YB83_SCHPO
ID YB83_SCHPO Reviewed; 398 AA.
AC O59668;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=LisH domain-containing protein C29A3.03c;
GN ORFNames=SPBC29A3.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAA18380.1; -; Genomic_DNA.
DR PIR; T40074; T40074.
DR RefSeq; NP_595831.1; NM_001021735.2.
DR AlphaFoldDB; O59668; -.
DR BioGRID; 276993; 2.
DR STRING; 4896.SPBC29A3.03c.1; -.
DR MaxQB; O59668; -.
DR PaxDb; O59668; -.
DR EnsemblFungi; SPBC29A3.03c.1; SPBC29A3.03c.1:pep; SPBC29A3.03c.
DR GeneID; 2540465; -.
DR KEGG; spo:SPBC29A3.03c; -.
DR PomBase; SPBC29A3.03c; -.
DR VEuPathDB; FungiDB:SPBC29A3.03c; -.
DR eggNOG; KOG2817; Eukaryota.
DR HOGENOM; CLU_020227_0_0_1; -.
DR InParanoid; O59668; -.
DR OMA; CRQGMDD; -.
DR PhylomeDB; O59668; -.
DR PRO; PR:O59668; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0034657; C:GID complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISO:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR CDD; cd16652; dRing_Rmd5p_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR027711; Rmd5.
DR InterPro; IPR037683; Rmd5_dRing.
DR InterPro; IPR044063; ZF_RING_GID.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12170; PTHR12170; 1.
DR PANTHER; PTHR12170:SF3; PTHR12170:SF3; 1.
DR Pfam; PF10607; CLTH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00757; CRA; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 4: Predicted;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..398
FT /note="LisH domain-containing protein C29A3.03c"
FT /id="PRO_0000372348"
FT DOMAIN 99..131
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT ZN_FING 341..384
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 398 AA; 45631 MW; F090AA05A0F73F65 CRC64;
MNIDEWQRIE ETAPGNKCLA KLNELESILK DAKKSCLKDP TTSMKELVAC SEKTQQVFDD
LKRTEKKFHT SLNRFGKTLE KKFNFDLEDI KLHSSFESKK REIDTALSLH FFRQGDVELA
HLFCKEAGIE EPSESLHVFT LLKSIVQGIR DKDLKLPIEW ASQCRGYLER KGSSLEYTLQ
KYRLVSNYLT TKDIMAAIRY CRTNMAEFQK KHLADIQKTM IALFFCSRNE VLSGTNDSHD
SIHHIISNNA QLNIPQEYID VLDLDWKSLE LLFVREFCAA LGMSLESPLD IVVNAGAIAL
PILLKMSSIM KKKHTEWTSQ GELPVEIFLP SSYHFHSVFT CPVSKEQATE ENPPMMMSCG
HVIVKESLRQ LSRNGSQRFK CPYCPNENVA ADAIRVYF
