ID   LIN_MEDTR               Reviewed;        1488 AA.
AC   D1FP53;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Putative E3 ubiquitin-protein ligase LIN;
DE            Short=MtLIN {ECO:0000303|PubMed:19776163};
DE            EC=2.3.2.27 {ECO:0000303|PubMed:19776163};
DE   AltName: Full=RING-type E3 ubiquitin transferase {ECO:0000305};
GN   Name=LIN {ECO:0000312|EMBL:ACL14419.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RX   PubMed=19776163; DOI=10.1104/pp.109.143933;
RA   Kiss E., Olah B., Kalo P., Morales M., Heckmann A.B., Borbola A., Lozsa A.,
RA   Kontar K., Middleton P., Downie J.A., Oldroyd G.E., Endre G.;
RT   "LIN, a novel type of U-box/WD40 protein, controls early infection by
RT   rhizobia in legumes.";
RL   Plant Physiol. 151:1239-1249(2009).
CC   -!- FUNCTION: Putative E3 ubiquitin ligase involved in the rhizobial
CC       infection process. Plays an important role in the early steps of
CC       infection thread formation and in growth and differentiation of
CC       nodules. {ECO:0000269|PubMed:19776163, ECO:0000303|PubMed:19776163}.
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:19776163};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000303|PubMed:19776163}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and nodules.
CC       {ECO:0000269|PubMed:19776163}.
CC   -!- INDUCTION: By rhizobial infection. Promoter activity is detected at 3
CC       days post-inoculation (dpi) in dividing cortical cells in roots and at
CC       6 dpi in young emerging nodules. At 21 dpi strong promoter activity is
CC       detected in mature nodules in the nodule apices including the infection
CC       zone, with lower activity detected in the nitrogen-fixing zone.
CC       {ECO:0000269|PubMed:19776163}.
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DR   EMBL; EU926660; ACL14419.1; -; Genomic_DNA.
DR   EMBL; EU926661; ACL14420.1; -; mRNA.
DR   RefSeq; XP_013469258.1; XM_013613804.1.
DR   AlphaFoldDB; D1FP53; -.
DR   SMR; D1FP53; -.
DR   STRING; 3880.AES61911; -.
DR   EnsemblPlants; KEH43296; KEH43296; MTR_1g090320.
DR   GeneID; 11418360; -.
DR   Gramene; KEH43296; KEH43296; MTR_1g090320.
DR   eggNOG; KOG0167; Eukaryota.
DR   UniPathway; UPA00143; -.
DR   ExpressionAtlas; D1FP53; differential.
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; -; 1.
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..1488
FT                   /note="Putative E3 ubiquitin-protein ligase LIN"
FT                   /id="PRO_0000413001"
FT   DOMAIN          512..587
FT                   /note="U-box"
FT   REPEAT          1207..1244
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1249..1290
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1412..1451
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1456..1488
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REGION          297..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..462
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1488 AA;  166849 MW;  269B814CBB792A7F CRC64;
     MSGNFRFMMD QKDIVRFLTT TIDSFIQDRL INKEQRTQHK DQCAERLAAE DGNTDKETEV
     EYSDQAVLAN LDWGIEALEE AINTYNMETK LARLDYAEKM LQVCAMLNPK QKTAGVPNSY
     LSAWAHLNLS YLWKLRNNIK SCIYHSLEMF IVDPFFSRID FAPELWKNLF LPHMSSIVGW
     YSEERHKLMM EVLPESTDFS YTADFDKVFN ESLVFSMRPN QLEKLQKLEQ LYGESLDENT
     RLYAKYYNDC MNPDSTSSKK VVPMLPIAEP PMTPLHELSR SVPDFVKFGP ILPKSSGFSM
     TTRRSNDGLN ETTRENIASN SNHSKGEQSS LWAAKESIIE EIEDDLDSEH YDASVDSDKI
     NIFSPEPKKN IKDEDVEPKV YRSNQKNQMN SPNISPMESP RRASNYSSTN PLRRKKESKF
     LRLLSNRFTG SIVSDHSLSS SPDTSSDHIF TGDEEVMVRN NIKRKNDSQT PSMNQDNENS
     LVLNDSSHCE SEDGYQSSSS FPKLEKLTIG SKPPKDFVCP ITGQIFSDPV TLETGQTYER
     KAIQEWLGTG NTTCPITRQA LSANILPKTN YVLKRLIVSW KEQNPELAQE FSNSNTPRGS
     SCSPSAKDIT MVSSIQRTTD SPSQKYKDDY IRQRNNRFTR VSVGASPTSV LSQAAVETII
     NSLTPYITSL CTSENLQDCE QAVLEIARLW KDSKTDPQIH SYLSKPTVVS GLVEILSASL
     NREVLRRSIY ILSELIFSDE RVGETLNSVD SDFDCLAMLL KNGLAEAALL IYQLRPVFAQ
     LSEHELIPSL IQVIQNKSED IDDFQLAIDP KAAAIAILEQ ILIGGDEYNR SVNASSVISA
     NGIPAIVKYL DKTEGRRPVI SILLCCMQAE KSCKSSIANR IELSPVLELF HAGNDSVRGI
     CVEFLSELVR LNRRTSSNQT LQIIKDEGAF STMHTFLVYL QMAPMEHQIA VASLLLQLDL
     LAEPRKMSIY REEAVETLIE ALWQKDFSNN QMKALDALLF LIGHVTSSGK SYTEAGLLKI
     AGFDQPYNVL MKAEQLGHSD NDFMETMEDE KNAMKSWQKR VASVLCNHEN GSIFQALEEC
     LKSNSLKMAK SCLVLATWLT HMLFTLPDTG VRDVARKSLL EALMNVLQSS KNLEEKILAS
     LALKSFISDP TVHEVLRVYA KSIYRILRKL KKYSTVAADI LKALLNLNSV DVTELWSCKE
     VVELDLSSNG EVLSLHYLNG QVLSGHADGT IKVWDARKRI PRVIQETREH KKAVTSLCSS
     VDKLYSSSLD KTIRVWTIKP DGIKCIDVYD VKEAVYELAA NAKLACYVTQ GTGVKVFNWL
     DAPKFINFNK YVKCLAVSGD KLYCGCSGYS IQEVDLSKYT STSFFTGTRK LLGKQTIHSL
     QIHDDLLFAC GSSIDATAGK IFSLSSKMVV GSLSTGLDVH RVAINSDFIF AGTKFGTIEV
     WLKDKFTRVA SIKMAGGNTK ITSLASDADG MMLFVGSSDG KIQVWALD