ID F2SFJ5_TRIRC Unreviewed; 1249 AA.
AC F2SFJ5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=RanBD1 domain-containing protein {ECO:0000259|PROSITE:PS50196};
GN ORFNames=TERG_01183 {ECO:0000313|EMBL:EGD84910.1};
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:EGD84910.1, 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).
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DR EMBL; GG700648; EGD84910.1; -; Genomic_DNA.
DR RefSeq; XP_003239201.1; XM_003239153.1.
DR AlphaFoldDB; F2SFJ5; -.
DR STRING; 559305.F2SFJ5; -.
DR GeneID; 10374106; -.
DR VEuPathDB; FungiDB:TERG_01183; -.
DR eggNOG; KOG0866; Eukaryota.
DR HOGENOM; CLU_255442_0_0_1; -.
DR InParanoid; F2SFJ5; -.
DR OMA; AFGNMFS; -.
DR OrthoDB; 1953543at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR CDD; cd13170; RanBD_NUP50; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR PANTHER; PTHR38697; NUCLEAR PORE COMPLEX PROTEIN SIMILAR TO S. CEREVISIAE NUP2 (EUROFUNG); 1.
DR PANTHER; PTHR38697:SF1; NUCLEAR PORE COMPLEX PROTEIN SIMILAR TO S. CEREVISIAE NUP2 (EUROFUNG); 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT DOMAIN 1140..1249
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..860
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1249 AA; 128531 MW; A1F17CB09B380AC6 CRC64;
MSSNDAPKRA TAAQIANRKI KAARERRTRV GSPSLPQPAA NPFSSVGTDT ASASAFTAPS
NGFTFGQSQG FSRPATATGT SNNIPSASSS FDNNQSNAPG TFKLFGSQTT SAPPSFDFSS
NNAQQVSNPF SNMSSNQNTG FQGFKGSMFN IPGASQPENK KPENQQNGSG GFFGQAPAQT
SAPLFGATPT TSASLFSSSA GPNMFGQSNN NNPPTNIFGS ATMPSPTKST GGEAMQMSPD
GPKSTAGQAM FNVSAPAPPI FKPTFSTPST GSIFNMGGAT ATTSAATPAF SFKPTASASA
PPASSGGSIL FGASKPEESK AAPAVSSGNF MFGASASTPA STPLFGQQKP AEAPQATTTT
AAPATTTSTT KPSSIFGANT SFSTAPSGGS LFSHLAQPNN AAASASAANG TSSIFSNLGQ
PKPDATPSPT KETNSLFGHL AQPKTDAAPA PAKETGSIFG HLAQPKAETV TSPAKESPPL
FSAPSTSKPL FGAPSTATAQ PPTQPAFSFF GQTTKPTESP KPASATTGGQ TPSIFPIPSS
NSIFQAQQQP TATQTENKTP AQSPMFAAST NIPPVTQPKP MFTSSVNAGT SGAAKPFSPT
FGASPVPAPA APVEAPAPPK PKYVDASTET VFEASVTMVN FRPTEAEYPP NATPEVREQF
LRLWRLSALN ASFQEEIASV NCWSQDLDPI IGRYVMLRKL IGHPHPIVTQ YIPTTPGSKL
PCKPLPPFSD YDAEYERERA QAGAENSVSN GDAAPPGPSG VSHKRKASDA AEEESISSDK
TGKRAKFDAD KAKHSGDKAD EAGEATPSKT LSLFANSFVA QKSRASAADG DDEADAESDA
DGASSEESGE SNEEEESTDT EKQEEKTTTP SVSPPSTSNG GGRSLFDRIQ RDENGQPIRQ
VQADELNEEA KSLANEANEL ASSVLGGSRT GSPFNAGSLT PLTGSTNGLD STRSPSPTDP
PKAKTSTPSI FANLAPSGSS NIFGASNSFT STSSAGGSKP TTTSNIFGAP PSSATSSATS
GSAPATSIFA APSPTSTPPP SNIFGAPPST SAPAQTSVFA TPSSAPTPTS NSSLAPPTTN
IFGHLKPGNS SAQPGLSPFP LSAATSVDPS PAQSDTDATN DPSDEVEKHT QVDFTRSGPG
EEDEDAVFEC RSRAYQHING QWEVKGLGVL RILKHRTNKK SRILLRADPS GSVLLNTNLM
PEIEYQQNGT GVQFIVPSES GFQHWLLRVK TSEGACELKN SMEQHKKRD
//
