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INT2_MYCTU
ID   INT2_MYCTU              Reviewed;         375 AA.
AC   P9WMB3; L0TD68; P71956; Q7D6T7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Putative prophage phiRv2 integrase;
GN   OrderedLocusNames=Rv2659c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   INDUCTION BY HYPOXIA.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=11416222; DOI=10.1073/pnas.121172498;
RA   Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
RA   Schoolnik G.K.;
RT   "Regulation of the Mycobacterium tuberculosis hypoxic response gene
RT   encoding alpha -crystallin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Integrase is necessary for integration of the phage into the
CC       host genome by site-specific recombination. In conjunction with
CC       excisionase, integrase is also necessary for excision of the prophage
CC       from the host genome (By similarity). {ECO:0000250}.
CC   -!- INDUCTION: A possible member of the dormancy regulon. Induced in
CC       response to reduced oxygen tension (hypoxia). It is hoped that this
CC       regulon will give insight into the latent, or dormant phase of
CC       infection. {ECO:0000269|PubMed:11416222}.
CC   -!- SIMILARITY: Belongs to the 'phage' integrase family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP45457.1; -; Genomic_DNA.
DR   PIR; G70966; G70966.
DR   RefSeq; NP_217175.1; NC_000962.3.
DR   RefSeq; WP_003899420.1; NZ_NVQJ01000079.1.
DR   AlphaFoldDB; P9WMB3; -.
DR   SMR; P9WMB3; -.
DR   STRING; 83332.Rv2659c; -.
DR   PaxDb; P9WMB3; -.
DR   DNASU; 885098; -.
DR   GeneID; 885098; -.
DR   KEGG; mtu:Rv2659c; -.
DR   TubercuList; Rv2659c; -.
DR   eggNOG; COG0582; Bacteria.
DR   OMA; DVAIPPH; -.
DR   PhylomeDB; P9WMB3; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.150.130; -; 1.
DR   Gene3D; 1.10.443.10; -; 1.
DR   InterPro; IPR044068; CB.
DR   InterPro; IPR011010; DNA_brk_join_enz.
DR   InterPro; IPR013762; Integrase-like_cat_sf.
DR   InterPro; IPR002104; Integrase_catalytic.
DR   InterPro; IPR010998; Integrase_recombinase_N.
DR   InterPro; IPR004107; Integrase_SAM-like_N.
DR   Pfam; PF14659; Phage_int_SAM_3; 1.
DR   Pfam; PF00589; Phage_integrase; 1.
DR   SUPFAM; SSF56349; SSF56349; 1.
DR   PROSITE; PS51900; CB; 1.
DR   PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE   1: Evidence at protein level;
KW   DNA integration; DNA recombination; DNA-binding; Reference proteome;
KW   Viral genome integration; Virus entry into host cell.
FT   CHAIN           1..375
FT                   /note="Putative prophage phiRv2 integrase"
FT                   /id="PRO_0000392940"
FT   DOMAIN          75..153
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT   DOMAIN          175..364
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        209
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        316
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        319
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        342
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        351
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
SQ   SEQUENCE   375 AA;  42176 MW;  01ED932046AC4D54 CRC64;
     MTQTGKRQRR KFGRIRQFNS GRWQASYTGP DGRVYIAPKT FNAKIDAEAW LTDRRREIDR
     QLWSPASGQE DRPGAPFGEY AEGWLKQRGI KDRTRAHYRK LLDNHILATF ADTDLRDITP
     AAVRRWYATT AVGTPTMRAH SYSLLRAIMQ TALADDLIDS NPCRISGAST ARRVHKIRPA
     TLDELETITK AMPDPYQAFV LMAAWLAMRY GELTELRRKD IDLHGEVARV RRAVVRVGEG
     FKVTTPKSDA GVRDISIPPH LIPAIEDHLH KHVNPGRESL LFPSVNDPNR HLAPSALYRM
     FYKARKAAGR PDLRVHDLRH SGAVLAASTG ATLAELMQRL GHSTAGAALR YQHAAKGRDR
     EIAALLSKLA ENQEM
 
 
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