ID A7TTU4_VANPO Unreviewed; 319 AA.
AC A7TTU4;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN ORFNames=Kpol_154p2 {ECO:0000313|EMBL:EDO14314.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO14314.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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DR EMBL; DS480629; EDO14314.1; -; Genomic_DNA.
DR RefSeq; XP_001642172.1; XM_001642122.1.
DR AlphaFoldDB; A7TTU4; -.
DR STRING; 436907.A7TTU4; -.
DR GeneID; 5542283; -.
DR KEGG; vpo:Kpol_154p2; -.
DR eggNOG; KOG1039; Eukaryota.
DR HOGENOM; CLU_037646_0_0_1; -.
DR InParanoid; A7TTU4; -.
DR OrthoDB; 2906101at2759; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
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:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR Gene3D; 1.20.120.1350; Pneumovirus matrix protein 2 (M2), zinc-binding domain; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR045072; MKRN-like.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR PANTHER; PTHR11224:SF10; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000000267};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 32..59
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 63..90
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 32..59
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 63..90
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 150..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 319 AA; 36515 MW; 0EA768340FAE6B55 CRC64;
MGKQEFNHFP LQQQKVILEH LKITKHSTPS KNYSHVPCKF FKQGNCQAGD HCPFSHELKV
INSANSIPCK YYQKGNCKFG SNCANLHIDP PSQENQKSFS TSSQKISPKM SDSLLYGSTG
LDEFDEFEEY YIPSECSDLL TPEELKRRKS RSYSSSSVSS NSSYISNNNF SPPSSVSSST
LTSSPSYSYS SKFLTTFPTK YYPSTNQFNC EATPMTPNWN QQIPPQFQTY KLGQQKPSFQ
QSMLEERLVR RLDGNDLTRY RILEEDEDRI ESRPMSNAAT PINIPIPVQI SNHYDHRNIQ
DTQFFFDDLP VSPLNHSNR
//
