ID U1I277_ENDPU Unreviewed; 1418 AA.
AC U1I277;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=EPUS_01397 {ECO:0000313|EMBL:ERF76064.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF76064.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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}.
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DR EMBL; KE720780; ERF76064.1; -; Genomic_DNA.
DR RefSeq; XP_007786530.1; XM_007788340.1.
DR GeneID; 19236454; -.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_3_1; -.
DR OMA; QWGYSIV; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000019373; 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; cd02081; P-type_ATPase_Ca_PMCA-like; 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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 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; 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:RU361146};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW 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:UP000019373};
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 289..310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 493..514
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 534..561
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 987..1008
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1014..1036
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1057..1082
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1135..1162
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1168..1189
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 252..300
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 1014..1189
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1418 AA; 153532 MW; D05463EBB36B40B4 CRC64;
MSNSPEHGDP SADTDAPAGS GAPTINVDGP ERPRPLPRIQ TDGLSELPST IPAHPPSSAE
VQRETSVDTT NSHPTSAHNV SSATHKPNDS LGQNFLAVPN TRSRGSSIES NDSRSPSSYG
GDTYISSAGT AAEDGKENHN NSKIMNAADA LKPDPHNEAE FHVENNKFAF TPGQLNKMIN
PKSLEAFYAL GGLAGLEKGL RTNRQSGLSV DEADFDGTIS FDEAIRAGSA EKELGPVKRT
NTSGAMISPA ELTSNSFADR KRIFSDNRLP QKKAKTIWEL AWIAYNDKVL ILLSVAAVIS
LALGIFQSVR PRPGETEANV EWVEGVAIVV AILIVVTVGA ANDWQKERQF VKLNRKKEER
FVKVIRSGKS QEISVYDVLV GDLMHLEPGD LIPVDGIYIE GHNLKCDESS ATGESDIIKK
TPADQVFRAI ENHEPLGKMD PFILSGGKVT EGVGTFLVTS VGIYSSYGKT MMSLQDEGQT
TPLQSKLNVL AEYIAKLGLA AGLLLFIVLF IKFLAELNSI QGGADAKGQQ FLQIFIVAVT
VVVVAVPEGL PLAVTLALAF ATTRMLRDNN LVRVLRACET MGNATTVCSD KTGTLTQNKM
SVVAGTVGTS SRFSDAQTVS VAAGEKGDKE AEMPGDAQGV SSSELTSTLS KEVKELLKDS
IVLNSTAFEA EENGQVIFIG SKTETALLNF ANERLGIGSI AQERSNADVA QMIPFDSGRK
CMAVVIKMGN GNYRMLVKGA SEILLGRCTR IIRDPTQGAA ETTLTSENME SLNAIIKNYA
SRSLRTIGLL YRDYDRWPPL GAPTQKDDPR LADFDKIFKD MTFLGIVGIQ DPLRPGVTEA
VHKCQGAGVF VRMVTGDNLM TAKAIATECG IFTAGGIAME GPIFRRLTSK QMTQIIPRLQ
VLARSSPEDK RILVKQLRKL GETVAVTGDG TNDAPALKAA DVGFSMGIAG TEVAKEASAI
ILMDDNFTSI VKAISWGRTV NDAVKKFLQF QITVNITAVV LTFVSAVASG DESSVLTAVQ
LLWVNLIMDT FAALALATDP PTPSLLKRKP EPRSAPLITL TMWKMIIGQS IYQLVVCLIL
NFRGADIFGY TDPHELEQLP TLIFNTFVWM QIFNQYNARR LDNKFNIFEG ITKNYWFIGI
QFVIVGGQVM IIFVGGAAFA VTRLNGPQWG YSIVLGLLAV PVAIIIRLIP DELVRKLLSF
LPRRHSSTPS FMFEDDEQVQ EWNPALEDIR EELTFLKKVR GGRMSELAYK LQHPRQSFVP
RSRSGSRSRS NNSLPPSPQE PEKAVPPAAV SPPTPEKGKR RDRSRSNSRF GPAAAMAGII
AGSVAGGWSP VERGQEETDS IKFSKSQIHG GLGATNGIEV HPDTRPDDPV IVENPEKSRV
PPSQNPALTP RFDHATNNND STNSKRGHHH SHHASSNA
//
