ID A0A165P7B9_EXIGL Unreviewed; 1154 AA.
AC A0A165P7B9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Structural maintenance of chromosomes protein 5 {ECO:0000256|ARBA:ARBA00018687};
GN ORFNames=EXIGLDRAFT_717309 {ECO:0000313|EMBL:KZW01749.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW01749.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW01749.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW01749.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(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; KV425892; KZW01749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165P7B9; -.
DR STRING; 1314781.A0A165P7B9; -.
DR InParanoid; A0A165P7B9; -.
DR OrthoDB; 232016at2759; -.
DR Proteomes; UP000077266; 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; 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; 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; PF13476; AAA_23; 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 Hydrolase {ECO:0000313|EMBL:KZW01749.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 94..271
FT /note="Rad50/SbcC-type AAA"
FT /evidence="ECO:0000259|Pfam:PF13476"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 263..304
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 709..788
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 858..885
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 943..977
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 58..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 131609 MW; 0E38A5A92E13DAAF CRC64;
MSTNGVTRVK REKVAAASQS QRRATPSEPP PSKRIRISDA GDAAATQHDD EDEDGDGEVN
GRHDGDDDDD GPAPPRPVTL PRAEDGYVPG SIVRVMLKNF VTYDHVEFSP GPYLNMIIGP
NGTGKSSIAC ALCIGLGWPP SILGRASELK AFVKNGCEEG FIEIELKGAL GKGNLVIRRS
INATDNKSIW RLNGQEVTGN EVKSRVQGLN VQVDNLCTFL PQDKVSSFAH MTPQQLLKET
QKAAGHADLT KWHTRLIEGG KELKELEETL KVDRANVEDK EARNARLERE VAKYKERREI
EEKIAVYEIL LPFVVFWHLS QETAAAETDL LKKRRVMEKM QAKNQPLQDL KATLERIVND
QKNARQKTQA AMQAKNKEMS RKWGEAEKLE RDAEETQNKL NNIKQEEKRR KTRMENFRKE
IERLQDKIAN PPEVEDEEVL REDARKASDA ISRQKEAVDN VRDDMRRFLE EQSRAKMQAE
NRREQLRRLQ DVEHQRLESL RKWDQDTAIA VDWLRKNKDK FKMEVFEPAI LSARVRPGAN
VDQVEACMGS SQFKTFVAQC KEDYDAFNHY VNDATDLASG GRKLRVNVWF RPQGDLPPPP
MSAAELKELK FEGYALDFLD CPEGMKWYFM RDVNMHRTAL GSDAVDIGRA MELVVRGGGS
GSCSFISGRT MSTVARSQYG QRKVQNQTRD IRPARNWANN RGGVDEQKKQ ELLHEIAEFD
EQVKKLEVTI EEHNKREQKY KKEAKALMEE KAKVSARAEK RVKLLKEYGL AKESLRAAES
RLQTEEAQKP PEALRQQLKN DLLKIAKKRV RIAKDYTSLV RGFITEQENA TRAILEVCQA
EANLAALERL VTQTSDKFQR VLREVKEANE TYKTLKAKRD HADDHANRIL RDAPESVADK
YREKEEKGLT QTSSVDEVQA KIETEKAKLE LNIATNPAVV RQYEEREREI LALQATVAEK
EAKKKRLEKG IAKVKDQWLP ALKQLVASIN EKFSAAFERV HCAGEVHISE DEDYDKWAID
IMVKFRDSER LQLLTGHRQS GGERSLTTIL YLMSLTELAR APFSLVDEIN QGMDQRAERL
VHNQLVDVTC REESGQYFLI TPKLLPDLKY HERMKVLCIN NGEWLPEQKG LGSLQKMLDN
YIDRNGGRAR FGAN
//
