ID A0A2H3I461_FUSOX Unreviewed; 1307 AA.
AC A0A2H3I461;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Rad50/SbcC-type AAA domain-containing protein {ECO:0000259|Pfam:PF13476};
GN ORFNames=AU210_001566 {ECO:0000313|EMBL:PCD46154.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD46154.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD46154.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD46154.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD46154.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD46154.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCD46154.1}.
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DR EMBL; MABQ02000001; PCD46154.1; -; Genomic_DNA.
DR STRING; 327505.A0A2H3I461; -.
DR OrthoDB; 5477220at2759; -.
DR Proteomes; UP000219602; Chromosome 1.
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; 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.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000219602};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 6..234
FT /note="Rad50/SbcC-type AAA"
FT /evidence="ECO:0000259|Pfam:PF13476"
FT REGION 338..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 393..420
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 493..527
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 744..771
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 799..915
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 977..1074
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1307 AA; 149984 MW; D71FD79873A5F25D CRC64;
MSRIDKLSIS GVRSFSPSVR EAIQFNTPLT LIVGYNGSGK TTIIECLKYA TTGELPPNSK
GGAFIHDPKL CGEKEVMAQV KLQFRSINDR QHVATRSLQL TVKKTTRSQK TLDCSLVVVN
NGERTTTSTR QAQLDEMIPE RLGVSPAILD AVIFCHQDES LWPLSEPAAL KKRFDEIFEA
MKYTKAIDNL KVLRKKQVEQ LGKLQNDEAH NKVNKDRGDR AEKRMKALQA EIEGSRETCE
SISSEMEETQ DKIRNIRETA NSHLAIVQNL NTKREQLEYR EEAVKELKAT IDELPDDDGK
LEGDLAHYED RMQHLQDEAD QNKAQYNELQ TELGKSRKEL SAKLSEQGKH QSDKDKYERQ
LKIRMETIQE AAQSYGFSGF DGDLSDHHVK SFNDRLQKLL SEKKRDLERL QKENSAELDR
ATGVITELEG RKAARIQDRV SAKQRMGAIE KRTSVLQNES SQIDVDEGAK AVLDGQMQDL
EIRFQTAQKT FENADWDRQI SDENDKLHQL ENENDRLGRE LVECTRLASE RAQLDYRKKE
LGDRKRKLDT LTSTWKPKLD KILGSDWQPE TLDSKFQALV KDQSKIVSEV QKCREQIRQK
QQKVDFKLRT SKESHEKKSK EAATCQQQVV NALLAVRDNA TVEDYKEEIE VTESQVEELR
NDLSLFDALV DYYTKCKRLL DTKRKCLLCD RHFDDNQAAS MERLSKRIDK HLDPKGKVDT
EKDLKDTVAN LEKLRSVRGS YDTYERLNAE LPSLREECKV AEAKFDALER QVEEQGSVVS
AEEEKQKDLE DMSKTVLSIA QTVKDIAESE NQVDRIMSQQ MSGGVTRSPD EIHELQAGLS
DQMRNLKNRI VKLTTDRQRT KDQLNSLELE KSELRNKISR AAGQLDKKQD LQNQIQALKE
EASHQRDVIQ RADEELETIE PSITEARSAR DEVLRRGRAK EQVIADARDA VANSVNEMKM
MDADIQDYID RGGPSNLASN ERSIATLEKT IASTEKEVTD LTVRTNKLKQ DIDNGDRKKK
NIKDNLNYRK NLRTIDVIRQ EIAELEDRNA DEDYERLQAE ARMQENHYNR LLAERGSVMG
SMKTKDEELG RLLQEWEMDY KDAKRKYRES HIRVETTKAA IEDLAQCSSA VDKAVMQFHS
MKMAEVNRIA GELWQSTYQG TDIDTILIRS DNESNTGKRS YNYRLCMVKQ DTEMDMRGRC
SAGQKVLASI IIRLALAESF GVNCGLIALD EPTTNLDRDN IKSLAESLHM IIKARQAQSN
FQLIVITHDE DFLRHMRCSD FCDSFFRVKR DERQNSVISR ESITKIF
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