ID A0A0F7RSU4_9BASI Unreviewed; 1321 AA.
AC A0A0F7RSU4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN Name=SSCI27260.1 {ECO:0000313|EMBL:CDR99706.1};
GN ORFNames=SPSC_05294 {ECO:0000313|EMBL:CDU25401.1};
OS Sporisorium scitamineum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=49012 {ECO:0000313|EMBL:CDR99706.1, ECO:0000313|Proteomes:UP000242770};
RN [1] {ECO:0000313|EMBL:CDU25401.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SscI8 {ECO:0000313|EMBL:CDU25401.1};
RA Ju J., Zhang J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000242770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman P.J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CDR99706.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman J.Paul.;
RL Submitted (JUN-2014) 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; CCFA01001463; CDR99706.1; -; Genomic_DNA.
DR EMBL; LK056686; CDU25401.1; -; Genomic_DNA.
DR STRING; 49012.A0A0F7RSU4; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000242770; 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:0140358; F:P-type transmembrane transporter 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; 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; 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; 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 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 126..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 337..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 555..577
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 597..616
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1074..1091
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1111..1130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1150..1171
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1196..1214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1226..1245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1265..1294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 114..258
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 280..332
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT REGION 30..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1321 AA; 145021 MW; 9F9E2948FE912F4D CRC64;
MSNTSPLEPC PPDGAGHVAA RFTLLEPLHD SDFSKQLQPE SVSEPSRSSK ETALTTADRD
SIDEFPDHHL PPRPELLELA QQAKRDSRIS ISMSQDATSP SDNTRQDIYL ADEDIQLHLR
FYRRQLFLML IWYSLCILSA GILFIADAWA NNKFWTRFNT TPTALNDSKS NNKDKLIRIK
SKHREVDILR LKRVTFPSPI PITTIFPPTL AEPYRSPEEA AAAALNTASK LTQASAAAQA
DSLTHVDVLE YRATTFLLHP HSGKFYLLGV WHDPSWRSLD PSSGLSAQAV RDRQALFGDN
QVTVKGKSVF DLLVEEVLHP FYIFQIYSII LWCNDEYVPY AIVIAVVSVI GIVATTVTTK
AAIEKLKKMS RFSCPVSVLR PTSTLSPLDE KSAMVDSTDS EEKQLASASA SASSYSVLDS
EALVPGDIID LGAIDETTHH GHRLVETLPC DVVLIEGDCI VNEAMMTGES VPVVKAPISK
SDLANILAAG KDLSRLDKHI LYSGTKLVRV RPGSGNDTNT TRGLVIRTGF STAKGSLVRQ
MLFPRPISHK FYRDAFLFIG NLFIIAIVGM IATIIYFKII GVSSDEIALR SLDVLTIAVP
PALPATLSIC ITFSIARLKR SQIFCLSPQR INVAGMVNMF VFDKTGTLTE EGLGVMGIRM
VKDGKFTDLV QREQTEEVKE DGAKLSLIEA MATAHDLNLL DGEPIGEPLE VKMLEWTRRK
LQDDASLAPV HLSKEATSDP THPCRPLTKD GALARVPVIL PSATHPSLAV IRAFEFTAAL
RRMSVVVKRD NSLPAQVYCK GAAESIATLC DPASLPTDYD TVLDRCTRAG FRVLAVAGKT
IDALGWQGAQ DLTRPQADCE LQFLGLIVFE NKLKPATTAS IATIRDDAQL SIKMCTGDSV
LTAVSVAKEC GILSANAEVF TPRVSHKQSK NLVVGVEWVS VDGDQRRLDP YTLDPVGDGS
SAEQLKDVEL AVSGEILRTL FDTCSAETMS RVLVHCKVFG RFSPEQKQQL VERLQTLGYV
VAMAGDGAND CGALKSADVG LSLSEAEASV AAPFTSRVKD ISAITQLIRE GRSTLTVSFA
MFLFMSVYSL SEYFTVLLLY GKATSLNNAE YLFIDIFCVL LVAVGLANTL PAKKLFRIPP
EMRLSSTKPI ASMLGQSILG YVAQTIVYLV LHSKTWYQAP EFDPEDLTLN DMDNTALFRT
SVFTYIIAGF AFSLGPPHRQ LLCWNWILAP ALVVLTVFAF YFLFLTGGPF FDLFGFVDMP
DHFRWIIFGV VVAQFVLALV FEFVGVALVA RVVARPFGAV AKRLGRQRSR PYKAVEKAIY
S
//
