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Database: UniProt
Entry: A0A0B2X5E1_METAS
LinkDB: A0A0B2X5E1_METAS
Original site: A0A0B2X5E1_METAS 
ID   A0A0B2X5E1_METAS        Unreviewed;      1836 AA.
AC   A0A0B2X5E1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=BMR1-like protein {ECO:0000313|EMBL:KHO01599.1};
GN   ORFNames=MAM_00600 {ECO:0000313|EMBL:KHO01599.1};
OS   Metarhizium album (strain ARSEF 1941).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHO01599.1, ECO:0000313|Proteomes:UP000030816};
RN   [1] {ECO:0000313|EMBL:KHO01599.1, ECO:0000313|Proteomes:UP000030816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHO01599.1,
RC   ECO:0000313|Proteomes:UP000030816};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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       PDR (TC 3.A.1.205) subfamily. {ECO:0000256|ARBA:ARBA00006012}.
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:KHO01599.1}.
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DR   EMBL; AZHE01000001; KHO01599.1; -; Genomic_DNA.
DR   STRING; 1081103.A0A0B2X5E1; -.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   OrthoDB; 5473955at2759; -.
DR   Proteomes; UP000030816; 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; cd03233; ABCG_PDR_domain1; 1.
DR   CDD; cd03232; ABCG_PDR_domain2; 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; IPR029481; ABC_trans_N.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR034001; ABCG_PDR_1.
DR   InterPro; IPR034003; ABCG_PDR_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010929; PDR_CDR_ABC.
DR   InterPro; IPR008551; TANGO2.
DR   PANTHER; PTHR19241:SF685; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 1.
DR   PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
DR   Pfam; PF01061; ABC2_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF14510; ABC_trans_N; 1.
DR   Pfam; PF06422; PDR_CDR; 1.
DR   Pfam; PF05742; TANGO2; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
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:UP000030816};
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        526..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        556..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        598..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        630..651
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        663..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        773..794
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1182..1202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1214..1237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1258..1284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1296..1319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1331..1353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1448..1468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          154..411
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          847..1090
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1836 AA;  203973 MW;  FB93573F2EA68026 CRC64;
     MAPHHLAGQT EAQDDETHGR APASRCQSPD SDLTAGHGRT AGADTGRVLS GVSVEQAEAD
     FADLQREFTG ASRASRRGRA VKDGDPEKAG PADLGAADDD ESLFDLETAL RGDLAAGEAA
     GIKAKHIGAC WDGLTVKGIG GTANYVQTFP NAFINFFDVI TPLMGLLGLG RKPPEATLLD
     GFQGVCNPGE MVLVLGKPGS GCTTFLKAIA NQRHGYTCVQ GHVFYGPWTA KEFSRYRAEA
     VYNAEDDIHH PTLTVQQTLA FALDTKMPAK RPGNMTKAEF KEHVISTLLK MFNIQHTRNT
     VVGDHFVRGI SGGERKRVSI AEMMITNACI LSWDNSTRGL DASTALDFTR SLRILTNLYK
     TTTFVSLYQA SENIFRLFDK VLVIDEGKQV YFGPADEARS YFEGLGFASR PRQTTPDYLT
     GCTDEFERVY AAGRSENDSP HSADTLRRAF QKSHHQKKLE SQIAEYKANL EKEQHKHSDF
     QLAVKDSKRG ASKRSAYQVG FHLQVWALMK RQFILKLQDR FNLTLSWVRS IIIAIVLGTL
     YLNLERTSAS AFSKGGLLFV ALLFNAFQAF SELAGTMFGR AIVNKHKAFA FHRPSALWIG
     QIIVDQAFSA TEIMVFSIIV YFLSGLVRDA GAFFTFYLMI LSGNIAMTLV FRIIGCLSPD
     FDYAIKFAVV VITLFVTTSG YLIQYQSEKA WLRWLYWVNP LGLVFSSLMQ NEFQSIDMTC
     TADSLIPSGP GYTNISHQVC TLPGSKPGTT FVAGPDYIAQ GFSYYAGDLW RNWAIVFSII
     VLFLILNVVL GELVKFGMGG SSFKVYQRPN KERAALNEKL LQKREARRKD RSNEVGSDLS
     IKSESILTWE NLNYDVPVPG GTRRLLDNVF GYVRPGELTA LMGASGAGKT TLLDVLASRK
     NIGVITGDVF VDGFKPDKQF QRSTSYAEQL DLHEPTQTVR EALRFSADLR QPYETPLAER
     HLYVEEIIAL LEMEHIADCI IGNEEAGLTV EQRKRVTIGV ELAAKPELLL FLDEPTSGLD
     SQSAFNIVRF LKKLAAAGQA ILCTIHQPNA TLFENFDRLL LLQRGGRTIY FGEIGEDASI
     LRAYLKRNGA EAAPTDNVAE FMLEATGAGS SPRIGERDWA DVWDESPELA CVKKAIVEMR
     EERAAIAQIA NPVPEKEYAS PTHHQIKVVV RRMYRVFWRS PNYLFTRLFN HFAVAFVSGL
     TYLNLDTSRS SLQYTVFIIF QVTVLPPLII SQVEVMFYIK RAIFFREASS KMYSPTTFVT
     AIIAAEMPYS ILCAVVFFVC LYFMPGLDAT PSRAGYQFLM VLITEVFAVT LGQGLAALTP
     SPRISAQFNP FLTIIFALFC GVTVPAPQIP AFWRAWLYHL DPFTRLISGM VTTALHELPV
     DCTSSEVNRF IAPSNMTCGE YMAPFFERGA PGYLVRNDTQ DCEYCAHKVG DEFYERLNMS
     FDDRWRDLGI YVAFIVSNLI ILFIAYDFQE RFPRETSQHT PSTASSDLHQ DNMCIVLFTT
     AHPDYPLILI DNRDEFILRP TSRPHWWTHP TSGELVLSSR DLQRAEKGTW LGITKSGVFA
     VLTNYREANA YDASRPVHGR RSRGAVVTAW LAGLGNSIKD GVQRLVEDDG VKGVGGFSLV
     CGKLRKRGEG IAVISNRAED ADQVPIVAGQ RGETWGLSNT TFDAEVAWPK VEMGTRMLRA
     TVQRAAEDKA SEADLIKDLF KVLDTDTFPA IRAGTSFQEI TGLLRHSIFV PELGDESQRE
     SMDAARAKGK ATWARDEGKL KAVEEILLEQ QPELSAPAAN GFETGTYGTQ RQTVVLVDWD
     GNVKMVERAL WDRNGHGIGR GDGDVVIEFA IEGWDE
//
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