ID   D8Q9J1_SCHCM            Unreviewed;      1297 AA.
AC   D8Q9J1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Rad50/SbcC-type AAA domain-containing protein {ECO:0000259|Pfam:PF13476};
GN   ORFNames=SCHCODRAFT_77659 {ECO:0000313|EMBL:EFI95240.1};
OS   Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN   [1] {ECO:0000313|EMBL:EFI95240.1, ECO:0000313|Proteomes:UP000007431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX   PubMed=20622885; DOI=10.1038/nbt.1643;
RA   Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA   de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA   Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA   Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA   Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA   Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA   Woesten H.A.B.;
RT   "Genome sequence of the model mushroom Schizophyllum commune.";
RL   Nat. Biotechnol. 28:957-963(2010).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009439}.
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DR   EMBL; GL377308; EFI95240.1; -; Genomic_DNA.
DR   RefSeq; XP_003030143.1; XM_003030097.1.
DR   STRING; 578458.D8Q9J1; -.
DR   VEuPathDB; FungiDB:SCHCODRAFT_01155975; -.
DR   eggNOG; KOG0962; Eukaryota.
DR   HOGENOM; CLU_006184_0_0_1; -.
DR   InParanoid; D8Q9J1; -.
DR   OMA; FSDYYYR; -.
DR   OrthoDB; 5477220at2759; -.
DR   Proteomes; UP000007431; Unassembled WGS sequence.
DR   GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   InterPro; IPR004584; Rad50_eukaryotes.
DR   NCBIfam; TIGR00606; rad50; 1.
DR   PANTHER; PTHR18867:SF12; DNA REPAIR PROTEIN RAD50; 1.
DR   PANTHER; PTHR18867; RAD50; 1.
DR   Pfam; PF13476; AAA_23; 1.
DR   Pfam; PF13558; SbcC_Walker_B; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..236
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   COILED          216..445
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          470..520
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          569..596
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          711..902
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          971..1042
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1297 AA;  149789 MW;  189660A471B03B71 CRC64;
     MSSLEKLAIR GIRSFDDKQI SVIEFFNPVT VIVGHNGSGK TTIIECLKYA TTGDQPPNTR
     GGAFVHDPKM ANEKEVKAQV KLRFHAANGQ RMLAVRNLSV TLKKTTGMTM KTLESILAVA
     DEAQQGKKRG VISTKCAEMD TEIPQLLGVS KSVLENVIFC HQEDSYWPLS EPSTLKKKFD
     DIFEATKYTK ALDSIKSLRK DRVAELKTEK VRLEGLARDK AQYDKLKARI SELSQTIVAK
     EAEYDQVKVE YEAMVDANQK LYEQANAFRE TYMNVQNLEN RKKQLKQDIE EAKAEMKEEE
     GSDEELRERL RNHEKHIEKE KGRRLTEINA KEDLEEELKA MREEQMHDTA RLGKLRAEKE
     AQEQRIRDRE QIIRELAAKH GISGFNITPL GADKVVEFIS RLDDAYRKSK EELDAQTQDE
     HQKELLELEK KVDSLRTRKS TMKTALAEKQ ASITRDEATL DDMQDIPAQL ATVDSEIEDK
     TEKLKKLREQ IRTAAYDKQI EEKAREARLL DDQRNEASRE FRFLSSQAEI RAKLQLKRTE
     VQSKTKEVQA TIETSRVKFR KIMQKDPVAE TMEKDLDKAR IERESEQETL DKQATNAASV
     VQNSETAITT MRQEVKTNKE RIRVLDRNIK KVLGERPTIE KAIAEAKEEI EFRRKRIEGL
     KGGKTLLERW LQIGEEHKKC PACVRMMDDR ELREFEKTMR EHIGNADPKK LDGTKNEMEE
     WEQELVELEG LIPQQLELER LKEETPALEA KIKAQEDALP ELSAQADEIT DKIDLLRKQA
     NEVQALKLQA ANITRLQKDV ERLKEEIEEI EHDLSATGST KSTDDLQAEI EKMTDQIRLL
     EREKNHLTAD SNRMNNSVIS TERELHSLQT RRMELTSKVE KMKTLETNIA EAKKRIEEIA
     VDQKDIDVRI REAQGPIDAL NAQWESIRAE LRAIIETASE HTRALSLDSD KLNNINKALQ
     SYVKEKSQRI LDECSNTVEQ RKVEINELSE RVEAQRRVIE KIDKEINESG ASQASLRENI
     RVRKMQKEIV EIQTEIDKVD MEEIARSRRA FKDQYKPAKE KETELQGQYS HIGGMLTSSR
     EQLSTWEHDL RDFKDINKKY TEQLIRVKMS DMANNDLEKY AKALDSAIMK YHSLKMEEVN
     DTMRHLWNKT YQGTDIDGIK IRSDVEGGAS KRSYNYRVVM TKDQVEMDMR GRCSAGQKML
     ASIIIRLALS DSFGQNCGIL ALDEPTNALD TENIDALASS LVDIINERKN HSNFQLIIIT
     HDENFLRKLG QSEVMEHYWR VVRDSRQKSI IERQRFH
//