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Conserved domains on  [gi|1609559069|ref|NP_001356404|]
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nuclear factor 1 B-type isoform 22 [Homo sapiens]

Protein Classification

nuclear factor I( domain architecture ID 12106880)

nuclear factor I (NFI) is a CCAAT-box-binding protein active in transcription and DNA replication

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CTF_NFI super family cl25839
CTF/NF-I family transcription modulation region;
134-341 1.81e-82

CTF/NF-I family transcription modulation region;


The actual alignment was detected with superfamily member pfam00859:

Pssm-ID: 459967 [Multi-domain]  Cd Length: 288  Bit Score: 254.45  E-value: 1.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609559069 134 EDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSqPYYHDMNSGVNLQRSLSSPPS--SKRPKTISIDENMEPSPT 211
Cdd:pfam00859   1 QDSFVTSGVFSVTELVRVSRTPVATGTGPNFSLGELQG-PLYYDLNPGVGLRRSLPSTSSsgSKRHKSGSMEDDVDTSPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609559069 212 GDFYPSPSSPAAGSRTW-HERDQDMSSPTTMKKPEKPLFSSASPQDSSPRLSTFPQHHHPGIpgVAHSVIStRTPPPPSP 290
Cdd:pfam00859  80 GDYYRSPSSPASSSRNWpHDVEGGMSSPVKKKKPDKSDFSSPSPQDSSPRLMAFTQHHRPVI--AVHSGIS-RSPHPSSA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1609559069 291 LPFPTQAILpPAPSSYFSHPTIRYPPHLnPQDTLKNYVP--SYDPSSPQTSQL 341
Cdd:pfam00859 157 LHFPSSSIL-QQPSSYFPHPAIRYPPHL-PQDPLKDLVSlaCYDPSSQQPSQP 207
NfI_DNAbd_pre-N pfam10524
Nuclear factor I protein pre-N-terminus; The Nuclear factor I (NFI) family of site-specific ...
 10-47 8.67e-19

Nuclear factor I protein pre-N-terminus; The Nuclear factor I (NFI) family of site-specific DNA-binding proteins (also known as CTF or CAAT box transcription factor) functions both in viral DNA replication and in the regulation of gene expression in higher organizms. The N-terminal 200 residues contains the DNA-binding and dimerization domain, but also has an 8-47 residue highly conserved region 5' of this, whose function is not known. Deletion of the N-terminal 200 amino acids removes the DNA-binding activity, dimerization-ability and the stimulation of adenovirus DNA replication.


:

Pssm-ID: 463134  Cd Length: 41  Bit Score: 79.19  E-value: 8.67e-19
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1609559069  10 QDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEK 47
Cdd:pfam10524   4 QEDFHPFIEALLPYVKAFAYTWFNLQAAKRRHYKKHDK 41
MH1 super family cl00055
N-terminal Mad Homology 1 (MH1) domain; The MH1 is a small DNA-binding domain present in SMAD ...
 68-120 1.21e-04

N-terminal Mad Homology 1 (MH1) domain; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. Receptor-regulated SMAD proteins (R-SMADs, including SMAD1, SMAD2, SMAD3, SMAD5, and SMAD9) are activated by phosphorylation by transforming growth factor (TGF)-beta type I receptors. The active R-SMAD associates with a common mediator SMAD (Co-SMAD or SMAD4) and other cofactors, which together translocate to the nucleus to regulate gene expression. The inhibitory or antagonistic SMADs (I-SMADs, including SMAD6 and SMAD7) negatively regulate TGF-beta signaling by competing with R-SMADs for type I receptor or Co-SMADs. MH1 domains of R-SMAD and SMAD4 contain a nuclear localization signal as well as DNA-binding activity. The activated R-SMAD/SMAD4 complex then binds with very low affinity to a DNA sequence CAGAC called SMAD-binding element (SBE) via the MH1 domain.


The actual alignment was detected with superfamily member smart00523:

Pssm-ID: 469592  Cd Length: 109  Bit Score: 41.21  E-value: 1.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1609559069   68 IKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPC--CVLSNPDQK----DSGQSGSP 120
Cdd:smart00523   1 VEEKWAKKATESLLKKLKKKQLEELLQAVESKGGPPtrCVLIPRSLDgrlqVAHRKGLP 59
PRK15127 super family cl39118
multidrug efflux RND transporter permease subunit AcrB;
310-400 2.37e-04

multidrug efflux RND transporter permease subunit AcrB;


The actual alignment was detected with superfamily member PRK15127:

Pssm-ID: 185081 [Multi-domain]  Cd Length: 1049  Bit Score: 43.35  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609559069  310 PTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQLRICDWTMNQNGRHLYPSTSEDTLG-----ITWQSpGTWASLVPFQVSN 384
Cdd:PRK15127    31 PVAQYPTIAPPAVTISASYPGADAKTVQDTVTQVIEQNMNGIDNLMYMSSNSDSTGtvqitLTFES-GTDADIAQVQVQN 109

                           90       100
                   ....*....|....*....|
gi 1609559069  385 R----TPILPANVQNYGLNI 400
Cdd:PRK15127   110 KlqlaMPLLPQEVQQQGVSV 129
 
Name Accession Description Interval E-value
CTF_NFI pfam00859
CTF/NF-I family transcription modulation region;
134-341 1.81e-82

CTF/NF-I family transcription modulation region;


Pssm-ID: 459967 [Multi-domain]  Cd Length: 288  Bit Score: 254.45  E-value: 1.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609559069 134 EDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSqPYYHDMNSGVNLQRSLSSPPS--SKRPKTISIDENMEPSPT 211
Cdd:pfam00859   1 QDSFVTSGVFSVTELVRVSRTPVATGTGPNFSLGELQG-PLYYDLNPGVGLRRSLPSTSSsgSKRHKSGSMEDDVDTSPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609559069 212 GDFYPSPSSPAAGSRTW-HERDQDMSSPTTMKKPEKPLFSSASPQDSSPRLSTFPQHHHPGIpgVAHSVIStRTPPPPSP 290
Cdd:pfam00859  80 GDYYRSPSSPASSSRNWpHDVEGGMSSPVKKKKPDKSDFSSPSPQDSSPRLMAFTQHHRPVI--AVHSGIS-RSPHPSSA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1609559069 291 LPFPTQAILpPAPSSYFSHPTIRYPPHLnPQDTLKNYVP--SYDPSSPQTSQL 341
Cdd:pfam00859 157 LHFPSSSIL-QQPSSYFPHPAIRYPPHL-PQDPLKDLVSlaCYDPSSQQPSQP 207
NfI_DNAbd_pre-N pfam10524
Nuclear factor I protein pre-N-terminus; The Nuclear factor I (NFI) family of site-specific ...
 10-47 8.67e-19

Nuclear factor I protein pre-N-terminus; The Nuclear factor I (NFI) family of site-specific DNA-binding proteins (also known as CTF or CAAT box transcription factor) functions both in viral DNA replication and in the regulation of gene expression in higher organizms. The N-terminal 200 residues contains the DNA-binding and dimerization domain, but also has an 8-47 residue highly conserved region 5' of this, whose function is not known. Deletion of the N-terminal 200 amino acids removes the DNA-binding activity, dimerization-ability and the stimulation of adenovirus DNA replication.


Pssm-ID: 463134  Cd Length: 41  Bit Score: 79.19  E-value: 8.67e-19
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1609559069  10 QDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEK 47
Cdd:pfam10524   4 QEDFHPFIEALLPYVKAFAYTWFNLQAAKRRHYKKHDK 41
DWA smart00523
Domain A in dwarfin family proteins;
68-120 1.21e-04

Domain A in dwarfin family proteins;


Pssm-ID: 214708  Cd Length: 109  Bit Score: 41.21  E-value: 1.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1609559069   68 IKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPC--CVLSNPDQK----DSGQSGSP 120
Cdd:smart00523   1 VEEKWAKKATESLLKKLKKKQLEELLQAVESKGGPPtrCVLIPRSLDgrlqVAHRKGLP 59
PRK15127 PRK15127
multidrug efflux RND transporter permease subunit AcrB;
310-400 2.37e-04

multidrug efflux RND transporter permease subunit AcrB;


Pssm-ID: 185081 [Multi-domain]  Cd Length: 1049  Bit Score: 43.35  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609559069  310 PTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQLRICDWTMNQNGRHLYPSTSEDTLG-----ITWQSpGTWASLVPFQVSN 384
Cdd:PRK15127    31 PVAQYPTIAPPAVTISASYPGADAKTVQDTVTQVIEQNMNGIDNLMYMSSNSDSTGtvqitLTFES-GTDADIAQVQVQN 109

                           90       100
                   ....*....|....*....|
gi 1609559069  385 R----TPILPANVQNYGLNI 400
Cdd:PRK15127   110 KlqlaMPLLPQEVQQQGVSV 129
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 190-339 1.43e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609559069 190 SPPSSKRPKTISIDEnmepSPTGDFYP-SPSSPAAGSR-TWHERDQDMSSPTTMKKPEKPlfssASPQDSSPRLSTFPQH 267
Cdd:PTZ00449  608 RPKSPKLPELLDIPK----SPKRPESPkSPKRPPPPQRpSSPERPEGPKIIKSPKPPKSP----KPPFDPKFKEKFYDDY 679

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609559069 268 hhpgIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPtiRYPPHLNPQDTLKNYVPSYDPSSPQTS 339
Cdd:PTZ00449  680 ----LDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTP--RPLPPKLPRDEEFPFEPIGDPDAEQPD 745
 
Name Accession Description Interval E-value
CTF_NFI pfam00859
CTF/NF-I family transcription modulation region;
134-341 1.81e-82

CTF/NF-I family transcription modulation region;


Pssm-ID: 459967 [Multi-domain]  Cd Length: 288  Bit Score: 254.45  E-value: 1.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609559069 134 EDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSqPYYHDMNSGVNLQRSLSSPPS--SKRPKTISIDENMEPSPT 211
Cdd:pfam00859   1 QDSFVTSGVFSVTELVRVSRTPVATGTGPNFSLGELQG-PLYYDLNPGVGLRRSLPSTSSsgSKRHKSGSMEDDVDTSPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609559069 212 GDFYPSPSSPAAGSRTW-HERDQDMSSPTTMKKPEKPLFSSASPQDSSPRLSTFPQHHHPGIpgVAHSVIStRTPPPPSP 290
Cdd:pfam00859  80 GDYYRSPSSPASSSRNWpHDVEGGMSSPVKKKKPDKSDFSSPSPQDSSPRLMAFTQHHRPVI--AVHSGIS-RSPHPSSA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1609559069 291 LPFPTQAILpPAPSSYFSHPTIRYPPHLnPQDTLKNYVP--SYDPSSPQTSQL 341
Cdd:pfam00859 157 LHFPSSSIL-QQPSSYFPHPAIRYPPHL-PQDPLKDLVSlaCYDPSSQQPSQP 207
NfI_DNAbd_pre-N pfam10524
Nuclear factor I protein pre-N-terminus; The Nuclear factor I (NFI) family of site-specific ...
 10-47 8.67e-19

Nuclear factor I protein pre-N-terminus; The Nuclear factor I (NFI) family of site-specific DNA-binding proteins (also known as CTF or CAAT box transcription factor) functions both in viral DNA replication and in the regulation of gene expression in higher organizms. The N-terminal 200 residues contains the DNA-binding and dimerization domain, but also has an 8-47 residue highly conserved region 5' of this, whose function is not known. Deletion of the N-terminal 200 amino acids removes the DNA-binding activity, dimerization-ability and the stimulation of adenovirus DNA replication.


Pssm-ID: 463134  Cd Length: 41  Bit Score: 79.19  E-value: 8.67e-19
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1609559069  10 QDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEK 47
Cdd:pfam10524   4 QEDFHPFIEALLPYVKAFAYTWFNLQAAKRRHYKKHDK 41
DWA smart00523
Domain A in dwarfin family proteins;
68-120 1.21e-04

Domain A in dwarfin family proteins;


Pssm-ID: 214708  Cd Length: 109  Bit Score: 41.21  E-value: 1.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1609559069   68 IKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPC--CVLSNPDQK----DSGQSGSP 120
Cdd:smart00523   1 VEEKWAKKATESLLKKLKKKQLEELLQAVESKGGPPtrCVLIPRSLDgrlqVAHRKGLP 59
PRK15127 PRK15127
multidrug efflux RND transporter permease subunit AcrB;
310-400 2.37e-04

multidrug efflux RND transporter permease subunit AcrB;


Pssm-ID: 185081 [Multi-domain]  Cd Length: 1049  Bit Score: 43.35  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609559069  310 PTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQLRICDWTMNQNGRHLYPSTSEDTLG-----ITWQSpGTWASLVPFQVSN 384
Cdd:PRK15127    31 PVAQYPTIAPPAVTISASYPGADAKTVQDTVTQVIEQNMNGIDNLMYMSSNSDSTGtvqitLTFES-GTDADIAQVQVQN 109

                           90       100
                   ....*....|....*....|
gi 1609559069  385 R----TPILPANVQNYGLNI 400
Cdd:PRK15127   110 KlqlaMPLLPQEVQQQGVSV 129
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 190-339 1.43e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609559069 190 SPPSSKRPKTISIDEnmepSPTGDFYP-SPSSPAAGSR-TWHERDQDMSSPTTMKKPEKPlfssASPQDSSPRLSTFPQH 267
Cdd:PTZ00449  608 RPKSPKLPELLDIPK----SPKRPESPkSPKRPPPPQRpSSPERPEGPKIIKSPKPPKSP----KPPFDPKFKEKFYDDY 679

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609559069 268 hhpgIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPtiRYPPHLNPQDTLKNYVPSYDPSSPQTS 339
Cdd:PTZ00449  680 ----LDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTP--RPLPPKLPRDEEFPFEPIGDPDAEQPD 745
Enamelin pfam15362
Enamelin; ENAMELIN is involved in the mineralization and structural organization of enamel. It ...
 214-254 1.95e-03

Enamelin; ENAMELIN is involved in the mineralization and structural organization of enamel. It is necessary for the extension of enamel during the secretory stage of dental enamel formation. The proteins are expressed in teeth, particularly in odontoblasts, ameloblasts and cementoblasts.


Pssm-ID: 464672 [Multi-domain]  Cd Length: 907  Bit Score: 40.58  E-value: 1.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1609559069 214 FYPSPSSPAAGSRTWHERDQdmsSPTTMKKPEKPLFSSASP 254
Cdd:pfam15362 393 YDPRENSPYLRSNTWDERDD---SPNTMGQPENPLYPMNTP 430
 
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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