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CYSA_ANTAG
ID   CYSA_ANTAG              Reviewed;         381 AA.
AC   Q85A69;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Sulfate/thiosulfate import ATP-binding protein CysA {ECO:0000255|HAMAP-Rule:MF_01701};
DE            EC=7.3.2.3 {ECO:0000255|HAMAP-Rule:MF_01701};
DE   AltName: Full=Sulfate-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01701};
GN   Name=cysA {ECO:0000255|HAMAP-Rule:MF_01701};
OS   Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC   Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC   Anthoceros.
OX   NCBI_TaxID=48387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX   PubMed=12527781; DOI=10.1093/nar/gkg155;
RA   Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT   "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT   chloroplast genome: insight into the earliest land plants.";
RL   Nucleic Acids Res. 31:716-721(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC   TISSUE=Thallus;
RX   PubMed=12711687; DOI=10.1093/nar/gkg327;
RA   Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT   "RNA editing in hornwort chloroplasts makes more than half the genes
RT   functional.";
RL   Nucleic Acids Res. 31:2417-2423(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex involved in
CC       sulfate/thiosulfate import. Responsible for energy coupling to the
CC       transport system. {ECO:0000255|HAMAP-Rule:MF_01701}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + sulfate(out) = ADP + H(+) + phosphate +
CC         sulfate(in); Xref=Rhea:RHEA:10192, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01701};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + thiosulfate(out) = ADP + H(+) + phosphate +
CC         thiosulfate(in); Xref=Rhea:RHEA:29871, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33542,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01701};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 4 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 18 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 33 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 34 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 72 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 80 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 86 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 95 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 121 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 123 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 154 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 155 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 156 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 163 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 169 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 193 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 196 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 233 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 295 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 346 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}; Note=The initiator methionine is created
CC       by RNA editing. The nonsense codons at positions 72, 121, 169, 193 and
CC       346 are modified to sense codons.;
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       Sulfate/tungstate importer (TC 3.A.1.6) family. {ECO:0000255|HAMAP-
CC       Rule:MF_01701}.
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DR   EMBL; AB086179; BAC55343.1; -; Genomic_DNA.
DR   EMBL; AB087436; BAC55436.1; -; mRNA.
DR   RefSeq; NP_777407.1; NC_004543.1.
DR   AlphaFoldDB; Q85A69; -.
DR   SMR; Q85A69; -.
DR   PRIDE; Q85A69; -.
DR   GeneID; 2553491; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0015419; F:ABC-type sulfate transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0102025; F:ABC-type thiosulfate transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51237; CYSA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Nucleotide-binding; Plastid; RNA editing;
KW   Sulfate transport; Translocase; Transport.
FT   CHAIN           1..381
FT                   /note="Sulfate/thiosulfate import ATP-binding protein CysA"
FT                   /id="PRO_0000092306"
FT   DOMAIN          3..233
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01701"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01701"
SQ   SEQUENCE   381 AA;  43655 MW;  E140215B6FF1BA0A CRC64;
     MSILVYEVSK SLGNLKVLDR VSLYVRKVSL VALLGPSGSG KSSLLRIIAG LDSPDYGSVW
     LHGTDMTNTS TQYRHMAFVF QHYALFKNMT VYENISFGLR LRGFSYQKIR NKVNDLLDCL
     RISDIVSEYP GKLSGGQKQR VALARSLAIK SDFLLLDEPF GALDGELRRH LSKWLKRYLK
     DNGITTIMVT HDQKEAISMA DEIVVLKQGR FLQQGRSKNL YDEPIDYFVG IFSGSFIEFP
     QLEESLDAPL GSSSSSSSST KKSMEKDFTP FIPDLIWSQI FTNQSIHHYH FFLRPHELYL
     ESQIDLKAIP VQIKKIIYKR TFVQLDLSIT PSSWNITIPI GYQAFRKLNI QSFVQKLYIK
     PRNQVYLRAY PKKKNIISKQ I
 
 
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