapesfvdldgvp 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1983961952 837 ----------DNTVNPSVFVIFHKDQMYPAYVIEY 861
Cdd:pfam00644 159 lgklvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
 116-143 2.33e-15

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: 70.19  E-value: 2.33e-15
                          10        20
                  ....*....|....*....|....*...
gi 1983961952 116 PFFMPEICKSYKGEGRKQICSQQPPCER 143
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 574-648 1.65e-12

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: 63.08  E-value: 1.65e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983961952 574 VWYWKNESDQWIEYGEEsnnqpgsniDSTYLESMFQS-YPRGVVPFQAGSRNYELNFQGMIQTNIISKTQKDvVRR 648
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 573-650 1.16e-08

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 52.34  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952  573 WVWYWKNESDQWIEYGEESNnqpgSNIDSTYL--ESMFQSYPRGvvpfqagsRNYELNFQGMIQTNIISKTQKdVVRRPT 650
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVS----EDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTR-KVRRVT 67
PHA03132 PHA03132
thymidine kinase; Provisional
 196-394 2.49e-03

thymidine kinase; Provisional


Pssm-ID: 222997 [Multi-domain]  Cd Length: 580  Bit Score: 41.29  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 196 HARRNPSGPRAPTPHRRAGMTRGRSKSRDRFLPESQEFPPSASAAAQNSRTSSPDVVGQRLFLKDvgvgdltyRFTYLGS 275
Cdd:PHA03132   67 ATSTIYTVPRPPRGPEQTLDKPDSLPASRELPPGPTPVPPGGFRGASSPRLGADSTSPRFLYQVN--------FPVILAP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 276 QDRTPPSSllskapglggpGQVGSSQKFSENGSSDRLFYRNHSDSTPSSSQKGSPTWQNDQGPRRDNvffpgqASGGSPL 355
Cdd:PHA03132  139 IGESNSSS-----------EELSEEEEHSRPPPSESLKVKNGGKVYPKGFSKHKTHKRSEFSGLTKK------AARKRKG 201

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1983961952 356 GLGKTPETVtTRKSTAILSPDLVNVKGQNGTQDTQRHVP 394
Cdd:PHA03132  202 SFVFKPSQL-KELSGSLKNLLHLDDSAETDPATRQVPVP 239
 
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 ...
 752-861 5.99e-39

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: 140.53  E-value: 5.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 752 LLFYATSRTNVDYICSYNFNWSVHGLHEIKYGKGNHFAKEAFSSHKNCQDD---VKSLVMFVARVLVGNVAEGRMTYRMP 828
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSpkaDGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1983961952 829 PP--------RSDSCVDNTVNPSVFVIFHKDQMYPAYVIEY 861
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 6.44e-34

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: 124.05  E-value: 6.44e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1983961952   5 EVCCFITKILCAHGGRMSLEALLDKIALSEVQLCEVLEAAGPDRFVVLETGSRAGVTRSVVA 66
Cdd:pfam18606   1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 705-861 8.59e-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: 85.46  E-value: 8.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 705 SAEYANISDYFKASM-----KNFKIERIKKIHNQELEKNFERKKSEMQteEKLLFYATSRTNVDYICSYNF--NWSVHGL 777
Cdd:pfam00644   1 SEEYQIIEKYFLSTHdpthgYPLFILEIFRVQRDGEWERFQPKKKLRN--RRLLWHGSRLTNFLGILSQGLriAPPEAPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 778 HEIKYGKGNHFAKEAFSSHKNCQDDV--KSLVMFVARVLVGNVAE-GRMTY-RMPPPRSDSCV----------------- 836
Cdd:pfam00644  79 TGYMFGKGIYFADDASKSANYCPPSEahGNGLMLLSEVALGDMNElKKADYaEKLPPGKHSVKglgktapesfvdldgvp 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1983961952 837 ----------DNTVNPSVFVIFHKDQMYPAYVIEY 861
Cdd:pfam00644 159 lgklvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
 116-143 2.33e-15

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: 70.19  E-value: 2.33e-15
                          10        20
                  ....*....|....*....|....*...
gi 1983961952 116 PFFMPEICKSYKGEGRKQICSQQPPCER 143
Cdd:pfam18633   1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 574-648 1.65e-12

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: 63.08  E-value: 1.65e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983961952 574 VWYWKNESDQWIEYGEEsnnqpgsniDSTYLESMFQS-YPRGVVPFQAGSRNYELNFQGMIQTNIISKTQKDvVRR 648
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRP-VRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 573-650 1.16e-08

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 52.34  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952  573 WVWYWKNESDQWIEYGEESNnqpgSNIDSTYL--ESMFQSYPRGvvpfqagsRNYELNFQGMIQTNIISKTQKdVVRRPT 650
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRVS----EDIEEAYAagKKLCELSICG--------FPYTIDFNAMTQYNQATGTTR-KVRRVT 67
PHA03132 PHA03132
thymidine kinase; Provisional
 196-394 2.49e-03

thymidine kinase; Provisional


Pssm-ID: 222997 [Multi-domain]  Cd Length: 580  Bit Score: 41.29  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 196 HARRNPSGPRAPTPHRRAGMTRGRSKSRDRFLPESQEFPPSASAAAQNSRTSSPDVVGQRLFLKDvgvgdltyRFTYLGS 275
Cdd:PHA03132   67 ATSTIYTVPRPPRGPEQTLDKPDSLPASRELPPGPTPVPPGGFRGASSPRLGADSTSPRFLYQVN--------FPVILAP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983961952 276 QDRTPPSSllskapglggpGQVGSSQKFSENGSSDRLFYRNHSDSTPSSSQKGSPTWQNDQGPRRDNvffpgqASGGSPL 355
Cdd:PHA03132  139 IGESNSSS-----------EELSEEEEHSRPPPSESLKVKNGGKVYPKGFSKHKTHKRSEFSGLTKK------AARKRKG 201

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1983961952 356 GLGKTPETVtTRKSTAILSPDLVNVKGQNGTQDTQRHVP 394
Cdd:PHA03132  202 SFVFKPSQL-KELSGSLKNLLHLDDSAETDPATRQVPVP 239
 
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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