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Conserved domains on  [gi|665821191|ref|NP_001287878|]
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zinc finger protein 101 isoform 2 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 1000026)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  11361095|22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5048 super family cl34881
FOG: Zn-finger [General function prediction only];
117-290 6.05e-04

FOG: Zn-finger [General function prediction only];


The actual alignment was detected with superfamily member COG5048:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821191 117 PSLFQIHVRTHTG-EKPYKCKQCGKAFISAGYLRTHE-IRSHALE--KSHQC--QECGKKLSCSSSLHRHERTHSGGKLY 190
Cdd:COG5048  273 SSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrSVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPA 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821191 191 EC--QKCAKVF------RCPTSLQAHERAHTgERPYEC--NKCGKTFNYPSCFRRHKKTHSGEKPYEC--TRCGKAFGWC 258
Cdd:COG5048  353 KEklLNSSSKFspllnnEPPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRH 431

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 665821191 259 SSLRRHEMTHTGEKPFDCKQCGKVF---TFSNYLR 290
Cdd:COG5048  432 YNLIPHKKIHTNHAPLLCSILKSFRrdlDLSNHGK 466
lambda-1 super family cl17035
inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays ...
 29-89 2.38e-03

inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses.


The actual alignment was detected with superfamily member cd11674:

Pssm-ID: 212564  Cd Length: 1166  Bit Score: 39.76  E-value: 2.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665821191   29 ASISPSSGARrtVTPTRKRPYECKVCGKAFNSPNLFQIHQRT-H-----TGKRSYKCREIVRAFTVS 89
Cdd:cd11674    56 AVISPPQSKK--ATPINPSSYVCNVCMAEFSSMDQLAEHQRTtHsigasSLLTSPAINQAIESFLTS 120
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
117-290 6.05e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821191 117 PSLFQIHVRTHTG-EKPYKCKQCGKAFISAGYLRTHE-IRSHALE--KSHQC--QECGKKLSCSSSLHRHERTHSGGKLY 190
Cdd:COG5048  273 SSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrSVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPA 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821191 191 EC--QKCAKVF------RCPTSLQAHERAHTgERPYEC--NKCGKTFNYPSCFRRHKKTHSGEKPYEC--TRCGKAFGWC 258
Cdd:COG5048  353 KEklLNSSSKFspllnnEPPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRH 431

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 665821191 259 SSLRRHEMTHTGEKPFDCKQCGKVF---TFSNYLR 290
Cdd:COG5048  432 YNLIPHKKIHTNHAPLLCSILKSFRrdlDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
120-144 1.97e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 1.97e-03
                          10        20
                  ....*....|....*....|....*
gi 665821191  120 FQIHVRTHTGEKPYKCKQCGKAFIS 144
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
lambda-1 cd11674
inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays ...
 29-89 2.38e-03

inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses.


Pssm-ID: 212564  Cd Length: 1166  Bit Score: 39.76  E-value: 2.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665821191   29 ASISPSSGARrtVTPTRKRPYECKVCGKAFNSPNLFQIHQRT-H-----TGKRSYKCREIVRAFTVS 89
Cdd:cd11674    56 AVISPPQSKK--ATPINPSSYVCNVCMAEFSSMDQLAEHQRTtHsigasSLLTSPAINQAIESFLTS 120
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
117-290 6.05e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821191 117 PSLFQIHVRTHTG-EKPYKCKQCGKAFISAGYLRTHE-IRSHALE--KSHQC--QECGKKLSCSSSLHRHERTHSGGKLY 190
Cdd:COG5048  273 SSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrSVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPA 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821191 191 EC--QKCAKVF------RCPTSLQAHERAHTgERPYEC--NKCGKTFNYPSCFRRHKKTHSGEKPYEC--TRCGKAFGWC 258
Cdd:COG5048  353 KEklLNSSSKFspllnnEPPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRH 431

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 665821191 259 SSLRRHEMTHTGEKPFDCKQCGKVF---TFSNYLR 290
Cdd:COG5048  432 YNLIPHKKIHTNHAPLLCSILKSFRrdlDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
120-144 1.97e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 1.97e-03
                          10        20
                  ....*....|....*....|....*
gi 665821191  120 FQIHVRTHTGEKPYKCKQCGKAFIS 144
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
lambda-1 cd11674
inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays ...
 29-89 2.38e-03

inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses.


Pssm-ID: 212564  Cd Length: 1166  Bit Score: 39.76  E-value: 2.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665821191   29 ASISPSSGARrtVTPTRKRPYECKVCGKAFNSPNLFQIHQRT-H-----TGKRSYKCREIVRAFTVS 89
Cdd:cd11674    56 AVISPPQSKK--ATPINPSSYVCNVCMAEFSSMDQLAEHQRTtHsigasSLLTSPAINQAIESFLTS 120
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
216-287 2.60e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.29  E-value: 2.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665821191 216 RPYECNKCGKTFNYPSCFRRHKKTHSGEKPYECTR--CGKAFGWCSSLRRHEMTHTGEKPFDCKQCGKVFTFSN 287
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKA 105
zf-H2C2_2 pfam13465
Zinc-finger double domain;
260-284 3.70e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 3.70e-03
                          10        20
                  ....*....|....*....|....*
gi 665821191  260 SLRRHEMTHTGEKPFDCKQCGKVFT 284
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
233-255 9.32e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.11  E-value: 9.32e-03
                          10        20
                  ....*....|....*....|...
gi 665821191  233 FRRHKKTHSGEKPYECTRCGKAF 255
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
 
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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