DMC1_LILLO
ID DMC1_LILLO Reviewed; 349 AA.
AC P37384;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Meiotic recombination protein DMC1 homolog;
GN Name=LIM15;
OS Lilium longiflorum (Trumpet lily).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Lilium.
OX NCBI_TaxID=4690;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Flower bud;
RX PubMed=7584025; DOI=10.1093/dnares/1.1.15;
RA Kobayashi T., Kobayashi E., Sato S., Hotta Y., Miyajima N., Tanaka A.,
RA Tabata S.;
RT "Characterization of cDNAs induced in meiotic prophase in lily
RT microsporocytes.";
RL DNA Res. 1:15-26(1994).
CC -!- FUNCTION: May participate in meiotic recombination.
CC -!- SUBUNIT: Double stacked ring-shaped homooctamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RecA family. DMC1 subfamily. {ECO:0000305}.
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DR EMBL; D21821; BAA04845.1; -; mRNA.
DR PIR; JC2214; JC2214.
DR AlphaFoldDB; P37384; -.
DR SMR; P37384; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000150; F:DNA strand exchange activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IEA:InterPro.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011940; Dmc1.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02238; recomb_DMC1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; DNA-binding; Meiosis; Nucleotide-binding; Nucleus.
FT CHAIN 1..349
FT /note="Meiotic recombination protein DMC1 homolog"
FT /id="PRO_0000122921"
FT BINDING 138..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 240
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 240
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 243
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 246
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 246
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 252
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 252
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 320
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
SQ SEQUENCE 349 AA; 38272 MW; CDA444A1166DBEC6 CRC64;
MVDVKFEERR FESPGQLQLL DRQEAEEEEE DCFESIDKLI SQGINAGDVK KLQDAGIYTC
NGLMMHTKKN LTGIKGLSEA KVDKICEAAE KLVNVGYITG SDVLLKRKSV IRITTGSQAL
DELLGGGIET LQITEAFGEF RSGKTQIAHT LCVSTQLPVS MHGGNGKVAY IDTEGTFRPD
RIVPIAERFG MDASAVLDNI IYARAYTYEH QYNLLLALAA KMSEEPFRLL IVDSVIALFR
VDFSGRGELA ERQQKLAQML SRLTKIAEEF NVAVYMTNQV IADPGGGMFI SDPKKPAGGH
VLAHAATVRL MLRKGKGEQR VCKIFDAPNL PESEAVFQIT PGGVADAKD