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Database: UniProt
Entry: A0A139WTN6_9CYAN
LinkDB: A0A139WTN6_9CYAN
Original site: A0A139WTN6_9CYAN 
ID   A0A139WTN6_9CYAN        Unreviewed;       920 AA.
AC   A0A139WTN6;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:KYC35773.1};
GN   ORFNames=WA1_06820 {ECO:0000313|EMBL:KYC35773.1};
OS   Scytonema hofmannii PCC 7110.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC   Scytonema.
OX   NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC35773.1, ECO:0000313|Proteomes:UP000076925};
RN   [1] {ECO:0000313|EMBL:KYC35773.1, ECO:0000313|Proteomes:UP000076925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC35773.1,
RC   ECO:0000313|Proteomes:UP000076925};
RX   PubMed=23221676; DOI=10.1093/gbe/evs117;
RA   Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA   Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA   Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT   "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT   of oxygenic photosynthesis from prokaryotes to plastids.";
RL   Genome Biol. Evol. 5:31-44(2013).
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:KYC35773.1}.
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DR   EMBL; ANNX02000051; KYC35773.1; -; Genomic_DNA.
DR   RefSeq; WP_017747805.1; NZ_KQ976354.1.
DR   AlphaFoldDB; A0A139WTN6; -.
DR   STRING; 128403.WA1_06820; -.
DR   OrthoDB; 499468at2; -.
DR   Proteomes; UP000076925; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd02080; P-type_ATPase_cation; 1.
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; 2.
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; PF08282; Hydrolase_3; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076925};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        60..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        284..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        705..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        733..754
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        782..800
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        820..840
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        852..872
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        884..904
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..87
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   920 AA;  99953 MW;  67A515AA3F89B12C CRC64;
     MAASVTSQVQ EHQWHNLLER EIARHLDTNL ETGLTAAEVT KRQEHFGANE LKGKPGKSPF
     VRFLLQFHQP LLYILLVAGA IKALLGQWVN AGVIWGVTLI NAIIGFVQES KAESAIAALA
     SSVETNATIL RNSEKVQVPS TELVPGDIVL LASGDKVPAD VRLIQARNLQ VNESALTGES
     VAVEKDTQSL RPDTPLAERT NMAYAGSFVT FGSGRGVVVA TGEATETGRI SQLMEQGTSL
     KTPLTRKFDK FSKTLLYVIL GIAALVFAVG LGYGYSWAEM FEAAVAFAVS AIPEGLPAVV
     TVTLAIGVSR MARRHAIVRK LPAVETLGGA TVICSDKTGT LTENQMTVQA IYAGGKNFIV
     TGTGYSPIGQ ILLDENPVNW KNAPALKECL IAGLLCNDSH IEKKHDQWQV FGDPTEGALV
     AVASKVGLTR TDIEQKMPRL DAIPFESEFQ YMVTLHESGS KENSLLRTIY VKGSVEAILN
     RCQQMLDSQG NLTPLEAETV HQEVDTMAHQ GLRVLAFAKK YVSESHERVE HTDIKQDLIF
     LGLQGMIDPP RTEAVRAVQA CQEAGIKVKM ITGDHAVTAA AIASRMGFNK NGKVPAFTGS
     QLAQIEKHEL ATAVEDGVVF ARVAPEQKLR IVEALQSKGE IVAMTGDGVN DAPALRQADI
     GIAMGGAGTE VAKEASDMIL TDDNFASIEA AVEEGRTVYQ NLLKAIAFIL PVNGGESMTI
     LISVLLAREL PILSLQVLWL NMVNSITMTV PLAFEPKSEE VMKQPPRNPN QSLLSKSLVR
     RILIISVFNW ILIFGVFEWI EQTTGNIDLA RTMAIQALVV GRIFYLLSIS KLGVAIINNL
     RGIRQKIEDA RAIITGIICT VVLQIIFSQW SLMNNLFYTT PLNLNQWLFC LLVGLPMIAV
     AAIVNRIASL SIYAKNLHYR
//
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