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Database: UniProt
Entry: A0A0G4F4I1_VITBC
LinkDB: A0A0G4F4I1_VITBC
Original site: A0A0G4F4I1_VITBC 
ID   A0A0G4F4I1_VITBC        Unreviewed;       390 AA.
AC   A0A0G4F4I1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Alpha-carbonic anhydrase domain-containing protein {ECO:0000259|PROSITE:PS51144};
GN   ORFNames=Vbra_8840 {ECO:0000313|EMBL:CEM06956.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM06956.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM06956.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CDMY01000373; CEM06956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4F4I1; -.
DR   STRING; 1169540.A0A0G4F4I1; -.
DR   VEuPathDB; CryptoDB:Vbra_8840; -.
DR   InParanoid; A0A0G4F4I1; -.
DR   OrthoDB; 751784at2759; -.
DR   PhylomeDB; A0A0G4F4I1; -.
DR   Proteomes; UP000041254; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR   InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF265; CARBONIC ANHYDRASE; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..390
FT                   /note="Alpha-carbonic anhydrase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005188291"
FT   TRANSMEM        295..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..265
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   REGION          359..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..381
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  42600 MW;  A2CF71C890319B43 CRC64;
     MREHRRLWLI LTGVVACLPE CILGSLTWNY NQQGADWTMG DCTSAERQSP INIASQHTTA
     LDEPFRYNYE TKGGKISLIN NGHTLEVIGQ QALGHLDYRG NVYRLEQIHF HAPSEHTFEN
     QARELEMHLL HMNDDHGLMV VSLTFSSVGA SAAHPFLTVL EAKGFPSENG RVEINMEGGD
     EFNLNTLISD TEDFYKYAGS LTTPPCTENA QWFVMAQPLL AKASQLELFT KAFAYPGTQG
     NFRIIQNTPD LMKNPQHVTR VKSTYSPDDP ALQIQQDTTG ETIKQELTGL GTTGMIVLVI
     GSILILAGVV TLSLACIINH CKRARLEAEE EDYGPTRTLQ GSYQNYAASL NAPTVPVNYN
     MPGAGPPGQP APPPPPPLAP AAAAAASEAN
//
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