ID A0A1M5GWL2_STRHI Unreviewed; 1200 AA.
AC A0A1M5GWL2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN05444320_106293 {ECO:0000313|EMBL:SHG07995.1};
OS Streptoalloteichus hindustanus.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Streptoalloteichus.
OX NCBI_TaxID=2017 {ECO:0000313|EMBL:SHG07995.1, ECO:0000313|Proteomes:UP000184501};
RN [1] {ECO:0000313|EMBL:SHG07995.1, ECO:0000313|Proteomes:UP000184501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44523 {ECO:0000313|EMBL:SHG07995.1,
RC ECO:0000313|Proteomes:UP000184501};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQVN01000006; SHG07995.1; -; Genomic_DNA.
DR RefSeq; WP_073485516.1; NZ_FQVN01000006.1.
DR AlphaFoldDB; A0A1M5GWL2; -.
DR STRING; 2017.SAMN05444320_106293; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000184501; 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; 1.20.1060.20; -; 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:UP000184501}.
FT DOMAIN 512..633
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 424..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..228
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 348..382
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1013..1047
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 1200 AA; 130002 MW; E2C05FBFBF64280B CRC64;
MHLKSLTLKG FKSFASSTTL RFEPGITCVV GPNGSGKSNV LDALAWVMGE QGAKALRGGK
MEDVIFAGTA GRQPLGRAEV TLTVDNSDGA LPIDYTEVSI TRRMFRDGAS EYEINGNSCR
LLDIQELLSD SGIGREMHVI VGQGQLADIL QAKPEERRAF VEEAAGVLKH RKRKEKALRK
LDAMQANLTR LTDLTAELRR QLKPLGKQAE IARRAQQVQA ELRDARLRLL ADDLVTARAD
LARDEADEAA ARARRGEVER ALQLGQAEQN ALEEQVAADA PRLAGAQDTW YRLSALEERL
RGTVRLAAER ARHLSAEVEQ PRGGRDPDQL DAEAELAAGQ EAELAEGVAV AREALAEAAE
TRAELEESLK AAERAHLAAV RAVADRREGL ARLSGQVDAL RSKTEAGAEE IERMSAALAE
AADRAERARL EHEEASAAST AEDEGGLDLD ERRAAADEAH RQARARVEEL VAAERAAEKE
IASWRARVDA LSLGLTRRDG AGALLAAGAR LPGLLGSVAA LLTVEPGAEV ALAAALGAIA
DAVAVADPDA ALAALELLKA DDAGRAGLLV GADTAGVDAA ADSARRAGWP ALPAGARWAV
DLVRAPRELR PALGRALDRL AVVDDLAAAR ALVAAHDGVR AVTVDGDVLG ADWAVGGSSR
SQSVIEVQAA VDEAEEALTA AERRCEQASA ALTGARAEEK ERRAAVAAAQ EAVNDARVRR
ARGAERLARL DQAARSAENE VERLTRQRVR VEQAREEALA RLAELEERLA AAHSEQSAED
EPDTEERDEI ASRLAVARQE EVEARLALRT AEERHRSLQG RADQLRRAAR AEREARERAE
RARRTRARGA AVAHAVVAGG ETALGRIALS LVRATEERDE AQRRRTEHEE ALAKVRARVR
ELSTELEKLT DAVHRDEVLR AEQRLRIEQL ETRIGDDHGI GLDDLVAEYG PTVPVPPSPG
ELAEYEAAKE RGEQVTAPQP VPYDRATQER RAKRAERDLS LLGKVNPLAL EEFAALEERY
KFLSTQLEDL KASRRDLLTV VKEVDEKILE LFGSAFEDVA REFEVVFRTL FPGGEGRLLL
TDPDDLLTTG VDVEARPPGK KVKRLSLLSG GEKSLTAVAM LVAIFRARPS PFYVMDEVEA
ALDDTNLRRL IGLLEELRET SQLIIITHQK PTMEIADALY GVSMRGDGIS AVISQRLRGR
//
