ID S3DH58_GLAL2 Unreviewed; 1243 AA.
AC S3DH58;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=GLAREA_01820 {ECO:0000313|EMBL:EPE25908.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE25908.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE25908.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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; KE145371; EPE25908.1; -; Genomic_DNA.
DR RefSeq; XP_008087227.1; XM_008089036.1.
DR AlphaFoldDB; S3DH58; -.
DR STRING; 1116229.S3DH58; -.
DR GeneID; 19460878; -.
DR KEGG; glz:GLAREA_01820; -.
DR eggNOG; KOG0018; Eukaryota.
DR HOGENOM; CLU_001042_0_1_1; -.
DR OMA; SYIRDHT; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000016922; 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; 1.10.287.1490; -; 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.
DR SUPFAM; SSF57997; Tropomyosin; 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 Hydrolase {ECO:0000313|EMBL:EPE25908.1};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT DOMAIN 549..664
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 78..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 200..255
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 281..392
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 444..516
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 699..935
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1020..1081
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1243 AA; 142327 MW; B823239A5AEA0243 CRC64;
MGKLVRLELF NFKSYKGHHI LLFGDSYFTS IIGPNGSGKS NSMDAISFVL GIKSSHLRSA
HLRDLVYRGR VLKTSKINDD GSAATPATNG HANGDAEGSD GESQSQKPAR NDPKSAWVMA
VYEDDAGDEQ KWKRTITNQG ASEYRINDRI VTAQGYNEAL EAENILIKAR NFLVFQGDVE
QIASQSPKDL TRLIEMVSGS LEHKAEYERL QEEAEQAAEN QNYNLHRRRG INSEIKQYQE
QKKEAEAFQN KQDERDHAIV QHILWKLYHF QRVMDESSAS IGEHQENLKE FRRGVEKYEK
QLEDARQAAL KVTKDVSKVE RNIKRKEKEI EEKENSLVPI DEKADYTNSQ IEKLRRRLTA
LTKERDENHT KMQDLKKQLV TVEKAQKQFQ TQWEESLKKQ GRQLNEDDLK EYNILRSQVI
TKTSSNQSQL DNLIRTMKTD EVTYNSLKGK VELHQSSVEK LQAEIKSIEE RKGATKSSVK
EISGEIDTKK KEFNNIQSER VRVNQARTEL DEKLHEVLKT LHEATAGQRQ SDKETRTRET
LVSLKRIFPG VKGRVGELCK PKQKKYDEAV ITALGRDFDS VVVETEKIGQ ECVQYLKDQR
SPPMTFIPLD NIKVTAVESN LKNLSKARLT IDTIDFDSSL ERAFSYVCGS SIVCDDLPTA
KEICHKRKIQ VKAVTLQGYI IHKAGSMTGG RGPEGGKKRK FEDQDVENLR KQQQKLQTQI
EALPNVSRRG SAEETLQNDL NGLEQRLSYA KSELAAFEQN LASRRKELTH EKRQLAEMEP
KYREKESELA SIREKVEEFQ SAVAKVEDSI FKKFCERLGY SDVRRYEAQQ GTLEQEAAEK
KNEFEVQKKR LDQALSWETA RWREVDGRVK KMEAQISTWL QDIESYNAEK AELENAIDVD
RAHQTEMEDE LQKQKEKLLS KNEKVNAARN ELHKRSKEID NRTKAITALE TELQRNSAGR
YALLRRCRLE QITIPLTPES KKLDSLPVDE NLLQTDPDEM DVDEEEGTVE TAGPDDDDVE
EQLQQKIADL NSELEKLNPN MRAVDRLDGV EARLKSTEKD FEDARKKAKQ SRDQFNEVKE
KRFELFNKAF THISEQISHV YKDLTRSAAY PLGGQAYLDT EDGDSPYLSG IKYHAMPPLK
RFRDMEHLSG GEKTMAALAL LFAVHSYQPS PFFVLDEVDA ALDNANVEKI KNYIREHAGP
GMQFIVISLK TGLFQGSESL VGVFRDQEAN SSKTLTLDLR KYV
//