ID   RMI1_BOVIN              Reviewed;         624 AA.
AC   A4IF98;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=RecQ-mediated genome instability protein 1;
GN   Name=RMI1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential component of the RMI complex, a complex that plays
CC       an important role in the processing of homologous recombination
CC       intermediates to limit DNA crossover formation in cells. Promotes TOP3A
CC       binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-
CC       mediated dissolution. Required for BLM phosphorylation during mitosis.
CC       Within the BLM complex, required for BLM and TOP3A stability (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RMI complex, containing at least TOP3A, RMI1
CC       and RMI2. The RMI complex interacts with BLM. Directly interacts with
CC       RMI2 and TOP3A. May bind DHJ. Interacts (via N-terminal region) with
CC       BLM; the interaction is direct (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Forms foci in
CC       response to DNA damage. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RMI1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC134472; AAI34473.1; -; mRNA.
DR   RefSeq; NP_001077234.1; NM_001083765.1.
DR   AlphaFoldDB; A4IF98; -.
DR   SMR; A4IF98; -.
DR   PRIDE; A4IF98; -.
DR   Ensembl; ENSBTAT00000028164; ENSBTAP00000063708; ENSBTAG00000021135.
DR   GeneID; 614063; -.
DR   KEGG; bta:614063; -.
DR   CTD; 80010; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021135; -.
DR   VGNC; VGNC:59200; RMI1.
DR   GeneTree; ENSGT00940000161055; -.
DR   InParanoid; A4IF98; -.
DR   OMA; STWHVKV; -.
DR   OrthoDB; 531291at2759; -.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000021135; Expressed in pharyngeal tonsil and 107 other tissues.
DR   GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR   GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; IBA:GO_Central.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0002023; P:reduction of food intake in response to dietary excess; IEA:Ensembl.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR   GO; GO:0071139; P:resolution of recombination intermediates; IEA:Ensembl.
DR   GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR   Gene3D; 1.10.8.1020; -; 1.
DR   Gene3D; 2.40.50.770; -; 1.
DR   InterPro; IPR033472; DUF1767.
DR   InterPro; IPR032199; RMI1_C.
DR   InterPro; IPR013894; RMI1_N.
DR   InterPro; IPR042470; RMI1_N_C_sf.
DR   InterPro; IPR044881; RMI1_N_N_sf.
DR   Pfam; PF16099; RMI1_C; 1.
DR   Pfam; PF08585; RMI1_N; 1.
DR   SMART; SM01161; DUF1767; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..624
FT                   /note="RecQ-mediated genome instability protein 1"
FT                   /id="PRO_0000361549"
FT   REGION          378..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9A7"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9A7"
FT   MOD_RES         292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9A7"
FT   CROSSLNK        334
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9A7"
FT   CROSSLNK        387
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9A7"
FT   CROSSLNK        425
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9A7"
SQ   SEQUENCE   624 AA;  70051 MW;  6D71BEAD57D6D361 CRC64;
     MSVTSIALRV ETWLSATWHV KVPVTWLEAC INWIQEENDH VNLSQAQMNK QVFEQWLLTD
     LRDLEHRLLP SGILETPKGE LNGFFALQIN SLVDVSQPAY AQIQKLRGKN TTNDLITAET
     QVTPKPWEAK PSRMLMLQLT DGIVQIQGME YQSIPALHSD LPPGTKILIY GNISFRLGVL
     LLKPENVKML GGEVDALLEE YAQEKVLARL IGEPDPIVSV IPNNSNQIIP RITDVLDPAL
     GPSDEELLAS LDENDELAAN NNTSLERSCF IGNSSNTVPI RQSDFETELV ISPRPREKPR
     NQSMLFTDEE LDDFSLEEAL LLEEAVQKEQ METKELQLLT LNRTTDESIE KFSHRSNTLN
     NFSFICKNGN NNWSEKNLSE QMTSEDKSLS CPSTRDQNSS SLSVNHNVPL PHDFTNKGKS
     SETYKIKQIS SSDGHSLNNK MFNGELVSNV PKRSSDVPNE NEHHLQTCSL QLSENSTGLP
     ITMDLYSPPF IYLSVLMASK PKEVTTVKVK AFIVTLTGNL SSSGGIWSVR AKISDGTAYL
     DVDFVDEILT SLIGFSVSEM KRLKKDPCKY QKFLEGLQKC QRELIDLCCL MTISFNPSLS
     KAMVLALQDV NTDHLENLKR RLKK