ID Q7RZE4_NEUCR Unreviewed; 1292 AA.
AC Q7RZE4;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 3.
DT 27-MAR-2024, entry version 142.
DE SubName: Full=Copper resistance-associated P-type ATPase {ECO:0000313|EMBL:EAA28455.3};
GN ORFNames=NCU04076 {ECO:0000313|EMBL:EAA28455.3};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA28455.3, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:EAA28455.3, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002241; EAA28455.3; -; Genomic_DNA.
DR RefSeq; XP_957691.3; XM_952598.3.
DR STRING; 367110.Q7RZE4; -.
DR PaxDb; 5141-EFNCRP00000003621; -.
DR EnsemblFungi; EAA28455; EAA28455; NCU04076.
DR GeneID; 3873781; -.
DR KEGG; ncr:NCU04076; -.
DR VEuPathDB; FungiDB:NCU04076; -.
DR HOGENOM; CLU_001771_0_2_1; -.
DR InParanoid; Q7RZE4; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
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 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; 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; 3.
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:UP000001805};
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 538..562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 582..601
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 670..688
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 826..849
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 869..897
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1222..1243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1255..1275
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 36..118
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 260..325
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 353..418
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1292 AA; 138820 MW; B77C5F85B0CC6D15 CRC64;
MIPTNDMPTP RRRQQQQQQS SSATGTETSD IPAKTITTSF LISNLHCPSC VSAIKDVLLG
EPSTGSHIRW VSPNVVTSVV TVEHDSGSSD NNNNSAASAS SLIRDMQRAL EDSGFEVSGV
TTTATVGDHD NDNDDNGGFP VRDLGIQAEG EFCTFSRWVT TASRRTNSPF GSQKRAETHF
QNCEQCRTSK ATTGHHVPEK TSEKEKESPV SGVRGIHAPP DLLTNPPKNM ASTSTNQSFS
TDTVVDLGGK VPSSQPPPLY RVTVAIGGMT CAACVNTITN ELNKKDWIAH VSVNLINNSA
AIDIHDESRA TELVEAIEDL GYDVKLDKVI ALADPSKPPP KPKAGGEILS DAWRATVSIG
GMTCASCANS ITNEMKKRDW IQDITVNLLT NSATVEFAGR ENANKLVGEI EDLGFEATLN
EETLVNVAIH EGGPNPEEEQ QQRREVEIRI QGMYCEHCPS RVSASLAGFR RQLDVISQPS
HKRPIVKIVY VPDAPEFTIR HILKAIEASD PAFKASIYHP PSLEEQSKAI QRHHQMQILW
RVLFSLVVAI PTFIIGIVYM NLIKASSGNK SREFLMKPWT SGISRGQIAL FILATPVYFF
AADIFHKRAY KEIRTLWRRS SRVPLLQRFY RFGSMNTLMS LGTTIAYVSS VCQMIAAGAQ
KVHMVDNANF YFDSVVFLTF FLLLGRLLES YSKSRTGDAV EMLGKLRPTT AILVEGYGTA
KERDEVVQAD SLDYGDVVRI PHGASPPADG IVVRGEGSLD ESSLTGESRP VKKIVGDEVY
TGTVNKDAPL LVRVTGVAGK SMLDEVVKAV REGQTKRAPI EQVADILTAY FVPVVTAIAV
ATWIIWLAVG YSGHVSNDLL GDTKGGWVVF ALQFAISVFV VACPCGLALA APTAIFVGGG
IAAKHGILAK GGGEAFEKAS RVDCVVFDKT GTLTMGGEPK ITESEVFHDA AADGEAGTVF
AALKAVEENS SHPIAKAIVA FCAAKTSAKA QVEDLQEIAG KGMKARCIGV DSQNDFDLIV
GNESLMEDFC VTVSNETVQT LQKWKREAKS VALVAIRRHQ SNDPNRWLLA VTLAISDPIR
PEAPLIVDAL QSRGTRVWML SGDNPVTAAA VAHQLGIPAD QVIAGVLPTG KADKIGYLQG
TEKARVGKGS ESSTRRALVA MVGDGINDSP ALATADIGIA IGSGADIAIS SADFVLINSD
LRGVVTLLDL SSAVFQRIKF NFGWAVIYNC IGVPVAAGAF YPIVSHGHHV TLNPAWASLA
MALSSISVVL SSLALRSRVP GAGFRARKIG QE
//
