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Database: UniProt
Entry: F2SPJ0_TRIRC
LinkDB: F2SPJ0_TRIRC
Original site: F2SPJ0_TRIRC 
ID   F2SPJ0_TRIRC            Unreviewed;       622 AA.
AC   F2SPJ0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=ABC transporter ATP-binding protein ARB1 {ECO:0000313|EMBL:EGD87742.1};
GN   ORFNames=TERG_03988 {ECO:0000313|EMBL:EGD87742.1};
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:EGD87742.1, 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}.
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DR   EMBL; GG700651; EGD87742.1; -; Genomic_DNA.
DR   RefSeq; XP_003234937.1; XM_003234889.1.
DR   AlphaFoldDB; F2SPJ0; -.
DR   STRING; 559305.F2SPJ0; -.
DR   GeneID; 10376240; -.
DR   VEuPathDB; FungiDB:TERG_03988; -.
DR   eggNOG; KOG0927; Eukaryota.
DR   HOGENOM; CLU_000604_36_0_1; -.
DR   InParanoid; F2SPJ0; -.
DR   OMA; HDRDFMN; -.
DR   OrthoDB; 25181at2759; -.
DR   Proteomes; UP000008864; Unassembled WGS sequence.
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   CDD; cd03221; ABCF_EF-3; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032781; ABC_tran_Xtn.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR19211:SF15; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 2; 1.
DR   PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF12848; ABC_tran_Xtn; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:EGD87742.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          90..331
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          401..620
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  69039 MW;  166151737C3A8FD1 CRC64;
     MVSASKAARQ AKRAAEGDKK KTATSKLSSK ANSKNVSTAS SVNGDDAEEG ATSAAKMSDV
     KKLTEQTDKF GLSDRVTTGV LASVPSSRDV KMSSISLVFH GRVLITDSTL ELTYGKRYGL
     LGENGCGKST LLKAISKREF PIPEHIDIYL LNEGAPPSEL GALDWVVTEA QNELDRLEKL
     AEEVLENEGP DSPVLEDIYE RMDGMDPSTF HTRASLILTG LGFNKVTIKK MTKDMSGGWR
     MRVALAKALF VKPSLLLLDD PTAHLDLEAC VWLEEYLKKW DRTLILVSHS MDFLNGVCTT
     MIDMRMKQLM YYGGNYDSYQ KTRAEQETNQ MKAYHKQQEE IAHIKKFIAS AGTYANLVRQ
     AKSRQKILDK MEADGFIQPV IPDKVFTFRF ADVEKLPPPV LSFDDVTFSY SGDAKDNLYE
     NLDFGVDMDS RTALVGPNGV GKSTLLRIMT GKLAPTSGIV TRHTHLKLGM YSQHSAEQLD
     LTKSALDFVR DKYSEKSQDY QYWRQQLGRY GLSGESQTAL MGTLSEGQKS RIVFAILAIE
     SPNMLLLDEP TNGLDIPTID SLADAINAFS GGVVVVSHDF RLLDKIAKDI MVCENKTVRR
     WDGTIGEYKN HLRKKMINAG QV
//
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