ID A0A0A1T1D1_9HYPO Unreviewed; 1626 AA.
AC A0A0A1T1D1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=VHEMI06721 {ECO:0000313|EMBL:CEJ90971.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ90971.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ90971.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CDHN01000003; CEJ90971.1; -; Genomic_DNA.
DR STRING; 1531966.A0A0A1T1D1; -.
DR HOGENOM; CLU_001640_2_0_1; -.
DR OrthoDB; 6951at2759; -.
DR Proteomes; UP000039046; 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; cd03263; ABC_subfamily_A; 2.
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; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229:SF36; ATP-BINDING CASSETTE SUB-FAMILY A MEMBER 5 ISOFORM X1; 1.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR Pfam; PF12698; ABC2_membrane_3; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
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 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:UP000039046};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 229..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 833..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1010..1029
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1049..1074
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1086..1109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1115..1140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1152..1173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1193..1217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 469..703
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1263..1490
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 777..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1626 AA; 177906 MW; 51DE6EAE71E8F24C CRC64;
MAFFRQVWTL MSKNLRTMLF RHLTLCIFMA FLVPLILASF FSFAKNLFAP PAKYGISQPY
PVMSIGDALR IGVRQDRNKI VLINNGFTGG NIDRVLNEVE TAIKDANSAV DIVHLSNETN
LPLECRSTLR GVTRCFGAVV MRSSPNEGPG GIWNYTIRTD AAFYTSAVTI NINKNDNVEQ
VYLLPIQRTI DAIIGQDANP GSKTALDNIK EYPFTSLTSE ERDTKVRELF HNAVINFMGV
AFIANVIWIT YHLTGIIASE RESGMSQLID AMMPVRWAFL GQAARFISHH LSFSLIYLPA
WVIGSLIIRY GLFPNTSIAI VLIYQILAGA SFASMSILFA SFFKKAQLSG ITATLSTLLL
GILAQALTRP GTVPVAILSA IFAPCNYVFF IIHMARFEKR DMGANLTTIP KGSSWQLTGI
VFWILMIIQI IVYPLIGAFV ERGFYGTSTK GRKLVTGSSG EQAMGDNAVV LENFTKVYKP
GFFTRLFAFG QASEPVVAVD KLSFQAGRGQ IICLLGANGS GKSTTLDAIA GLHKLTSGSI
TIDGTGGLGI APQKNVLWDD LNVEEHLRIF NRLKSPNTRA TTEEIHALIK AIDLWTKRKA
LSKTLSGGQK RKLQLGMMLT GGSAVCCIDE VSSGLDPLSR RKIWDILLAE RGKRTLILTT
HFLDEADLLA DHLAILSKGT LRAAGSSVEL KDTLGGGYRV HAYKSSGQKT MPSVPQVKKV
DAFDMVTYTA PASALAANVI KELEAVGIHD YRFSGPTIED VFLQLAEEIR DEEIMRGSEK
AVGASEKTPD DAKSQRSASQ RQGITLVDGQ RIGYFKQARI LFAKRLIILK RNWILYFVAF
ILPIIAAALT SLYVKGKPQT GCSPLDQVSQ SSTQDAFSQV KSDKVIMFVA GPSSAISQNN
LLQLFKPILG GIKGVSSIAA GAALKNLKIV DSYALFDDFI KNNRKNVTTG LWLGGDGVDP
TFAWVGNLYL TSSLSAQQFM DVIRTNTSIA TTWSSFDVPF NPGIGDALNL AIYIGLALSI
YPAFFALYPS NERRRFVRAL QYSNGVHPFP LWVSYLLFDF IIVLLSSAIV TALWSGLSGI
WYHIEYIFIV FFLYGLTSTL LSYIISLYAK SQLATFAWAA VGQCVCFLIY LIAYVCILTY
VSVRKMDSAI HIAHFVISAV APIGSAMRAV FLVTNLFSTA CDGNELSSNP GGLLAYGGPI
LYLVVQAVIL FGLLIWLDGG SPGSSIRSLF ERHHDNATEN DNDEEIANEL ARVNSDAGTH
DGLRVMNLTK SFGKNTAVDN VTFGIKRGEV FALLGPNGAG KSTTISLIRG DLKPSHNGGD
IFVEDKSVIR NIAAARQNLG VCPQIDAMDQ MTVREHLEFY AKIRGIADIQ HNVTAIMEAV
GLTAFETRMA FALSGGNKRK LSLGIALMGN PAVVLLDEPS SGLDAASKRI MWKTLEATVP
GRSILLTTHS MEEADALAGR AGIIARRMLA LGTPDNLRRR FGDDLHVHLV SNTAPRTSDA
EMERIMRWVQ AKLPSATVED KSYHGQTRFS VRAADILALS GREVSEKSLG SEDDADVNNT
RETQSALGQL VVLLEEHKQE LGISHFSVSP TTLDQVFLTI VGQHNVREEN YEEKRRSAWK
RTCCIG
//
