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Database: UniProt
Entry: A0A2T4C7A9_TRILO
LinkDB: A0A2T4C7A9_TRILO
Original site: A0A2T4C7A9_TRILO 
ID   A0A2T4C7A9_TRILO        Unreviewed;      1471 AA.
AC   A0A2T4C7A9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN   ORFNames=M440DRAFT_1330220 {ECO:0000313|EMBL:PTB77467.1};
OS   Trichoderma longibrachiatum ATCC 18648.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB77467.1, ECO:0000313|Proteomes:UP000240760};
RN   [1] {ECO:0000313|EMBL:PTB77467.1, ECO:0000313|Proteomes:UP000240760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB77467.1,
RC   ECO:0000313|Proteomes:UP000240760};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-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       PDR (TC 3.A.1.205) subfamily. {ECO:0000256|ARBA:ARBA00006012}.
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DR   EMBL; KZ679130; PTB77467.1; -; Genomic_DNA.
DR   STRING; 983965.A0A2T4C7A9; -.
DR   Proteomes; UP000240760; 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   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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240760};
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        519..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        554..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        595..620
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        632..651
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        663..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        688..707
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        771..792
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1181..1202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1214..1234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1255..1280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1292..1315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1327..1345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1445..1462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          162..409
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          845..1087
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          454..481
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1471 AA;  164030 MW;  06ADC882DD69E01E CRC64;
     MSGEQPPNGE SLPSTANSEL AKDLNEQLDS TSVETHVEGQ RSSNELARVR TGVSVEQAEA
     HFAGLQREFT GVSRASRRNK HQSSSDPEKG ATVTAEDDAS VFDLEAALRG DLDASTEAGI
     RSKHIGTCWD GLTVKGIGGF TNFVKTFPDA FIDTFNVLTP LLSLVGLGPK FTEATLLDKF
     QGVCKPGEMV LVLGTPGSGC TTFLKAIANQ RYGYTSVTGD VFYGPWTADE FKRYRGEAVY
     NAEDDVHHPT LTVEQTLGFA LDVKMPAKRP GNMSKAEFKE HVITLLLKMF NIEHTRKTIV
     GDAFVRGVSG GERKRVSIAE MMITNACILC WDNSTRGLDA STALDFAKSL RIQTDLYKTC
     TFVSLYQASE NIYSLFDKVM VIDEGRQVYF GPAKEARAYF EGLGFLPQPR QTTPDYVTGC
     TDEFEREYQP GRSPENAPHS PDTLLEAFKA SRYQKMIEDE IAEYKANLEK EKQAHEDFLA
     AFKESKRGTS KRSPYQVGFH IQVWSIMKRQ FILKLQDRFN LIVGWTRSIL VAIVLGTLYL
     NLGQTSASAF SKGGLLFVAL LFNAFQAFSE LGGTMTGRPL VARHKAYAFH RPSALWIAQI
     FVDQAFAASQ ILIFSIIVYF MTNLVRDAGA FFTFYLMILS GNIAMTLFFR ILGCVSPDFD
     SAIKFAVVII TLFITTSGYL IQYQSEKVWL RWIYWINVLG LAFSSLMENE FERIDLTCTA
     ESLIPSGPEY TDINHQVCVL PGSTAGTTFV RGRDYVAQGF DYLPGDLWRN WGIVMALIVF
     FLFLNVVLGE VVTFGMGGNS FKVYAKPTKE LDELNKRLLE KREAKRKDKS DEAGSDLIIN
     STSVLTWENL NYDVPVPGGT RRLLNNVFGY VKPGELTALM GASGAGKTTL LDVLAARKNI
     GVIHGDVLVD GVKPGKQFQR STSYAEQLDV HEPTQTVREA LRFSAELRQP YETPMSERYA
     YVEEIISLLE MENIADCIIG SPEAGLTVEQ RKRVTIGVEL AAKPELLLFL DEPTSGLDSQ
     SAFNIVRFLK KLAAAGQAIL CTIHQPNAAL FQNFDRLLLL QRGGRTVYFG DIGKDAAILR
     AYLARHGAEA APTDNVAEFM LDAIGAGSMP RIGDRDWADI WEDSPEFAHV KDTIVELKRE
     RVAANQASPG VEKEYASPLS HQMKVVVRRM FRSFWRSPNY LFTRLYAHVA VALITGLTYL
     NLDNSKASLQ YKVFVMFQIT VLPAIIMSQV EIMYAIKRAL FFRESSSKMY STSSFVTAII
     LAEMPYSVLC AVGFFLPLYF MPGFQTNPTR AGFQFFMVLI TELFSVTLGQ GLSALTPSPR
     VSTQFDPFIT IVFALFCGVT IPYTQMPEGW RVWLYQLDPF TRLIGACVTT ALHGLEVVCK
     SSELNRFTAP NGMTCGEYMR PFFENGGPGY LVSNSTQDCE YCSYSVGDEF YAPLNLSFDH
     RWRDLGIFLC FVVSNITILY LGSRFVNYNK R
//
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