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Database: UniProt
Entry: A0A0C9U788_PAXIN
LinkDB: A0A0C9U788_PAXIN
Original site: A0A0C9U788_PAXIN 
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
//
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