GenomeNet

Database: UniProt
Entry: A0A100Y1E8_9ACTN
LinkDB: A0A100Y1E8_9ACTN
Original site: A0A100Y1E8_9ACTN 
ID   A0A100Y1E8_9ACTN        Unreviewed;      1284 AA.
AC   A0A100Y1E8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=ATE80_26700 {ECO:0000313|EMBL:KUH35863.1};
OS   Streptomyces kanasensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=936756 {ECO:0000313|EMBL:KUH35863.1, ECO:0000313|Proteomes:UP000054011};
RN   [1] {ECO:0000313|EMBL:KUH35863.1, ECO:0000313|Proteomes:UP000054011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZX01 {ECO:0000313|EMBL:KUH35863.1,
RC   ECO:0000313|Proteomes:UP000054011};
RA   Zhang G., Han L., Feng J., Zhang X.;
RT   "Genome-wide analysis reveals the secondary metabolome in Streptomyces
RT   kanasensis ZX01.";
RL   Submitted (NOV-2015) 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       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KUH35863.1}.
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; LNSV01000106; KUH35863.1; -; Genomic_DNA.
DR   RefSeq; WP_058944839.1; NZ_LNSV01000106.1.
DR   STRING; 936756.ATE80_26700; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000054011; 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   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 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:UP000054011}.
FT   DOMAIN          512..688
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          571..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1004..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          167..201
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          241..275
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          330..480
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          796..830
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          876..910
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          1071..1133
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COMPBIAS        573..587
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1064
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   1284 AA;  137462 MW;  8F49542C322A0992 CRC64;
     MHLKALTLRG FKSFASATTL RFEPGITCVV GPNGSGKSNV VDALSWVMGE QGAKSLRGGK
     MEDVIFAGTT GRPPLGRAEV SLTIDNSDGA LPIDYAEVTI TRIMFRNGGS EYQINGDTCR
     LLDIQELLSD SGIGREMHVI VGQGQLDSVL HADPMGRRAF IEEAAGVLKH RKRKEKALRK
     LDAMRANLAR VQDLTDELRR QLKPLGRQAA VARRAAVIQA ELRDARLRLL ADDLVRLREA
     LDAEIADEAA LRERKERAEA DLKAAAARES ALEDEVRRLA PRLERAQHTW YELSRLAERV
     RGTVSLADAR VTSATARPVE ERRGRDPEEL EREAARVREQ EAELTAALEA ADRALEDTVA
     HRAELEQALA VEERRLRDAA RAIADRREGL ARLSGQAGAA RSRAAAAQAE IDRLTAARDE
     ARERAAVAHE EYEALRAEVD GLDAGDADLA AAHEAATREL ADAEAALTTT REALTSAERR
     RAATQARHEA LSLGLRRKDG TGALLDAAGR LTGLLGPAAE LLTVAPGHEV PIVAALGAAA
     DALAVTGPAT AAEAIRLLRK EDAGRAALLV AGATEPPPPP GPGVWEPSPV AGPDVREPAP
     LSGPGAQEPL SAGPDGRAAR QPPSAAPSAA VPPRAAAPAV DAARPGLPGG ALPAAGLVSG
     PDELMPALRR LLRDVVVVGT LEEAEALVYA RPALTAVTAD GDLLGAHFAQ GGSAGAPSLL
     EVQASVDEAA ADLAELAVRC RELAAAQEEA AGRRRACADR VEELGERRRA ADREKSAVAQ
     RLGGLAGQAR GAAGEAERAD AAVARAQEAV ERATEEAEEL AERLLVAQEA PTEDEPDTSV
     RDRLAADGAN ARQTEMEARL QARTHEERVK ALAGRADSLD RAARAEREAR ARAERERARL
     RHEAEVAAAV ASGARQLLAH VEVSLVRAEA ERSAAEEGRA VRERELAAAR ARGRELKAEL
     DKLTDSVHRG EVLGAEKRLR IEQLETRALE ELGVDPAVLV AEYGPDQPVP AAPPAPGEQR
     PAPGEDASAA HRREPAAAED ASAAHRREPA PGGDRPDDPG RAGDALRPFV RAEQEKRLKA
     AERAYQQLGK VNPLALEEFA ALEERHRFLS EQLEDLKRTR ADLLQVVKEV DERVQQVFAE
     AFRDTAREFE GVFSRLFPGG EGRLVLTDPG DLLGTGVEVE ARPPGKKVKR LSLLSGGERS
     LTAVAMLVAI FKARPSPFYV MDEVEAALDD TNLQRLIRIM RELQESSQLI VITHQKRTME
     VADALYGVSM QGDGVSKVVS QRLR
//
DBGET integrated database retrieval system