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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//