ID W9XZB8_9EURO Unreviewed; 1333 AA.
AC W9XZB8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=A1O5_00121 {ECO:0000313|EMBL:EXJ75614.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ75614.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ75614.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ75614.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC ECO:0000256|RuleBase:RU362082}.
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:EXJ75614.1}.
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DR EMBL; AMGX01000001; EXJ75614.1; -; Genomic_DNA.
DR RefSeq; XP_007738931.1; XM_007740741.1.
DR STRING; 1182543.W9XZB8; -.
DR GeneID; 19184858; -.
DR eggNOG; KOG0208; Eukaryota.
DR HOGENOM; CLU_001828_3_1_1; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000019471; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR CDD; cd07542; 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; 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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR047821; P5B-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630:SF8; CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362082};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000019471};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}.
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 580..608
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1120..1139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1160..1179
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1207..1226
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1233..1254
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1274..1292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 169..287
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1333 AA; 149982 MW; A70A9F7E06AB0553 CRC64;
MDCSAHHEGA ARRSSRRRSS SAGRMHRRDS NLSTASIVSD VEMSTTDVFS GPVSESVPSS
VTGFAYRVPR RRAGSISSFT YFTEQEQEVP SVFSDEEAVE SDEEQGHIPH EDRDLEAGLE
PTTSHRKSSS RYRSSSDQPL LYRHDSARSD TQKHEDGGNF SQKLYIENED LTMAIAGFTT
STIGYLTYMA ICVFTAGIGY LVFRWMPRWR ISLVGSPSPL RKCSWVVVEN QWGEFTVHYV
VSDDYGHPMS TVFTRSGKEK LNGYRYDNDA ELRRLRYLDY RYMRLLYYPV EDKFVLNNDW
WDPQWVSVKA LREGLDTEER DPRDQVFGKN MIEIQQKTIP ELLLDEAFHP FYIFQVASLI
LWSLDEYYYY AAAIFVISVF SITTTVVETR STMRRLREIS RFECDVRVLR NSFWRSALSS
ELVPGDVYEV SDPSLSQLPC DSLLLAGDCI INESMLTGES IPVSKIPITD EALPYIDLGA
TSIHPSVARH FLFCGTKIIR ARRPQDTEDD EAVALAMVVR TGFNTTKGAL VRSMLFPKPS
GFRFYRDSFR YISVMGIIAA VGFIASFINF VKLGLAWHLI IVRALDLITI VVPPALPATL
TIGTNFALGR LRKQQIFCIS PQRVNVAGKL DVVCFDKTGT LTEDGLDVLG VRLVQHPEIR
FGDILEEARE LLPPASYDRD PTVDYRVNKN MLYTMATCHS LRLVEDELIG DPLDLKMFQF
TEWSFEEGSR STSHFIEPGT QQTAPSVARP PHGFEYDLED SQDNDNPVRV ELGILRSFEF
VSHLRRASVI VRQHCDPGVN IYVKGAPEVM KDICTASSIP DDFDDLLNYY THKGFRVIAC
ASKYISRFSW DDVQNMERSE AESRLSLIGF IIFENKLKEI TTAVIEELNE AKIRNVMCTG
DNILTAISVA RECGIIDRNA HCFVPHFIEG DKMDAQARIS WESVDNQIYQ LDEHTMLPQP
LPAEDDNAAP YDAIAIGDYT LAVTGDAFRW IIDFGSTEAV QRMLAKGAVF ARMSPDEKHE
LVEKLQSIDY CCGFCGDGAN DCGALKAADV GISLSEAEAS VAAPFTSHIF DISCVPALIK
EGRAALVTSF CCFKYMSLYS AIQFTSVSFL YASASNLGDF QFLFIDLALI LPLAIFMGWT
GAYPVLSKKR PTASLVSRKV LTPLLGQILL SVLVQLGVFE TVQNQPWYIP PRLDKEKSNV
DNSQNTALFL VSCFQYTLSS VVLSVGPPFR QSLATNVPFC VTIVTALLIS LYMLLDPAKW
VADFMDLTEM SVDYKGFLLV LAMAGFAVAY LAEQYIFPLL AKYIGRLKLR LRPGHPKKRK
QYKIIAEEIQ AST
//
