ID A0A200PW19_9MAGN Unreviewed; 1241 AA.
AC A0A200PW19;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=BVC80_9099g200 {ECO:0000313|EMBL:OVA02394.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA02394.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA02394.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA02394.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
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}.
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:OVA02394.1}.
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DR EMBL; MVGT01003956; OVA02394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200PW19; -.
DR STRING; 56857.A0A200PW19; -.
DR InParanoid; A0A200PW19; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000195402; 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:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_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; 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; 2.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402}.
FT DOMAIN 517..650
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1177..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 163..271
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 307..362
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 405..502
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 740..788
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 846..957
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1018..1059
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1179..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 143766 MW; C110AA6CF1E7C585 CRC64;
MPSLIYPGKI LRLELENFKS YKGLQVIGPF YDFTAIIGPN GAGKSNLMDA ISFVLGVRSV
QLRGAQLKDL IYAFDDKEKE QKGRRAFVRL VYQMGNGTEL QFTRTITSSG GSEYRLDGKI
VTWDEYNSKL KSLGILVKAR NFLVFQGDVE SIASKNPKEL TGLLEQISGS DDLKREYEDL
EEQKARAEQK SALVYQSKRT IVMERKQKKE QKEEAEKHIR LQDQLKALKK DHFLWQLLNL
ERDMDKTNVD LEAEKKSRED VLKEQEKYEL EESEKKKEQA GYLKEITLCE KRIADKKSRL
DKKQPELLKL KEEVHRITAK IKNKKKELDK KREERRKHGE EIKRLENDLR DVTEKLNDLH
EKGQDGSGKL QLADNQVLEY HRIKEDAGMK TAKLRDEKEV QDRQQQADVE AQNNLEENLQ
QLRNREQELE SQEEQMQTRL KKIVDALGKH KEERTRVKKE LSEMQDKHRK SRNNYESLKV
KISELENQLR ELKADRHENE RDARLSQAVE TLKRLFPGVR GRITDLCRPT QKKYNLAVTV
AMGRFMDAVV VEDEHTGKEC IKYLKEQRLP PQTFIPLQSV RVKPVIEKLR TLGGTAKLIF
DVIQYPFLNS LILVLNLAYC TFDPSLERAI LYAVGNTLVC DKLEEAKDLS WSGERYKVVT
VDGILLTKSG TMTGGISGGM EARSKQWDDK KIEGLKKSKE RYESEMEELG SIREMQMKES
EASGKISGLE KKIQYSEIEK INIQDKLSKL KQEKLNIKEE ISSTEPELQK LKSQTTKRMT
EIKKLERRIN EIVDRIYKDF SESVGVQNIR EYEENQLKGA QQMAERRISL SHQMSKLKSQ
LEYEQKRDME SRITDLESYL ESLDKELKQV QKKDADTKQV TERATNEMDQ LNEEVQEWKS
KSDECEKSMQ ELKKRRSSIA TSIGKLNRQI NLKETQIEQL QSRKQEILEK CELEQIKLPI
VNDPMETGSS TPSPVFDYNQ LNRSHLQEMR PSEREKLDLE FKQKMDTLIS EIERTAPNLK
ALDQYEALQE KEKAVTEEFE AARREEKEIT DKYNAVKQRR YELFMEAFNH ISNNIDKIYK
QLTKSGTHPL GGTAYLNLEN EDDPFLHGIK YTAMPPTKRF RDMEQLSGGE KTVAALALLF
SIHSYRPSPF FILDEVDAAL DNLNVAKVAG FIRSKSCESS VRGGGNNNQE DSEGGGSGFQ
SIVISLKDSF YDKAEALVGV YRDSERSCSR TLTFDLTKYR E
//
