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Database: UniProt
Entry: A0A1C1A0D2_9BACL
LinkDB: A0A1C1A0D2_9BACL
Original site: A0A1C1A0D2_9BACL 
ID   A0A1C1A0D2_9BACL        Unreviewed;      1191 AA.
AC   A0A1C1A0D2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-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=A8709_19935 {ECO:0000313|EMBL:OCT13846.1};
OS   Paenibacillus pectinilyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=512399 {ECO:0000313|EMBL:OCT13846.1, ECO:0000313|Proteomes:UP000093309};
RN   [1] {ECO:0000313|Proteomes:UP000093309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC13222 {ECO:0000313|Proteomes:UP000093309};
RA   Zhang J., Zhang X.;
RT   "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL   Submitted (MAY-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}.
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:OCT13846.1}.
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DR   EMBL; LYPC01000022; OCT13846.1; -; Genomic_DNA.
DR   RefSeq; WP_065853944.1; NZ_LYPC01000022.1.
DR   AlphaFoldDB; A0A1C1A0D2; -.
DR   STRING; 512399.A8709_19935; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000093309; 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|HAMAP-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|HAMAP-Rule:MF_01894};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093309}.
FT   DOMAIN          521..640
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          742..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          167..201
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          269..296
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          386..497
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          892..947
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COMPBIAS        748..771
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   1191 AA;  135329 MW;  671B196B6D5B103C CRC64;
     MFLKRIELSG FKSFADRTEL EFVRGITAVV GPNGSGKSNI SDGIRWVLGE QSAKSLRGGK
     MEDVIFAGSD ARRAVNYGEV SLTLDNTSQS LPLDFNEVTV TRRVHRNGDS EYLINKQPCR
     LKDITELFMD TGIGKEAYSI IGQGRIEEIL STKSEDRRGI FEEASGIVKY KSRKREAEKK
     LNDTEQNLLR IHDLVSELED QVEPLREQSE KAIRFKELKE TLKSSEISMY VHQIDQIYIA
     WNDATQLLEK LTKEQTELST IVNQHDAHLE KHRWETRRLE EELETLQESL LGLSEEFEKC
     EGHGEVLKER KKNYVTNHQQ LSTTIAMQEQ RKLDKEADLS EQRDKIISIG AQLFEFQAKL
     TAEEQRLQGV SGGISSSPED QLKGELLETL NRMAQSRNEI RYAEQQIESI GRRLERLDEE
     RQKWADQRES ITRRKQELSA KLEETVADIE KARLQYVQLT QALKSKQGLL DEAQAMVRKW
     EQKLDALISR RDTMKEMAND YDGFQQGVKE VLKAKTRKDL RGIRGAVAEL VKVPANVEIA
     IETALGGALQ NIIVETEADG REAIAFLKRR QMGRATFLPM NVIRGRSISD HESHTLKASK
     GFVGIAVDLV SFDATYTNIF SSLLGNVVVA ESLEDANHIA AKAQYRYRVV TLEGDVVNPG
     GSMTGGSLQK KSTNLLGRQR QIEELDAEIA SSEGQLSGLR SQSSSLKREI TDEMLAVEQL
     RQLGEQQRIT EQQIRAELNP LESESRTVEA QLKIDSQDRG ALQEERTEFG RKKVESEAAL
     AQLQEEEASL QQAIRDAESS RKASESEKEE LQSQLTDLKV KVASTSQEKQ SLQDQQRRLQ
     QDLSDVEREI ELNRGLLSQL DRDMATLEQE TVQQIELLND LKLRKQQCSE SIDFKRAERT
     EWLQKLEQGE NETRTQRVQL KQVEENLHQT EVRVTRLDVE LENLLKKLAE EYELGYELAK
     LRYPVPEDIQ GTQQKVREFK REIASLGDVN LGAIEEYARV SERFEFLSSQ KDDLIEAKTT
     LYQVIREMDI EMSKRFKTTF DAIRSHFGVV FAKLFGGGRA DLILSEPENM LDTGIEIVAQ
     PPGKKLQNLQ LLSGGERALT AIALLFSIIR VKPVPFCVLD EVEAALDEAN VSRFAEYLRE
     FSEMTQFIVV THRKGTMEEA DVLYGVTMQE GGVSKLVSVR LEDEEATMTA S
//
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