ID A0A1Q9LHS5_9PSEU Unreviewed; 1246 AA.
AC A0A1Q9LHS5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=BJP25_25710 {ECO:0000313|EMBL:OLR91564.1};
OS Actinokineospora bangkokensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=1193682 {ECO:0000313|EMBL:OLR91564.1, ECO:0000313|Proteomes:UP000186040};
RN [1] {ECO:0000313|EMBL:OLR91564.1, ECO:0000313|Proteomes:UP000186040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44EHW {ECO:0000313|EMBL:OLR91564.1,
RC ECO:0000313|Proteomes:UP000186040};
RA Greule A., Intra B., Flemming S., Rommel M.G., Panbangred W., Bechthold A.;
RT "The Draft Genome Sequence of Actinokineospora bangkokensis 44EHWT reveals
RT the biosynthetic pathway of antifungal compounds Thailandins with unusual
RT extender unit butylmalonyl-CoA.";
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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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:OLR91564.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MKQR01000021; OLR91564.1; -; Genomic_DNA.
DR RefSeq; WP_075976634.1; NZ_MKQR01000021.1.
DR AlphaFoldDB; A0A1Q9LHS5; -.
DR STRING; 1193682.BJP25_25710; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000186040; 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:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; 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:UP000186040}.
FT DOMAIN 512..625
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 805..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 239..275
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 348..375
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 411..487
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 883..924
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1004..1038
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 1246 AA; 135655 MW; 23D565D36083D959 CRC64;
MHLKSLTLKG FKSFASATTL KFEPGITCVV GPNGSGKSNV LDALRWVMGE GSAKGLRGGK
MEDVIFAGTA GRAPLGRAEV TLTIDNADGA LPIEYAEVSI TRRMFRDGAS EYEINGNGCR
LMDVQELLSD SGIGREMHVI VGQGQLSAIL ESKPEERRAF IEEAAGVLKH RKRKEKAIRK
LDAMQANLTR LTDLTAELRR QLKPLGKQAE IARRAQTVQA ELRDARLRLH ADDLVSQRAD
IAREEADEAT ARRKRAEVEQ ALELGQARQQ ELEEDLAADQ PLLAAAQETW YRLSALEERL
RGTVRLAVER ARHLSAATET RTGGRDPEEL EEEAEVTAMR EAELFEAVAE ARYALAESTE
RRAELERMVQ AAEKAHLAAV RAIADRREGL ARLSGQVEAL RSTVNATGAE VERLSSSLGE
ARRRAEVAAE ELAEAEAGTE VEDTDDAGLA ERHQRASAAA DDARARVDEL VRAERQAERD
IASWRARVDA LSMGLRRKDG TGALLAAADR LPGLLGSVAA LLTVRPGHEG ALAAALGPVA
DAVAVRDPHG AVEALRMLRA GDAGRAGLLV GGDGPVDRSG WPALPPSAHW AVDLVQAPDA
LLPAVHRALD RVAVVDDLPA ARALVDEHPA VRAVTAEGDL LGAHWAIGGS EKAQSAIEVQ
AAVDEAGTRL AAAERALEHA AAQLEGARAE QQARRDDVSA VKELMNEAKV RAARSSERLN
RLRQVLRSAE AEVERALTQR GKVEASREDA LAKLADLEER LLAVQEEHVE DEPDSAERDE
YSASLSAARQ EEMDARLSLR TAEERHRALQ GKADQLRRAA RAEREARERA ARAMAARRRA
ATVADAVVEG GELALERIAR SLARAAEERD VVAARRADRE RVLTDVRAKV RELSAELEKL
VDAVHRDEVL RAEQRLRLEQ LEQRITEQFG IGLDDLVAEY GPDVEVPPPA GELAEYEAAR
ERGEDVVRPP STRYDRDTQA RRAKRAERDL ATLGKVNPLA LEEFAALEER YRFLSTQLED
LKDTRRDLLT VVKEVDDKIL EVFTTAYADV AREFEVVFDV LFPGGEGRMV LTEPEDMLVT
GVDVEARPPG KKVKRLSLLS GGEKSLVAVA MLVAIFRARP SPFYVMDEVE AALDDTNMRR
LIGLLDQLRE SSQLIIITHQ KPTMEIADAL YGVSMRGDGI TQVISQRLNE TRKPPARITA
PPAPAQDAAP AEAPAAVDPV AGDAAPAEVE VAEPPTEEPA EAAPEV
//
