ID S0DNJ4_GIBF5 Unreviewed; 1230 AA.
AC S0DNJ4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Probable P-type ATPase {ECO:0000313|EMBL:CCT64000.1};
GN ORFNames=FFUJ_04824 {ECO:0000313|EMBL:CCT64000.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT64000.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|EMBL:CCT64000.1, ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
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; HF679024; CCT64000.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DNJ4; -.
DR STRING; 1279085.S0DNJ4; -.
DR EnsemblFungi; CCT64000; CCT64000; FFUJ_04824.
DR VEuPathDB; FungiDB:FFUJ_04824; -.
DR HOGENOM; CLU_001771_0_0_1; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000016800; Chromosome 2.
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 PRINTS; PR00120; HATPASE.
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 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:UP000016800};
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 582..603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 609..627
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 831..857
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 869..895
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1179..1200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1206..1225
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 431..498
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1230 AA; 130480 MW; 9ECBD81D599D3474 CRC64;
MGCDCCGPPA PAAESVTAET PPPSDIGSCK DACRDGSDAA TQVKEEEPAN KEQDDDCCAS
GSCEEPNKDD APECCRGKTS PCCNASCIDR IAIRECELSA SHKPDATGCG SSSSSCNGAA
DGKACSKHSL SALDRYGATL KALGCICRAL VALGQESCCE TKGRSVVTKQ CSRKSSSRSL
IRKSTDYCCT TGSVTKEKAA ENRLRLRKGS NESARSAKQP SVKESCTKPC CSVVKPDKEA
ASKKCTSSCC SGDNGKYNCA DPKPVKDKDK DNCSAGCCSK KAAPKSPLVE KSCASNCCSD
GDLSKKIVES SGCPDKCCTT QPEESFTAKN GRVAEVAKSN CAKSCCDEEI AAIVKELPKS
TYASSCCKPA EKIVTKSSDS CANSCCEKAP SITCRDSPAD ACCVSTSPER RVKIETTQNP
ADVEKQATGK EHVVLSISGM TCTGCETKLN RTLATVPAVN DLKTSLVLSR AEFNIDLRLG
SVDEVIKHLE RTTEFKCERL QTKGSSLDFI VNGSTSEFTG QAWLEGVLDM SLVDKDTVRV
SFDPKIVGAR DLAERSWDPP VQLAPPRGDS SLEAGSKHVR HVGYTTILSA VLTIPVLVMA
WAPLPEREVA YSSASLALAT IVQIVVAGPF YPKAIKALVF SRVIEMDLLI VLSTSAAYVF
SVVSFGYLIA GNPLSTGQFF ETSTLLVTLI MVGRWVAALA RQKAVESISI RSLQSSTAIL
VDEQTGTERE IDARLLQYGD VFKVLPDTRI PTDGTVMSGS SEVDESMLTG ESKPVEKQFR
GVVIAGSING PGVMAVRLNR LPSENTINAI AAMVDEAKLS KPKLQDLADR VASYFVPVVV
ALTITTFVIW VAIGITVRGY GGSKATTEAI TYAIAVLIVS CPCAIGLAVP MVIVIMSGVA
AERGIVFKSA DAIEVAHKTS HVVFDKTGTL TQGKLSVVAN ECVDESTLPL LLGLIENSRH
PVSMAVTSYL RSIGIEPLSV GEPKSLTGKG VEAVVRGQRL KAGNSTWLNL SDNPPIQPML
SQGHTVFCFT INDELQAVYG LQDEPRKDAF AAVEALHMRG ISVHVVSGDD DTAVQNLASK
LNIQQDNVRS RTSPSGKRDY IQTLLGTSTD HKKPVVVFCG DGTNDAVALA QATIGVHMNE
GTDVAQSAAD VVLMRPALGG IITMIDASRK SVNRIKFNFG WSFVYNTFAV LLAAGAFVNA
RIPPEYAGLG ELVSVLPVIL AAVLLRWSKI
//