ID A0A3S2VNV7_9PROT Unreviewed; 1222 AA.
AC A0A3S2VNV7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=EOI86_19570 {ECO:0000313|EMBL:RVU35031.1};
OS Hwanghaeella grinnelliae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Hwanghaeella.
OX NCBI_TaxID=2500179 {ECO:0000313|EMBL:RVU35031.1, ECO:0000313|Proteomes:UP000287447};
RN [1] {ECO:0000313|Proteomes:UP000287447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gri0909 {ECO:0000313|Proteomes:UP000287447};
RA Kim J., Jeong S.E., Jeon C.O.;
RT "Gri0909 isolated from a small marine red alga.";
RL Submitted (JAN-2019) 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:RVU35031.1}.
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DR EMBL; SADE01000003; RVU35031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2VNV7; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000287447; 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; 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; 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; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 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:UP000287447}.
FT DOMAIN 4..1205
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 784..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..211
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 237..264
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 293..534
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 665..741
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 839..901
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 998..1060
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 921..960
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 1222 AA; 134152 MW; E71CB55A407D8A0C CRC64;
MHFSRMKLSG FKSFVDPAEL VIDGGITGVV GPNGCGKSNV IEALRWVMGE TSAKRMRGSE
MDDVIFGGSS QRPARNIAEV SLFLDNSNKD APAPYDTLEE LEITRRIERG AGSNYRINGK
EVRARDVQLL FADMATGANS TAIVSQGRIG AIIGAKPTER RTLLEEAAGI RGLHSRRHEA
ELRLKAAESN LERLDDVIGA LETQHQGLQR QARQTNRYRR LSDHIRRHEA ILLHLRWQDA
KRAMDIARQR LNEAEALVHE KAQNAAFAAR EQADAAASLP TLRQADAEAA AGLQHLQLAV
RELENEQERI LAARDALAQR LAQITSDRER EDSLFDDAKQ AVERLTAEAA TIEEARAAET
ETLEQARTEA EAASKAVEEK EAELSELTEQ AAGVEAQRNA LQRQLAESGQ RLTVLENRLR
GLDDQEAKLK QETESLAEIE TAEARVAECE AAVSTAREAA AAAEAVLAEC REKESAARSA
LQESDRLARE HLAEVQADAR ETVETAERAA REAVDALEQR FRALDAEIRA LADLVETQDD
TLDPAFRPLI DSLSVQQGYE AALGAAFGEE LDASTDGKAQ IHWTELPPLT GSTGFPAGVE
PLSKFVDGPK ALSRRLSYIG VVPDGTAGDA LQKDLAAGQR LVSRDGGLWR WDGYSMAAGA
PTAAAKRLEQ RNRLAEIREE FAKVEKDLTE ERQAADKRLE EARLKAEAKV QEANRSTEAN
LTELRAQAES AEAEAAEKAA SQKAASQALQ EAFSALNQAQ QAQSALAGKA ADLRSRLQGI
SENRERLQAD AAEARDQTES AKKAMDVLED PLATRERINA LRATVAELRS ALIDKRGAVE
RFQRESQARE ARLEAIAQEQ ASWQQRMSGA DGRMKSLADR AQQAEEENAA LESRPAEIQA
QHHALNDKIV VAEAKRNTAA DALSEGEKKQ QETDKALRDS EAAMASARED RVRRESEVEQ
ADQAAQTIRE RISESLDCAP DAVLQAGGVE PDEELPPRDD IERKLERLTR ERENMGAVNL
RAEQEATELE EQITSMHTER DDLLAAISRL RQGINALNRE GRERLLAAFE QVNAHFKDLF
VRLFGGGEAH LTLTEADDPL EAGLEIMASP PGKRMQIMSL LSGGEQALTA LSLLFGVFLT
NPAPICVLDE VDAPLDDSNV DRFCTLLDEI AHTGKTRFLV VTHHRMTMAR MDRLFGVTMA
ERGISQLVSV DLREAARLRD SA
//
