ID A0A0D9VBW3_9ORYZ Unreviewed; 2020 AA.
AC A0A0D9VBW3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=SMC hinge domain-containing protein {ECO:0000259|SMART:SM00968};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR02G02500.2, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR02G02500.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR02G02500.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR02G02500.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EnsemblPlants; LPERR02G02500.2; LPERR02G02500.2; LPERR02G02500.
DR Gramene; LPERR02G02500.2; LPERR02G02500.2; LPERR02G02500.
DR HOGENOM; CLU_230386_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 2.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR CDD; cd03272; ABC_SMC3_euk; 2.
DR Gene3D; 1.20.1060.20; -; 2.
DR Gene3D; 3.30.70.1620; -; 2.
DR Gene3D; 6.10.250.3110; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; PF06470; SMC_hinge; 2.
DR Pfam; PF02463; SMC_N; 2.
DR SMART; SM00968; SMC_hinge; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF75553; Smc hinge domain; 2.
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:UP000032180}.
FT DOMAIN 546..658
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT DOMAIN 1698..1800
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1057..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 210..276
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 472..520
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 713..775
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 854..912
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1362..1392
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1443..1484
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1582..1672
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1877..1937
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1967..2015
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2020 AA; 231487 MW; 63A9119CE58EA1E4 CRC64;
MTCVSYSGLL AVPCRVSPLL TLLLSPAGLP PFPFLGYYCS STRAAECRLR PALSIFAREE
ISTEPFSPKV NVVVGANGSG KSNFFHAIRF VLSDMFQNLR SEDRGALLHE GAGHSVVSAF
VEIVFDNSDN RIPVDKDEVR LRRTVASKKD EYYLDGKHVS KTEVMNLLES AGFSRSNPYY
VVQQGKIASL TLMKDSERLD LLKEIGANKR KQIDQVVHYL EERLRELDEE KEELKKYQQL
DKQRRSLEYT ILDHELNDAR NELASMDDNR RQISERMSHA DNEVVDVREK IKSFDKEIKY
STKGINDTKA QKEGVEKKRT EALKGVAQIE LDLRDIKDRI LNEKRAKDEA ARDLQSVRME
SDKSKSELAE IIKVHQAKLK EEEEISKSIM DREKRLSILY QKQGRATQFA NKAARDKWLQ
KEIDDLERVL LSNRKQEGLL QEEIQKLKDE INNMNSYIES RKGESSKLES ALAKRHNDYN
DLRKQRDELQ EERKSFWKEE ADVNAEIDRL RDDLVKAQKS LDHATPGDIR RGLNSVSRII
KDHGITGVFG PVLELVDCEE KFFTAVEVTA GNSLFHVVVE NDDISTKIIQ VLTREKGGRV
TFIPLNRVKV PDVSCPQSPD FVPLLKKLKY RADHRRAFEQ VFGRTVICRD LETATKVARG
NGLDCITLDG DQVARKGGMT GGFYDSRRSK LKFVKIIRDN KTAIEKKAAH LDNQQMDAER
DHAKSELEQY KADIASAMKQ IASLEKALGK KEKSLDNIRN QIEQIQSGIA MKNDEMGTEL
IDQLTSEERD LLSRLNPEIT ELKEKFLLCK NSRIEIETRK EELETNLSTN LMRRQKELEA
IISSADSKTL PLEAESKEQE LKSSKRSLDE LTAMLKANVD AINNFTRKME ELKRQRDDLK
TLEANLEQTV QDGAKDLEQL MSSRSMHLAK QDECMKKIRD LGSLPADAFE TYKRKNKKQL
QKMLYDCNEQ LQQFSHVNKK ALDQYVNFTE QREQLQRRRA ELDAGDQKIR ELISVLDQRK
DESIERTFKG VARHFREVFS ELVQGGHGHL VMMRKKDGDA ADDDNDEDGP REPDPEGRIE
KYIGVKVSFT GKGETQSMKQ LSGGQKTVVA LTLIFAIQRC DPAPFYLFDE IDAALDPQYR
TAVGNMIRRL ADMADTQFIA TTFRPEIAKV ADKIYGVTHK NRADANEEIV EQDDASHLLD
VVIEGFKSYR EEISTQPFSP KVNVVVGANG SGKSNFFHAI RFVLNDMFQN LHNEDRAVLL
HEGDGPSVFS AFVEIVFDNS DYRIPVDKKE VRLCRTVAAK KDEYYLDGKR VSKTEVMNLL
ESAGFSHSNP YYIVQQGKIA SLTLMKDSER LDLLKEIGAN KRKQIDQVVH YLEERLRELD
EEKVKLKKYE QLDKQRRSLE YTILDHEPND ARKELASMDD SRRKISERIS HADNEAVDVR
EKIKSIDKEI KFLAKRINDT KAQNEGAEKE RTEALNVVAQ IELDLKDIND RILNEKWAKD
EAARDLQSVR MESEKSKSEL AVISKVHQAK LKEEEEVSKS IMDCEKQLSI LYQKQDWADQ
FANKATRDKW LRKEIGGREC LLLLNKKQEA LLQEEIQKLK DETNNMNSYI ESHKSESNKL
ESALVKKHND YNGLRKQRNE LQEERKSLWK EEADVTAEKH RLKEDLVKAQ KKLDHAIPGD
IRRVLNSAIR IIRDHGIKGV FGPLLELVNC EDNLFHVVVE NDDTATKILH ILIQQGGGVV
TFIALNRVKV PDVRVPQSPD IVFVPLLNKL EYRADHRLAF ELVFGRTVIC KDLETATKVA
RANGLDCITL DGDQVARKGD MRGGFYDSTC SKLKIVKIIR DNTMAIQIKE AHLKDVGSKL
RDMTDLITKQ QQMGSKRDRA KLELEQFNKN IASAMKLMGS LERALGTKLT SEEQDLLSRL
NPEITELKER LKQEELETNL SINLMMHQKE LEAIISSTDS KTLPLEAESK EQELESSKMN
LDNLTAMLED NMNIINNFTR KMEELKRKRD DLKTLQASLE
//
