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ENDPH_SALPA
ID   ENDPH_SALPA             Reviewed;         800 AA.
AC   Q5PES4;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Probable replication endonuclease from prophage-like region;
DE            EC=3.1.-.-;
GN   OrderedLocusNames=SPA2590;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- FUNCTION: Possible endonuclease which induces a single-strand cut and
CC       initiates DNA replication. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phage GPA family. {ECO:0000305}.
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DR   EMBL; CP000026; AAV78457.1; -; Genomic_DNA.
DR   RefSeq; WP_000301196.1; NC_006511.1.
DR   AlphaFoldDB; Q5PES4; -.
DR   EnsemblBacteria; AAV78457; AAV78457; SPA2590.
DR   KEGG; spt:SPA2590; -.
DR   HOGENOM; CLU_013772_2_0_6; -.
DR   OMA; ENERCQE; -.
DR   Proteomes; UP000008185; Chromosome.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR008766; Replication_gene_A.
DR   Pfam; PF05840; Phage_GPA; 1.
PE   3: Inferred from homology;
KW   DNA replication; Endonuclease; Hydrolase; Nuclease.
FT   CHAIN           1..800
FT                   /note="Probable replication endonuclease from prophage-like
FT                   region"
FT                   /id="PRO_0000278165"
FT   ACT_SITE        503
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        507
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   800 AA;  91502 MW;  2A8035EF657F8CA1 CRC64;
     MAVSKITLHY AQTTGGSNEA AAAFPWNTPK KAVNPYLDPA EFAPESALSN LIALYAVDNE
     QEQLRRETLS DEVWERYFFN ESRDPVQREM EQDRLISHAK TAREQQRFNP DLVIIANVGA
     QPAHISKPLL ERIKYFHSLG RAKAYSRYLQ KTIRPCLERL ERVRDSQVSA SFRFMASHDG
     LEGLLVLPEM NQDQVKRLST LVAAHMSMCL DAACGDLFVS DDVKPEEIRQ AWERVAAEAM
     RLEVIPPAFE QLRRKKRRRK PVPYELIPPS LARMLCADWW YRKLWQMRCE WREEQLRAVC
     LVNKKASPYV SYEAVIHKRE QRRKSLEFFR SHELINEDGD TLDMEDVVNA SNSNPAHRRN
     EMMACVKGLE LIAEMRGDCA VFYTITCPSR FHATLNNGRP NPKWTSATVR QSSDYLVDTF
     AAFRKAMHKA GLRWYGVRVA EPHHDGTVHW HLLCFMRKKD RRSITALLRK FAIREDREEL
     GANTGPRFKP ELINPRKGTP TSYIAKYISK NIDGRGLAKE ISKETGRSLR DSAEHVSAWA
     SLHRVQQFRF FGIPGRQAYR ELRLLAGQAA RVQGERKAGA PVLDNPRLDA VLAAADAGCF
     ATYIMKQGGV LVPRKHHLVR TAYELNDEPS AYGDHGIRIY GIWSPIAEGK ICTHAVKWKK
     VRKAVDVQEA AADQGACAPW TRGNNCPPVE NLNKSGGDLP DIKTMNEKEL QDYLHNMGQK
     ERRELTARLR LVKPKRKTVY KQNISEQQRL QLEAELTARG FEGSASEIDL LLRGGSIPSG
     AGLRIFYRNH RLQEDDKWRQ
 
 
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