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Conserved domains on  [gi|1776177581|ref|XP_031471002|]
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DNA replication complex GINS protein PSF2 [Phasianus colchicus]

Protein Classification

DNA replication complex GINS protein PSF2( domain architecture ID 16902698)

DNA replication complex GINS protein PSF2 is a component of the heterotetrameric GINS complex; the GINS complex is essential for both the initiation and elongation stages of eukaryotic DNA replication

CATH:  1.20.58.1020|3.40.5.50
Gene Ontology:  GO:0006260
PubMed:  22918584|20070258

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GINS_A_psf2 cd11712
Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of ...
 133-252 3.62e-59

Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of GINS tetrameric protein complex and has been found to play important roles in normal eye development in Xenopus laevis. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


:

Pssm-ID: 212550  Cd Length: 119  Bit Score: 183.58  E-value: 3.62e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581 133 RQKCRLIPPEWMDVEKLEEIRDQERKEDTFTPMPsPYYMELTKLLLNYASDNIPKADEIRTLVKDTWDTRMAKLRLSADS 212
Cdd:cd11712     1 RNKCRIVPPDWLTVEYLKEILEEEKKSETFSPLP-FHYLEIAKLLLEVASDDIPDADEIRSLVEDIRDVRQAKLRSGLEK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1776177581 213 FVRQQEAHAKLDNLTLMEINTIGTFLTQALDHMYKLRTNL 252
Cdd:cd11712    80 LLGSGEVHAKLDNLTAMEINEIRPFLSGALDKLRKLRASA 119
GINS_B_Psf2 cd21694
beta-strand (B) domain of GINS complex protein Psf2; Psf2 (partner of Sld5 2) is a component ...
 80-141 3.22e-35

beta-strand (B) domain of GINS complex protein Psf2; Psf2 (partner of Sld5 2) is a component of GINS (named from the Japanese go-ichi-ni-san, meaning 5-1-2-3 for the Sld5, Psf1, Psf2, and Psf3 subunits) tetrameric protein complex and has been found to play important roles in normal eye development in Xenopus laevis and in ICL (interstrand crosslinks) repair. ICLs are toxic lesions that covalently attach opposite strands of DNA. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) and is involved in both the initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits Sld5, Psf1, Psf2, and Psf3 are homologous, and homologs are also found in archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, called the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3. This model represents the B-domain of GINS subunit Psf2.


:

Pssm-ID: 412030  Cd Length: 62  Bit Score: 120.32  E-value: 3.22e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776177581  80 EPAEAEFLAEKELVTIVPSFSMDRVHLIGGDLGPFNPGLPVEVPVWLAINLKQRQKCRLIPP 141
Cdd:cd21694     1 TPEEVEFLAEDELVTIIPNFSLDKLNLISGDYGPFRPGRPVEVPLWLAINLKKRQKCRIVPP 62
 
Name Accession Description Interval E-value
GINS_A_psf2 cd11712
Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of ...
 133-252 3.62e-59

Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of GINS tetrameric protein complex and has been found to play important roles in normal eye development in Xenopus laevis. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


Pssm-ID: 212550  Cd Length: 119  Bit Score: 183.58  E-value: 3.62e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581 133 RQKCRLIPPEWMDVEKLEEIRDQERKEDTFTPMPsPYYMELTKLLLNYASDNIPKADEIRTLVKDTWDTRMAKLRLSADS 212
Cdd:cd11712     1 RNKCRIVPPDWLTVEYLKEILEEEKKSETFSPLP-FHYLEIAKLLLEVASDDIPDADEIRSLVEDIRDVRQAKLRSGLEK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1776177581 213 FVRQQEAHAKLDNLTLMEINTIGTFLTQALDHMYKLRTNL 252
Cdd:cd11712    80 LLGSGEVHAKLDNLTAMEINEIRPFLSGALDKLRKLRASA 119
COG5093 COG5093
Uncharacterized conserved protein [Function unknown];
81-250 2.63e-36

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227424 [Multi-domain]  Cd Length: 185  Bit Score: 127.31  E-value: 2.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581  81 PAEAEFLAEKELVTIVPSFSMDRVHLI-GGDLGPFNPGLPVEVPVWLAINLKQRQKCRLIPPEWMDVEKLE-EIRDQERK 158
Cdd:COG5093    13 PEEILFIAYNELIEIEPMTTIPQLRLLeRATYPPMMPLDIARVPLWAALLLKKQNMCKIVLPSWLQLESLKmSIDVEIEK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581 159 EDTFTPMPsPYYMELTKLLLNYASDNIPKADEIRTLVKDTWDTRMAKLRLSADSFvrqQEAHAKLDNLTLMEINTIGTFL 238
Cdd:COG5093    93 ADEFSELP-PYWLPLATELLNENCDDVEDIEESRMIVEDIREIRQAKTLKGLKCL---NEKALNLDNLTLFEINEIRPLI 168

                         170
                  ....*....|..
gi 1776177581 239 TQALDHMYKLRT 250
Cdd:COG5093   169 LESMDVGRRIED 180
GINS_B_Psf2 cd21694
beta-strand (B) domain of GINS complex protein Psf2; Psf2 (partner of Sld5 2) is a component ...
 80-141 3.22e-35

beta-strand (B) domain of GINS complex protein Psf2; Psf2 (partner of Sld5 2) is a component of GINS (named from the Japanese go-ichi-ni-san, meaning 5-1-2-3 for the Sld5, Psf1, Psf2, and Psf3 subunits) tetrameric protein complex and has been found to play important roles in normal eye development in Xenopus laevis and in ICL (interstrand crosslinks) repair. ICLs are toxic lesions that covalently attach opposite strands of DNA. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) and is involved in both the initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits Sld5, Psf1, Psf2, and Psf3 are homologous, and homologs are also found in archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, called the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3. This model represents the B-domain of GINS subunit Psf2.


Pssm-ID: 412030  Cd Length: 62  Bit Score: 120.32  E-value: 3.22e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776177581  80 EPAEAEFLAEKELVTIVPSFSMDRVHLIGGDLGPFNPGLPVEVPVWLAINLKQRQKCRLIPP 141
Cdd:cd21694     1 TPEEVEFLAEDELVTIIPNFSLDKLNLISGDYGPFRPGRPVEVPLWLAINLKKRQKCRIVPP 62
Sld5 pfam05916
GINS complex protein; The eukaryotic GINS complex is essential for the initiation and ...
 120-231 1.02e-26

GINS complex protein; The eukaryotic GINS complex is essential for the initiation and elongation phases of DNA replication. It consists of four paralogous protein subunits (Sld5, Psf1, Psf2 and Psf3), all of which are included in this family. The GINS complex is conserved from yeast to humans, and has been shown in human to bind directly to DNA primase.


Pssm-ID: 399129  Cd Length: 105  Bit Score: 99.88  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581 120 VEVPVWLAINLKQRQKCRLIPPEWMDVEKLEEIRDQERKEDtfTPMPSPYYMELTKLLLNYASDnipkaDEIRTLVKDTW 199
Cdd:pfam05916   1 PELPLWLAELLKRRGLVEIEPPEWLSIEELEAILADETKND--LSLLPPYFYELAVLLLELERD-----DELKRLLRDYL 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1776177581 200 DTRMAKLRLSADSFVRQQEAHAKLDNLTLMEI 231
Cdd:pfam05916  74 RIRLAKIRKLAWHLNGSLSPSDLLDNLSEEEL 105
PTZ00362 PTZ00362
hypothetical protein; Provisional
 88-238 4.03e-04

hypothetical protein; Provisional


Pssm-ID: 240380 [Multi-domain]  Cd Length: 479  Bit Score: 41.28  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581  88 AEKELVTI-----VPSFSMDRVHliGGDLGPFNPGLPVEVPVWLAINLKQRQKCRLIPPEWMDVEKLEEIRDQERKE-DT 161
Cdd:PTZ00362  282 ALDELVVVkalvdIPYIDLSEIE--GFDFKEMKSGERQWLPIYIAKELSHFGLVTVEFPFWFYIKNLKNIYEREFEDqNE 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581 162 FTPMPSPYYMELTKLLLN---YASDNIPKADEIRT----------LVKDTWDTRMAKLRLSADSFvRQQEAHAKLDNLTL 228
Cdd:PTZ00362  360 LTDLPSPYFFEISSMFLEnniFKKVTPIETIGQRTvykyiskvagLVEDIRYKRLKKIMNHLENQ-DVHSSIIYIDNLQI 438

                         170
                  ....*....|
gi 1776177581 229 MEINTIGTFL 238
Cdd:PTZ00362  439 SETYCVNQLL 448
 
Name Accession Description Interval E-value
GINS_A_psf2 cd11712
Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of ...
 133-252 3.62e-59

Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of GINS tetrameric protein complex and has been found to play important roles in normal eye development in Xenopus laevis. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


Pssm-ID: 212550  Cd Length: 119  Bit Score: 183.58  E-value: 3.62e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581 133 RQKCRLIPPEWMDVEKLEEIRDQERKEDTFTPMPsPYYMELTKLLLNYASDNIPKADEIRTLVKDTWDTRMAKLRLSADS 212
Cdd:cd11712     1 RNKCRIVPPDWLTVEYLKEILEEEKKSETFSPLP-FHYLEIAKLLLEVASDDIPDADEIRSLVEDIRDVRQAKLRSGLEK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1776177581 213 FVRQQEAHAKLDNLTLMEINTIGTFLTQALDHMYKLRTNL 252
Cdd:cd11712    80 LLGSGEVHAKLDNLTAMEINEIRPFLSGALDKLRKLRASA 119
COG5093 COG5093
Uncharacterized conserved protein [Function unknown];
81-250 2.63e-36

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227424 [Multi-domain]  Cd Length: 185  Bit Score: 127.31  E-value: 2.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581  81 PAEAEFLAEKELVTIVPSFSMDRVHLI-GGDLGPFNPGLPVEVPVWLAINLKQRQKCRLIPPEWMDVEKLE-EIRDQERK 158
Cdd:COG5093    13 PEEILFIAYNELIEIEPMTTIPQLRLLeRATYPPMMPLDIARVPLWAALLLKKQNMCKIVLPSWLQLESLKmSIDVEIEK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581 159 EDTFTPMPsPYYMELTKLLLNYASDNIPKADEIRTLVKDTWDTRMAKLRLSADSFvrqQEAHAKLDNLTLMEINTIGTFL 238
Cdd:COG5093    93 ADEFSELP-PYWLPLATELLNENCDDVEDIEESRMIVEDIREIRQAKTLKGLKCL---NEKALNLDNLTLFEINEIRPLI 168

                         170
                  ....*....|..
gi 1776177581 239 TQALDHMYKLRT 250
Cdd:COG5093   169 LESMDVGRRIED 180
GINS_B_Psf2 cd21694
beta-strand (B) domain of GINS complex protein Psf2; Psf2 (partner of Sld5 2) is a component ...
 80-141 3.22e-35

beta-strand (B) domain of GINS complex protein Psf2; Psf2 (partner of Sld5 2) is a component of GINS (named from the Japanese go-ichi-ni-san, meaning 5-1-2-3 for the Sld5, Psf1, Psf2, and Psf3 subunits) tetrameric protein complex and has been found to play important roles in normal eye development in Xenopus laevis and in ICL (interstrand crosslinks) repair. ICLs are toxic lesions that covalently attach opposite strands of DNA. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) and is involved in both the initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits Sld5, Psf1, Psf2, and Psf3 are homologous, and homologs are also found in archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, called the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3. This model represents the B-domain of GINS subunit Psf2.


Pssm-ID: 412030  Cd Length: 62  Bit Score: 120.32  E-value: 3.22e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776177581  80 EPAEAEFLAEKELVTIVPSFSMDRVHLIGGDLGPFNPGLPVEVPVWLAINLKQRQKCRLIPP 141
Cdd:cd21694     1 TPEEVEFLAEDELVTIIPNFSLDKLNLISGDYGPFRPGRPVEVPLWLAINLKKRQKCRIVPP 62
Sld5 pfam05916
GINS complex protein; The eukaryotic GINS complex is essential for the initiation and ...
 120-231 1.02e-26

GINS complex protein; The eukaryotic GINS complex is essential for the initiation and elongation phases of DNA replication. It consists of four paralogous protein subunits (Sld5, Psf1, Psf2 and Psf3), all of which are included in this family. The GINS complex is conserved from yeast to humans, and has been shown in human to bind directly to DNA primase.


Pssm-ID: 399129  Cd Length: 105  Bit Score: 99.88  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581 120 VEVPVWLAINLKQRQKCRLIPPEWMDVEKLEEIRDQERKEDtfTPMPSPYYMELTKLLLNYASDnipkaDEIRTLVKDTW 199
Cdd:pfam05916   1 PELPLWLAELLKRRGLVEIEPPEWLSIEELEAILADETKND--LSLLPPYFYELAVLLLELERD-----DELKRLLRDYL 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1776177581 200 DTRMAKLRLSADSFVRQQEAHAKLDNLTLMEI 231
Cdd:pfam05916  74 RIRLAKIRKLAWHLNGSLSPSDLLDNLSEEEL 105
GINS_A cd11581
Alpha-helical domain of GINS complex proteins; Sld5, Psf1, Psf2 and Psf3; The GINS complex is ...
 146-243 1.39e-15

Alpha-helical domain of GINS complex proteins; Sld5, Psf1, Psf2 and Psf3; The GINS complex is involved in both initiation and elongation stages of eukaryotic chromosome replication, with GINS being the component that most likely serves as the replicative helicase that unwinds duplex DNA ahead of the moving replication fork. In eukaryotes, GINS is a tetrameric arrangement of four subunits Sld5, Psf1, Psf2 and Psf3. The GINS complex has been found in eukaryotes and archaea, but not in bacteria. The four subunits of the complex are homologous and consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


Pssm-ID: 212547  Cd Length: 103  Bit Score: 70.60  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581 146 VEKLEEIRDQERKEDTFTPMPsPYYMELTKLLLNYASDN--------------IPKADEIRTLVKDTWDTRMAKLRLSAD 211
Cdd:cd11581     1 VEKLAEAIHNERKSENLLPPP-PDFMEEVKELLHRLSKRqrsetqeilehrlkILELSYIRDLLKTYLNSRLDKIRDLSP 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1776177581 212 SFvrqqeahaKLDNLTLMEINTIGTFLTQALD 243
Cdd:cd11581    80 EF--------LPSNLTEEEIGYFQTYWKEVAE 103
GINS_B cd21396
beta-strand (B) domain of GINS complex proteins: Sld5, Psf1, Psf2, Psf3, Gins51 and Gins23; ...
 92-139 6.04e-10

beta-strand (B) domain of GINS complex proteins: Sld5, Psf1, Psf2, Psf3, Gins51 and Gins23; The GINS (named from the Japanese go-ichi-ni-san, meaning 5-1-2-3 for the Sld5, Psf1, Psf2, and Psf3 subunits) complex is involved in both the initiation and elongation stages of eukaryotic chromosome replication, with GINS being the component that most likely serves as the replicative helicase that unwinds duplex DNA ahead of the moving replication fork. This complex is found in eukaryotes and archaea, but not in bacteria. In eukaryotes, GINS is a tetrameric arrangement of four subunits Sld5, Psf1, Psf2 and Psf3, while in archaea, it consists of two different proteins named Gins51 and Gins23. The archaeal GINS complex can be either an alpha2beta2-type heterotetramer composed of Gins51 and Gins23, or a Gins51-only alpha4-type homotetramer. All GINS subunits are homologous and consist of two domains, called the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1/Gins51 are permuted with respect to Psf1/Psf3/Gins23. The overall tetrameric assemblies of GINS are similar, but the relative locations of the C-terminal small domains are different with respect to the alpha-helical domain, resulting in different subunit contacts. However, the basic function of GINS in DNA replication is conserved across eukaryotes and archaea. This model represents the beta-strand domain (B-domain) of GINS complex proteins.


Pssm-ID: 412027  Cd Length: 49  Bit Score: 53.62  E-value: 6.04e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1776177581  92 LVTIVPSFSMDRVHLIG-GDLGPFNPGLPVEVPVWLAINLKQRQKCRLI 139
Cdd:cd21396     1 KVAVRVEKDLPRILAEFaETVGPFPKGSQVEVPLWLARGLVQRGALRLI 49
PTZ00362 PTZ00362
hypothetical protein; Provisional
 88-238 4.03e-04

hypothetical protein; Provisional


Pssm-ID: 240380 [Multi-domain]  Cd Length: 479  Bit Score: 41.28  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581  88 AEKELVTI-----VPSFSMDRVHliGGDLGPFNPGLPVEVPVWLAINLKQRQKCRLIPPEWMDVEKLEEIRDQERKE-DT 161
Cdd:PTZ00362  282 ALDELVVVkalvdIPYIDLSEIE--GFDFKEMKSGERQWLPIYIAKELSHFGLVTVEFPFWFYIKNLKNIYEREFEDqNE 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776177581 162 FTPMPSPYYMELTKLLLN---YASDNIPKADEIRT----------LVKDTWDTRMAKLRLSADSFvRQQEAHAKLDNLTL 228
Cdd:PTZ00362  360 LTDLPSPYFFEISSMFLEnniFKKVTPIETIGQRTvykyiskvagLVEDIRYKRLKKIMNHLENQ-DVHSSIIYIDNLQI 438

                         170
                  ....*....|
gi 1776177581 229 MEINTIGTFL 238
Cdd:PTZ00362  439 SETYCVNQLL 448
 
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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