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Conserved domains on  [gi|15226451|ref|NP_179702|]
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glycine-rich protein 2B [Arabidopsis thaliana]

Protein Classification

cold shock domain-containing protein; zinc finger CCHC domain-containing protein( domain architecture ID 13626150)

cold shock domain-containing protein similar to mammalian Y-box-binding proteins, which are DNA- and RNA-binding proteins involved in various processes, such as translational repression, RNA stabilization, mRNA splicing, DNA repair and transcription regulation| zinc finger CCHC (ZCCHC) domain-containing protein with a retrotransposon gag domain, contains a zinc knuckle or a zinc binding motif, CX2CX4HX4C, where X can be any amino acid, and may bind single-stranded RNA; similar to Pyrenophora graminea gag protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CSD pfam00313
'Cold-shock' DNA-binding domain;
15-81 4.49e-28

'Cold-shock' DNA-binding domain;


:

Pssm-ID: 278729  Cd Length: 66  Bit Score: 100.39  E-value: 4.49e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226451    15 RKGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVeVDNSGRPKAIEVSGP 81
Cdd:pfam00313   1 MTGTVKWFNAKKGFGFITPEDGDKDVFVHFSAIQGDGFRSLQEGQKVEFEV-VEGTKGPQAANVTKP 66
PTZ00368 super family cl31762
universal minicircle sequence binding protein (UMSBP); Provisional
 135-198 9.04e-09

universal minicircle sequence binding protein (UMSBP); Provisional


The actual alignment was detected with superfamily member PTZ00368:

Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 52.12  E-value: 9.04e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226451  135 DNSCFKCGEPGHMARECSQggggysggggggrygsgggGGGGGGGLSCYSCGESGHFARDCTSG 198
Cdd:PTZ00368  52 ERSCYNCGKTGHLSRECPE-------------------APPGSGPRSCYNCGQTGHISRECPNR 96
 
Name Accession Description Interval E-value
CSD pfam00313
'Cold-shock' DNA-binding domain;
15-81 4.49e-28

'Cold-shock' DNA-binding domain;


Pssm-ID: 278729  Cd Length: 66  Bit Score: 100.39  E-value: 4.49e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226451    15 RKGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVeVDNSGRPKAIEVSGP 81
Cdd:pfam00313   1 MTGTVKWFNAKKGFGFITPEDGDKDVFVHFSAIQGDGFRSLQEGQKVEFEV-VEGTKGPQAANVTKP 66
CSP_CDS cd04458
Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in ...
 15-80 7.82e-25

Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in eukaryotes, prokaryotes, and archaea. CSP's include the major cold-shock proteins CspA and CspB in bacteria and the eukaryotic gene regulatory factor Y-box protein. CSP expression is up-regulated by an abrupt drop in growth temperature. CSP's are also expressed under normal condition at lower level. The function of cold-shock proteins is not fully understood. They preferentially bind poly-pyrimidine region of single-stranded RNA and DNA. CSP's are thought to bind mRNA and regulate ribosomal translation, mRNA degradation, and the rate of transcription termination. The human Y-box protein, which contains a CSD, regulates transcription and translation of genes that contain the Y-box sequence in their promoters. This specific ssDNA-binding properties of CSD are required for the binding of Y-box protein to the promoter's Y-box sequence, thereby regulating transcription.


Pssm-ID: 239905  Cd Length: 65  Bit Score: 91.87  E-value: 7.82e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226451  15 RKGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVEVDNsGRPKAIEVSG 80
Cdd:cd04458   1 VTGTVKWFDDEKGFGFITPDDGGEDVFVHISALEGDGFRSLEEGDRVEFELEEGD-KGPQAVNVRL 65
CspC COG1278
Cold shock protein, CspA family [Transcription];
14-78 1.43e-24

Cold shock protein, CspA family [Transcription];


Pssm-ID: 440889  Cd Length: 67  Bit Score: 91.41  E-value: 1.43e-24
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226451  14 RRKGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVEVDNSGrPKAIEV 78
Cdd:COG1278   1 MATGTVKWFNAEKGFGFITPDDGGEDVFVHISALQRSGFRTLREGQRVEFEVEQGDKG-PQAVNV 64
cspE PRK09507
cold shock-like protein CspE;
16-78 5.80e-19

cold shock-like protein CspE;


Pssm-ID: 169931  Cd Length: 69  Bit Score: 77.00  E-value: 5.80e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226451   16 KGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVeVDNSGRPKAIEV 78
Cdd:PRK09507   5 KGNVKWFNESKGFGFITPEDGSKDVFVHFSAIQTNGFKTLAEGQRVEFEI-TNGAKGPSAANV 66
CSP smart00357
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ...
 16-81 1.96e-15

Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria and is involved in regulating translation in eukaryotes. Contains sub-family of RNA-binding domains in the Rho transcription termination factor.


Pssm-ID: 214633 [Multi-domain]  Cd Length: 64  Bit Score: 67.62  E-value: 1.96e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226451     16 KGTVKWFDtqKGFGFITPSDGGDDLFVHQSSIRSeGFRSLAAEESVEFDVEVDNS-GRPKAIEVSGP 81
Cdd:smart00357   1 TGVVKWFN--KGFGFIRPDDGGKDVFVHPSQIQG-GLKSLREGDEVEFKVVSPEGgEKPEAENVVKL 64
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 135-198 9.04e-09

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 52.12  E-value: 9.04e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226451  135 DNSCFKCGEPGHMARECSQggggysggggggrygsgggGGGGGGGLSCYSCGESGHFARDCTSG 198
Cdd:PTZ00368  52 ERSCYNCGKTGHLSRECPE-------------------APPGSGPRSCYNCGQTGHISRECPNR 96
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 136-153 4.65e-04

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 36.35  E-value: 4.65e-04
                          10
                  ....*....|....*...
gi 15226451   136 NSCFKCGEPGHMARECSQ 153
Cdd:pfam00098   1 GKCYNCGEPGHIARDCPK 18
ZnF_C2HC smart00343
zinc finger;
138-151 2.26e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 34.34  E-value: 2.26e-03
                           10
                   ....*....|....
gi 15226451    138 CFKCGEPGHMAREC 151
Cdd:smart00343   2 CYNCGKEGHIARDC 15
AIR1 COG5082
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ...
 138-195 5.31e-03

Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


Pssm-ID: 227414 [Multi-domain]  Cd Length: 190  Bit Score: 36.37  E-value: 5.31e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15226451 138 CFKCGEPGHMARECSQGGGGYSGGGGGGRYGSGGGGGggggglsCYSCGESGHFARDC 195
Cdd:COG5082  63 CFNCGQNGHLRRDCPHSICYNCSWDGHRSNHCPKPKK-------CYNCGETGHLSRDC 113
 
Name Accession Description Interval E-value
CSD pfam00313
'Cold-shock' DNA-binding domain;
15-81 4.49e-28

'Cold-shock' DNA-binding domain;


Pssm-ID: 278729  Cd Length: 66  Bit Score: 100.39  E-value: 4.49e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226451    15 RKGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVeVDNSGRPKAIEVSGP 81
Cdd:pfam00313   1 MTGTVKWFNAKKGFGFITPEDGDKDVFVHFSAIQGDGFRSLQEGQKVEFEV-VEGTKGPQAANVTKP 66
CSP_CDS cd04458
Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in ...
 15-80 7.82e-25

Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in eukaryotes, prokaryotes, and archaea. CSP's include the major cold-shock proteins CspA and CspB in bacteria and the eukaryotic gene regulatory factor Y-box protein. CSP expression is up-regulated by an abrupt drop in growth temperature. CSP's are also expressed under normal condition at lower level. The function of cold-shock proteins is not fully understood. They preferentially bind poly-pyrimidine region of single-stranded RNA and DNA. CSP's are thought to bind mRNA and regulate ribosomal translation, mRNA degradation, and the rate of transcription termination. The human Y-box protein, which contains a CSD, regulates transcription and translation of genes that contain the Y-box sequence in their promoters. This specific ssDNA-binding properties of CSD are required for the binding of Y-box protein to the promoter's Y-box sequence, thereby regulating transcription.


Pssm-ID: 239905  Cd Length: 65  Bit Score: 91.87  E-value: 7.82e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226451  15 RKGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVEVDNsGRPKAIEVSG 80
Cdd:cd04458   1 VTGTVKWFDDEKGFGFITPDDGGEDVFVHISALEGDGFRSLEEGDRVEFELEEGD-KGPQAVNVRL 65
CspC COG1278
Cold shock protein, CspA family [Transcription];
14-78 1.43e-24

Cold shock protein, CspA family [Transcription];


Pssm-ID: 440889  Cd Length: 67  Bit Score: 91.41  E-value: 1.43e-24
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226451  14 RRKGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVEVDNSGrPKAIEV 78
Cdd:COG1278   1 MATGTVKWFNAEKGFGFITPDDGGEDVFVHISALQRSGFRTLREGQRVEFEVEQGDKG-PQAVNV 64
cspE PRK09507
cold shock-like protein CspE;
16-78 5.80e-19

cold shock-like protein CspE;


Pssm-ID: 169931  Cd Length: 69  Bit Score: 77.00  E-value: 5.80e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226451   16 KGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVeVDNSGRPKAIEV 78
Cdd:PRK09507   5 KGNVKWFNESKGFGFITPEDGSKDVFVHFSAIQTNGFKTLAEGQRVEFEI-TNGAKGPSAANV 66
PRK09937 PRK09937
cold shock-like protein CspD;
16-78 1.69e-17

cold shock-like protein CspD;


Pssm-ID: 77494  Cd Length: 74  Bit Score: 73.23  E-value: 1.69e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226451   16 KGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVEVDNSGRPKAIEV 78
Cdd:PRK09937   3 KGTVKWFNNAKGFGFICPEGGGEDIFAHYSTIQMDGYRTLKAGQSVQFDVHQGPKGNHASVIV 65
PRK10943 PRK10943
cold shock-like protein CspC; Provisional
 16-79 3.13e-16

cold shock-like protein CspC; Provisional


Pssm-ID: 170841  Cd Length: 69  Bit Score: 70.10  E-value: 3.13e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226451   16 KGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVEvDNSGRPKAIEVS 79
Cdd:PRK10943   5 KGQVKWFNESKGFGFITPADGSKDVFVHFSAIQGNGFKTLAEGQNVEFEIQ-DGQKGPAAVNVT 67
PRK09890 PRK09890
cold shock protein CspG; Provisional
 13-78 4.17e-16

cold shock protein CspG; Provisional


Pssm-ID: 77467  Cd Length: 70  Bit Score: 69.79  E-value: 4.17e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226451   13 DRRKGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVEVDNSGrPKAIEV 78
Cdd:PRK09890   3 NKMTGLVKWFNADKGFGFITPDDGSKDVFVHFTAIQSNEFRTLNENQKVEFSIEQGQRG-PAAANV 67
PRK10354 PRK10354
RNA chaperone/antiterminator CspA;
13-79 1.83e-15

RNA chaperone/antiterminator CspA;


Pssm-ID: 182402  Cd Length: 70  Bit Score: 68.08  E-value: 1.83e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226451   13 DRRKGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVEVDNSGrPKAIEVS 79
Cdd:PRK10354   3 GKMTGIVKWFNADKGFGFITPDDGSKDVFVHFSAIQNDGYKSLDEGQKVSFTIESGAKG-PAAGNVT 68
CSP smart00357
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ...
 16-81 1.96e-15

Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria and is involved in regulating translation in eukaryotes. Contains sub-family of RNA-binding domains in the Rho transcription termination factor.


Pssm-ID: 214633 [Multi-domain]  Cd Length: 64  Bit Score: 67.62  E-value: 1.96e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226451     16 KGTVKWFDtqKGFGFITPSDGGDDLFVHQSSIRSeGFRSLAAEESVEFDVEVDNS-GRPKAIEVSGP 81
Cdd:smart00357   1 TGVVKWFN--KGFGFIRPDDGGKDVFVHPSQIQG-GLKSLREGDEVEFKVVSPEGgEKPEAENVVKL 64
PRK14998 PRK14998
cold shock-like protein CspD; Provisional
 17-78 7.29e-15

cold shock-like protein CspD; Provisional


Pssm-ID: 184960  Cd Length: 73  Bit Score: 66.61  E-value: 7.29e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226451   17 GTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEFDVEVDNSGRPKAIEV 78
Cdd:PRK14998   4 GTVKWFNNAKGFGFICPEGGGEDIFAHYSTIQMDGYRTLKAGQSVRFDVHQGPKGNHASVIV 65
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 135-198 9.04e-09

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 52.12  E-value: 9.04e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226451  135 DNSCFKCGEPGHMARECSQggggysggggggrygsgggGGGGGGGLSCYSCGESGHFARDCTSG 198
Cdd:PTZ00368  52 ERSCYNCGKTGHLSRECPE-------------------APPGSGPRSCYNCGQTGHISRECPNR 96
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 136-197 6.35e-07

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 47.11  E-value: 6.35e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226451  136 NSCFKCGEPGHMARECSQGGGGYSGGGGggrygsgggggggggglSCYSCGESGHFARDCTS 197
Cdd:PTZ00368   1 MVCYRCGGVGHQSRECPNSAPAGAAKAR-----------------PCYKCGEPGHLSRECPS 45
PRK15463 PRK15463
cold shock-like protein CspF; Provisional
 13-63 2.08e-06

cold shock-like protein CspF; Provisional


Pssm-ID: 185360  Cd Length: 70  Bit Score: 43.74  E-value: 2.08e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15226451   13 DRRKGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEF 63
Cdd:PRK15463   3 RKMTGIVKTFDGKSGKGLITPSDGRKDVQVHISALNLRDAEELTTGLRVEF 53
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 135-197 7.01e-06

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 44.03  E-value: 7.01e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226451  135 DNSCFKCGEPGHMARECSQGGGGYSGGGgggrygsgggggggggglSCYSCGESGHFARDCTS 197
Cdd:PTZ00368 103 RRACYNCGGEGHISRDCPNAGKRPGGDK------------------TCYNCGQTGHLSRDCPD 147
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 136-153 4.65e-04

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 36.35  E-value: 4.65e-04
                          10
                  ....*....|....*...
gi 15226451   136 NSCFKCGEPGHMARECSQ 153
Cdd:pfam00098   1 GKCYNCGEPGHIARDCPK 18
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 182-197 9.05e-04

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 35.58  E-value: 9.05e-04
                          10
                  ....*....|....*.
gi 15226451   182 CYSCGESGHFARDCTS 197
Cdd:pfam00098   3 CYNCGEPGHIARDCPK 18
PRK15464 PRK15464
cold shock-like protein CspH; Provisional
 14-63 9.52e-04

cold shock-like protein CspH; Provisional


Pssm-ID: 185361  Cd Length: 70  Bit Score: 36.61  E-value: 9.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 15226451   14 RRKGTVKWFDTQKGFGFITPSDGGDDLFVHQSSIRSEGFRSLAAEESVEF 63
Cdd:PRK15464   4 KMTGIVKTFDRKSGKGFIIPSDGRKEVQVHISAFTPRDAEVLIPGLRVEF 53
ZnF_C2HC smart00343
zinc finger;
138-151 2.26e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 34.34  E-value: 2.26e-03
                           10
                   ....*....|....
gi 15226451    138 CFKCGEPGHMAREC 151
Cdd:smart00343   2 CYNCGKEGHIARDC 15
AIR1 COG5082
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ...
 138-195 5.31e-03

Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


Pssm-ID: 227414 [Multi-domain]  Cd Length: 190  Bit Score: 36.37  E-value: 5.31e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15226451 138 CFKCGEPGHMARECSQGGGGYSGGGGGGRYGSGGGGGggggglsCYSCGESGHFARDC 195
Cdd:COG5082  63 CFNCGQNGHLRRDCPHSICYNCSWDGHRSNHCPKPKK-------CYNCGETGHLSRDC 113
ZnF_C2HC smart00343
zinc finger;
182-197 5.40e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 33.19  E-value: 5.40e-03
                           10
                   ....*....|....*.
gi 15226451    182 CYSCGESGHFARDCTS 197
Cdd:smart00343   2 CYNCGKEGHIARDCPS 17
 
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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