ID   A0A165FFK2_XYLHT        Unreviewed;      1121 AA.
AC   A0A165FFK2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Structural maintenance of chromosomes protein 5 {ECO:0000256|ARBA:ARBA00018687};
GN   ORFNames=L228DRAFT_270184 {ECO:0000313|EMBL:KZF20919.1};
OS   Xylona heveae (strain CBS 132557 / TC161).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC   Xylonales; Xylonaceae; Xylona.
OX   NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF20919.1, ECO:0000313|Proteomes:UP000076632};
RN   [1] {ECO:0000313|EMBL:KZF20919.1, ECO:0000313|Proteomes:UP000076632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC161 {ECO:0000313|EMBL:KZF20919.1,
RC   ECO:0000313|Proteomes:UP000076632};
RX   PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA   Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA   Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The genome of Xylona heveae provides a window into fungal endophytism.";
RL   Fungal Biol. 120:26-42(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010171}.
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DR   EMBL; KV407462; KZF20919.1; -; Genomic_DNA.
DR   RefSeq; XP_018186474.1; XM_018335384.1.
DR   AlphaFoldDB; A0A165FFK2; -.
DR   STRING; 1328760.A0A165FFK2; -.
DR   GeneID; 28900521; -.
DR   InParanoid; A0A165FFK2; -.
DR   OMA; RFWTSQP; -.
DR   OrthoDB; 232016at2759; -.
DR   Proteomes; UP000076632; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030915; C:Smc5-Smc6 complex; 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:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR   Gene3D; 1.20.920.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR027131; SMC5.
DR   PANTHER; PTHR45916; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 5; 1.
DR   PANTHER; PTHR45916:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 5; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076632}.
FT   DOMAIN          76..1074
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          263..329
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          458..492
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          686..748
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          913..950
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1121 AA;  129130 MW;  40EC610E91C03B87 CRC64;
     MPALPQRRRR SSLSLENENR EEEEIDGLVH ASNKRARIDR SNGSLPNGHL ASSLPVATFD
     ASRTDDHHYK YQPGSIVRVR LTDFVTYTSA EFLPGPSLNM VIGPNGTGKS TLVCAICLGL
     GWGPVHLGRA KEVSEFVKHG CSEATIEIEL AADPSKQRRN PIIKRLIKRE TNKSMFFVND
     KQCTKAEIAA ITASFSIQID NLCQFLPQDK VCEFAALTPV ELLHSTQRAA APPYMLEWHQ
     QLKQLRGDQK RLLVQQDNDK DALTNLEGRQ NMQRADVDRL RERAEIVQRL KMLEKARPFA
     RYREARLKVQ AAKEKKRTAQ AELEQLEHEL EPSLRAVNGK QTYRSKVEHV VKDRRGVVES
     ADASAESLLA KQKDLLEKVN DLRTEYQAET NGFKSRKQEI PRIEANITRI KRLLEDTPVE
     FDAAVYNEQI REKSRLLREI QIKAGESKQK QTDLVSQKDE RKEMLEHAEA ELRSLESQAG
     QQGNKLRQIS RETYRAWEWV QANQDQFEKH VYGPPVVECS VKDPKYVDAI ESLLQKNDFL
     AFTCQTRADF KKLQEQLYGN MKLADINIRT YSETLLEKFQ PPVSPEEQRR LAFEGWALDY
     VSGPAPVLAM LCGECRLHQT GVALRDINDD QYAAIERSPI SSWVTGRFSY QITRRKEYGP
     SAVSTRVRDL KRAQVWTNQP VDSGAKRELQ ENIHAWTEEV QQLSHDIEEV RQELAQLKEQ
     HDEIEGEKRD LEAEKQTKQK ALSDFKALPT KLAQQEERRE VIRQFGSEVK QRCLAINKKI
     EDYTLERAEV AIEYTRSIET LRIAHKELYQ VELMLIEATS EVEQLTERSR TVREMLAEKR
     KEFDKVAQET ESISRVARQL LEQCKEMIQE GGEEIQEFVN TLPQGQMPDE LEADIDSTKA
     RLELVHEGNP DTIRQFEERQ KKIEKLHERL AEHENRLEAF TRDISDLRES WEPQLDELVK
     NISDAFAYSF EKIGCAGQVA VHKDEDFDQW SIEIQVKFRE NESLAILDAH RQSGGERAVS
     TIFYLMALQS LARAPFRVVD EINQGMDPRN ERMVHERMVD IACAENTAQY FLITPKLLHD
     LKYHPRMKVL CIASGEYMPS NYRELDFKSC LNQMRAIKAG G
//