ID A0A059IYH6_TRIIM Unreviewed; 1009 AA.
AC A0A059IYH6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=H109_07535 {ECO:0000313|EMBL:KDB20508.1};
OS Trichophyton interdigitale (strain MR816).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB20508.1, ECO:0000313|Proteomes:UP000024533};
RN [1] {ECO:0000313|EMBL:KDB20508.1, ECO:0000313|Proteomes:UP000024533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR816 {ECO:0000313|EMBL:KDB20508.1,
RC ECO:0000313|Proteomes:UP000024533};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Trichophyton interdigitale MR816.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000256|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
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:KDB20508.1}.
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DR EMBL; AOKY01000771; KDB20508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059IYH6; -.
DR STRING; 1215338.A0A059IYH6; -.
DR HOGENOM; CLU_002360_3_2_1; -.
DR OMA; PLWNNMM; -.
DR Proteomes; UP000024533; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02083; P-type_ATPase_SERCA; 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; 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; IPR005782; P-type_ATPase_IIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF127; CALCIUM-TRANSPORTING ATPASE SARCOPLASMIC_ENDOPLASMIC RETICULUM TYPE; 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 PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW Calcium {ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|RuleBase:RU361146};
KW Ion transport {ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000024533};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361146};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 61..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 84..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 257..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 288..317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 754..775
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 787..806
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 827..849
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 890..910
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 922..946
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 3..77
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1009 AA; 109531 MW; 3AF1108D6F227F3F CRC64;
MERSFLSTPQ EVLAHFGVTE DAGLPESQVA KNREKYGSNA LEEEPPTPLW QLILEQFKDQ
LVIILLGSAV VSFVLALFEE GEGWTAFVDP IVILTILVLN AIVGVSQESS AEKAIAALQE
YSANEAKVVR DGAIHRIKAE ELVPGDIISV AVGDRVPADC RLLTIQSNSF RVDQAILTGE
SQSVSKTTNA IQDPQAVKQD QINLIFSGTT VVTGHATAIV VLTGASTAIG DIHESITAQI
SEPTPLKQKL NNFGDSLAKV ITVICILVWL INIEHFGDPS HGSWAKGAIY YLKIAVSLGV
AAIPEGLAVV ITTCLALGTR KMAAKNAVVR SLPSVETLGS CSVICSDKTG TLTTNQMSVS
RIVYLNEAGN GLEEIEVEGT TFAPHGDLKL HGKVLKDLAA SSATIQQMTE VMALCNEAEL
AYDTKTGTFS NIGEPTEGAL RTLAEKIGTD SAAINAKIRS LPPAECVHAV SKHYETRSPV
QATYEFCRDR KSMSVLAGKG RSQKLLVKGA PESILERCSH AITGPNGDKV PLTKKLVSLI
QQEVADYGDQ GLRIIAIANI VNVPETPLLH TAQTSEEYEK LEQDMTLIGL VAMLDPPRPE
VRASIEKCRE AGIRVIVITG DNQHTAESIC RQIGIFGKNE DLRGKSFTGR EFDELSEQGK
LEAAKNGMLF SRTEPTHKSK LVDLLQSIGH VVAMTGDGVN DAPALKKSDI GVAMGSGTDV
AKLAADMVLA DDNFATIEVA IEEGRSIYSN TQQFIRYLIS SNIGEVVSIF LTAALGMPEA
LVPVQLLWVN LVTDGLPATA LSFNPADHDI MRRPPRKRDE PLVGGWLFFR YMVIGIYVGA
ATVFGYAWYF MFNPEGPQIS FWQLSHFHKC SREFSEIGCD MFTNDMSKSA STISLSILVV
IEMLNAMNAL SSSESLFTFP LWNNMMLVYA IMLSMSLHFA ILYIPFLQSL FNILPLNWLE
WKAVLAISAP VIVIDELLKY IERALYVTHV TPSHEAESQN GSNTKPKAS
//
