ID F2PJV7_TRIEC Unreviewed; 733 AA.
AC F2PJV7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=CCCH zinc finger and RRM domain-containing protein {ECO:0000313|EMBL:EGE02175.1};
GN ORFNames=TEQG_01215 {ECO:0000313|EMBL:EGE02175.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
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 -!- FUNCTION: May be involved in the turnover of nuclear polyadenylated
CC (pA+) RNA. {ECO:0000256|ARBA:ARBA00043866}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS995721; EGE02175.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PJV7; -.
DR VEuPathDB; FungiDB:TEQG_01215; -.
DR eggNOG; KOG2135; Eukaryota.
DR HOGENOM; CLU_017928_1_0_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd12257; RRM1_RBM26_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.20.1390.10; PWI domain; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR036483; PWI_dom_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045137; RBM26/27.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14398; RNA RECOGNITION RRM/RNP DOMAIN; 1.
DR PANTHER; PTHR14398:SF0; ZINC FINGER PROTEIN SWM; 1.
DR Pfam; PF01480; PWI; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF101233; PWI domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 256..284
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 354..426
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 256..284
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 75..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..249
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 80518 MW; FF3821830402697A CRC64;
MQFTEEKAAE VKSWVVKKLE DISDADSEVL ADYVLALIST DAPDDEIRKA SVENLEDFLK
ENTVPFVDEI FEKFHPKPEQ RALPTNTQQA DIDMSSSVHS PPFGQQSPSA DMMAQFAQAQ
QGTMGQQGSA PFDNNDKQFN TRKRTFNDSQ GDDQGPYQRN ADRPHKSARG RRGRGGWDNR
QNPSPHGQGY SPNMPSGFRG GPGTPQPSFP PFNPNDPIAQ MLSMSGMNFP QIPGMPPMPP
LPSLNGQPQP SGSPPNKIAE RCKNYDNMGF CVLGSTCPYQ HGQALSKDDE YDPTKSNIVS
GHSANGANGH GSSGRGDRGR GRGRGRNDRG GHGSQRRNRA EFSHAGPNDD RRITTIVVEQ
IPEDKFDEAT VREFFSEFGE ITEVTMKPYK HLALVKYDSY DAAHRAWSSP KVIFDNRFVK
VYWYKPTESR GDTNGFKKTS ADEPSFDMEA FEKQQAEAQK AHEEKVRKRK ETEEAILEHK
KKTEELLKRH KEEQAKLLQK LEAKGAGKDT ASPESGVSAN DKTASLRAQL ASLEAEAKSM
GIDPNAQTES PFGRGRGRGY AGFRGRGGFA PRGRGFDPSF RGGFRGRGAF RGRGGVIRLD
NRPKKVAISG VEFDTNRDEA LRQYLLGIGE YESIDPSPDR PGALVVSFKD RYVAEKLVHG
PSDIPSVGKV EFTWVANAPA SSTQPPGAAA SAPKASEDVS MTDSNATAAS VPEKEPAHEV
DYDVAEMDDS WAD
//
