ID A0A1Q3DYJ3_LENED Unreviewed; 941 AA.
AC A0A1Q3DYJ3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Condensin complex subunit SMC1 {ECO:0000313|EMBL:GAV99818.1};
GN ORFNames=LENED_001301 {ECO:0000313|EMBL:GAV99818.1};
OS Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX NCBI_TaxID=5353 {ECO:0000313|EMBL:GAV99818.1, ECO:0000313|Proteomes:UP000188533};
RN [1] {ECO:0000313|EMBL:GAV99818.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAV99818.1,
RC ECO:0000313|Proteomes:UP000188533};
RG Lentinula edodes genome sequencing consortium;
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAV99818.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAV99818.1,
RC ECO:0000313|Proteomes:UP000188533};
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RT "A genome survey and senescence transcriptome analysis in Lentinula
RT edodes.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC {ECO:0000256|ARBA:ARBA00005597}.
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:GAV99818.1}.
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DR EMBL; BDGU01000019; GAV99818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3DYJ3; -.
DR STRING; 5353.A0A1Q3DYJ3; -.
DR Proteomes; UP000188533; 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; 1.
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; 1.
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}.
FT DOMAIN 230..346
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 25..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 435..518
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 550..640
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 25..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 941 AA; 107224 MW; 2670DEC1FCB3E004 CRC64;
MEKKIKRGEK ALDSKRPDLV SVEAQITHST RKTNNANKAK QDVAKTQSDL EDRVNNLEAE
LVKVKRDADK AQEAQRIMSQ NNLALSDEIL EEYRSLKTSA NLLAIEERQK LEKLTREEKA
VIRAFNALRE KHQGLEEKRD SRSEEITSQT TKKTELEEKI AGLQDELTNK KQELENQQSE
RTKISQLEAQ ANEKLQSVYQ QLLQAGVDRN ESERERKLKD TLTSLQRIFP GVRGRVIDLC
KPSQRKYETA VSVVLGRNID AVVVDEEKTA IDCIEYMRNQ RAGQATFIPL DTIQVKPISD
KFRSFAKGAR LAVDVIQYEP AVERAMHHAC GNALVCDTMD VAKYVCYEKG QEVKAVTLEG
TIIHKSGLIT GGRSTHGGEK KWDEKDVQGL QKSRDSLLAK LRDLSKQKPR GKTDENLIAE
ISQLESYITI ARDELSACKT RLSGLKEELR HLDREIQKNG PELKKAQKEH GKLQEQIATL
AEAVNSAEDE VFTDFCRKIR VENIRDFEER QLKLAQEESE ARLRYDNQIA RLTHQLEYET
EALRSSRERL SHLQELVKTE EVNLAKLQER KKTVEQELAD LQEGISTHKE ELTELQEVLD
EKSKTVEQAK RTALRSSRIL EQTLKEISAN NDEIEKLAME RSTTYRKCRL EEIKLPLLEG
NLKNVPMEEN LRDEVAMDVD DDEDGTQRPK AVQNYGIEVD FADIDDEERE DGSPDALAEF
DAQIAKLTTE IERIAPNMKA MERLDDVEQK LAETEAETEK ARKDSKTARE HFQDVQRRRT
ELFMKAYTHI SDRIDQVYKD LTKGKAAPMG GVAYLSLDDS EEPYSGGIKY HAMPPMKRFR
DMEQLSGGEK TVAALALLFA IHSYQPAPFF VLDEVDAALD NTNVAKVANY IKSQASSSFQ
FVVISLKGSL YERGDSLVGI YRDQEANSSR TLTLDLTQYD E
//