ID   MMS22_DANRE             Reviewed;        1240 AA.
AC   B3DIY3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Protein MMS22-like;
DE   AltName: Full=Methyl methanesulfonate-sensitivity protein 22-like;
GN   Name=mms22l; ORFNames=zgc:194596;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the MMS22L-TONSL complex, a complex that
CC       promotes homologous recombination-mediated repair of double-strand
CC       breaks (DSBs) at stalled or collapsed replication forks. The MMS22L-
CC       TONSL complex is required to maintain genome integrity during DNA
CC       replication. It mediates the assembly of RAD51 filaments on single-
CC       stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs
CC       following histone replacement by histone chaperones and eviction of the
CC       replication protein A complex (RPA/RP-A) from DSBs. Following
CC       recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of
CC       RAD51 filaments and subsequent homologous recombination. Within the
CC       complex, MMS22L acts by binding ssDNA. {ECO:0000250|UniProtKB:Q6ZRQ5}.
CC   -!- SUBUNIT: Component of the MMS22L-TONSL complex.
CC       {ECO:0000250|UniProtKB:Q6ZRQ5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6ZRQ5}.
CC       Chromosome {ECO:0000250|UniProtKB:Q6ZRQ5}. Note=Localizes to DNA damage
CC       sites, accumulates at stressed replication forks.
CC       {ECO:0000250|UniProtKB:Q6ZRQ5}.
CC   -!- SIMILARITY: Belongs to the MMS22 family. MMS22L subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC163291; AAI63291.1; -; mRNA.
DR   RefSeq; NP_001124073.1; NM_001130601.1.
DR   AlphaFoldDB; B3DIY3; -.
DR   STRING; 7955.ENSDARP00000115566; -.
DR   PaxDb; B3DIY3; -.
DR   PeptideAtlas; B3DIY3; -.
DR   GeneID; 563411; -.
DR   KEGG; dre:563411; -.
DR   CTD; 253714; -.
DR   ZFIN; ZDB-GENE-030131-3869; mms22l.
DR   eggNOG; ENOG502QQCR; Eukaryota.
DR   InParanoid; B3DIY3; -.
DR   PhylomeDB; B3DIY3; -.
DR   PRO; PR:B3DIY3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB.
DR   GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR042320; MMS22-like.
DR   InterPro; IPR029424; MMS22L_C.
DR   InterPro; IPR029425; MMS22L_N.
DR   PANTHER; PTHR28547; PTHR28547; 1.
DR   Pfam; PF14911; MMS22L_C; 1.
DR   Pfam; PF14910; MMS22L_N; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Chromosome; DNA damage; DNA repair; DNA-binding;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..1240
FT                   /note="Protein MMS22-like"
FT                   /id="PRO_0000360033"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1240 AA;  138402 MW;  5F0DF8970D3E978E CRC64;
     MESEFSQSLT PPVSPSALNH YGESAPSRPP CFTCAYEAGR EDTGRLSSNG YISRGALKRL
     LLKLDPAPAD FGGDTVDIFD FPWVTETALV ESTKLLFGLF RQKVLKLETL VQSSSHDFGQ
     ASSLHYEAEE LRQQCVLFLS YIKVFIYRFL EPSQSLDEGP VHPFKDAEAQ LPSVLVEELF
     SITLLIGRIG NLPANVQSAF TIQHQGKLFP PSWQLLHLHL DIHWSVLEIL HLLEQRMMGQ
     VVYAHQFVNL TGETLTNISL FEDQVNNLFC DLIGLAMNKY NKVRPTETLN THHYHCLCTK
     ELWILLIHLL EHRSKSIHTQ SFWSYINALL QTVLKGTTSG DRDPGFPVHC KDPEGFTWWL
     LTHLAQIGMH NRNGTAQQEK QLEDNWSFVI GLLKSICDPK KAAQEEQIRV VVHCCLSLSL
     MWGPNVSAVT TFWEYYSKNL NSSFTVPWLG VSGLGSICRT PLCLLQQAKS CCSPAPVGSS
     SHTQLYRTAN SFHIFLRILA LHLSQEHAGG APWRQIKGRL YSKFHQRRMM ELSDMGLLHF
     LLLFLVLAQC AELEDVASRA CDLLAMLPTN STPLALRALQ WRGQLALVLL YLEKGLDVGA
     LAEQLAVYFS QAAREFYLKT TEPSRKLALW APLSSYLEGV SEVFETSPNL TLSEERLLNE
     GFGLLLPACR QSELSSALGF LQTVLAQLRR VHQRCGQPSH SVDSPSWAPL PSVAKERHQA
     VAAALWSHFF PFLCSMRLSQ TPPPQLADAA AGFTLLALDM PGSAPQNLQP HPIQSIMQSF
     GWDEMLHPLL VTHYLNHLLQ NGELVSWVSS GQGSGSAQAL CVRAWIRCVL QQYLHKSPDA
     PDARAGRNLD EQLAELTRQV FRLPEVEFVL QRAGLQSAAV KDPKAAMAVF LKAVGRSYCE
     LQLLSERSSA VSRALEYVGD ILKYIKPYLQ NKSREGLQLA YWTIGCLVKH WSHLLATSKA
     QQLLFRIVDV LLLPHALLQQ DTAAHTQMLS ALKDSLPMFL QGLSVAVSVS HSQGAYLKQQ
     QHSVISQYLS RFLPATPSTG AVVNHPVLLA ACESTPSPQG ERLRKSILHV LRENFLQFKG
     LAPPPRLAAV LCFLLELLKR NSDRDPALLT IPLPSVLRCL MLVNEPQVKR LSSEVTQLIV
     ERCTAAVGEQ PCEHTTAILR AFVDENEGVY DQQVYNVLEV VAVLHPFTVA ALIPFLTLSL
     RKTECKRGLG KNTSLRNGYR RLLALLGDSG QAEMISLEED