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Database: UniProt
Entry: A0A1E3H9M4_9TREE
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Original site: A0A1E3H9M4_9TREE 
ID   A0A1E3H9M4_9TREE        Unreviewed;      1700 AA.
AC   A0A1E3H9M4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ATP-binding cassette transporter {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L202_08432 {ECO:0000313|EMBL:ODN73037.1};
OS   Cryptococcus amylolentus CBS 6039.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN73037.1, ECO:0000313|Proteomes:UP000094065};
RN   [1] {ECO:0000313|EMBL:ODN73037.1, ECO:0000313|Proteomes:UP000094065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN73037.1,
RC   ECO:0000313|Proteomes:UP000094065};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (JUN-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   -!- 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:ODN73037.1}.
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DR   EMBL; AWGJ01000014; ODN73037.1; -; Genomic_DNA.
DR   RefSeq; XP_018988978.1; XM_019143314.1.
DR   STRING; 1295533.A0A1E3H9M4; -.
DR   GeneID; 30159741; -.
DR   OrthoDB; 3295317at2759; -.
DR   Proteomes; UP000094065; 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; cd18596; ABC_6TM_VMR1_D1_like; 1.
DR   CDD; cd18604; ABC_6TM_VMR1_D2_like; 1.
DR   CDD; cd03250; ABCC_MRP_domain1; 1.
DR   CDD; cd03244; ABCC_MRP_domain2; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
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   PANTHER; PTHR24223:SF353; ABC TRANSPORTER ATP-BINDING PROTEIN_PERMEASE VMR1-RELATED; 1.
DR   PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 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:UP000094065};
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        139..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        339..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        388..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        480..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        505..523
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        583..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1018..1037
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1113..1137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1209..1229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1297..1314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1321..1342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          354..647
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          690..933
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          1030..1350
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1388..1679
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          930..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..953
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..978
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1700 AA;  187343 MW;  B87B551E5C1B87D1 CRC64;
     MSYPSWATTL AHEPWSCDSV WTGIDFSPCF KERYLQNAPY ALIALSILYL LATLPSRLSS
     SHKPPLSTST LVSPTNSSDL AKLESTVILE ALATNLLPTT PTSSTNKPTE KLAGGESEAI
     IEDFLSGASK RRDVSRWQGA RFWVGLIGAV VWFEVELARV IVQGSWASIV FPAYISVIAI
     IPGSHITPLV TFHAILSLLL FRSLVISPNP STLHITAYAV EIVYWFALLG LPYHESLDRL
     LSGGKSARGG SNGSYGNQLP KHCEEPASAF SRGSYNFMLP LLFKHYFKPI TLEEIPAIRE
     DDSSAAAIGG FRAFQARKDG EWIKKHKQGA RRKHIGVDLL WFFTPDVLWQ VMYSILFIFF
     QYLPPTGLRL LLQFVKERET RPQPTHVAVL YVGMMVVGQC TSVIFLGQAL ALGRRIGVRI
     RAIIVSEVFA KALRRRDLAG DVKKTETKEG EEKKSDVAGE GKVANMVSVD AFTTGEVCAY
     SYYIFSCPIG ITVNCVLLYQ TLGVASIAGI ALLVLLMPVQ YLVSKLYMYC QRMFMSATDA
     RLEGVTEVIS HIKLIKFNAW EGKFYERMMD TRENELKMLR KRFGATVLFQ VLVWSTPVIV
     TGAAFAVHTA WLGRPLTADT AFASLILFSM LKDPLALSQD ITTRLIQAYT SCTRIQAYLD
     EPDTLKYRQL SAPGPGDPQI GFKNATLGYL TVEETSKLGD DQADPFQLSN LNLSFPVGKV
     SLVCGPVGSG KTTLILGLLG ESLLLDGQVF MPDDHANRDI CLVDPTTGLV DSIAYCAQTA
     WLVGASIREN IVFGSKWDKT RYDAVVKACA LERDFEIFEL GDETEVGEKG TTCSGGQKAR
     IALARAFYSS AKTIVLDDVL SAVDAHTARH LYNHVLQGPL VQGRTVILVT HQVSLVAPAA
     ELVVLLDNGG VAASGTPSEL QSSGQLELFE EEGSEKDVGT SNAESSSSTA IEDEVVIEEQ
     LDSPAEEERA EQKKLVDAHA SFDSPTPAPV GKDAKQSKQL VAAETSSQGT VEGKTYSLYF
     KAMGGLALWA VMFAFFFGSQ FMQVATNAWI KEWANADDRA VSSTTTAVSA VHHLVDQSTF
     ALYQSFFNVR DTAQSAYTEV FERQHGTAYY LTIYWLISIF YLASIAGRVG ITFVGALKAS
     RGMYGRLLSR ILGAKMRFFD STPSGRILNR LSKDMSSIDQ ETAEVLMYFV NSCLSAAAIL
     VVVTLSTPAF IFAIVLICFL YWVVGSLYVT TNREIKRIDS VTRSPIFISF SEVLVGMSTI
     RSYGDSARFM RKLFHELDQN TRCFWYLWQC NRVLNNWSNY VGALVTIFAS LFALKNEKMT
     AGAVGLSVGY ALSFTEYVLW VVRMYAAVEM SMNSVERVGE YLDLEVEEEP DAKGREPPAY
     WPASDGSIVV ENLTCRYAPQ LDPVLRDVSF TIGPKEKIGV CGRTGSGKST LALSFFRFLF
     QESGRILIDG EDISKLSLHT LRSRLTILPQ EAQLFSGTVR DNLDPFDQHS DSDIWEALAQ
     CGLVGKSRYP SRVVSRIGSR TDLRSAAQAA GGEADSLVKT VLKKKLEDAR DGQGDGEGEE
     EERVVIKSLE ENVAVGGKNF SQGQRQLLAL ARGLLKLRNS SFLIMDESTA NLDHATDATI
     QNVLRTALED VQMLVIAHRL MTVCGLDKIL VLDHGKVMEY GTPWELLQKE GGFFRDLCKQ
     SGEEAQLWEI AKSVHDKKTA
//
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