ID A0A421JP92_9ASCO Unreviewed; 1602 AA.
AC A0A421JP92;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative ABC transporter ATP-binding protein/permease {ECO:0000313|EMBL:RLV93064.1};
GN ORFNames=JA1_002658 {ECO:0000313|EMBL:RLV93064.1};
OS Spathaspora sp. JA1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV93064.1, ECO:0000313|Proteomes:UP000285775};
RN [1] {ECO:0000313|EMBL:RLV93064.1, ECO:0000313|Proteomes:UP000285775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA1 {ECO:0000313|EMBL:RLV93064.1,
RC ECO:0000313|Proteomes:UP000285775};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily.
CC {ECO:0000256|ARBA:ARBA00005814}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV93064.1}.
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DR EMBL; NSGQ01000018; RLV93064.1; -; Genomic_DNA.
DR STRING; 2028339.A0A421JP92; -.
DR Proteomes; UP000285775; 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; cd02859; E_set_AMPKbeta_like_N; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1.
DR PANTHER; PTHR48041:SF139; PROTEIN SCARLET; 1.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:RLV93064.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000285775};
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 375..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1057..1074
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1106..1122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1129..1150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1156..1176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..279
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 686..938
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 649..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1565..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1602 AA; 179378 MW; 3D52F4BFBBD9057B CRC64;
MSTPNILQIP YSQKVGLSVH HLSVSVKSQI PKDIEKDQEA LGELDQSHKI LNDVNFELES
GEIMAIMGGS GSGKTTLLNT LSQRTNITNK KLQFTGSIAY IRQNDLAHIN HAYMLQDDSF
LPGLTVYETL KTQADLRLPP HITQVEKLQL IDYILEVLGL VHVKNTRVSN FSTHSTVLSG
GEQRRVSLAV QLLSRPSIVF LDEPTTGLDS STSLKLVTLL KKLSWEFGMS IVVSIHQPRS
EIVELFDKIC LLTRGGRMVY YGDVTHAKTY FDNIDFLEGS STDYFNHIEY IMGLSVKDTT
SQERELQTIA RIDKLVKMWK EKYQLEANPN DELQQFESFE DNLKLFTRGK SDRISFLREL
IVLTKRTFVL SYRDVQGLLV LNLGAIIISV AIGWMFFQPA HDLAGIRSIT STLYVILEVV
AFCPMYIEVE RLWLTDGIFF YREYSENWVS IPGFIISRRL GKFLIEDLPM SISFAVITYF
MWGLGLSNGS NFGIYFAIVL ILELCCMASS LLCFTIAPSF AITAVAINIF YQVQNSACGY
FVNAATMPVY VRWTKYIAYF WYAFGALTVN QFSDWNGDCP FSENDPRCFS YTGEYQLQIL
GFPNGWIGEP IGILICWIVG FLLFSGVAIS FKRFDVGVAK TRENRYEVEE EHHDIEIHHT
RDEDIQQKTT TSPPTPDKDI NDYFQINIEN IHLSAKKTRF HTHAKCILDG ISATFSPNSV
NVIMGPSGSG KTTLLNYLSN RLPKSSTYIK QGVIKFNKQQ IITQEELGKV GAYVTQHDTS
LIHNLTVRET LYYQARIRLP LKDHKNIHAI INRLIRQTGL VDCADTIIGS EYVKGISGGE
KRRVSIAIQL LSRPKVLFLD EPTSGLDSFT AEMIYSLLET LAKENGTTVI LTIHQPSYEM
FCMFGSLLLL GYGGKVIYQG ASMGIVQYLE HLGYQMNNDT NIADFVLDLI SQKVQEEGST
SSYLSSNWNQ KQEKSITSCC SCDDLDIKQY YNQRLPFRVT FRTIVERQIL TSYRAKDVVF
SRAGQTFFLG IVHTLYFAPL RNTQDGISNR LGLVQEVLNL YFVGLVNNIS LYPFERNLFY
QEYKDGVYGV SEFGISYLIN ELPTEIIPSL FFSALIVFAC GLPRTAEMYF AMFGTAVISI
NCGESLGIFV NSCFNHLGVA TNVLTVVVMM AIFMGGTMSL HMPMFFKVFN YISPMKYAVA
ICANLGFTGQ VFKCSEGMEE CVFNSGEAVL DYYNLRAHLG AMIGGLIACL VVYRSFAIAP
SVDAHVKSIQ ITGSFDNWAR SIPPKTDLSK GYTQEIVTDE KQNIIFKFVL NDSDWITNDQ
FKIQHDESGN SNNVIEADEL IEVSVPVSEP INKTEEPEVV QNKAEIEEKA VSEEVVQPPV
GQKEVTAPIE QFEEDKDYSP ENEINASAVI VSEEDPVQVE TPELSIQSPI ITSEDEIISD
IDDKSTSPVS SPQPAQQQSL SQILTSSSSF AAVSLPPSSS DQDYEHLQGE EVEEEFNTPT
NSLGNSSVLK PNDEFTLSSN QATATTATTA TTAGSANIDK PVKPVLLSQP SESTIEVSEE
NIIKIPGGYP ASPEPKTTAS VSPRKEAGKR ENLISRFKSL FR
//
