ID K5X8X3_AGABU Unreviewed; 1325 AA.
AC K5X8X3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AGABI1DRAFT_74549 {ECO:0000313|EMBL:EKM79477.1};
OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS 10392) (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM79477.1, ECO:0000313|Proteomes:UP000008493};
RN [1] {ECO:0000313|Proteomes:UP000008493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC {ECO:0000313|Proteomes:UP000008493};
RX PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT "Genome sequence of the button mushroom Agaricus bisporus reveals
RT mechanisms governing adaptation to a humic-rich ecological niche.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JH971390; EKM79477.1; -; Genomic_DNA.
DR RefSeq; XP_007329798.1; XM_007329736.1.
DR STRING; 597362.K5X8X3; -.
DR GeneID; 18831195; -.
DR KEGG; abp:AGABI1DRAFT74549; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_8_1; -.
DR InParanoid; K5X8X3; -.
DR OMA; GFGQEEQ; -.
DR OrthoDB; 1067095at2759; -.
DR Proteomes; UP000008493; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24222; ABC TRANSPORTER B FAMILY; 1.
DR PANTHER; PTHR24222:SF76; MYCOBACTIN IMPORT ATP-BINDING_PERMEASE PROTEIN IRTA; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008493};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 80..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 751..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 798..825
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 980..1002
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1014..1036
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..384
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 419..664
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 754..1041
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1078..1318
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 28..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1325 AA; 144888 MW; 2A04C8360EC9C3BB CRC64;
MSDSRPSTAD EKVTVVDHQA ATKRSMFFSR KKSTKHLSSD DKHDEKGDET TAEQAAEEKK
EEIVPVGFFA MFRFSTKFEI TLDIIGLIAA AAAGAAQPLM TLLFGKLTQD FVNFEQVVQD
PTQQDRIPAA LDSFRTSAAL NASYLCYIGL GIFVCTFIYM YTWVYTGEVN AKRIRERYLT
AVLRQDIQYF DTVGAGEVAT RIQTDTHLVQ QGISEKVALV VNFLGAFVCG FALAYARSWR
LALALSSILP CIAITGGVMN KFISTYMQLS LKHVAEGGNL AEEVISTVRT AQAFGSQAVL
AKLYDESINK SLQVDMKAAV WHGSGLGVFF FVIYAAYALA FSFGTTLINQ GHANPGIVIN
VFFAILIGSF SLALLAPEMQ AVTHGRGAAA KLFATIDRIP DIDSADPGGL QPERVQGEIR
LEDIHFTYPS RPNVPIVKGL NLTFRAGKTA ALVGASGSGK STVISLVERF YDPTSGIVKL
DGVNLKDLNL KWLRSQIGLV SQEPTLFATS IKGNVAHGLI GTKYEHASEE EKFALIKEAC
VKANADSFIS KLPEGYNTMV GERGFLLSGG QKQRVAIARA IVSDPMILLL DEATSALDTR
SEGVVQDALD KASAGRTTIT IAHRLSTIKD ADVIYVMGDG LVLESGSHDE LLAASGAYST
LVQAQKLREG KQHSGNVGDE DESDPSEDAK EDLEKMIREE IPLGRRNTNR SLASEILEQK
RVASAQLETK SKYNMAYLFY RMGLLMRDYQ WHYLVGVLAA TLTGMVYPAF GIVFAKGIEG
FSQDDPKVRR FQGDRNALWL FIIAIISTFA IAAQNYLFAY CAAALTAKLR MFSFRAILRQ
DIEFFDRDEH STGALTSDLS DNPQKVNGLA GVTLGAIVQS IATIISGLIL GLVFIWKLAL
VAMACTPLLI STGYIRLRVV VLKDQANKKS HEESAQLACE AAGSIRTVAS LTREEDCAKL
YSESLETPLR RSNRNAIWSN LLYAFSQAIS FFVIALIFWY GAKLVSNREY STTQFFVGLI
SSTFGAIQAG NVFSFVPDMS SAKGAASDII KLMDSLPEID AESPEGNVLD DSKVQGHIKL
ENIHFRYPTR PDVRVLRDLS LEVESGTYIA LVGASGCGKS TVIQMIERFY DPLAGEIYLD
GQKVSELNIQ SYRKQIALVS QEPTLYAGTV RFNILLGAVK PAEEVTQEEI EQACRDANIL
DFIQSLPDGF DTEVGGKGSQ LSGGQKQRIA IARALLRNPK VLLLDEATSA LDSNSEKVVQ
AALDQAAKGR TTIAIAHRLS TIQNADRIYF IKEGRVSESG THDQLLTQRG DYFEYVQLQA
LSTNE
//
