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Database: UniProt
Entry: A0A178ZS71_9EURO
LinkDB: A0A178ZS71_9EURO
Original site: A0A178ZS71_9EURO 
ID   A0A178ZS71_9EURO        Unreviewed;      1090 AA.
AC   A0A178ZS71;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ABC transporter domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AYL99_04494 {ECO:0000313|EMBL:OAP62291.1};
OS   Fonsecaea erecta.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP62291.1, ECO:0000313|Proteomes:UP000078343};
RN   [1] {ECO:0000313|EMBL:OAP62291.1, ECO:0000313|Proteomes:UP000078343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP62291.1,
RC   ECO:0000313|Proteomes:UP000078343};
RA   Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA   Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA   Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA   Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA   Attili D.S., Gorbushina A.;
RT   "Draft genome of Fonsecaea erecta CBS 125763.";
RL   Submitted (APR-2016) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:OAP62291.1}.
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DR   EMBL; LVYI01000003; OAP62291.1; -; Genomic_DNA.
DR   RefSeq; XP_018695658.1; XM_018836008.1.
DR   AlphaFoldDB; A0A178ZS71; -.
DR   STRING; 1367422.A0A178ZS71; -.
DR   GeneID; 30008663; -.
DR   OrthoDB; 359054at2759; -.
DR   Proteomes; UP000078343; 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; cd03213; ABCG_EPDR; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR000742; EGF-like_dom.
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; 1.
DR   Pfam; PF19055; ABC2_membrane_7; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078343};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1090
FT                   /note="ABC transporter domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008098751"
FT   TRANSMEM        314..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        833..854
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        866..888
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        909..934
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        946..969
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        976..996
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1064..1087
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          78..116
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          370..612
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          637..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..672
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        87..104
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        106..115
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1090 AA;  119574 MW;  72F6BFFCAD16863F CRC64;
     MNLHGVATAL LLVAPTLLAT AYPNDTSSAL MQDPFLDLVD GCPPCPRCFD CHYDEFKCLQ
     FASCSNANGK CVCPPGFGGD DCAEPLCGSL SDGKNRSPRR GDKCDCKDGW EGINCNVCTS
     NEACNALMPL GQGGVCYQKG ALVHENYQVC NVTNKAILDQ IDPRIPEVTF SCNAEEATCN
     FQFWVDHKES FYCALDNCTW TYQDTNVRNT TKYQCENIKC SCIPDRFLCG EDGSVNIDEF
     LEQEIKGPAS FYSQHTYGGS SKDGSRFEEP AMNNLISMIF GDEYISLQCR AGECLYETDV
     PGYTRPIKEI NTPLIAGIIA GCALLIVAIT LISWYLSRRA ALKRWGAIRL GEGGENDPSL
     SMINHTPMAL QFENVSYGLK GKEILSGISG IAHPGQITAI MGASGAGKST FLDILARKNK
     RGTVLGHMYV NGEKILDGEY RNVVGYVDQE DTLLPTLTVH ETILTSALLR LPADMGVSVK
     EQRVIEVMQQ LGIYHIKDQV IGSEEGNGRG ISGGEKRRVG IACELVTSPS ILFLDEPTSG
     LDAFNAFNVV ECLVTLAKTY NRTVIFTIHQ PRSNIVALFD QLILLAKGQT VYSGPFSSCQ
     SYFDHIGYSC PPGFNIADYL VDLTMHASLP RSPIFEDVPK DLLDRDGPGT ESSSTRAVKS
     IASVSNVSVE SPREAPTRGK PKRRISLKQK QDRQLFTRKK TTGSETPPTP KTDDEDTVMG
     RATGSMRSWL QMSRRDGSNP PPLLEDPDDI PPDANTDLDI LVTSFKNSDV AQTIHDEITA
     SIQAASAANG HGGGEAVTEA VTGSIKGFRR VSLPRQFLIL SRRTWRNLYR NPILMLTHYA
     VAILLAVLSG WLFYGVTDDI GGFQNRLGLF FFLLALFGFS ALTSLNVFSA ERLIFVRERA
     NGYYSPITYY AAKLLFDIVP LRLIPPIIMG VIIYPMSGLL PKWGVFFTFM LILVLFNLAA
     AAICLTIGIV FKDPAVANLI GSLVMLFSLL FAGLLLNLNH DTIQKAAQWL QMLSIFHYGY
     EALIVNEVAK LRLKDHRYGL DIEVPGASIL SAFGFDNLAL WNDVIGLGVF AGAFIIIAYG
     AMHFLLVEKR
//
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