ID A7X9R7_PENJA Unreviewed; 1115 AA.
AC A7X9R7;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Copper transporting P-type ATPase protein {ECO:0000313|EMBL:ABU80435.1};
DE Flags: Fragment;
GN Name=PcpA {ECO:0000313|EMBL:ABU80435.1};
OS Penicillium janthinellum (Penicillium vitale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5079 {ECO:0000313|EMBL:ABU80435.1};
RN [1] {ECO:0000313|EMBL:ABU80435.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GXCR {ECO:0000313|EMBL:ABU80435.1};
RA Lai H.-M., Tang H.-Y., Li Y.-Z.;
RT "Penicillium janthinellum strain GXCR copper-transporting P-type ATPase
RT gene.";
RL Submitted (JUL-2007) 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; EU054430; ABU80435.1; -; mRNA.
DR AlphaFoldDB; A7X9R7; -.
DR BRENDA; 7.2.2.9; 4621.
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 CDD; cd02094; P-type_ATPase_Cu-like; 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 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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 2: Evidence at transcript level;
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 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 467..487
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 493..512
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 533..555
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 716..737
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 757..785
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1064..1085
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1091..1110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 316..383
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 68..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABU80435.1"
SQ SEQUENCE 1115 AA; 119120 MW; C312A3557A4CB39C CRC64;
HKACSQHSLS ALDRYGATLQ ALGCICRALI ALGQETCCEI RERQTLGRKQ CSRKSSARSL
LRTSLDSYSS NGSLTKDQAA QNHLRLRRGS RESAKSVKKP CADPCVDSFC STDKASKEPP
FESKCPKSCY SGGQPVKEPY PKSNFDDSCC TEDNIKETPT KTKCSYSRFL EAPRVEDSPS
KVSCPGSCCP GDQPVKDNDS KSTYADSSSS KIKPIVESPT SGCAGSCCGK GEDTITQEPS
NAASFGSCCK PPKQDILKTS KTSCTDSCCT EKQPVSPRGS CTDACNSSTA NNSGLEIEKA
PNRAITDLES QGIGDEHVVL SISGMTCTGC ETKLNRTLAT VRAVKDLKTS LVLSRAEFNI
DLRLGSVEDV IKHLERTTEF KCERVQNQGS SLDLIVPDEP SKFISQTWPD GVLDMAPVDK
QTVRVAFDPR IVGARDLTEK LWGRPIELAP PRGDPSLEAG SKHVRHVGYM TLLSAALTIP
VLVMAWAPLP ERAVAYASAS LTLATIVQVV IAGPFYPKAL KALVFSRVIE MDLLIVLSTS
AAYIFSVVSF GYLVAEQPLS TGQFFETSTL LVTLIMAGRW VAALTRQRAI ASISIRSLQA
STAILVDEET GTEREIDARL FQYGDTFKVL PDTKIPTDGT VINGSSEVDE SMLTGESRPV
EKYAESVVIA GSINGPGVMT VRLNRLPSDN TINAIAAMVD EAKLSKPKLQ DLADRVASYF
VPVVVALTII TFVIWVAVGM TLRGHDGSEA TIQAITYAIT VLIVSCPCAI GLAVPMVIVI
VSGVVAERGI IFKSADAIEV AHKTSHVVFD KTGTLTQGKL SVVAKNCVKV DNLPLLLGLI
ETSRHPVSVS VATYLKETGV TASTVSESKS LTGKGIETTF GGRKLQAGNS RWLNLSENEH
VQQMLAQGYT VFCFTIDNAL QAVYGLEDEL RPDAAATIET LQKRDVSVHV VSGDDDGAVH
SLASKLGIPG GNVRSRSSPA DKKDYIQTLL GTGADGNKPV VVFCGDGTND AAALAQATIG
VHINEGTDVA QSAADEVLMR PSLAGICTMM NASQKSVNRI KLNFIWSFVY NTFAVLLAAG
ASVNARIPPE FAGLGELVSV LPVIAAAVLL RWSKI
//
