ID A0A0A1CZG1_9MICC Unreviewed; 1219 AA.
AC A0A0A1CZG1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=ART_1187 {ECO:0000313|EMBL:AIY00786.1};
OS Arthrobacter sp. PAMC 25486.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIY00786.1, ECO:0000313|Proteomes:UP000030301};
RN [1] {ECO:0000313|EMBL:AIY00786.1, ECO:0000313|Proteomes:UP000030301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC25486 {ECO:0000313|EMBL:AIY00786.1,
RC ECO:0000313|Proteomes:UP000030301};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-I.;
RT "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from the
RT Arctic.";
RL Submitted (APR-2014) 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}.
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DR EMBL; CP007595; AIY00786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1CZG1; -.
DR SMR; A0A0A1CZG1; -.
DR STRING; 1494608.ART_1187; -.
DR KEGG; arm:ART_1187; -.
DR HOGENOM; CLU_001042_2_0_11; -.
DR Proteomes; UP000030301; Chromosome.
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 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:UP000030301}.
FT DOMAIN 503..646
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 571..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 323..403
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 761..788
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1000..1062
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1219 AA; 129369 MW; 8558057B730E662A CRC64;
MRGFKSFASA TTFDFEPGVT AVVGPNGSGK SNVVDALAWV MGEQGAKTLR GGKMEDVIFA
GTTGRPALGR AHVALTIDNS DGALPIDYAE VTISRTLFRA GGSEYAINGT SCRLLDIQEL
LSDSGLGREM HVIVGQGQLD KVLHATPEDR RGFIEEAAGI LKHRRRKEKT LRKLEAMGAN
LARLSDLTGE IRRQLAPLGK QAAVARRAQS VQFDVRDARA RLLADDIVTL TTAVEQDAAA
ELALKNRREL VEAQLQSGRA RQAELEQAGA AATPVLNAAR DNWYQLSATR EQLKALGVLA
AERQRHLGAT DAVPDPSRDP DKLAQQAVRL RAEEAELDLA LEEKRFGLET AMEIKEDAEA
AVRAEEQRVR DQLRATADRR EGLARLAGKV ASARSRVESA EAEIGRLHHS RAAGAERHST
AAEEFAALES QVAGVEAGEE RLDSDYEEAA AALGEVDARI DSAAAEQLAA ERERDSLTAR
RDALATGLLR QDAGAALLEA RPHGVLASMA QLIHVVPSHE TAIAAALNAA AEGVAVTDFG
AALAALDLVK THDSGRVTLI LADGGAGAAD GAGGSDHAGG SPAPATEHAA AQAALQQAAA
AAAGSVAGAA VGRSQVSGPD SLGHTLDALL AGVVLVPDVA AAQDILAIDA SLTAVTAAGD
VLTKWWVQGG SAMAPSLLEL QAAVDETEAA LAQAVARGEQ SRFALAGLQG RRGALAAAET
DALAALHESD ARLAAVAERL GALGATLRSA AGESERHAQA VQAATANLGR EQQALEEVAR
RLAKAQEAPA DVEPSMEERD TLGASAAAAR AVELETRLSL RSTEEALNTV RTRAAALERA
AATEKLAREQ AAQRARRRLF QARKAAAVAM AAERIAAFVA DSIELAEHVR DEAEEQRAAR
EVDLMAVRGS TAGAEKELAL LTDTVHKDEL ARAAQRLRIE TLENKSIEEL GLSVDHLIRE
YGPDTLVPLG PGEVTDRWAA LRVEVDETGA EIRESTPFVR AEQEKRLKRA ERDLAALGKV
NPLALEEFAA LEERHQFLSS QLEDLKASRK DLMDIIKEVD ARVEEVFTAA YEDTAAQFER
VFARLFPGGE GKLVLTDPSD MLTTGIEVEA RPAGKKIKRL SLLSGGERSL TAVALLVAIF
KARPSPFYVM DEVEAALDDT NLGRLLTIFE ELRESSQLII ITHQKRTMEV ADALYGVSMR
GDGVSTVISQ RMDRADSPA
//
