ID K0KT59_WICCF Unreviewed; 1207 AA.
AC K0KT59;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=SMC3 {ECO:0000313|EMBL:CCH46336.1};
GN ORFNames=BN7_5929 {ECO:0000313|EMBL:CCH46336.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH46336.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH46336.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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:CCH46336.1}.
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DR EMBL; CAIF01000241; CCH46336.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KT59; -.
DR STRING; 1206466.K0KT59; -.
DR eggNOG; KOG0964; Eukaryota.
DR HOGENOM; CLU_001042_5_0_1; -.
DR InParanoid; K0KT59; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
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:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProt.
DR CDD; cd03272; ABC_SMC3_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; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR041741; SMC3_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; 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; 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:UP000009328}.
FT DOMAIN 523..635
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 164..373
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 412..504
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 702..808
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 843..912
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1207 AA; 138827 MW; 86ABA3B58F0C5DBA CRC64;
MHIKKIVIQG FKTFKNTTVI DNLSPSHNVV VGRNGSGKSN FFAAIRFVLS DQYTRMSKEE
RQGLIHEGSG TVLSAYVEIV FDNSEGRFPT GKDEVVIRRT IGLKKDDYSL DYKSSTRQDI
MQLLESAGFS KSNPYYIVPQ GRITSLTNAK DVERLNLLKE VAGAKVFENK LKESTKEMSK
TKNQRDKIDE MLEFIEERLS DLDSEKEELK NFQNLEKDKK IYEFVLYDRE LNEISNSIEQ
IESEYQNGVD ESQNFVLELE KRETLISEIE SDIDSAKQSL KLLNIDRNEH SENFEEVSKK
IYDINANLVE IRNNLNKYNK TQTNIEKQIK IAKEKIKSHE SKVSEKQPYV SKLKNQEAQL
DTQLSNLKTK QNLLYSKQNR FSKFNSVEER NHWLNNQIQD LSGRKQGSIN QINSGTQRLT
ELSNKIQNLE ASITQLQDSI NGDSAQEETN KIENQLMELR RQLSMENDSR KTLWKDEARF
KAILESLEDE LRKATRQVSQ TMDRQQSQGL EAVKRITSRL GLTGVYGPLG ELIEVNDKYR
TAVEVVAGNS LFHVVVDNDE TASTLMDELV RERAGRITFV PLNRVRPQDV TYPDSNDCVP
LIKKIGFDPE IENAVKQTFG KSIVAINLER GYELSRQYKL NAITLDGDKA DKKGVLTGGY
HDFKKSRLES MKIKQDKFKE LRDEEKGLFQ VKTEITRKDQ LILKINDNMK KVSNELENLH
SSKQPLKSKL SNLLNEKFKA NDEIKLLKDQ LVQLENSKTN LTTKIEQLQN ELNSNFEEGL
SSQEKIEISN LSKQISELEI RYNKVADELL THDTELNNLI VELEEELVPR YNELVKEQEK
TNQGSLDNDL QNLSQDLENL EEHKASVYEE LKKVERHIKD TETHLKKKEE ALDKANDQQR
KLIRNVENFQ KSSEKYLSKK SLLSSRREET QRKIRELGAL PEEAFQEFEN LSSGQLLQKL
NKVTKNLEKF SHVNKKALEQ YLSFTKQRDG LVDRRKELTK SESSIDDLIN VLETRKDEAI
QRTFQQVSAS FTEVFEKLVP RGIGKLIMQQ RDKNAPSSQA VDEDGDVEID EDEENGDSII
DNYSGISIQV SFNSKEDEQQ RIEQLSGGQK SLCAIALILA IQKSDPAPFY LFDEIDANLD
TQYRTAVANM IHELSQNAQF ICTTFRPEML QVASKFFGVM FNNKISTVSE INRSDALGFV
EGQQQRA
//
