ID S9XE66_SCHCR Unreviewed; 335 AA.
AC S9XE66;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=RecA family ATPase Dmc1 {ECO:0000313|EMBL:EPY52071.1};
GN ORFNames=SPOG_00491 {ECO:0000313|EMBL:EPY52071.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY52071.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY52071.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RecA family. DMC1 subfamily.
CC {ECO:0000256|ARBA:ARBA00008897}.
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DR EMBL; KE546990; EPY52071.1; -; Genomic_DNA.
DR RefSeq; XP_013023454.1; XM_013168000.1.
DR AlphaFoldDB; S9XE66; -.
DR STRING; 653667.S9XE66; -.
DR EnsemblFungi; EPY52071; EPY52071; SPOG_00491.
DR GeneID; 25034823; -.
DR eggNOG; KOG1434; Eukaryota.
DR HOGENOM; CLU_041732_0_0_1; -.
DR OMA; REATYVI; -.
DR OrthoDB; 5477610at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000150; F:DNA strand exchange activity; IEA:EnsemblFungi.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:1905334; F:Swi5-Sfr1 complex binding; IEA:EnsemblFungi.
DR GO; GO:0000730; P:DNA recombinase assembly; IEA:EnsemblFungi.
DR GO; GO:0006311; P:meiotic gene conversion; IEA:EnsemblFungi.
DR GO; GO:0000709; P:meiotic joint molecule formation; IEA:EnsemblFungi.
DR GO; GO:0010774; P:meiotic strand invasion involved in reciprocal meiotic recombination; IEA:EnsemblFungi.
DR GO; GO:0051260; P:protein homooligomerization; IEA:EnsemblFungi.
DR CDD; cd19514; DMC1; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR NCBIfam; TIGR02238; recomb_DMC1; 1.
DR PANTHER; PTHR22942:SF30; MEIOTIC RECOMBINATION PROTEIN DMC1_LIM15 HOMOLOG; 1.
DR PANTHER; PTHR22942; RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER; 1.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47794; Rad51 N-terminal domain-like; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003422};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003422};
KW Reference proteome {ECO:0000313|Proteomes:UP000015464}.
FT DOMAIN 94..266
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT DOMAIN 273..335
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
SQ SEQUENCE 335 AA; 36700 MW; 9CF917F668C76E58 CRC64;
MSTMADVVDT AGEEQMPFSD IEELTSHGIG MTDIVRLKQA GICTVQGVHM STKRFLLKIK
GFSEAKVDKL KEAASKMCPV NFATAMELSQ TRKRVWNIST GSEALNGILG GGIQSMSITE
VFGEFRCGKT QMSHTLCVTA QLPKEMGGAE GKVAFIDTEG TFRPDRIKAI ADRYGIDPDL
TMENIIVSRA YNSEQQMDYI TKLGTIFAED GQYRLLIVDS IMALFRVDYS GRGELSERQQ
KLNIMLARLN HISEEFNIAV FVTNQVQADP GAALMFASND RKPVGGHVMA HASATRLLLR
KGRGEERVAK LNDSPDMPEA ECSYVITPGG IADVS
//
