ID S2JC98_MUCC1 Unreviewed; 1361 AA.
AC S2JC98;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=HMPREF1544_05283 {ECO:0000313|EMBL:EPB87876.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB87876.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., 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 Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-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}.
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DR EMBL; KE123960; EPB87876.1; -; Genomic_DNA.
DR STRING; 1220926.S2JC98; -.
DR VEuPathDB; FungiDB:HMPREF1544_05283; -.
DR eggNOG; KOG0208; Eukaryota.
DR InParanoid; S2JC98; -.
DR OMA; FSCFQYM; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000014254; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; 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; 1.
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; PF13246; Cation_ATPase; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000014254};
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 190..211
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 559..583
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 595..616
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1113..1131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1137..1156
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1177..1199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1224..1244
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1256..1279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1291..1314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 173..302
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 324..375
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1361 AA; 153801 MW; 64CF42744F09792F CRC64;
MSGNPLTKTR SVYGTSSVDS KQKLESTTKP STRRDSAAPL MNTPPIQPVI GIDPLDVTGT
SYRSSNHIIT SGSYARHGGH RTGLFRRRRN SQSSQENDSE DEQQLDSDRE LNTSDEESSA
DDEDDLDEDD ESDTEHTIQH LVASRNNTEI RISGLNDIPN DTKDQQTLLL EEEDVQIHIQ
AYRFNRLNLF FYRVCSVLSL GIVWLVCRWV PKWYIAWIGV KVPLEKAEWV VFESQYNEIE
IIRPFREWYQ GTIGSIFSHD QMKEELLQFN VNTEEARHLL NMDHQINQLM LVEYRYIRLA
FHPLLHKFLI VGFWKDQSWV STKNFKLGLT TEKYHARLSV FGPNLINIRE KPTSKLLTDE
VLNPFYVFQI GSILLWCMDD YYYYAFCIFI ISAFSIISTL IETKETMKRM KDMSFFECSV
RVFRSGSWRN VSSVELVPGD LIDIANIHTV PCDAMLVSGD CILNESMLTG ESVPVSKMPI
NDVTLKKMNL SSSSIPAEIA KHFLFMGTKM VRVRGGDNVT TATAIVVRTG FSTAKGALVR
SMLFPKPNNF KFYRDSFRFI GVLSIIAFVG FLISSVNFIR LGIDSTTMIL RALDLITIVV
PPALPATLSI GTSFAISRLK KLGIFCISPP RVNIGGKIDC MCFDKTGTLT EDGLDIHGIR
AVTMTRDGRK LFDDECKSVA HVDPNNDDTI TTQAKILRTM TTCHSLKIVN GELLGDPLDL
KMFEFTQWEL EESGGASSMG LKPRSELAAL QAKKSAKVGI MPTVVRPPGG RQDINLHMET
TTTEQAPPIE FGIIHTFEFV SSLRRMSVIV RRLANPTMEV FVKGAPEVMK DICTPESMPE
DYQERLYKYT HRGYRVIACA SRQLLGVKWH KLHKLKRNEV ETGLTFLGFI VFENKLKPRT
ASAISTLRNA NIRQIMCTGK FTKACDNVLT AVSVARECGL IDPAAEIYIP RFLKGSSTEP
DSELSWESVM QEGNELSTDT LQPHMTNDFT RHDQEYHLAV TGEAFRWMVD HSTLESLYRM
LVKGAIYARM SPDEKQELVM ELQNIGYCVG FCGDGANDCG ALKAGDIGIS LSEAEASVAA
PFTSNTMDIE CVIDVIKEGR AALVTSFSCF KYMALYSLIQ FTSVTLLYAF GSNLGDFQFL
YIDLFLILPI AVYMGHTAAW PHLDRKRPTA SLVSKKVLTS LIGQIVINSS IQFLAYWAIH
QQSWYTPPVF DPNGDNIECL ENTVLFLVSS YQYMLIAVVF SVGPPYRKPL WTNGRLVLTL
AILISLTSWF VLIPPAFVMD LMEIEPMPMS FRWFILFLAA MNLVVSLLCE KYLFHQMMDK
MTQFLSKRSF GYSLVGSSSS HSKRGYDKTY RRVMDEMGIH E
//
