ID A0A0C9U788_PAXIN Unreviewed; 1144 AA.
AC A0A0C9U788;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Rad50/SbcC-type AAA domain-containing protein {ECO:0000259|Pfam:PF13476};
GN ORFNames=PAXINDRAFT_99796 {ECO:0000313|EMBL:KIJ15011.1};
OS Paxillus involutus ATCC 200175.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ15011.1, ECO:0000313|Proteomes:UP000053647};
RN [1] {ECO:0000313|EMBL:KIJ15011.1, ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ15011.1,
RC ECO:0000313|Proteomes:UP000053647};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN819339; KIJ15011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9U788; -.
DR HOGENOM; CLU_006184_0_0_1; -.
DR OrthoDB; 5477220at2759; -.
DR Proteomes; UP000053647; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
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:0006996; P:organelle organization; IEA:UniProt.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR PANTHER; PTHR18867:SF12; DNA REPAIR PROTEIN RAD50; 1.
DR PANTHER; PTHR18867; RAD50; 1.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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:UP000053647};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 6..221
FT /note="Rad50/SbcC-type AAA"
FT /evidence="ECO:0000259|Pfam:PF13476"
FT REGION 316..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 584..643
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 719..957
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1038..1126
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 320..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1144 AA; 130670 MW; 65F4B4F7FB06B51A CRC64;
MASLNKLAIR GIRSFDDKQI SVIEFFSPVT VIVGHNGSGK TTIIECLKYA TTGDQPPNTR
GGAFIHDPKM ANEKEVKAQV KLRFHAANGQ RMLVVRNLSV TAKKTGMTMK TLESILALAD
SNAEKGGKRG VISTKCAEMD SEIPHLLGVS KSVLENVIFC HQEDSWWPLA EPAALKKKFD
DIFEATRYTK ALDSIKALRK DRVADLKADK ERLESLSKEK THADKLRARI GEINSAITSK
QLQYEECKAH YEELVKNNSR FYESATKFRE LYVKVENLQQ KKEHYQQELA EARETVQETE
GTGSDEELQA RLQNFDENIS QQKKNRRRQE SERQDLEDEL AKARRTHVEL VNEQGELAAE
AKAFTPLLLA HERRLSEREE LIREISDKHN IKGYSHSPLE REKVNEFIAR LGDLQRRQRS
EFEKLRQESQ TKNDEFNRKS RQLDTELQSF KMQRSNAREQ IKEKQTAISK AESSVETMQG
LASELRTLAG DIEEKKLRLA KVKNDIKAAN FEERLSERAS KARSMEDKRD GLNHELRGLS
LQADARARLD LKRAETRSRA TEVKNTLEMS NAKFRKLVGK DARTETMERE LDRIAREKEE
ELAEAEDASA AANKILQGAE TTLSQAKAQI KVKRDEFKNL EKILKEGTLG GVPLSDALEE
ARHTVADLTS NTSNKAGMAE VYETLLKVGK DKKTCQACNR HMDDRELAVF EKFLKEQIKR
NSSESREDSS AQLKEWKEEL DRLEAFLPFQ ASRDRIKGNE IPTLEHQIKS AETEIPSASE
QSEQAAQKVN DIKKDVRDIS ALKQHAATVS RNQTEIERLK TEIANLEEEL SATGSAKTAD
DVQTELDALS NEIRANERER QAIMTERDRQ NSSLRTYESD LHAMEKKENT LSNQIRDKDD
MEERIITMAN EVTALNSKLK ELDVKLAEAR APIERLEQEY QQAQSELNAR IAEAQSSSQG
MNMSVDKLDN INKIVDRYVR EKRARLLTEC AEKVEHYEGE ITELGIKIES IREAIANIDR
EINESGSSVS NLRDNIRLRR LVKDIAATQA EIDSYDMEAA AKAKRNFEDR YQVEKQRETE
MQSKYAHIGG EISSHNETLK QVERDLREYK DVNKQYTDQL VKVKKRCHGI LLACFARFKA
EVSD
//