ID A0A255EIM9_9ACTN Unreviewed; 1187 AA.
AC A0A255EIM9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN ECO:0000313|EMBL:OYN91364.1};
GN ORFNames=CGZ91_08025 {ECO:0000313|EMBL:OYN91364.1};
OS Parenemella sanctibonifatiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Parenemella.
OX NCBI_TaxID=2016505 {ECO:0000313|EMBL:OYN91364.1, ECO:0000313|Proteomes:UP000216300};
RN [1] {ECO:0000313|EMBL:OYN91364.1, ECO:0000313|Proteomes:UP000216300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 150081 {ECO:0000313|EMBL:OYN91364.1,
RC ECO:0000313|Proteomes:UP000216300};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC each terminus and a third globular domain forming a flexible hinge near
CC the middle of the molecule. These domains are separated by coiled-coil
CC structures. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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:OYN91364.1}.
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DR EMBL; NMVJ01000006; OYN91364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255EIM9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000216300; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03278; ABC_SMC_barmotin; 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 HAMAP; MF_01894; Smc_prok; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR InterPro; IPR011890; SMC_prok.
DR NCBIfam; TIGR02168; SMC_prok_B; 1.
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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01894};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01894};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Reference proteome {ECO:0000313|Proteomes:UP000216300}.
FT DOMAIN 510..622
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 339..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 390..480
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 816..892
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 967..1015
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1187 AA; 128293 MW; 1D09891B9D6BBFAD CRC64;
MHLKSLTLRG FKSFASATSF EFEPGITCIV GPNGSGKSNV VDALSWVMGE QGAKSLRGGK
MEDVIFAGTS GRAPLGRAEV VLTIDNSDNA LPIDYTEVTI SRTMFRNGGS EYAINGNPAR
LLDVQDLLSD SGIGREMHVI VGQGQLDSIL QATPEGRRGF VEEAAGVLKH RKRKEKALRK
LEATEGNLHR LEDLVQEIRR QLKPLGRQAE VARKAAVIQA EARDARARLL ADDLVQAQLS
LAADLADERE LERQQAAAAA AAQAAREGEA AAEQAVAEHR PALQQAADTW YALAGLTERA
SATAAIAQER IRHAKNQPTE ERRGKSPDEL LAEADQIGKE EAKLTEQVGQ RRETLTTASE
ERAAAEATAQ AEAKAYSAQL RAVADRREGL AKLKGQVGSA ESRAAAADEE VERLEASRAA
AQQRAQEATR RFQSLETKVA QFDSGESDLD EEWERAEEAV GAAEQELTKV RQQESELDRR
HASLSARLEG LRAGLERGQS VDVHAMDLAA EVLGPVTGRI TVTPGNEAAV AAALGPYAES
VAVGGVRDAA DIIGQLRAGE HGRTALLLAG VEATPAPIQE LPTGARPAID LVSADESVRG
AIAWLLASTV VVADLAAAGA LVAERPELTA VTADGDVLSG YAATGGSGSG PSLIELQAAV
DAAQAEQTTV EHERDRSRFD LSKAEEKLTR AQAAEQAALA KLHESDAEMA ALAEQLGQAS
QQARSATAEA DRLQASIEQA RRAGEEHRTK LAELTERLTH ASDEDVSDPD PAARDAAEAA
ERRARGQEME ARLALRTLEE RVRSLAGRAG ALRDAAAVER KARHEAQERR ARLKRDADRA
RAVAAGVAWL QERLTRSSAI AGERRATLQA QAQGAEEQLT AARQAVRDSN ARVSELADAA
HRDELARQQQ RLRVEALAER AMEELGLTAE VLAQEYGPDQ LVPVLTRPDG SALTDEDETP
EPVPFVRAEQ EKRFKRAERN LRELGKVNPL ALEEFDALKE RHQFLSEQLA DLTRTRQDLL
DIVTEVDRRV EQVFAEAYAD VEKAFNHVFA RLFPGGEGRL VLTEPGQWLT TGIEVEARPP
GKKIKRLSLL SGGERSLVAV AFLVSLFMAR PSPFYILDEV EAALDDVNLG RLLDIYTELR
ESSQLLVITH QKRTMEIADA LYGVTMRGDG VTTVISQKLP HDQTAVD
//
