ID A0A165EFV9_EXIGL Unreviewed; 1233 AA.
AC A0A165EFV9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=EXIGLDRAFT_840470 {ECO:0000313|EMBL:KZV86844.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV86844.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV86844.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV86844.1,
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 ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC {ECO:0000256|ARBA:ARBA00005597}.
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DR EMBL; KV426143; KZV86844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EFV9; -.
DR STRING; 1314781.A0A165EFV9; -.
DR InParanoid; A0A165EFV9; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0008278; C:cohesin complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 2.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 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; IPR024704; SMC.
DR InterPro; IPR028468; Smc1_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF12; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 523..639
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 312..367
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 418..490
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 672..706
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 755..782
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 821..932
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1028..1062
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1233 AA; 139639 MW; 062723FF5262D8EF CRC64;
MPLLRIEVCD FKSYRGQQVI GPFSTFTSVI GPNGAGKSNL MDAISFVLGV KSMQLRSSQL
KDLIYRGRRL AEGTQSQSQN EPAGEGDATK AWVRAILEDK DGNELTFQRT VSINGASEYR
LNNRVVTYQA YNTALEDQNI LVKAKNFLVF QGDVEAIASQ SPKDLSRLIE QISGSLDLAG
EYERAKAAQE RATENATFNF TKRRGIAGEI KQFKEQKAEA ERFQKLVDER DHAVLERLLW
KLYHIEERIE NNTREIKKDS KVLGELRAQQ THNDQAAETA RVAYATARSE VITREKRIKK
QEKALEKKQP DLLDIEAKIA HVERKAANAT KMIETINADV TSRETKIAQQ RKEMAAVRKA
ADAAAEEQRK ASTTNLSLSQ ESLDEYRQLE AAAALEAVSE RQQLEQLGRE EKTDGRVLAG
NEAKLAEFEK TLERLETEVE QEKEKKNELD EKLRTASEDW EKVKAELDKL HSERTRIAKL
EKEINEKLNT IHHDLLQAGV DQRESEREAR LKDTLASLQR VFPGVRGRVV DLCKPTQRKY
ETAVSVVLGR NIDAVVVDTE KTAIECIEYM RNQRAGQATF IPLDTIQVKP INDKYRSFAK
GARLAVDVIQ FDPAVERAMH HACGNALVCD TMDVARFVCW EKGQEVKAVT LQGTIIHKSG
LITGGQSLHN SKKWEEKEVQ NLRRARESLM QQLQELSKQK PRSNADEPLQ AENSRLESQM
ALLRDDLSVC KHSLTGKKDE LKHVQREIKK LRPVVDKARA DRDALKKRME DLASVVHAAE
DKIFAAFCDK IGVPDIRAYR DHQLRATQEA QEARLRFDKQ LARMTHVLKF DEEELVSLQE
RLANMERAGK GDGAGLVKLK EQRDALRQEL DGMRETIEKM QKELEKFNEG VEEQRKELED
LKKTAAKSAK ALDKVLKDIA TKNDEIEQAA IERSGIYRKC KMEKIELPLL KGKMTNVPME
ENLRDEVAMD VDDEDGTQQP KTVQDYGIEV NFDTLDDEER EDGSPEMAAQ LDGAIVKLTT
EIERLVPNMK ATNRLDDVEN KLAETEREAE QARKESKTTR DDFNSVKKQR CDLFNKAYSH
ISDCIDQVYK DLTKGKAAPM GGVAYLSLED SDEPYLGGIK YHAMPPMKRF RDMEQLSGGE
KTVAALALLF AIHSYQPAPF FVLDEVDAAL DNTNVAKIAN YIQAHASEAF QFIVISLKGS
LYERGRSLVG VYRDQDLNSS RSLTLDLTQY AKD
//
