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Database: UniProt
Entry: L2G1A3_COLFN
LinkDB: L2G1A3_COLFN
Original site: L2G1A3_COLFN 
ID   L2G1A3_COLFN            Unreviewed;      1207 AA.
AC   L2G1A3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Copper resistance-associated p-type atpase {ECO:0000313|EMBL:ELA32347.1};
GN   ORFNames=CGGC5_7583 {ECO:0000313|EMBL:ELA32347.1};
OS   Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS   (Colletotrichum gloeosporioides (strain Nara gc5)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA32347.1};
RN   [1] {ECO:0000313|EMBL:ELA32347.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA32347.1};
RA   Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT   fructicola.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KB020710; ELA32347.1; -; Genomic_DNA.
DR   RefSeq; XP_007278619.1; XM_007278557.1.
DR   AlphaFoldDB; L2G1A3; -.
DR   STRING; 1213859.L2G1A3; -.
DR   EnsemblFungi; ELA32347; ELA32347; CGGC5_7583.
DR   HOGENOM; CLU_001771_0_2_1; -.
DR   OrthoDB; 5480493at2759; -.
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:0005507; F:copper ion binding; IEA:InterPro.
DR   CDD; cd00371; HMA; 3.
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; IPR006122; HMA_Cu_ion-bd.
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; 2.
DR   NCBIfam; TIGR00003; copper ion binding protein; 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; SFLDS00003; Haloacid_Dehalogenase; 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; 2.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022796};
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   Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT   TRANSMEM        449..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        494..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        545..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        579..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        737..759
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        779..807
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        1137..1158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        1170..1190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          192..257
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          273..338
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   1207 AA;  130880 MW;  19EAAB7F464205DF CRC64;
     MPSGLRIIDT WAWFQTYPLQ YNPLTVLNFV LYGFQEDKPF GGSTFLVPNI HCPTCTGFIE
     PLLRELTPSP KSIITSIINH SVTVEHDKAL SAKKVSRVLA DAGYEVDSII IGPQVQEPES
     GRVPQPPNAV VPVSLLRRLY EALGCIGTQI NEDEKQRRHA EHCMQCREEE LEGHGEAISG
     VAIGNDQSLK LHRAIISIDG MTCSSCVGNV TSALEAQTWV QSVNVGLITR AATIEFFDEN
     KTNELVNIIE SLGYDPTLER VEEVAESSTD NLWQASLSIM GMTCSSCVGT VTGALEKLPY
     TESVNVNLVT SSAVVNFHDK SHLNNIVSTI EDLGYEATPN NLIEVTSDQS KDSHRVLSIR
     VTGMYCAHCP GRVLAAFSPF GDRLSVKEQG TLENPIFTVT YVPQAPDFTV RAILESIMGT
     DGAFVPTVYH PPTMEERSQQ MMHRTRFRLM LRVLLCFVAA IPTLIIGIVY MNLVSPENHG
     RHYLMQPLNG VSRAEWSLLI MATPVYFFAA DVFHRRAIKE LYSLWRPGSP VPILRRLYRF
     GSMDMLVSFA TTIAYFSSIA EIVIAATNNH HMEMQSRPSH MDAVVFLTLF LLVGRMIEAY
     SKAKTGEAVS KLGTLRPKDA LLLLDDQNGE SQVKTIGVDL LDCGDRVRVV HGGSPPWDGV
     LIDGFNAEFV ESSLTGESKP VEKRLGDYIY SGTVNNGGPI TMQITGASGD SLLDQIIKVV
     RDGQARRAPI ERVADSITGY FVPVVTLIAI ATWLIWLGLG LAGRLPADYK DVVVGGWPFW
     SLQFAIAVFV IACPCGIGLA APTALFVGGG LAAKHGILAK GGGEAFQEAS NLDIIVFDKT
     GTLTEGGEPT LTDHRILAID DAQKGAWDEN IILGCLVELE SNSSHPIAKA ITTFCGPQRR
     NSFKSTSITE VPGKGIKGTF TGASFSAPFE IIVGNEALMA DHGAFFDEQT LEKLDSWKSQ
     AKSVVLAAGK FVSSDDGVRW NPLAIFAVSD AIRPEAKPVL DALREQGIDV WMLSGDNAKT
     ARAVGAMVGI PEDHIIAGVL PEQKAEKIEY LQKSQIKVES FLGIGNSRYR RPTVAMVGDG
     INDSPALTVA DVGIAIGSGS DVAISAADFV LINSSLATLL TLTSLSRAVF RRVKFNFAWA
     LVYNLVALPI AAGVLYPIKT NGSNTRLDPV WAALAMALSS LSVITSSLLL RLPLPVVGYK
     TKTIGNL
//
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