ID M9MFK2_PSEA3 Unreviewed; 1487 AA.
AC M9MFK2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Structural maintenance of chromosome protein 3 {ECO:0000313|EMBL:GAC74402.1};
GN ORFNames=PANT_11c00042 {ECO:0000313|EMBL:GAC74402.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC74402.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; DF196777; GAC74402.1; -; Genomic_DNA.
DR STRING; 1151754.M9MFK2; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
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; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
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; PF00781; DAGK_cat; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR PROSITE; PS50146; DAGK; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976}.
FT DOMAIN 1095..1243
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT COILED 191..250
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 293..320
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 408..505
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 734..796
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 844..892
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1487 AA; 166586 MW; 92F5C3A79562DE4B CRC64;
MYIKTLTIQG FKSYRDQTAV EPFSPHHNVV VGRNGSGKSN FFSAIRFVLS DAYTSMSREE
RQSLLHDSSS STSATLSAFV EIVFDNSDNR FPTNGTEVVL RRTIGLKKDE YSIDRKSASK
ADVANLLESA GFSRSNPYYI VPQGRITHLT NAKDHERLGL LKEVAGTRVY EQRRAESIKI
MEDTTAKRSK IDDLLEYIEN RLRELDDEKE ELREYYERDR ERRCIEYSLH QRELTECAEL
LDKLEDERRR DLDASNVRRA EFNEREKRLA RLEAELAATG QSIEQRTLEK TQLELERRDV
AKHLAQIESL VEELEEVGEK RADRRTALDA QLVRIRADIQ SKQAQLDQLQ PTLAGVHTEA
EQLRAALQDT TARVSALYSK QGRSAQFRTQ QERDEYLRTQ MAELDHFLRS QQTRIDDTAR
ERTQATERRT AALRKVTEIE ENLESRKDTV QQLATEYAAK RDRRDELSEL RKDLWKEEES
LRSSLAFAAN ELSNAQRKLV GMMDKATVQG LSAVDKIAAS LGLQDNVKGP VYQLFSVDDK
YKTAVEVVAG ASLFHVVVDT DETASKLLEV MNREKSGRVT FMPLNRLHPK ETDFPATQDA
LLMVKKLQFE RALAPAMQQI FGRSIICPNL EIAAAYVRSH GVNAVTLDGD KVERKGALSG
GYQDPRRSRL DAVNDVRKWK AQSEADTAKQ AEVQRRLGEI EQEITALMSD MYALQHRRDE
ARNSRAPLTE ELQIGEREKR IKAVEAELDR LTQSIQDTQA GYDKTKAEQA EDARSIARQQ
KNVERYLSKR SRLVEQRDRC NQDIRDLGVL PEEAFEKYTN TSSDRLLKAL HKVNEALKKF
SHVNKKAVEQ YNSFTKQRDQ LLERRAELEQ SADSIQELID VLDQRKDEAI ERTFKQVSKY
FEEVFEKLVP AGRGRLIMQR RADLTTGAAE GDSDDEPSAG QVENYTGVAI KVSFNSKHDE
GLRIQQLSGG QKSLVALATV FAIQKCDPAP FYLFDEIDAN LDALYRTAVA NMIRELAHKA
QFITTTFRPE MVQVASKHYG VLFDANKVSS IRSISRDEAN EFVEAAATTE PSAAVLDPDC
ASRAELDFAP RRSFAEDKMV EVVLNAAAGS GLAESLYTTH LLPLLGPEQL RVHRTASSGD
GVRIGRTLID SHTSLHPSAP LDLILVGGDG TTHEVLNGIY LSGARGSVQV RLGVVPAGTA
NALFAALYPE HWTQDVQRSV AAAQSASELD SDVVDAMLRS VKTLAASIRS GEGCVDLPLM
HVDLGDRQVV AHLVTSHALH AAILHDADTA TMRARHTGIE RFKAAAALNA TRWTHATLTL
HPLPGGVQQY SPQTSSFSRI EEGKLVLEGP FLYLNAMLTD RLESAFIPAP LSSALALPRD
AVDVVVIRPT RDPELAGDPK DGETFAQTRL GPITAGMYAG GTHIDLTYDT TLPMVEYFRC
AGYDFTAGAG DKDRLVCTDG FVSEAERVRV ARWQPQEGAL SPPLIWR
//
