ID D4DIF0_TRIVH Unreviewed; 1113 AA.
AC D4DIF0;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=TRV_06958 {ECO:0000313|EMBL:EFE38302.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE38302.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000256|ARBA:ARBA00011054}.
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:EFE38302.1}.
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DR EMBL; ACYE01000406; EFE38302.1; -; Genomic_DNA.
DR RefSeq; XP_003018947.1; XM_003018901.1.
DR AlphaFoldDB; D4DIF0; -.
DR GeneID; 9582105; -.
DR KEGG; tve:TRV_06958; -.
DR HOGENOM; CLU_002848_0_1_1; -.
DR OrthoDB; 49929at2759; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR CDD; cd03221; ABCF_EF-3; 1.
DR CDD; cd18626; CD_eEF3; 1.
DR Gene3D; 2.40.50.990; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR015688; eEF3_ABC2_chromodomain-like.
DR InterPro; IPR047038; eEF3_chromodomain-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19211:SF14; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 3; 1.
DR PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 482..700
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 726..1043
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1046..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 123239 MW; F37EB365427A4BDF CRC64;
MPLLETAPMQ SERIVPVASK AADGAIGDDV AHLLKTVFEA QTSQQALDAS YGLTNLLIST
GSVRCLQTFN VVPEIKKAAT DKKNGARRES SMLILGALFE QYPLKNPLSE VVFLLENGGL
LYLALDLLAD KDAVVREAAQ YAIDALFACL KEESLVHALV EPLAQYLSKP TGKWQGTVGA
YKLLEKVAKR AEIGTESKEK EELKDLLRLN LGQKLKDLIP IVEGGMHDLK AEVAKQAVKT
MTALSTFLDN DDVAPRIPLL LKTMEKPSTE TLQKAIHALS QTTFVAIVTS PVLALLTPLL
ERSLNTPTTT QEVLRQTVVV VENLTRLVHD PVEARTFLPK LKPGVQRVKD GASLPEVREL
ATRAMNVINK AMGDDEAGTI DSRATTEQVE AVLEEHMKPY MKFNHTDEKR FWETSRNYIA
NMVRDDANSR LLERIQLCVG PYLQSFVPDG KHDEIAAAVK AHFVEEDERR FGVPVKEDDG
EIEIVNANFS LGYGGRLLLS HANLRLLKGH RYGLCGRNGV GKSTLMRSIA NGKLEGFPPQ
DVLKTCFVEH NQGEDAELSV LEFVTKDPEM AAAGEEKISA ALNEVGFTPG PEGRQQQPVG
SLSGGWKMKL ALARAMVMGA DVLLLDEPTN HLDVHNVKWL QEYLKKHTEV TSLIVSHDSG
FLDEVCTDIY HYEQKKLVHY KGNLADFVKV KPEAKSYYTL SSANAHFKFP PPGILSGVKS
ATRIILRMTN CSYTYPGSSK PSLVDASCAL TLSSRVAIIG GNGAGKSTLM KLLTGETIPQ
TGKVEKHPNL RIGYIKQHAL EHVEMHMEKT PNQYLQWRYA NGDDREVLLK QTRILTEEDK
IQMAKPVDIG DGKGPRNIEA LMGRQKYKKT FQYEVKWKNM LPKHNTQISR ETLLELGFQK
LVQEFDDHEA SREGLGYRVL EPKVISKHFE DIGLDPEIAN HNEIGGLSGG QKVKVVLAGA
MWNNPHLLVL DEPTNFLDRD FLGGLAVAIR EFKGGVVMIS HNDEFVGALC PERWYVENGR
MTHAGTTAVA LDRFEDQSRN PSTVASSVVS SAAPSAVNSG AEDGGELKFK AKKKKKMTRA
QLKEREVRRR LRHIEWLNSP AGTPHPPDTD DEQ
//
