ID F2SNB8_TRIRC Unreviewed; 843 AA.
AC F2SNB8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=TERG_04429 {ECO:0000313|EMBL:EGD88179.2};
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:EGD88179.2, 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).
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DR EMBL; GG700651; EGD88179.2; -; Genomic_DNA.
DR AlphaFoldDB; F2SNB8; -.
DR STRING; 559305.F2SNB8; -.
DR VEuPathDB; FungiDB:TERG_04429; -.
DR eggNOG; KOG0231; Eukaryota.
DR eggNOG; KOG1571; Eukaryota.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_021936_0_0_1; -.
DR InParanoid; F2SNB8; -.
DR OMA; FHPDLDD; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR43215; RADIAL SPOKE HEAD 1 HOMOLOG; 1.
DR PANTHER; PTHR43215:SF14; RADIAL SPOKE HEAD 1 HOMOLOG; 1.
DR Pfam; PF02493; MORN; 3.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00698; MORN; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 796..831
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 332..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 94736 MW; 01E491957F043CAF CRC64;
MSDESLNMLP RDFNSRIRIT SENTESIQSG VTEYLKAREG KWSLPPVLQI ELSRQKFDKK
ARQWKFLVNR VHRNEELDLS SFVDSGVQGK YTLFSFIAHK GHRTSRWYYP LVRPAGQGTH
WLAFKGEDPY RIECLTAKAA TESYEGLDIA EVGNGEPVNA EIAVAFIYIR NDLQDQYLTP
KLESWTPSPA WHRYMQGLSP DKSAVEPEQQ IPVVFYGING VSKDTRNPAA AYDVIDHLTS
EKDTITMTVP VSMNVGELRA KLAAQLSTDE NPVANERIRM WTIGAPHEVR LFNFSMEPLV
SMGFQLSSLG WNALRIWVQI LNEEDVKYFS IPEFVTPPPV PNETDMKEDL PAPPSQPLVE
NEEQPQPAQE IQPSSQDEDV EMNDASPEEA PTQPNQNRDE PEHPSEHIPS APELPEHEMS
DNAPEQPGTN GIEPTSVPEA QTDEQAANEA IIASIIAQDL ALLDQSQEMD TSGSFTEANG
ISPPPPMIDE EAADSPRNEA EESREVQEHH SGSEDSQMEG SPIVESQNDA PEETNAQTSQ
EEVQREEPVI LEPPVTKSDL ILPCDQVYYF VQEFDADKQT VETVGAFFAR SSCNVREQVR
KTLGLSEDQG YNFWSRRKAV ASVHSVSSSH KFRDLINDVG CIIFGKTIPK RRQTELVEEG
CFLTPDRLLE YLWAVDRQHP NKSFTGKKTI EAVLNGEYYS GDLCKGYYHG NGTHISETGD
TYTGDFVQGR RQGTGMIEHS SGDTYTGDWF EDQPHGQGTW VEHKTGNKYV GGYRNGKRHG
KGVSYWEVAD EEMNLCQICY TEEQDSLFYT CGHVCACGTC ARQVEICPVC REKVISVVKI
FRC
//
