ID A0A1I2K5U1_9ACTN Unreviewed; 1275 AA.
AC A0A1I2K5U1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN05216251_121102 {ECO:0000313|EMBL:SFF61803.1};
OS Actinacidiphila alni.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=380248 {ECO:0000313|EMBL:SFF61803.1, ECO:0000313|Proteomes:UP000199323};
RN [1] {ECO:0000313|EMBL:SFF61803.1, ECO:0000313|Proteomes:UP000199323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFF61803.1,
RC ECO:0000313|Proteomes:UP000199323};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FONG01000021; SFF61803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2K5U1; -.
DR STRING; 380248.SAMN05216251_121102; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000199323; 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; 2.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.1060.20; -; 2.
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 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; 1.
DR PIRSF; PIRSF005719; SMC; 2.
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:UP000199323}.
FT DOMAIN 510..707
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 308..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..194
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 738..849
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 937..969
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1083..1117
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 1040..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1275 AA; 137198 MW; 8A86BE7FC93C4E73 CRC64;
MHLKSLTLRG FKSFASATTL RFEPGITCVV GPNGSGKSNV VDALSWVMGE QGAKSLRGGK
MEDVIFAGTT GRPPLGRAEV SLTIDNSDGV LPIEYAEVTI TRIMFRNGGS EYQLNGDTCR
LLDIQELLSD SGIGREMHVI VGQGQLDSVL HADPMGRRAF IEEAAGVLKH RKRKEKALRK
LDAMQANLAR VTDLTGELRR QLKPLGRQAQ VARRAAVIQA DLRDARLRLL ADDLVTLREA
LRAEVADEAA LKERKDAVEA DLAVAVQREA RLEEQVRALT PRLNDAQATW YALSQLAERV
RGTIGLAEQR HRHATSQPAE ERRGRDPEDM EREAARIREQ EAELSEALDA AQRALDDTVD
HRAELERRLA EEETRLRAAA RAIADRREGL ARLNAQVNAA RSKAAAAEAE IGRLAAARDE
ARDRAESAQG EYEELRAQVE GLDADDSELE ERFEAARREQ AAAEEAFSAA REAATAAERR
RAAVAARRDA LAPSLRRKDG TGALLGADLG GVLGPAAALL RVTPGYEIPL AAALGAAADA
VAVTGPGAAA EALRLLRKGD AGRAALLLAA PADSPEPVAA HDQARTGTAA DTVTEAGPAT
EAGGQAVPGQ PSAGGHDGAA PRLPYDGRPA AAGGGSHDPA VPGQAGPAGG DAHAGVPGPR
PESAGLPGEA RWAADLVTAG PELRAAVARL LDRVVVVESL EEAEALVVRR PELTAVTAEG
DVLSAHLAQG GSAKAPSLLE VQAQVDEATA ELEGLDARCA ELAAEQADAK ERRAAAAREV
DALTQRRRAA EKEKSSVAQQ LGRFGGQARA AAGEAERAAA AVGRSEEALA AAREELEELS
YRLSEAQEAP GEEEPDTSVR DRLSADGANA RQTEMEARLQ VRTHEERVKG LAGRADGLDR
AARAERETRS RAERRRTRLA YEASVAAAVR DGARGLLEYV QVSLARAEAE RAAAERARAE
REAELGQERR RGRELKSELD RLTGDVHKGE VLGAEKRLRI EQLEAKALEE HGMEPAGLVA
EYGPDQLVPP SPPAEGEILP EDPEDPRNQP RPYRRPEQEK RLKAAEKAYA QLGKVNPLAL
EEFAALEERH KFLTEQLEDL RKTRADLLQV VKDVDERVEQ VFTAAFHDTA REFEGVFSRL
FPGGEGRLLL TDPDNMLTTG VEVEARPPGK KVKRLSLLSG GERSLTAVAM LVSIFKARPS
PFYVMDEVEA ALDDTNLQRL IRIMEELQES SQLIVITHQK RTMEVADALY GVSMQGDGVS
KVISQRLRNG KQQPA
//
