ID F2STI6_TRIRC Unreviewed; 411 AA.
AC F2STI6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Protein FYV10 {ECO:0000256|ARBA:ARBA00018741};
DE AltName: Full=Protein fyv10 {ECO:0000256|ARBA:ARBA00017917};
GN ORFNames=TERG_05784 {ECO:0000313|EMBL:EGD89546.1};
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:EGD89546.1, 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; GG700653; EGD89546.1; -; Genomic_DNA.
DR RefSeq; XP_003233915.1; XM_003233867.1.
DR AlphaFoldDB; F2STI6; -.
DR STRING; 559305.F2STI6; -.
DR GeneID; 10375997; -.
DR VEuPathDB; FungiDB:TERG_05784; -.
DR eggNOG; KOG2817; Eukaryota.
DR HOGENOM; CLU_020227_0_0_1; -.
DR InParanoid; F2STI6; -.
DR OMA; HWTEICE; -.
DR OrthoDB; 208500at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd16652; dRING_Rmd5p-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR037683; Rmd5_dRing.
DR InterPro; IPR044063; ZF_RING_GID.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12170:SF3; GH10162P; 1.
DR PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR Pfam; PF10607; CTLH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00757; CRA; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 356..397
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 356..397
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 411 AA; 46318 MW; 808CCE7723CBC8CE CRC64;
MDQVQKEHQR LWKKAQASKC INDVQATIDL LLEARRTIEN DPNSTSITLA KLQNPIKASF
EATNNDLKEG YSGLNKYTKA LDKLFKDKPL PTTEYDSLSQ PALVNRAVAM HLLREGAFST
ADTFLAEVSR THAESELDTA MGQAEQQASE AIPDIEGLRS GEIRTQFLLM HELLHELTEN
RNLLPAIEWA RNHREALYVR GSNLEFELCQ LQFVWLFHGG GEAGISIQEG RLKALEYARR
EFSSFQGRYL LEIQRLLGAM AFAPNLEDSP YNAIFNNPDS WDRVATSFKG EFCALLNLSA
ESPLYVAATA GAIALPTLLK LQTIMKEKRT EWTSQNELPV EIPLPHSYQY HSIFVCPVSK
EQTTDMNPPM LMPCGHVIAH QSLIRISKGN KFKCPYCPTE SHAKDARKLL L
//
