ID A0A179A0I9_9EURO Unreviewed; 974 AA.
AC A0A179A0I9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN ORFNames=AYL99_01474 {ECO:0000313|EMBL:OAP65502.1};
OS Fonsecaea erecta.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP65502.1, ECO:0000313|Proteomes:UP000078343};
RN [1] {ECO:0000313|EMBL:OAP65502.1, ECO:0000313|Proteomes:UP000078343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP65502.1,
RC ECO:0000313|Proteomes:UP000078343};
RA Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA Attili D.S., Gorbushina A.;
RT "Draft genome of Fonsecaea erecta CBS 125763.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAP65502.1}.
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DR EMBL; LVYI01000001; OAP65502.1; -; Genomic_DNA.
DR RefSeq; XP_018698869.1; XM_018832990.1.
DR AlphaFoldDB; A0A179A0I9; -.
DR STRING; 1367422.A0A179A0I9; -.
DR GeneID; 30005644; -.
DR OrthoDB; 2906101at2759; -.
DR Proteomes; UP000078343; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.70.1660; -; 1.
DR Gene3D; 6.10.140.1950; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR43804; LD18447P; 1.
DR PANTHER; PTHR43804:SF7; LD18447P; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00937; PCRF; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF75620; Release factor; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Reference proteome {ECO:0000313|Proteomes:UP000078343};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 97..124
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 126..153
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 97..124
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 126..153
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 22..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 105667 MW; B196BEF125F0878B CRC64;
MSAALPRLTS DPAAAWNDHE QYGTMNRGHS KSTTQHPGSM MHGPSRQRNG FGGNGEKAVP
VPGSTVFGNG ADRKSSISQA QPLFDIARSP PTTSSKNTKH VPCKFFRQGA CQAGNACPFS
HSLDPMTQQA PCKYFMKGNC KFGAKCALAH YLPDGRRVNR ADLDAGFAMA GRNFNYANRA
DQAPFPSQEP SLADPVLNQP PYNSDYFPGQ GFPLMDSDEA DAFQDRYNQY QPPSTLDSGL
NSPPTSQFGS PPNDFQFPKS PVENLRTALN APLPQSFDAN GVSHIAKYGP LGQSVPDKFG
MRSPASSSLS RQLGSPPESI VNVRNANLGS NLRNVSPLGL SPQNAEESIG QRIMHSQRPV
KSRGLSASVP RPYLPYEWEE GLGAETDLLP NSLHDEVLTP QEKMRRTSRA DQEHSSKDHV
HALAIPSGTS SKVGSPPAGS PSRFSALWAE QREKKAAENN GPSSFGHVGS PLRGSWMPNE
STPSVQISGI SQAMARMQLN RVDSGELNGL RLQSSGLRHS SAPIGRFDRG ISSPGLSSKK
IDEEVEGVFF PMDGDDRTPN WSGQSPRLVP LRDRSNGTIG SGNGPEISPI LLQRARAVAA
EHQQLAAANA ENYDVAVAKK IGELGPVSTA LKEWDDAQNS LRELNALLHD PSSDSELRSL
AETDIQATTA SLHSLASNLK RSLIPPHPFA SMPCLIEIHP GAGGSEASLF AQSLLNMYTD
FCTRKRWPTT LASYTPDDST HEAGLTDALL EINHPGSYDV LRTEAGVHRV QRVPTTEKKG
RTHTSAVSVL VLPNLPDSPA HAEGLDYDDP NSDYYISAAE VKSETMRARG AGGQHVNKTD
SAVRLTHMPT GTVVAMQESR SQHKNREKAW TLLRAKLAQM RREQREAEVI SMRRAAMGGV
ARTGREDKVR TYNFSQNRVT DHRCGVETSD LDGVLAGGES LEEVMGSVRE WMNEEEVRGL
VAEEEMKMKS TVRA
//
