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YGIQ_SHIFL
ID   YGIQ_SHIFL              Reviewed;         739 AA.
AC   Q83JL2; Q7UBJ9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=UPF0313 protein YgiQ {ECO:0000255|HAMAP-Rule:MF_01251};
GN   Name=ygiQ {ECO:0000255|HAMAP-Rule:MF_01251};
GN   OrderedLocusNames=SF3060, S3263;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01251};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_01251};
CC   -!- SIMILARITY: Belongs to the UPF0313 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01251}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN44538.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAP18350.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN44538.2; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP18350.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000095159.1; NZ_WPGW01000034.1.
DR   AlphaFoldDB; Q83JL2; -.
DR   STRING; 198214.SF3060; -.
DR   EnsemblBacteria; AAN44538; AAN44538; SF3060.
DR   EnsemblBacteria; AAP18350; AAP18350; S3263.
DR   KEGG; sft:NCTC1_03313; -.
DR   KEGG; sfx:S3263; -.
DR   PATRIC; fig|623.158.peg.3348; -.
DR   HOGENOM; CLU_018288_1_1_6; -.
DR   OrthoDB; 229299at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.80.30.20; -; 1.
DR   HAMAP; MF_01251; UPF0313; 1.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR020612; Methylthiotransferase_CS.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR022946; UPF0313.
DR   InterPro; IPR024560; UPF0313_C.
DR   InterPro; IPR013704; UPF0313_N.
DR   PANTHER; PTHR32331; PTHR32331; 1.
DR   Pfam; PF11842; DUF3362; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF08497; Radical_SAM_N; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SFLD; SFLDG01069; UPF0313; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR03904; SAM_YgiQ; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW   S-adenosyl-L-methionine.
FT   CHAIN           1..739
FT                   /note="UPF0313 protein YgiQ"
FT                   /id="PRO_0000076396"
FT   DOMAIN          372..650
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   REGION          685..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         386
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01251"
FT   BINDING         390
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01251"
FT   BINDING         393
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01251"
SQ   SEQUENCE   739 AA;  83493 MW;  517E26AFB226F410 CRC64;
     MSSISLIQPD RDLFSWPQYW AACFGPAPFL PMSREEMDQL GWDSCDIILV TGDAYVDHPS
     FGMAICGRML EAQGFRVGII AQPDWSSKDD FMRLGKPNLF FGVTAGNMDS MINRYTADRR
     LRHDDAYTPD NVAGKRPDRA TLVYTQRCKE AWKDVPVILG GIEASLRRTA HYDYWSDTVR
     RSVLVDSKAD MLMFGNGERP LVEVAHRLAM GEPISEIRDV RNTAIIVKEA LPGWSGVDST
     RLDTLGKIDP IPHPYGEDLP CADNKPVAPK KQEAKAVIVQ PPRQKPWEKT YVLLPSFEKV
     KGDKVLYAHA SRILHHETNP GCARALMQKH GDRYVWINPP AIPLSTEEMD SVFALPYKRV
     PHPAYGNARI PAYEMIRFSV NIMRGCFGGC SFCSITEHEG RIIQSRSEDS IINEIEAIRD
     TVPGFTGVIS DLGGPTANMY MLRCKSPRAE QTCRRLSCVY PDICPHMDTN HEPTINLYRR
     ARDLKGIKKI LIASGVRYDI AVEDPRYIKE LATHHVGGYL KIAPEHTEEG PLSKMMKPGM
     GSYDRFKELF DTYSKQAGKE QYLIPYFISA HPGTRDEDMV NLALWLKKHR FRLDQVQNFY
     PSPLANSTTM YYTGKKPLAK IGYKSEGVFV PKGDKQRRLH KALLRYHDPA NWPLIRQALE
     AMGKKHLIGS RRDCLVPAPT IEEMREARRQ NRNTRPALTK HTPMATQRQT PATAKKASST
     QSRPVNAGAK KRPKAAVGR
 
 
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