ID F2SQE3_TRIRC Unreviewed; 892 AA.
AC F2SQE3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=TERG_04806 {ECO:0000313|EMBL:EGD88561.2};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD88561.2, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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 Eye pigment precursor importer (TC 3.A.1.204) subfamily.
CC {ECO:0000256|ARBA:ARBA00005814}.
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DR EMBL; GG700652; EGD88561.2; -; Genomic_DNA.
DR AlphaFoldDB; F2SQE3; -.
DR STRING; 559305.F2SQE3; -.
DR VEuPathDB; FungiDB:TERG_04806; -.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_1_1; -.
DR InParanoid; F2SQE3; -.
DR OMA; NCQLDAF; -.
DR OrthoDB; 359054at2759; -.
DR Proteomes; UP000008864; 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; cd03213; ABCG_EPDR; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1.
DR PANTHER; PTHR48041:SF139; PROTEIN SCARLET; 1.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
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:UP000008864};
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 111..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 637..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 670..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 718..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 780..800
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 866..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 165..407
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 474..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 97778 MW; 4322BD2D29481EEC CRC64;
MDITENQNIT TYQCDNIKCG CVPDRMLCET TGVSLEPLFG QLTGPAKFTS TSTKGGSPKD
GSAFSEPVID KVISDLFGDK SILLDCYSSE CLYKTAVPGY KPPVKVINTP LIAGVIAGCS
LFIVGVILLI WYLSRRKAYN QYHALADDSD DEGSKLMADH KPASLQFENI SYYINGQQIL
SGIRGIAKPG QVTAIMGASG AGKTTFLDIL ARKNKRGIVH GDIYVNGEKF NDSEYKKVVG
FVDQEDTMLP TLTVHETILN SALLRLPRDM SDAAKQQRVY EVEKQLGIHH IKDQLIGSEE
GKGRGISGGE KKRVSIACEL VTSPSILFLD EPTSGLDAFN AFNVIECLVN LAKSYNRTVI
FTIHQPRSNI VALFDQLILL GKGKTVFSGP YSSCQSYFDN IGYSCPPGFN IADYLVDLTM
HASQSRSTEE PTVNVDSHDN NFRTASSSLR AVKSVASASI ASIDNASAVD SGQELLLRPK
DKRRSSLKQR QDRQLYTRKR GSGLESPPDP QTDNEDGHVM SLAERAQQWL PLSRQQGQVP
PQIIQDPDHL PPIASGFVTD LDVLVSYYAN SNVANAIRDE ISSSVQDALA ANGQANTSQQ
ASDVVTGQMT GYARVGLIRQ FIILSSRTWK NLYRNPMLML THYATAILLA VLSGYLFYGL
TDDIKGFQNR LGLFFFLLAL FGFSTLTSLT VFSSERLLFV RERANGYYSP VTYFTAKVLF
DIVPLRLIPP IIMGVIVYPM VGLIPDWPEF SKFILVLVLF NLAAAGICLL IGIVFRDPGV
ANLIGSLVML FSLLFAGLLL NHDAIPASAL WLQTLSIFHY AFEALIVNEV TFLTLIDHKY
GLDIEVPGAS ILSAFGFNNL ALWNDVAGLG VISGISIIMA YAAMHFLLVE KR
//
