ID A0A010QP82_9PEZI Unreviewed; 1253 AA.
AC A0A010QP82;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:EXF81897.1};
GN ORFNames=CFIO01_02605 {ECO:0000313|EMBL:EXF81897.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF81897.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF81897.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF81897.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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}.
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:EXF81897.1}.
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DR EMBL; JARH01000344; EXF81897.1; -; Genomic_DNA.
DR RefSeq; XP_007594400.1; XM_007594338.1.
DR AlphaFoldDB; A0A010QP82; -.
DR STRING; 1445577.A0A010QP82; -.
DR KEGG; cfj:CFIO01_02605; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_0_1; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000020467; 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; 1.
DR Gene3D; 3.30.70.100; -; 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; 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; 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; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR46594:SF4; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 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|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467};
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 594..614
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 621..640
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 660..681
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 842..868
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 880..906
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1202..1223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1229..1248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 442..509
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1253 AA; 132558 MW; A1AA155BA5D27C5B CRC64;
MACGSGCCGP PQEQAVARDG PPPVASPPDE LDRDDPGVVD TCCANVVFET KVDKCKTTDH
GKDKDSGNAA IRQCCAASND GSIDSAHAED DCCAPKVKID DCVNACCGSN NEHFAAISPE
ANSIAEPATE SAKKLPGVGC QFEQDDLASK SIVESSNTSE VSQGFCAPKP KDCSSGCCGS
ARGKRPTDSP ETTSIGAIAG KAISVTESDG DKAIKICSDD GEKGCCSSGP TTEVHGQKTP
SCCEGKTSPC CDSTCIDRLA LRECASRKAS KLRQSYQASG DEDCTGGQDG KACRGHSRSV
REIYQSKLDA LGCICRALLA LGQESCCAPR ERSSIERKRS SRKSSSLHRI SADSCCASVV
NKSASRPSAR SCGKKTTRSS TSGNKPSARN DGCCSKPTSG RIVRSCANSC CDKSPSRPIN
QPLPPESKDV KGDLERGLVG KEHVVLSISG MTCTGCETKL RRTLATVNAV KNLKTSLVLA
RAEFDLNIAA GSVDEVIKHL ERTTEFKCEK ITAQGAASVD IICPGDPQEF INQPWPNGVT
DIRVIDKTNV HVEFDAKVVG ARDLVETGWR TPVTLAPLRA DPSLEAGNKH IRNMGWITLL
STILTIPVLI MAWAPLQKRE IAYGSASLAL ATIVQVAIAG PFYPKALKSL IFSGVIEMDL
LIVLSTSTAY IFSVVSFGLL VSQKPLSTGE FFETSTLLVT LIMVGRYVSA LARQKAVESI
SIRSLQTSTA LIINSVGEDE EIDARLLQYG DNFKVVPDSR IPTDGTVILG SSEVDESMMT
GESERIDKCT GSSVIAGTMN GSGALTIRLT RLPGNNTISN IAGMVNEAKL SKPKVQDIAD
RVASYFVPVI VAITIITFSI WIAVGIAVRK QSGSEATIQA VTYAITVLIV SCPCAIGLAV
PMVILIASGV AAEKGVVFKS ADSIELAYKT SHVVFDKTGT LTTGNLRVVD ESYFTQDQET
IRSVLLGLVG TIRHPVSVAI FTHLKTHVGT PTAVTDLKAL TGKGVEAKLD GATLRAGNSR
WLGLSTDPRV QPVLSKSYTA FCLTVDNSLV AVFGLEDSIR TDALETISNL QASGISVHIL
SGDDDGAVRT VASRLSVPDL NVRSRCTPRD KQEYIQNLLS QPLSDPHRVR AKNPKEPVVI
FCGDGTNDAV ALAQATIGVH MSEGTDVAKS AADVVLVRPS LTGILTIIAI SKKATHRIAF
NFGWSFVYNL FAILLGAGAF VNARIPPEFA GLGELVSVLP VIATAVLLRW TAI
//
