(data stored in SCRATCH zone)

SWISSPROT: B6H219_PENRW

ID   B6H219_PENRW            Unreviewed;      1360 AA.
AC   B6H219;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 64.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=3.6.3.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=Pc13g03700 {ECO:0000313|EMBL:CAP91439.1}, PCH_Pc13g03700
GN   {ECO:0000313|EMBL:CAP91439.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP91439.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP91439.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
CC       phosphate + phospholipid(Side 2). {ECO:0000256|RuleBase:RU362033,
CC       ECO:0000256|SAAS:SAAS00036652}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362033};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU362033}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
CC       3.A.3) family. Type IV subfamily. {ECO:0000256|RuleBase:RU362033,
CC       ECO:0000256|SAAS:SAAS00533978}.
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DR   EMBL; AM920428; CAP91439.1; -; Genomic_DNA.
DR   RefSeq; XP_002558807.1; XM_002558761.1.
DR   ProteinModelPortal; B6H219; -.
DR   STRING; 500485.XP_002558807.1; -.
DR   EnsemblFungi; CAP91439; CAP91439; PCH_Pc13g03700.
DR   GeneID; 8313470; -.
DR   KEGG; pcs:Pc13g03700; -.
DR   eggNOG; ENOG410ITKD; Eukaryota.
DR   eggNOG; ENOG410XPYK; LUCA.
DR   HOGENOM; HOG000202528; -.
DR   KO; K14802; -.
DR   OMA; RMRKQRG; -.
DR   OrthoDB; EOG092C0BQ4; -.
DR   BioCyc; PCHR:PC13G03700-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1110.10; -; 2.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006539; P-type_ATPase_IV.
DR   InterPro; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   PANTHER; PTHR24092; PTHR24092; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   SUPFAM; SSF56784; SSF56784; 3.
DR   SUPFAM; SSF81653; SSF81653; 2.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 3.
DR   TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6H219.
DR   SWISS-2DPAGE; B6H219.
KW   ATP-binding {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00076996};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Hydrolase {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00076955, ECO:0000313|EMBL:CAP91439.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00076983};
KW   Membrane {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00414835};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00076966};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transmembrane {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00076989};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00076942}.
FT   TRANSMEM    498    521       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM    549    570       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM   1101   1123       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM   1144   1168       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM   1180   1197       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM   1209   1232       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM   1252   1271       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   DOMAIN      235    301       PhoLip_ATPase_N. {ECO:0000259|Pfam:
FT                                PF16209}.
FT   DOMAIN     1030   1282       PhoLip_ATPase_C. {ECO:0000259|Pfam:
FT                                PF16212}.
SQ   SEQUENCE   1360 AA;  152635 MW;  CA422B314AF3A0DE CRC64;
     MASGRPPGSH PAAGRDDDLL LDSGPMYSTG QGPPVNDEHL LERYNIDDSE QPYAQTQPRP
     SVSYDNFVGS SVQQGATRHN VASGPAHPPV NPGLHSNDPY SSGTRDRTYS QTSGLDNYRR
     YSLDDFDDGH SGYYDLDADE DRIASSHHVR KANERNSVLG LGGGFMGKAK YMFGMGSSQY
     SEMDLPLTES GARRATVGSD ASPAPPPKQR KKFRASDLNI FSRKVDPSTL GPRMIQLNNP
     PANATHKFVS NFVSTAKYNI FTFIPKFLFE QFSKYANLFF LFTAVLQQIP NVSPTNRYTT
     IVPLAIVLAV SAIKELVEDY KRRMSDRGLN YSKTQVLKGS SFHEAKWVDV VVGDIVRVES
     EQPFPADLVL LASSEPEGLC YIETANLDGE TNLKVKQAIP ETAHLVSPSD LSRLSGRVRS
     EQPNSSLYTY EATLTMNAGG GEKELPLAPD QLLLRGATLR NTPWIHGIVV FSGHETKLMR
     NATATPIKRT AVERTVNIQI LMLVSILIVL SVISSVGDLA IRKTRSSTLA YLGYGGSVKL
     VKQFFMDIFT YWVLYSNLVP ISLFVTIEIV KYFQAFLINS DLDIYYDKTD TPAICRTSSL
     VEELGQIEYI FSDKTGTLTC NMMEFKQVSI AGVQYGDDVP EDRRATVEDG AEIGIHDFKT
     LKKNLQSHPS QNAIREFLTL LATCHTVIPE RNSEDPNVIK YQAASPDEGA LVDGAASLGF
     RFTNRRPRSV IFEVGGQELE YELLAVCEFN STRKRMSTIF RCPDGKVRVY CKGADTVILE
     RLHPDNPTVE ATLQHLEEYA SDGLRTLCLA MREVPENEFQ QWHQIYDKAS TTVDGNRADE
     LDKAAELIEK DFYLLGATAI EDRLQDGVPD TIHTLQTAGI KIWVLTGDRQ ETAINIGMSC
     KLISEDMTLL IINEETSEAT RDSLQKKMDA VQSQISAGDS EPLALVIDGR SLTFALEKDM
     EKLFLDLAVI CKAVVCCRVS PLQKALVVKL VKRHKKALLL AIGDGANDVS MIQAAHVGVG
     ISGVEGLQAA RSADVAIGQF RFLRKLLLVH GAWSYSRISR VILYSYYKNI TLYMTQFWYS
     FQNAFSGEVI YESWTLSFYN VLFTVLPPFA MGIFDQFISA RLLDRYPQLY QLGQRGIFFK
     KHSFWAWILN GFFHSLILYI VSELLYYWDL PMENGHVAGH WVWGESLYTA VLGTVLGKAA
     LITNVWTKYT FIAIPGSMAL WLIFLPAYGY AAPALGFSRE YYGTIPVLFK SPIFYLMAIV
     LPCICLLRDY AWKYAKRMYY PQQYHHVQEI QKYNVQDYRP RMEQFQKAIR KVRQVQRMRK
     QRGYAFSQAD DGGQMRVLNA YDTTRSRGRY GEMASSRPMA
//

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