ID   UBR11_SCHPO             Reviewed;        2052 AA.
AC   O13731;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=E3 ubiquitin-protein ligase ubr11;
DE            EC=2.3.2.27;
DE   AltName: Full=N-end-recognizing protein 11;
DE            Short=N-recognin-11;
DE   AltName: Full=RING-type E3 ubiquitin transferase ubr11;
GN   Name=ubr11; ORFNames=SPAC15A10.11;
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 [GENOMIC DNA].
RX   PubMed=11702950; DOI=10.1016/s1534-5807(01)00037-5;
RA   Kitamura K., Katayama S., Dhut S., Sato M., Watanabe Y., Yamamoto M.,
RA   Toda T.;
RT   "Phosphorylation of Mei2 and Ste11 by Pat1 kinase inhibits sexual
RT   differentiation via ubiquitin proteolysis and 14-3-3 protein in fission
RT   yeast.";
RL   Dev. Cell 1:389-399(2001).
RN   [2]
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a His
CC       ligand in place of the fourth Cys of the classical motif.
CC   -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
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DR   EMBL; AB079543; BAB84668.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB10108.1; -; Genomic_DNA.
DR   PIR; T37711; T37711.
DR   RefSeq; NP_594298.1; NM_001019721.2.
DR   AlphaFoldDB; O13731; -.
DR   SMR; O13731; -.
DR   BioGRID; 279257; 29.
DR   STRING; 4896.SPAC15A10.11.1; -.
DR   MaxQB; O13731; -.
DR   PaxDb; O13731; -.
DR   PRIDE; O13731; -.
DR   EnsemblFungi; SPAC15A10.11.1; SPAC15A10.11.1:pep; SPAC15A10.11.
DR   GeneID; 2542809; -.
DR   KEGG; spo:SPAC15A10.11; -.
DR   PomBase; SPAC15A10.11; ubr11.
DR   VEuPathDB; FungiDB:SPAC15A10.11; -.
DR   eggNOG; KOG1140; Eukaryota.
DR   HOGENOM; CLU_000684_1_0_1; -.
DR   InParanoid; O13731; -.
DR   OMA; EQLPKRM; -.
DR   PhylomeDB; O13731; -.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:O13731; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IMP:PomBase.
DR   Gene3D; 1.10.10.2670; -; 1.
DR   InterPro; IPR003769; ClpS_core.
DR   InterPro; IPR042065; E3_ELL-like.
DR   InterPro; IPR044046; E3_ligase_UBR-like_C.
DR   InterPro; IPR039164; UBR1-like.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   InterPro; IPR003126; Znf_UBR.
DR   PANTHER; PTHR21497; PTHR21497; 1.
DR   Pfam; PF02617; ClpS; 1.
DR   Pfam; PF18995; PRT6_C; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..2052
FT                   /note="E3 ubiquitin-protein ligase ubr11"
FT                   /id="PRO_0000056143"
FT   ZN_FING         96..168
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT   ZN_FING         1339..1474
FT                   /note="RING-type; atypical"
FT   REGION          471..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2052 AA;  234043 MW;  2AEA9E9E991D0453 CRC64;
     MQLHDPPAPL SQPSASRLQK YLLESAEKHA YDSNEESKTH LLQEVFLSLL NYNEDNWKYF
     LKEKPGAITS DFRLSRLQHS EPECAQELQD KRSGSKVCGH VFRAGEVIYR CKNCGLDNTC
     VLCAPCFHAT NHEGHETHVS ISTSYSGICD CGDPEAWNVD LNCKIHNVPD DEEQKKPEEV
     IPLELQHSIR TTIHILLDFI LDVFSCSPVN LKAQSTVGSI LADEEASRLS SAKYGVADRP
     CNVFRVMLWN DEVHTFDAVV GSVLEALDSS NTAFGLEVAQ RVDSIGRFAV ATSASVHEAI
     RIANAISKEN LAVNVRTARD FFREDICGIL LEWFDDLLES HVCYFADYLQ IIVCDEILKN
     WSPGLEKPAK PEVNFNNLPL EIVNDDDSED DIYAAEELLD VIANLQDETG VTRIANLGGD
     EDFEADMTDP TIAGFDHPLD DDNDVNDLLD FETEREDIDD LTDEVMETEE NEAAEADYPG
     VNRNTRQDDV QDISMETESQ NETDESQNTE NVDYNPQTHT PVPIPTTATQ DVVTIRPEFN
     SQLLNNLRQI INARRRPRPA AVCQVSLRED YWKSPHPIPP SSYSFVESPS SILRLDYFLL
     FDLKFWKRLR GLLSKLYVVP FNRNLLFKRL MGIRFVIHYR SLATAFLFAD REPDHSVMFL
     SVQFFTTPSL AEAVVKDYDF LTNLNATTLS LLTQSNRPST LFSSDIEYTP TIQLNRQVLK
     TRRTYNLFSD LGYLLQHPQV KKLVVDDTRY VHQYIDLLRV FQGVIPQQRA ILSHVQWDFP
     HGKNILFVMQ RVAMLSNTVS SCFTQAPYER LFYAIKCIIT SITHPKLDIA ESLEPLSCIP
     SSSLTNFTQP LVPFSVSRDP ISFYHPLHWM LSNLFSYCRV DASSHWDKDT LLALLDHPLR
     VCVLLAQIDC NLWIRNGRSI LLTDAFYRQL NNIEVSYDKD ILAIQTILMF VDPNLVLNAV
     VQRFEFTDWL YNLTYNEHPN YDTERIPAML CKMLELLIAL ITEREQILHV DIQDIIRTRL
     AQQLCFGPLA YSALLSTISS NLVESLSFDK IREEVTSYKA PDGLHDFGVY SLKDEYYDLV
     DPYYFHYNKN EREESDTILK KRLAKKNNVS AESIIIEPKI RFLEKDGHDI FFAAVNASTF
     SLIIFRAIEY ALVQAESFGS SDIGNTILGD ALQLCLISMK IHEFSKSNDF CSRSCAERYP
     TDSSIMREFG GSAYCLAELC FAILKSPKYK DVHVKVNAVL AGLQKNDPSA YSNMLEATHF
     ELSTTSSTSD SNEIEKTQEK KRLALEKQKK IMQQFRDQQA SFLAQNTDFD IGEDQTEDEV
     TTEEPEEEVK YHEHIRGNCL LCQEECNDQA PYGVIGIIQG SSLLRKTDVH SEIILDEIYS
     VPPNLDRESH SRPFGKKYDT VVFNRSKDRL LSAYPPGNNI RGVFVSGCGH LMHLGCFKNY
     YVARSMYRND VTAGLSEYYY KYSTAKFFMC PLCRSLSNVL LPMPQIPKMC LNIDTLNFPR
     SMNGWLEEIG TMSSSSFEYQ LVRSSLSDTK DTFRSCFLRP WINSKIISAM LARLKIADGA
     LIDQSNNRDV SDLYDRYCET TKLAMKLVKG STFTNVSPHD LLNSLAYTVS SLEVSQRCSP
     KQSGATRSVW FNELGPLTLS FLPTLSDTVL KCVCDQIIKS DQQALLLMES QKLLVCKIFY
     RHSQLKSMLR NGRMSDHDQI QPFLLSNTFD DFVKISSLML IFGKQDNILY YVKLFYLSEI
     CKTIISMIKV VADSSVVPDL TINYSQQSKS QFYILCKNVL LWCGSSNNIE ILDDESNLLR
     LMSLVEKYSL PFLRRVALVL YCMFDISLEF NEFSNNEDDS ELERLSKLIK VPPLQELYSQ
     MSSDENNQIL ELIAGWCEHL AQNTWGDSTI SLEYPGIYEL VKLPHRLENL IDSMQESVCC
     MCHKTPILPA ICMLCGSVIC FNARQNTVSS RRLTGECNKH AATCTGSVGI FFITKACGIL
     LLDSISNTGT IMPTPYLDIH GETDLQLRRG CPQFLNQKRY DFVVREQWLR QTVLQKMARH
     MDMTEMQNWR MA