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ITT1_SCHPO
ID   ITT1_SCHPO              Reviewed;         435 AA.
AC   Q9US46;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=E3 ubiquitin-protein ligase itt1;
DE            EC=2.3.2.31;
DE   AltName: Full=RING finger protein itt1;
DE   AltName: Full=RING-type E3 ubiquitin transferase itt1 {ECO:0000305};
GN   Name=itt1; ORFNames=SPAC1002.14;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC       interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC       type E3 enzymes: they bind E2s via the first RING domain, but require
CC       an obligate trans-thiolation step during the ubiquitin transfer,
CC       requiring a conserved cysteine residue in the second RING domain.
CC       {ECO:0000250|UniProtKB:O60260}.
CC   -!- SIMILARITY: Belongs to the RBR family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB65614.1; -; Genomic_DNA.
DR   RefSeq; NP_593502.1; NM_001018936.2.
DR   AlphaFoldDB; Q9US46; -.
DR   BioGRID; 279692; 1.
DR   STRING; 4896.SPAC1002.14.1; -.
DR   PaxDb; Q9US46; -.
DR   EnsemblFungi; SPAC1002.14.1; SPAC1002.14.1:pep; SPAC1002.14.
DR   GeneID; 2543264; -.
DR   KEGG; spo:SPAC1002.14; -.
DR   PomBase; SPAC1002.14; itt1.
DR   VEuPathDB; FungiDB:SPAC1002.14; -.
DR   eggNOG; KOG1814; Eukaryota.
DR   HOGENOM; CLU_021364_2_2_1; -.
DR   InParanoid; Q9US46; -.
DR   OMA; RVAICED; -.
DR   PhylomeDB; Q9US46; -.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q9US46; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:1990580; P:regulation of cytoplasmic translational termination; ISO:PomBase.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.10.110.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; PTHR11685; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00591; RWD; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50908; RWD; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..435
FT                   /note="E3 ubiquitin-protein ligase itt1"
FT                   /id="PRO_0000372422"
FT   DOMAIN          16..135
FT                   /note="RWD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT   ZN_FING         174..224
FT                   /note="RING-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         245..308
FT                   /note="IBR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         368..396
FT                   /note="RING-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   REGION          170..420
FT                   /note="TRIAD supradomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         297
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         368
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         386
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         393
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         396
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         408
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         416
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ   SEQUENCE   435 AA;  50297 MW;  DD2B88FB2675DACA CRC64;
     MLEVEVESDN KHLVADELIA LQSIYPEIHL DGNNYGRLNI PVNTESDYFL SFKSPDESTL
     TDTIVVRHFP DLVMEFFLPE AYPFNSPPTF FLKSSWLPLK QKRVLTSSLI KLWNEIHDCV
     LFDAIEHVRS IATIAFHLPT EMVFPGGFDD LKKEILAFDK NAKLLEFQIR KFQCNVCFDE
     FNGTDCFQLT RCGHVSCQSC LRDYYTMCIQ EGMFSQIKCI DLDCGKDAPV LTLKELESIV
     GVQLTNRYKE LEEKRRYEND SNIIFCPRSF CQGPSKRDPG QKLAICQKCD FAFCSFCQAT
     WHGDLSPCKL EGDSKKLVEM YLNYQENEPE KALELEKRYG KRIIDRLVEQ VKNDEEAEKW
     VLLNGQRCPT CDRVVERIDG CCHMNCLCGT HFCFLCGAYL MEQNPYKHFN DPVSSCYGML
     FASAAEKQRF SENWT
 
 
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