ID A6R207_AJECN Unreviewed; 1092 AA.
AC A6R207;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Calcium-transporting ATPase 1 {ECO:0000313|EMBL:EDN07134.1};
GN ORFNames=HCAG_03665 {ECO:0000313|EMBL:EDN07134.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN07134.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CH476657; EDN07134.1; -; Genomic_DNA.
DR AlphaFoldDB; A6R207; -.
DR STRING; 339724.A6R207; -.
DR VEuPathDB; FungiDB:HCAG_03665; -.
DR HOGENOM; CLU_002360_3_2_1; -.
DR OMA; KMHACET; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0030001; P:metal ion transport; IEA:UniProt.
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; 2.
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; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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 SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000009297};
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 369..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 934..954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1014..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1046..1063
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..134
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 30..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1092 AA; 117590 MW; E15662203DD1A129 CRC64;
MSLQGVGGGR KGEGLGDGKR VCLKFQGGLP KRAKNGVAGN HVTPSPHRKS TVVSSSSTST
YSRLSPQEVA DRLQTSLSHG LSPADAHTRL LRDGPNELSS EDPEPLWMRF LKQFKEPLIL
LLLASAAISF FMSNYDDAIS IALAVTIVVS VGFVQEYRSE KSLEALNRMV PHYAHLIRNV
HHLDSLGHVA PQTANGVAEL ELQGLMTDGP HPVTSSPKAS TTVLASQLVP GDLVLFSTGD
RIPADLRIFS STGLSIDESN LTGENEPVAK SSESLGNANG SLQSIKENTG SISPYYHSPA
AGTVGTDLRL NEQHNIAFMG TLVRSGYGQG IVIATGSNTE FGSISASLRE IESPRTPLQL
SMDRLGQELS YVSFAVIGLI VLIGLLQGRK LLDMFTIGVS LAVAAIPEGL PIIVTVTLAL
GVFRMARRGA IVRRLPSVET LGSVNVVCSD KTGTLTLNHM TVTKMWHFDC DAPFEVNRDS
RSVNASPAAR TILRVGNIAN NARLSRAHAN SPATAASAAI LSSTVDQTSG AIRSRWVGQP
TDVAILDLLD AFAEDDIRDH ISSRVAETPF SSERKWMGVV IGGGSHLSEN GFGNGGCPET
AYIKGSIEEV LKRCDTYLTK DGREVILDET RRQIVREAAE SMAKEGLRVL GFASGPVRDI
GKGSRPLGSR SPTPGHSEKI QSKDDDLYTG LVFSGLVGMN DPPRKDVHRA LRKLMAGGVR
VIMITGDAET TAVAIARKLG MPVNTSPSAR EVLRGEDVDR MSTDELAQTI SATSIFARTS
PDHKMKIVRA LQSRGNVVAM TGDGVNDAPA LKKADIGISM GRLGTDVAKE AADMILTDDD
FSTILRAIEQ GKGIFYNIQN FITFQLSTSV AALSLVLFST TLGFKNPLNA MQILWINILM
DGPPAQSLGV EPVDPSIMSR PPRSKHARVL TKPLIRRVLT SALLIMLGTF AIYIHEMSDH
TDEVSGARSR IVTSRDTTMT FTCFVLFDMF NALTCRSETK SILRGELPLF GNKMFNYAVL
GSLVGHACVI YLPLLQGIFQ TEAIKLWDLF VLVCISSTVF WVDEGRKYLA WRKRNGGVGI
SGMRIGGYSV NV
//
