ID A3LU44_PICST Unreviewed; 1171 AA.
AC A3LU44;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 24-JAN-2024, entry version 100.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=SMC2 {ECO:0000313|EMBL:ABN66522.2};
GN ORFNames=PICST_59451 {ECO:0000313|EMBL:ABN66522.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN66522.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN66522.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005231}.
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DR EMBL; CP000498; ABN66522.2; -; Genomic_DNA.
DR RefSeq; XP_001384551.2; XM_001384514.1.
DR AlphaFoldDB; A3LU44; -.
DR STRING; 322104.A3LU44; -.
DR GeneID; 4838712; -.
DR KEGG; pic:PICST_59451; -.
DR eggNOG; KOG0933; Eukaryota.
DR HOGENOM; CLU_001042_9_0_1; -.
DR InParanoid; A3LU44; -.
DR OMA; HNKIAME; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000002258; Chromosome 4.
DR GO; GO:0005694; C:chromosome; 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:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProt.
DR CDD; cd03273; ABC_SMC2_euk; 1.
DR Gene3D; 1.10.287.1490; -; 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; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR027120; Smc2_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 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; 2.
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 DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT DOMAIN 522..643
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 171..198
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 253..381
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 424..465
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 684..721
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 748..933
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 962..1011
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1171 AA; 132337 MW; 17B9C65456344E50 CRC64;
MKVDELIIDG FKSYATRTVI SGWDGQFNAI TGLNGSGKSN ILDAICFVLG IASMATVRAS
NLQDLIYKRG QAGVTKASVT IVFDNSEVSK SPIGFENCST ISVTRQIILG GSSKYLINGH
KAQQQTVLNL FQSVQLNINN PNFLIMQGKI TKVLNMKPTE ILSLIEEASG TRTFEERKDK
AQKTMAKKEA KLTEIRSLLK EEIDPKLEKL RNEKRSFLEY QQTQTDLEKL SRIIAAHDYT
KLSHSFTNYS NSLSEHESRM AALTSEIDKL GNEIKNLNDD LTHVRKQREA ELNNEGKLKE
LESQEARLST EITRLNTSKE IAHDNLKDEQ NKKQKLENQI AEIQSNLENN SDTYNSVKND
FDNATEQLQK LKEEYTKKDE LLSTLSTGVS ATGDMSTGYS AQLKEFKTKL NTSQNFIKTS
KLKIAHLESQ ISNDKKKLVQ AKAENQNILS DMEAYRSDIA AMEQEVSSKL GFDPSVIAEL
KSQEKQFHND AYKLNGELNH MKREIGNIDF QYSRPSANFN DSLVRGIVAQ LFELPETSND
KALALQVCAG GRLYNVVVEN SEVATQLLER GQLKRRVTII PLDKIHASSI DPRTVDYAKK
LAPNKVELAI NLIEFQDELV KAMEYIFGTT FVCNDPNTAK TITFDPKIRS RSITLEGDVY
DPEGNLSGGS RKNDSSIIIK VQRYNKVSKR LSEVNYKLNE IRQEIQRMES LIENTKGLQN
ELLLKKHELS LLERKLENNP SSVILKQNQA NEAEISGLQE QIRQEESNCQ NFEKEINVIE
KDIREFNSDK GSKLKDLKKD VVALKKEVEK KQVVLDKLTD KYQAIEVEGE QQKSDLIQAR
ASLQTTIDTI QELTAKISSM EQKGAELNDT LVIVRVQLEE EKANLLGLDE EINELMKIIK
DKNESLSNSK LEMQKLNHEL EKSSTITKNL KNRLDAIISE NDWVTDANVV ENLVQQHPNI
NLDEGRDQLE VLQEKFQSMK RKVNVNIMSM IDNVEKKEAS LKQMVKTIEK DKSKIVNTIE
KLNGYKRETL NSTYQKVSTD FGQIFADLLP GSFAKLVPSN MMDVTKGLEV KVKLGEVWKE
SLVELSGGQR SLIALSLIMA LLQFKPAPMY ILDEVDAALD LSHTQNIGHL IKTRFKGSQF
IVVSLKEGMF TNANRLFRTR FQDGTSVVSA M
//
