ID G8BRL0_TETPH Unreviewed; 600 AA.
AC G8BRL0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN Name=TPHA0C02330 {ECO:0000313|EMBL:CCE62386.1};
GN OrderedLocusNames=TPHA_0C02330 {ECO:0000313|EMBL:CCE62386.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE62386.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE62386.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE612858; CCE62386.1; -; Genomic_DNA.
DR RefSeq; XP_003684820.1; XM_003684772.1.
DR AlphaFoldDB; G8BRL0; -.
DR STRING; 1071381.G8BRL0; -.
DR GeneID; 11533606; -.
DR KEGG; tpf:TPHA_0C02330; -.
DR eggNOG; KOG0845; Eukaryota.
DR HOGENOM; CLU_456507_0_0_1; -.
DR OMA; PNRHDIC; -.
DR OrthoDB; 232322at2759; -.
DR Proteomes; UP000005666; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR46527:SF1; NUCLEOPORIN NUP42; 1.
DR PANTHER; PTHR46527; NUCLEOPORIN-LIKE PROTEIN 2; 1.
DR Pfam; PF18345; zf_CCCH_4; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666};
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 8..35
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 8..35
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 36..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 63097 MW; 261F18304544E963 CRC64;
MSYYNRGRNN TTPCKYFQNG TCNKGSSCRF AHVYQNNSKH NNNNNNNNNN NNGTSRYGGS
SSNDQNSKGR SDAEKLNDFK NESRQNEIQK IINFDMNESK QFQVKPLTST YSYELPCMLN
LINGRDYSAE ESRFKYYQAQ KDGTSNAYQT EMTARENDMQ KAIMHVSAHP DWAARYLSKG
TKELSETGKT SFASEFINFP LDLIGQSYGS SAYGTTSAAF GSSSQAFGNA NLAFGSTNLA
FGGTNSAFGN SNSAFGNNTN ATTSGVFGAP VFGASNNTVS AFGATQTNPS SSVSAFGSSP
FGASAHTLSN SGTTGSAFGQ PTFGNSSKTG TSAFGTPAFS STSQPTSTAF GSPAFGSMTD
RNKATFGNQL GTSNNPLNSA FGASPFSNNT SANPFGSTQQ AATSGTSVFG APAFGTSAAT
GKSPFGSIQQ TSTPPFGQAA HNNNPLLPSA NGQQTNNNDV FGNTASSMST NLNSNNLSDS
LKNNQVITNS FGSNQGNQIA NTFDSASTNS LFGSQTTQNN SQGGFPSNGF QNVGSAFGRN
AASGVFNNNI SNSNLRQGPP TEDDRKTPDE LLPETLNQFQ AESFTLGKVP DIPPPLSLCT
//
