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Database: UniProt
Entry: A0A0C2QLX5_9CYAN
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Original site: A0A0C2QLX5_9CYAN 
ID   A0A0C2QLX5_9CYAN        Unreviewed;       910 AA.
AC   A0A0C2QLX5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:KIJ81078.1};
GN   ORFNames=SD80_25865 {ECO:0000313|EMBL:KIJ81078.1};
OS   Scytonema tolypothrichoides VB-61278.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC   Scytonema.
OX   NCBI_TaxID=1233231 {ECO:0000313|EMBL:KIJ81078.1};
RN   [1] {ECO:0000313|EMBL:KIJ81078.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB-61278 {ECO:0000313|EMBL:KIJ81078.1};
RA   Tripathy S., Das A., Panda A., Malar M.C., Adhikary S.P.;
RT   "Draft genome sequence of Scytonema tolypothrichoides VB-61278.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIJ81078.1}.
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DR   EMBL; JXCA01000014; KIJ81078.1; -; Genomic_DNA.
DR   STRING; 1233231.SD80_25865; -.
DR   OrthoDB; 499468at2; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   910 AA;  98787 MW;  BE688176AB7F0CD3 CRC64;
     MQDKLPENWH SQPIEQTIDL LKTDPVQGLS GIEIKERIAR FGFNELLGKK GKPWWLKFLL
     QYNQPLLYIL LIAGATKAII GEFVNAFVIW GVTTTNAIIG YVQESKAEGA IAALAKSITT
     EATVIREGQK LRIPSRELVP GDVVLLTSGD KVPADLRLIK VRNLQVDESA LTGESVAVEK
     EAGVETPPLP PDIPLAERKN MAYAGGFVTF GQATGIVVAT GNTTETGRIS QLLENKVDLS
     TPLTRKFDKF SKNWLYMVLG VATLTLMVGL QTKPWRDAIE ATVALIVGSI PEGLPAVVTV
     TLAIGVSRMA RRHAIIRKLP AVETLGGATV ICSDKTGTLT ENQMTVQAIY AGGHQYAVNG
     VGYSPEGKIL QDGKPIDLSG DLGLQECLSA GLLCNDSHLE TKNGKWVVVG DPTEGALITS
     ANKLGLIKPL LEQQMPRLDS IPFESEFQYM ATLHATPTSK TIYVKGSVEA IAKRCTFMLN
     SNGQLKRIDC QETLNTSSIE REVNIMARQG LRVLALAKKL VPNEQTTVDH VDIDTGLIFL
     GLQGMIDPPR ESAMKAVKAC QEAGIQVKMI TGDHAVTAQA IATRMGINKN GSVLAFSGAE
     LAKMDYQELA QVAEDGVVFA RVAPEQKLRL VEALQSKGEI VAMTGDGVND APALKQADIG
     IAMGMAGTEV AKEAADMLLT DDNFASIKAA VEEGRAVYKN LVKAMCFILP VNGGESMTIL
     FSTLVGRELP ILSLQILWLN VINSITMTVP LAFEPKPQNV MQQSPRRPNE ALLSGSRIKR
     ILAISLFNWI VIFGVFEYIR QTTGDINLAR TMAINSLIAG RIFYLLSLSQ LVPNLIAKMD
     GTIQENVDIP AIGFGIIGAI ILQLCFSYVP FINELFFTVP LRFDQWLFCL AVGLPMIPWA
     AFVNRFDPPN
//
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