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Database: UniProt
Entry: A0A1C5BF56_9ACTN
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ID   A0A1C5BF56_9ACTN        Unreviewed;       923 AA.
AC   A0A1C5BF56;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Carbonic anhydrase {ECO:0000313|EMBL:SCF57081.1};
GN   ORFNames=GA0115254_103884 {ECO:0000313|EMBL:SCF57081.1};
OS   Streptomyces sp. Ncost-T10-10d.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839774 {ECO:0000313|EMBL:SCF57081.1, ECO:0000313|Proteomes:UP000198750};
RN   [1] {ECO:0000313|Proteomes:UP000198750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ncost-T10-10d {ECO:0000313|Proteomes:UP000198750};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-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; FMDF01000033; SCF57081.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5BF56; -.
DR   OrthoDB; 9771198at2; -.
DR   Proteomes; UP000198750; 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; 2.
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:UP000198750};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        113..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        194..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        379..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        406..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        437..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          44..294
FT                   /note="SLC26A/SulP transporter"
FT                   /evidence="ECO:0000259|Pfam:PF00916"
FT   DOMAIN          340..440
FT                   /note="SLC26A/SulP transporter"
FT                   /evidence="ECO:0000259|Pfam:PF00916"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   923 AA;  95056 MW;  BFD5D7F2FD5BBC75 CRC64;
     MSACVPTRHD HTSRSSRPPR DSGIKRPHSP PPPPHGGRFR ITGADLSASV TVFLLAVPMS
     LGLAVAMDAP LEAGLISAAV GGIVAGLLGG TPLQVSGPSA GLTVVTAELI QIYGWRTTCA
     ITIGAGLLQI LLGSLRAARS ALAVSPAIVH GTLAGIGVAI ALAQLHIVLG GSPQSSAVAN
     ALALPDQWGR VSPAAPLIGA LTIAILTLWP RIPGRIGRVA RRIPAALAAV VTATVVAAIT
     APGIARVDLP SWRSHALPEM PHGPVLALAT AVLTVMLVAS LESLLAAVAV DKLSADRAGG
     QATARSKADL PSASSPASAS ASGRPGPACS SPPDPPVRRS DLDRELRAQG IANTLSGLVG
     GLAVSGGAVR SSANVRAGAT GRASTVLHGV WVVLAAGLLV TALEQIPLAA LGALVMMVGI
     QMVSFAHIRN VHKHREFLVY GATITGVLLF GVLKGVVIGI AVAVAVALHR LARTRIAVTE
     QAGQHLVVVQ GQLTFLAVPR LSRALARLPQ DGDAVVELDG FFMDHAAYET IQDWSTAQTA
     HGGRVVFTGR SGGRIAEPAS AAHSCCRPWT PWRNHHCHDR SGQTPETQHA RLDAGRAPDC
     GSGAVEDGSP EHHTSHDASG AHSTPGPAGS PTAAPRRIGS NRLFSGLSSF QRNTAPLVRE
     ELARLAREGQ RPSQLFITCA DSRLVTSMIT ASGPGDLFTV RNIGNLVPPP DAESSDDSVG
     AAIEYAVDVL KVESITVCGH SGCGAMQALL GARPGPDTPL SSLWRWLRHG LPSLERMRSR
     HHAWARISGR LPADAVEQLC LTNVVQQLDH LRAHGSVARR LAEGRLQLHG MYFHVGEAQA
     YLLAEGASAG HALDEVFNRV DPGDAHASSG SHTPAEAHAL AGAHPPADSR SPAGSRSPGD
     ADTPRPAAPG DPGGSGELER TGV
//
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