ID S7Q7G7_GLOTA Unreviewed; 1095 AA.
AC S7Q7G7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Ca-transporting ATPase {ECO:0000313|EMBL:EPQ55398.1};
GN ORFNames=GLOTRDRAFT_116296 {ECO:0000313|EMBL:EPQ55398.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ55398.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ55398.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ55398.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KB469302; EPQ55398.1; -; Genomic_DNA.
DR RefSeq; XP_007866524.1; XM_007868333.1.
DR AlphaFoldDB; S7Q7G7; -.
DR STRING; 670483.S7Q7G7; -.
DR GeneID; 19300163; -.
DR KEGG; gtr:GLOTRDRAFT_116296; -.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_3_1; -.
DR OMA; KMHACET; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000030669; 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; 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; 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 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 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:UP000030669};
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 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 888..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 961..983
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1024..1042
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1054..1072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 157..232
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 117283 MW; 7A060D7235A5D188 CRC64;
MGYERRKSPA RDLGNGFPMS SSSSYGLSHV SLSGRSQTML PYAQRSPSPP ASAYFTSIPP
DHGHEPEPSP GAAEHFAYST TLRRHHTEPF GPSASGSLPT LGSLGSVVSQ EGPSGLWNRA
VSFVKSRLGG QENDLENGNG YANGLRKEPH EETPSARFAH ISAEDTISHF HTSPTEGLPS
SHIPALREEY GYNEFSVSAP EPAYIKFAKT IYESPLILLL CGSAFISAIM GNIDDAVSIT
VAVLIVLTVG FVQERRSEKS LEALNKLVPH HCHLIRDGHS LTVLANELVP GDIVTFTTGD
RIPADVRLIS AVDLEIDESS LTGETTSRRK DAETCVSGGM GGPAALADRT CIAYMGTLVR
NGRGSGTVIA TGKDTEFGVI FSMMEDVEER RTPLQLKMDE LAKNLSILSF GIIGLICIIG
VLQQRSWLEM FTIGVSLAVA AIPEGLPIVT TVTLALGVLR MSNRKAIVKK LHSVEALGSV
SVICSDKTGT LTKNEQTVTE LYTVDEAVHI DPATRVHSAH QVSAAVKKAL EIGALCNNAS
ASRNEEGVFV GQSTDVALLN ILSSFNLDDP RKNFTRLSER PFNSEVKYMA VSGIHSGYSG
PTINGSPLEF YYIKGSIDAI LDRCKFYYVS DGSTPGLDST TKAMILQKAQ ATASRGLRVI
ALAYGYGSVD AQTEMASSNS LASVASRAGT PESEKAKTNL VFVGFQAMFD PPRKGVSDAI
SLLQQAGVQV VMITGDAEQT ALAIAKDLGL LVGRAMHGRA GSISGSGSLS AVAGSGSYCL
TGQMIDRMSK GQLKEMVGGV SVFARTTPRH KMAIVEAFQA RGAVVAMTGD GVNDAPALKM
ADIGVSMGKS GTDVAKEAAD MILVDDNFTT ILPAVEEGKS IFHNIQNFLA FQLSTAAAAL
SMITLSTMFG LSNPLNAMQI LFINILMDGP PSQSLGVDPV DPIVMRRPPR RKDEPIISRR
LMYRVLFSAS MIVIGTLYVY AYALSDDHMS KREQTMTFTS FVFLDLVSAL QNRGLACSLT
ANRMLLTTVS ISFLSQLALV YVPFMQSIFQ TEALGAGDMT TLLCLAGLSF GLHEARRRWE
RKLDREMGGW AGEMA
//
