ID   LIN1_LOTJA              Reviewed;        1485 AA.
AC   C6L7U1;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Putative E3 ubiquitin-protein ligase LIN-1 {ECO:0000250|UniProtKB:D1FP53};
DE            EC=2.3.2.27 {ECO:0000303|PubMed:19508425};
DE   AltName: Full=Protein cerberus {ECO:0000303|PubMed:19508425};
DE   AltName: Full=RING-type E3 ubiquitin transferase LIN-1 {ECO:0000305};
GN   Name=CERBERUS {ECO:0000312|EMBL:BAH86605.1};
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAH86605.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND INDUCTION.
RC   TISSUE=Root nodule {ECO:0000269|PubMed:19508425};
RX   PubMed=19508425; DOI=10.1111/j.1365-313x.2009.03943.x;
RA   Yano K., Shibata S., Chen W.-L., Sato S., Kaneko T., Jurkiewicz A.,
RA   Sandal N., Banba M., Imaizumi-Anraku H., Kojima T., Ohtomo R.,
RA   Szczyglowski K., Stougaard J., Tabata S., Hayashi M., Kouchi H.,
RA   Umehara Y.;
RT   "CERBERUS, a novel U-box protein containing WD-40 repeats, is required for
RT   formation of the infection thread and nodule development in the legume-
RT   Rhizobium symbiosis.";
RL   Plant J. 60:168-180(2009).
CC   -!- FUNCTION: Putative E3 ubiquitin-protein ligase involved in the
CC       rhizobial infection process. Plays an important role in the early steps
CC       of infection thread formation and in growth and differentiation of
CC       nodules. {ECO:0000269|PubMed:19508425}.
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; Evidence={ECO:0000303|PubMed:19508425};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000303|PubMed:19508425}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and nodules, and at very low
CC       levels in calli and seedling shoots. {ECO:0000269|PubMed:19508425}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at all stages of nodule development.
CC       {ECO:0000269|PubMed:19508425}.
CC   -!- INDUCTION: By rhizobial infection. In roots, expression increases up to
CC       fivefold at 3-7 days post-inoculation (dpi), with further increase at
CC       12 dpi. {ECO:0000269|PubMed:19508425}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAH86605.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAH86606.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB505797; BAH86605.1; ALT_INIT; mRNA.
DR   EMBL; AB505798; BAH86606.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C6L7U1; -.
DR   SMR; C6L7U1; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
DR   CDD; cd16664; RING-Ubox_PUB; 1.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 2.130.10.10; -; 2.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR045210; RING-Ubox_PUB.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00504; Ubox; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS51698; U_BOX; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   2: Evidence at transcript level;
KW   Nodulation; Repeat; Transferase; WD repeat.
FT   CHAIN           1..1485
FT                   /note="Putative E3 ubiquitin-protein ligase LIN-1"
FT                   /id="PRO_0000412999"
FT   DOMAIN          510..585
FT                   /note="U-box"
FT   REPEAT          1204..1241
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1246..1283
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1409..1448
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1454..1485
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REGION          337..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..351
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1485 AA;  166492 MW;  8E2BDF8E11BD6F7D CRC64;
     MARNFRFMMD QKDIVRFLTT TVDSFIQDRL INKEQRTQHK EQCAERLAAE DGSGDKDTEV
     EYSDQAVLAN LDWGIEALEE AINTYNMETK LARLDYAEKM LQVCAMLNPK QKIAGVPNSY
     LSAWAHLNLS YLWKLRNNVQ NCISHALEMF IVDPFFTRID FAPELWKSLF LPHMSSIVGW
     YSEERHRLMM EVIPDSADLS FTADFEQFFN ESLVLTMRPH QLEKLQKLEQ LYGESLDENT
     KLYAKYYNDC MNSDSSSSKK AVPMLPIAEP PMTPLHELSR TIPDFVKFGP ILPKSAGFSL
     APRSKDVLNE TIRENVTSSN LKEEKLSIWG AKDTIIEENE DDSDSELENE SVDSDDKNNI
     FSPGMKMMKY EGVETKVDLS CQRNQIPSPD IFSPLDSPRT APNNSSPNPD MHSKRDSKFL
     RLSSSRIREP TISDSLTSSP DISIDNISNA DNEVMVLKNI QRKNDNQTLS MNHENENSLI
     LNGSSLCESD DGYQSFNSLP KLEKLSMGSK PPKDFVCPIT GQIFCDPVTL ETGQTYERKA
     IQEWLRTGNT TCPITRQPLS ASILPKTNYV LKRLITSWKE QNPELAQEFS NVNTPRGSSC
     SPSAKDIPML STRQRTTDSP NHKNKDYARQ RSNRFMPAAI TTSPTSVLSQ AAVETIVNSL
     KPYISSLCTS ENLPECEEAV LKIARLLKDS KTNPQIHSYL SKPTIINGLV EILSASRNRE
     VLRTSIYILS ELIFTDDSVA ETLNSVDSDF DCLATLLKNG LAEAALLIYQ LRPVFAQLSA
     HELIPSLVDV IQNKNEELDD FQLVIDPKDA AIAILEQTLM GGDEYSRSLN ASSVISANGI
     PTLVKYLERM EGRRSVVSVL LCCMQAEKSC KNLIANRIEL SPVLELFHSG NDSVRGTCVE
     FLSELVQLNR RTSCNQILHT IKDEGAFSTM HTFLVYLQMA PMEHQLAVAS LLLQLDLLAE
     PRKMSIYREE AVETLIEALW QKDFSNTQMK ALDALLFLIG HISSSGKSYT EAWLLKIAGF
     DQPYNALMKV EQLGQHDNDL IETMEDEKNA LNSWQKRIAS VLCNHENGSI FKALEECLKS
     NSLKMAKSCL VLATWLTHML YTLPDTGVRD VARKSLLEEV INVLQSSKNL EEKILATLAL
     KTFISDPSTH EALRVYAKSI YRTLRRLKKY SVVAVDIMKV ILNLKSVDVT ELWSCKEVVE
     LDLSSNGEVL SMVYLNGQVL SGHTDGTIKV WDARKRIPRV IQETHEHTKA VTSLCSSGDR
     LYSGSLDKTI RVWTIKSDGI KCIDVYDIKE AVHELAANDK LACYVSQGTG VKVFNWSEAP
     KLINFSKYVK SLAVAGDKLY CGCSGYSIQE VDLSTYTSNS FFTGTRKLLG KQTIHSLQIH
     DDYLFACGSS VDATAGKIFS LSQKMVVGSL STGLDIHRIA INSDFIFAGT KFGTIEVWLK
     DKFTRVASIK MAGGHTKITS LVSDVDGMML FVGSSDGKIQ VWALD