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NIFSL_ASFB7
ID   NIFSL_ASFB7             Reviewed;         383 AA.
AC   Q65192;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=NifS-like protein;
GN   OrderedLocusNames=Ba71V-124; ORFNames=QP383R;
OS   African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10498;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA   Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA   Rodriguez J.F., Vinuela E.;
RT   "Analysis of the complete nucleotide sequence of African swine fever
RT   virus.";
RL   Virology 208:249-278(1995).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA   Alejo A., Matamoros T., Guerra M., Andres G.;
RT   "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL   J. Virol. 92:0-0(2018).
RN   [3]
RP   INDUCTION.
RX   PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA   Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA   Dixon L., Werner F.;
RT   "The African Swine Fever Virus Transcriptome.";
RL   J. Virol. 94:0-0(2020).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P0A6B9};
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30185597}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:32075923}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
CC   -!- CAUTION: Although related to the NifS/IscS subfamily, lacks the
CC       conserved active site, suggesting it has no transferase activity.
CC       {ECO:0000305}.
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DR   EMBL; U18466; AAA65352.1; -; Genomic_DNA.
DR   RefSeq; NP_042816.1; NC_001659.2.
DR   SMR; Q65192; -.
DR   GeneID; 22220353; -.
DR   KEGG; vg:22220353; -.
DR   Proteomes; UP000000624; Genome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   2: Evidence at transcript level;
KW   Late protein; Pyridoxal phosphate; Reference proteome; Virion.
FT   CHAIN           1..383
FT                   /note="NifS-like protein"
FT                   /id="PRO_0000373143"
FT   BINDING         58..59
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         184..186
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ   SEQUENCE   383 AA;  42519 MW;  E4C33FFC6FDAEE1F CRC64;
     MASILALDGL YAEVPKFLPE ALREGCAGKN PLSFYIQQIL NLMGCDGNEY HVLFTGSSEE
     ANTHMIMAAV RRHLLRTQQR PHVIIGAAEP PSVTECVKAL AQEKRCVYTI IPLKNFEIDP
     VAVYDAIQSN TCLACISGTN AVVKTFNKLQ DISKVLKGIP LHSEVSELVY QGCIKQNPPA
     DSFSINSLYG FLGVGVLGMK KKVMQGLGPL IFGGGLRGGS PNIPGIHAMY RTLTQQRPSM
     KKINTIHKLF MKTLKKHQHV YLPIGGVSAE DTSAENISTK DIPVEGPKEL PGYILFSVGR
     RAEELQKKIF TKFNIKVGRI VDLQEILFRI KIPQKYWETL LFIQLRDNLT KEDIKRVMVV
     LMHLDTITPR GSLPPPSYSS SFS
 
 
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