ID A0A2V0PBS2_9CHLO Unreviewed; 1041 AA.
AC A0A2V0PBS2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:GBF97304.1};
GN ORFNames=Rsub_09995 {ECO:0000313|EMBL:GBF97304.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF97304.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF97304.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF97304.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
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:GBF97304.1}.
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DR EMBL; BDRX01000096; GBF97304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0PBS2; -.
DR STRING; 307507.A0A2V0PBS2; -.
DR InParanoid; A0A2V0PBS2; -.
DR Proteomes; UP000247498; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 2.
DR PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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; PR00121; NAKATPASE.
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:UP000247498};
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 99..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 757..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..853
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 865..885
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 897..920
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..123
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 999..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1041 AA; 110667 MW; 6C286F387DAEA2A6 CRC64;
MAPKGCACCT KPEAIEGGPK DKAAILEIAQ GGKGTLETVV VQADDPEEPW HSADASVVVE
DLASDAAVGL TSEEAKRRLR EYGPNRLTPP RKTSFLERLW AQINNIVIWI LFAAAIIEGA
LQSWAEFGLV LAVIFLNTAM GMIQEGKAEK AADAIKAMLS PTAKVKRDGA PQVVAAEELV
PGDIVLLKSG DKLPADLRLI TATNLQVQEA MLTGESVPTS KEANKTFERH APLGDRRNMA
YSATSVVSGQ AEGIVIGTGD SAEIGQISRM VNTVEVVTNN LEKQMSVFGR WLAVIVLFIV
VAAFLLAKFR AGETWQDAFE SAVSIAVAVI PEGLPAMVTV VLAIGVTVMA RNHAIVRQLP
AVETLGSVNV ICSDKTGTLT KNEMTAVRLR TASTLYHIGG VGYAPVGDFT VADATGDAPG
AALTEAQTAA VRAIMEGAVL CNDSALTKAK DEGGADVYKP TGAPTEVALL TAGEKAGLDL
AALKAAKPRV ASIPFESEHK FMATVVSEGG KRVMYVKGAS DRLLPICKTQ ITGDDLKKTA
PLEIGFWNKA QSDLSAQGLR VLLLCRAELA ANENLEGLTA DSLQKRKPFL SAVCAFAILD
PPRIEVVAAI KEAHLAGITV KMITGDHALT ALAIGKMLGI AGGGLALTGP EVDAMSSEQL
KAVAPECNIY ARASPENKIR IVRALQDASP RRIVSMTGDG VNDAPALKAA DVGVAMGITG
TDVSKEAAKM VLADDNFTSI VAAVKEGRRV WDNIIRLLLF NLPVNMAQGI SVLWAYILGL
RESPLTVLQI LLVNMVTSTT LGMALAAEPA EPDVMERPPR PANKRLIGKL VIWRMLFVSH
VIVALVLGSF YWGERQGYSL DVRRAEAFCC LVATQIGYFI TCRFLKRTTL HYRVLFGNPL
AYASIVLTVG IMVFFTYVPV VNTFFNMAPL PGIPWARIAV SMVITYAVVE VEKALIDPVI
VPLLRPVLRW INGHAPKWLR LDFKPTRVAG KLCKAPRTAS MAPQRKGTLR RTSSSVATAA
AHATGGAAAP AGAANGKKAE V
//
