ID A0A093V9I1_TALMA Unreviewed; 1476 AA.
AC A0A093V9I1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative cation-transporting ATPase 1 {ECO:0000313|EMBL:KFX49197.1};
GN ORFNames=GQ26_0102070 {ECO:0000313|EMBL:KFX49197.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX49197.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX49197.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX49197.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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:KFX49197.1}.
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DR EMBL; JPOX01000010; KFX49197.1; -; Genomic_DNA.
DR eggNOG; KOG0209; Eukaryota.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum 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 GO; GO:0120013; F:lipid transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07543; 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; 1.10.3520.10; Glycolipid transfer protein; 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; IPR036497; GLTP_sf.
DR InterPro; IPR014830; Glycolipid_transfer_prot_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006544; P-type_TPase_V.
DR InterPro; IPR047820; P5A-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; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF08718; GLTP; 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; SSF110004; Glycolipid transfer protein, GLTP; 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.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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 212..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 604..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..171
FT /note="Glycolipid transfer protein"
FT /evidence="ECO:0000259|Pfam:PF08718"
FT REGION 1128..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..88
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1476 AA; 164190 MW; FE0FE6F23982B903 CRC64;
MSAPVIPPGK TWLDTLQKSF VDVPVDAAND NAISTKEFLD AVESFTTLFD VIGVMAFNTV
KSDLLGNVKK LRERYNAATA ESETLQALVL NELKTKKHTA TEGLLWLVRG LEFTAEAIRD
SLDAPNKELV DSFRAAYGNT LKPHHSFVIK PIFNAALSAT PYRKDFFDKL GFNAGVEPAM
KEYVSALQNQ QGLRVARYPQ IESASLHNPF PLFLHTYVWP FLIAWPVFFA FYLNPTSYDT
YIQGQEWTWV YSGSIITLQS LFWLMTKWSV NLNTLFTTTP ASEVDIAQLI KVIPITNAGA
PEICKLLRDN TRGKEITSFL FQKRRFLWYP EEGKFAPLSY ALDEEPKPAI KTFQKSRGLQ
SKSEIERIQH HYGDNTFDIP VPTFVELFQE HAVAPFFVFQ VFCVGLWMLD EYWYYSLFTL
FMLVTFESTV VWQRQRTLNE FRGMNIKPYD IWVFRENKWQ EITSDKVLPG DLVSVNRTKE
DGGVACDILL IQGSAIVNEA MLSGESTPLL KDSIQLRPGD DLIDPEGLDK NSFVHGGTKV
LQITHPNLGD LSEKAANAAS GVPKPPDNGA LGIIVKTGFE TSQGSLVRTM IYSTERVSAN
NAEALLFILF LLIFAIAAAW YVWQEGVDKD RKRSKLMLDC VLIITSVVPP ELPMELSLAV
NTSLAALSKF AIFCTEPFRI PFAGRVDIAC FDKTGTLTGE DLLVDGIAGL SLGQAGAKVD
KDGAHTEVIK VPEVGNETTL VLATAHALVK LEEGEIVGDP MEKATLSSLG WVLGKDDVLS
NKATGSQRSE SVQIKRRFQF SSALKRQSSI AHVTTTDKAS GKKHKATFVG VKGAPETIRT
MLVHTPPHYE ETFKYFTRNG ARVLALAYKY LSTDADFGQG RINNYSRENI ESGLHFAGFL
VLQCPLKEDA IKAVRMLNES SHRVVMITGD NPLTAVHVAR QVEIVDREVL ILDAPENDNT
GNRLVWRSTD DKVNIEVDPS HPLDREILQT KDLCVTGYAL AKFKDLPAFS DLLRHTWVYA
RVSPKQKEDI LLGMKAAGYT TLMCGDGTND VGALKQAHVG VALLNGSPED LTKIAEHARN
TKMKELYEKQ VQMMARFNQP PPPIPVHIAH LYPPSPTNPH YQKAIEREAQ KKGQPVPPPV
TGAVAAPAAP AQQALTPQQL RQQQAQATAA GFADKLTSSM LESELDDEPP TLKLGDASVA
APFTSKLAHV MAIPNIIRQG RCTLVATIQM YKILALNCLI SAYSLSVIYL DGIKFGDGQV
TISGMLMSVC FLSISRAKSV EGLSKERPQP NIFNPYIIGS VLGQFAIHIA TLIYLSRYVS
KIEPPTGEVD LEGEFEPSLL NSAVYLLQLI QQISTFSINY QGRPFRESIR ENRAMYWGLV
GASGVAFSCA TEFIPEINEK LRLVPFTEEF KMTLCVLMIL DYGGCWVVET VLKHLFSDFR
PKDIAVRRPD QLEREQARKL EEQAEAQAEA EKNRKI
//
