ID A0A1E4U3K0_PACTA Unreviewed; 1230 AA.
AC A0A1E4U3K0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=PACTADRAFT_64720 {ECO:0000313|EMBL:ODV98585.1};
OS Pachysolen tannophilus NRRL Y-2460.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Pachysolen.
OX NCBI_TaxID=669874 {ECO:0000313|EMBL:ODV98585.1, ECO:0000313|Proteomes:UP000094236};
RN [1] {ECO:0000313|Proteomes:UP000094236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2460 {ECO:0000313|Proteomes:UP000094236};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV454011; ODV98585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4U3K0; -.
DR STRING; 669874.A0A1E4U3K0; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000094236; 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:0007059; P:chromosome segregation; IEA:UniProt.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 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.
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|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000094236}.
FT DOMAIN 530..646
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 70..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..206
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 257..357
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 403..521
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 686..789
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 814..939
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1230 AA; 141311 MW; 7CF08D9AD146B5BB CRC64;
MGRLVGLELH NFKSYKGTTS IGFGTTFFTS IIGPNGSGKS NMMDAISFVL GIKTSNLRSH
NLKDLIYRGV RNRQDSEQQG DDDDDDHDDG NKKASRAYVM CIYEKSDGEI LKLKREITSN
GNSEYRINDR IVSAAEYSDI LKNENILNKT KNCLVFQGDV QKISAPLELT KIIEVVSGSS
KYIHEYNELK EQVENINEQT KKLFSTRRNI NAEFKQYKQE TVEAEIFEKK LIEKNDLIIL
QKIYQLYHHE KKYDLLLKTL QVKSTDLKKL KEMLKKEENN FKTANAQFSK DQIALNKIRS
KINKKVKTLE DTKRELIPFD TEKSIVLKKV SEYKKRIDEI TRNISNQQAI HDDIKQQLEI
VTDAKETFLN SINEGSGGSG NTNNNNEEIF NEYMEIKNKM FADNSLDDEL SELSNQKERT
EQKISSYNEQ RKLIEKMVAD LNNDIERLSQ SLSDSNSKLN DTLENLNTKK KELNDFKISK
EKNVQETWTI QKKLRTVLET INNINAEKKE TQREKKLREN TAKLRRMYPE GVIGLVHDLC
RPKQKKYELA VATTLGKHFD AIIVDTASTA TKCIEYLKDQ RAGVAAFIPL DSVESKPPQS
YLRNVHEQAR PVLDVVEFDF SLERAIQYCC SNTMVCDTID VARYIRWERN IDVKVVTLDG
SLIHKSGLMT GGRTEHDNRK FNKEDINSLT SVKLDLQKQL EELERKGPNS LLEKKLLDDI
DELELELQAS RSNRLQLERE LNDKKSHAKV QEESLTRNDE FLKKSESELN DLNTKVEQIE
GKINSMKADF YSDFCNKYGF DSIEDYEANN GSKLRKIMKE KSRFLKQIST LENKLNFESE
RLQESQSRLA KMKTEKQKND AVLESLNKKK SEVESNVDLL ESEVEVLNDE LKKMESISNN
KLKSNKALQE KVEDLRHDKD GVTNEIAILE ADMEEEISQK FEILKNCKIE NINIPLLSGS
LEDLPVDRAA VQEDLTHLLR SIAVNFNSLS STYKQNSELA DKIAEELSKI NDELDSLSPN
IKAVERLKEV EIKSKDVDGE FKRFKKDEME LMNHFNEVKE KRYALFNQAF EHISSHIDSI
YKELTRTNSV ISPLGGGGSA YLTLEDEDEP YLAGIKYHAM PPMKRFRDME LLSGGEKTIA
ALALLFAIHS FHPSPFFVLD EVDAALDNAN VNKLTNYIVN NSNEHLQFIV ISLKNSLFEK
SDALIGIFRD QEENSSKTVT LDLRSYPVEA
//