ID K1X7U1_MARBU Unreviewed; 1146 AA.
AC K1X7U1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Copper resistance-associated P-type ATPase {ECO:0000313|EMBL:EKD16688.1};
GN ORFNames=MBM_05157 {ECO:0000313|EMBL:EKD16688.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD16688.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD16688.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD16688.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|RuleBase:RU362081}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH921438; EKD16688.1; -; Genomic_DNA.
DR RefSeq; XP_007293046.1; XM_007292984.1.
DR AlphaFoldDB; K1X7U1; -.
DR STRING; 1072389.K1X7U1; -.
DR GeneID; 18761092; -.
DR KEGG; mbe:MBM_05157; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_2_1; -.
DR InParanoid; K1X7U1; -.
DR OMA; KFGSMNM; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 3.
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; 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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF32; COPPER RESISTANCE P-TYPE ATPASE (EUROFUNG); 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
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; SSF55008; HMA, heavy metal-associated domain; 3.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 367..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 415..437
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 464..485
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 497..515
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 669..693
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 713..743
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1074..1095
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1107..1127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 189..254
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1146 AA; 123505 MW; 2918D964E578C01D CRC64;
MDTTIIPEKM APSMLNMVIS SFILSNLHCP SCVSTIKNTL YALDPSPFSV SPSLVSSVVT
VEHSEALPAT EIQEALENAG FEIYDATGAP ILALGKSHMG SEEDAGYLDR IIDRFSSDQS
SRRRQKRQTS SSQHVQQCDA CRTGFSRSSD SNFSSSANLR NTNAMSSASS VSSLVVIDST
DSPIKPDLWR ASLAIGGMTC AACVSAITED LEKKDWVKKV VVNLISNSAT IEFIGEHHKD
DIVRSIEDIG YEAAIDTVVD ANQTNSVIRS GERTMEIQVD GMVCDHCPPR VHAALKSFGN
KVKVDRPVSL ENNILKITYI PQVPHFTIRN IIQALSEADN ALTPSIYHPP TLEERSRQLH
AREQLRILIR VILTLIVAIP ALIIGIIYMS LVPASNGGRM YLMKTLEAGV SRAQWALFIM
STPVYFLCAD VFHIRALKEI RSMWRRGSPT PILQRFYRFG SMNMLMSLGT SIAYISSVAQ
LIAAAVQRPK EVDNSEFYFD SVVFLTLFLL VGRLIESYSK SKTGDAVTLL GKLRPTEALL
VESGRRSSEH TLIDEQDANG TPSETTKNVN VDMLEFGDVV KILHGGSPPC DGAVVQGESK
FDESSLTGES RLVHKIFGDD VFSGTVNKGS PISVQITGVA GASMLDQIVK AVREGQTRRA
PMERIADALT GYFVPFVTLI ALMTWLVWLG LGMSGALPKS YLGTDKGGDT SEWVAWSLQF
AIAVFVVACP CGLALAAPTA LFVGGGLAAK YGILVKGGGE AFEKASKLDC VVFDKTGTLT
VGGEPVVTDF DILPFDSGMD HMESRMLILG MVGALESNSS HTIAKALVSL CKTHKTTDLD
VDLVEETAGR GLSGKFFLKE RGAEAKVIIG NEAFMKYNDV VLLGPTQSTI EKWKLEGKSI
ALVAISVNHS MSLLTPGSWE VAAMFAISDP IRPEAPGIIK ALQARGTDVW MLSGDNQMTA
DAIGTKIGIP TSNIIAGVLP SEKAEKINYL QRSLKACTSS GAEHSTNRAL VAMVGDGIND
SPALTTADVG IAIGSGSDIA ISSAEFVLVS SNLNSLITLL DLSKFVFRRI KFNFGWALIY
NLIALPVAAG VLYPIVSKGH HVRLDPVWGS LAMALSSISV VCSSLALRSR VPWIGFKAKE
AVGEKE
//
