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Database: UniProt
Entry: S0DNJ4_GIBF5
LinkDB: S0DNJ4_GIBF5
Original site: S0DNJ4_GIBF5 
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
//
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