ID   A0A1I2KYC7_9ACTN        Unreviewed;       753 AA.
AC   A0A1I2KYC7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Carbonic anhydrase {ECO:0000313|EMBL:SFF71319.1};
GN   ORFNames=SAMN05216251_12580 {ECO:0000313|EMBL:SFF71319.1};
OS   Actinacidiphila alni.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=380248 {ECO:0000313|EMBL:SFF71319.1, ECO:0000313|Proteomes:UP000199323};
RN   [1] {ECO:0000313|EMBL:SFF71319.1, ECO:0000313|Proteomes:UP000199323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFF71319.1,
RC   ECO:0000313|Proteomes:UP000199323};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide to form
CC       bicarbonate. {ECO:0000256|ARBA:ARBA00024993}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00006217}.
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DR   EMBL; FONG01000025; SFF71319.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2KYC7; -.
DR   STRING; 380248.SAMN05216251_12580; -.
DR   OrthoDB; 9771198at2; -.
DR   Proteomes; UP000199323; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR036874; Carbonic_anhydrase_sf.
DR   InterPro; IPR011547; SLC26A/SulP_dom.
DR   InterPro; IPR001902; SLC26A/SulP_fam.
DR   PANTHER; PTHR11814:SF227; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR   Pfam; PF00484; Pro_CA; 1.
DR   Pfam; PF00916; Sulfate_transp; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199323};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        365..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..363
FT                   /note="SLC26A/SulP transporter"
FT                   /evidence="ECO:0000259|Pfam:PF00916"
SQ   SEQUENCE   753 AA;  78025 MW;  DEC48C76221840A0 CRC64;
     MQRFHRSDLS ASITVFLIAV PLSLGLALAT GAPLQSGLVA AVVGGIVAGS LGGAPLQVSG
     AATSLVVVTA DLVHRYGWRA TCAVTVLAGL AQLLLGVLRV ARAALAVSPA IVHGMLAGIG
     TVIAVGQLHV VLGGSPQSST IANVTALPGQ LAVTDPTTPA IGAITVAVLL GWRRLRGRAG
     RLLGVIPAPL AAVVLATAVS AGLSLPRVDL PAWTAPVLPA MPTGPVLGIV AAVLTVTLVA
     SMESLLSAVA IDTLQARRPG PHAPPARLDR ELLGQGTANV VSGLLGGLPV AGGAIRGSAN
     VEAGAVTRRA TVLHGVWVLL CAGLAAWALE LIPLAALAAL VMLVGVRMVS FAHIRHVRRH
     REFPVYAATL GAVVLFGVLQ GVVVGVVVAL FLALRRLTHT RVTVTEEPEC HRVRVTGQLT
     FLAVPRLTRA FAQVPDGGNA VVELDGSFMD HAAYEALNAW CVRHRSRGGH ATLGDAAGRT
     VSEPVSAHAC RPWTPWRNHH CTRPAVAPAT GGGRGPSRSH GHDHGQLLGG VSAFQRNTAP
     LVREELARLA HEGQSPGQLF LTCADSRLVT SMITSSGPGD LFTVRNVGNL MPPPGSDSSC
     DSVAAAVEYA VEVLQVSNIT VCGHSGCGAM QALLSDHEPG AQTPLARWLR HGRPSLARLG
     RIGRLDRGEA ALADRPVADD LERLSLVNVM QQLDHLMAHP CVARRVGEGT LHLHGMYFHV
     GEAQAYILDR TTSVFSAVRP DTAPETTLEA AKV
//