GenomeNet

Database: UniProt
Entry: A0A0E0CF27_9ORYZ
LinkDB: A0A0E0CF27_9ORYZ
Original site: A0A0E0CF27_9ORYZ 
ID   A0A0E0CF27_9ORYZ        Unreviewed;      2274 AA.
AC   A0A0E0CF27;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=SMC hinge domain-containing protein {ECO:0000259|SMART:SM00968};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI02G03320.5};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI02G03320.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI02G03320.5};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI02G03320.5}
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; OMERI02G03320.5; OMERI02G03320.5; OMERI02G03320.
DR   Gramene; OMERI02G03320.5; OMERI02G03320.5; OMERI02G03320.
DR   Proteomes; UP000008021; 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   GO; GO:0006302; P:double-strand break repair; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
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; PF13304; AAA_21; 1.
DR   Pfam; PF13476; AAA_23; 1.
DR   Pfam; PF06470; SMC_hinge; 2.
DR   Pfam; PF02463; SMC_N; 1.
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:UP000008021}.
FT   DOMAIN          482..595
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   DOMAIN          1671..1755
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          323..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1066
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          184..271
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          380..456
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          749..776
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          870..900
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1335..1401
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1562..1645
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1791..1872
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1951..2009
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        323..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2274 AA;  260997 MW;  0AA217B203B00BF4 CRC64;
     MYIKKVVVEG FKSYREEIST EPFSPKVNVV VGANGSGKSN FFHAIRFVLS DMFQNLRSED
     RGALLHEGAD ISVLSAFVEI VFDNSDNRIP VEKKVVRLRR TVASKKDEYY LDGKHVSKTE
     VMNLLENAGF SHSNPYYVFQ QGKIAALTLM KDSERLELLK EIGGTRGTSC KWTLIHDLLA
     ANKRKQIDQV VHYLEERLRE LDEEKEEMKK YQQLDKQRRS LEYTILDHEL NDTRNELALM
     DDNRRKISER MSHADNEVVG AREKIRSFEK EIKFSTKGIN DNKAQKEDVE KKCTEVLKVV
     AQIELDLRDI KDRILNEKLA KNEAARDSQS VRMESERSKS ELAETSKGRA TQFANKAARD
     KWLQKEIDDL ERGGLLQEEI QKLKDKINNL NSYFEFYESE SNKLESTLAK KHSDYNDLRK
     QRDKLQEERK SFWMEEANVT AEKDRLEKDL VNAKEKLGNA TPGEIIRVLN CVSRITMEHG
     ITGVVGPILE LIDCDEKLFT AVEVTARNSL FHVVVENDDI STKIIQVLTR EKGGRVTFIP
     LNRVKVPDVS YPRSDDFVPL LERLECSKAN HRRAFEQVFG RTVICKDLET ATKVARDNGL
     NCITLDGDQV ARKGHMTGGF HDYRCSKLKF VKTIKNNMKA IEDKEEHLKN VERNLSDILS
     PCLHDADKKM TDLVTKQQQM DAESDYAKSE LEHFKVGIAS TMKQIGSLEK ALGKKEKSLD
     NIQNQIVQIQ SGIAMKYNEM GTEIIDQLTS EERDLLLQLN TELTELKEKF IETRKEELEA
     NLSTNLMRRQ KEFEAVTSSA DSKTLSLEAE SKEQELNSSK SSLDDLTAML KGIDALIDFL
     FPSALCLMLP KGSSVKLTQT IFLVANVDAI NNFTIKMEEL KRQRDNLKTL EANLDQTVRD
     GAKDLEQLMS SRSMHLAKQE ECMKKIRDLG PLPTDAFETY RQKNKKQLQK MLYNCNEQLQ
     QFRHVKKKAL DSVNFTEQRE QLERRRAELD AGDQKIRELM SILDQRKDES IKRTFKGVAR
     HFREVFSELV QGGHGHLVMM KKKDGDAANE DIDNDEDGPR EPDPEDRMEK YIGVKVKVSF
     TGQGETQSMK QLSGGQKTVV ALTLIFAIQR CDPAPFYLFD EIDAALDTQY RTAVGNMIRH
     LADMADTQFI ATTFRPEIVK VADKIYGVTY KNRVVIEGFK SYREEISTEP FSPKVNVVVG
     ANGSGKSNFF HAIRFVLSDM FQNLRSEDRG ALLHEGAGHS VVSAFVEIVF DNSDNRIPVD
     KEEVRLRRTV ASKKDEYYLD GKHVSKTEVM NLLESAGFSR SNPYYVVQQG KIASLTLMKD
     SERLDLLKEI GANKRKQIDQ VVHYLEERLR ELDEEKEELK KYQQLDKQRR SLEYTILDHE
     LNEARNELAS MDDNRRKISE RMSHADNEVV DVREKVKTFD KEIKYSTKGI NDTKAQKEGV
     EKKRTEALKV VAQIELDLRD IKDRILNEKR AKDEAAKDLQ SVRMESEKSK SELAEISKVH
     QAKLKEEEEI SKSIMDREKR LSILYQKQGR ATQFTNKAAR DKWLQKEIDD LERVLLSNRK
     QEGLLQEEIQ KLKDEINNLN SYIESRKSES SKLESALAKK HNDYNDLRKQ RDELQEERKS
     FWKEEADVTA EIDRLKDDLV KAQKSLDHAT PGDIRRGLNS VSRIIRDHGI TGVFGPVLEL
     VDCEEKFFTA VEVTAGNSLF HVVVENDDIS TRIIQVLTRE KGGRVTFIPL NRVKVPDVFG
     RTVICRDLET ATKVARGNGL DCITLDGDQV ARKGGMTGGF YDSRRSKLKF VKIIRDNKTA
     IEKKAAHLEN QQMDAERDHA KSELEQFKVD IASAMKQMAS LDKALGKKEK SLDNIRNQIE
     QIQSGIAMKN DEMGTELIDQ LTSEERDLLS RLNPEITELK EKFLLCKNSR IEIETRKEEL
     ETNLSTNLMR RQKELEAIIS SADSKTLPLE AESKEQELKS SKRSLDELTA MLKANVDAIN
     NFTRKMEELK RQRDDLKALE ANLEQTVQDG AKDLEQLMSS RSMHLAKQEE CMKKIRDLGS
     LPADAFETYK RKNKKQLQKM LYDCNEQLQQ FSHVNKKALD QYVNFTEQRE QLQRRRAELD
     AGDQKIRELI SVLDQRKDES IERTFKGVAR HFREVFSELV QGGHGHLVMM RKKVSFTGKG
     ETQSMKQLSG GQKTVVALTL IFAIQRCDPA PFYLFDEIDA ALDPQYRTAV GNMIRRLADM
     ADTQFIATTF RPEIAKVADK IYGVTHKNRV SYINVVSKEQ ALDFIEHDQT HNAS
//
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