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
//