ID A0A066X6F9_COLSU Unreviewed; 1165 AA.
AC A0A066X6F9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putative heavy metal translocating P-type ATPase {ECO:0000313|EMBL:KDN61605.1};
GN ORFNames=CSUB01_01430 {ECO:0000313|EMBL:KDN61605.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN61605.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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 -!- 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:KDN61605.1}.
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DR EMBL; JMSE01001398; KDN61605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066X6F9; -.
DR STRING; 1173701.A0A066X6F9; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_1_1; -.
DR OMA; GGKFMVC; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000027238; 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:0005507; F:copper ion binding; IEA:InterPro.
DR CDD; cd00371; HMA; 4.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 4.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 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; 3.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 4.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00942; CUATPASEI.
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; 4.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 4.
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|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
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 387..409
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 462..485
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 674..696
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 716..738
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1065..1088
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1094..1113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 30..96
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 123..189
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 212..278
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 295..361
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1165 AA; 123784 MW; C49EC2F2585D2E7A CRC64;
MAPPAIRVPG KFEAGGPTAT LATPTPTQWA TTTLKVGGMT CGACTSAVES GFRGVNGVGS
VSVSLVMERA VVMHNPEAIS AEKIAEIIED RGFDAEVLST DLPSPMFPTN KDLFDAEEEN
GFMTTTIAVE GMTCGACTSA VEGGFKDIPG VKNFSISLLS ERAVIEHDPE LLTAEQIAEI
IEDRGFGAEI IDSESTQEEK PRASSNPTSS VATTTVAIEG MTCGACTSAV EGGFKELEGV
LRFNISLLAE RAVITHDTTK LAAEKIAEII EDRGFGAEIL STAFETSAQG NGAASTAQFK
IYGSPDANSA MALEAKLLTI PGINSAKLSL ATSRLTVTHQ PTIVGLRGIV EAVEAEGLNA
LVSDNDDNNA QLESLAKTRE INEWRRAFKL SLTFAIPVFV ISMALPMFLP SLDFGSWELL
PGIFLGDLIC LALTIPVQFG IGKRFYVSGW KSIKHGSPTM DVLVILGTSC AFFFSIIAML
VSFLFPPHTK PATLFETSTM LITFVTLGRF LENRAKGQTS KALSRLMSLA PSMATIYADP
IAAEKAAEGW ENAAISGEPK TPNRDGNAAE ERVIPTELLQ VGDVVILRPG DKIPADGVLV
RGETYVDESM VTGEAMPVQK KKGSYLIGGT VNGHGRVDFR VTRAGRDTQL SQIVKLVQDA
QTTRAPIQRL ADTLAGYFVP SILVLGFLTF FVWMILSHVL TNPPKIFTQE ASGGKIMVCV
KLCISVIVFA CPCALGLATP TAVMVGTGIG AENGILVKGG AALETTTRIT QIVLDKTGTI
TYGKMTVAKM SLVSAWQDIE WRRRLWWHIV GLAEMGSEHP VGKAVLGAAK AELGVDEDAT
IEGSVGEFKA AVGKGINALV EPATGNDRTR YRVLIGNVRF LRENNVNIPD EAVDASEQLN
VKANSGSKNT SAGTTNIFIA IDGQYSGHLC LSDTIKEGAA AAIAVLHRMK IKTAIVTGDQ
RSTAVAVAAA VGISTEDVYA GVSPDQKQAI VQQLRDQGEV VGMVGDGIND SPALATADVG
IAMASGTDVA MEAADVVLMR PTDLMDIPAA LHLARSIFNR IKLNLAWACL YNAIGLPFAM
GIFLPFGLHL HPMAAGAAMA CSSVSVVISS LLLKFWTRPS YMVDPSARTQ RRGFGLLNRV
KYAVRKLRGR RTQDQGYVPL ANMAE
//
