ID   A0A1G4J8K3_9SACH        Unreviewed;      1425 AA.
AC   A0A1G4J8K3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=LANO_0C06304G {ECO:0000313|EMBL:SCU85991.1};
OS   Lachancea nothofagi CBS 11611.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1266666 {ECO:0000313|EMBL:SCU85991.1};
RN   [1] {ECO:0000313|EMBL:SCU85991.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006005}.
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; LT598446; SCU85991.1; -; Genomic_DNA.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000189911; Chromosome c.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProt.
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   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   PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 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   Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
FT   DOMAIN          658..771
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1114..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          312..339
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          379..504
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          821..855
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          894..942
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1021..1076
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1208..1269
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        50..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1115..1157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1425 AA;  162298 MW;  E52A3F6ECC1E771F CRC64;
     MDSPLSKKQK THVNQSDDSS QAEESPDVTR ASRSRTPRKL VLGSPDKRFA LSQPVSSSSN
     VPFLQPLKDE LPSSRGRVYS QSPPRSPNRS PTRKLELIQL SPMKKSRLEM QKLQESRNEL
     ESIERLCISR LVLHNFKSYA GTQVVGPFDS SFSAVVGPNG SGKSNVIDSL LFVFGFRANK
     MRQGRLSELI HKSEAFPDLN YCQVDILFQY VQDEPDGSTT VKTSKPELVI SRKALKNNSS
     KYYINGKEGT FTQVTQLLRK EGIDMDHKRF LILQGEVESI AQMKPKAEKE SDDGLLEYLE
     DIIGTAKYKP LIEQVLIEIE RLNEVCQVKE NRFEIVEREK SSLESGKDEA LEFLEKEKRL
     TILRSKLLQY RHWKNDDKLL STKNKKAVLE QKLAREKEKY TKQQEELKEL EDGIGSIKRD
     LKCHRDKENT VMVRKRNCDR ERVSSEEKLK NLEQKKVKWG KSQQVIKASI QTTEAKLKEL
     LRDQEELSAE FKELNESLAV EKTKLNEIKL SLRDKTGTIS EQIGSIESDL EPWNVQLQAK
     RSQIKLEETT ISVLKESHAK IAQEIKSTED EISNFHQNTA EHHAVIASLV QEQTEVRKQL
     TMGQSECDNA SIKIKEMKLV LTAHRQRSVD ARSSLSTFEN KNKVLAALHR LQNSGRISGF
     HGRLGDLGTI DDKYDVAIST ACPRLDDIVV ETVECGQQCI EYLRKNKLGY ARFILLDKLR
     SYNLRAIATP DGVPRLYDLV RPADEKFRSA FYSVLRDTLV ARDLPEANRV AYGKQRFRVV
     TLDGKLIDIS GAMSGGGNYK ASGMMKSKRQ ESVGTYTTEE VEQIDNELAE REKNFQIATE
     TLHEMEEALQ GLKDREPEIG LNISKREMDI DSLSLEIKSG ELKLITLRKE HQRRELSDHE
     LNEAESNLTI LRKECKELEE EMKSKKNEIK KLQEEIMRIG GTSLQIQNSK VDSISQRLEI
     ILAKQKRDRT ALKKAESDVK RFRKQEEELA RDVETCSGEL SKIANSLSAS EAEICELNKN
     LEKLASDIED SEEHMRQAEE CLKEKSSEDN GFKVLEVDLN NQLEKLNDLI RHVEKEGYLL
     QKEIDALKIR DVTTTLQMLD EDILPQNYLE ATLGSSKSDK KDASDDHNIG AMDLDDSEEL
     GTASRDLEAK AGSVDGDMQS DDDMQSDDDM QVDDNVQPDH DMQVKDSNGK AHVGLAKLIQ
     PQLEALNVEE IELEMGQLED YLENAHANIE VLEEYAKSLV DFRARKLDLN QAVQKRDQIR
     QSSEDLKKNR LDEFMNGFNT ISLTLKEMYQ MITMGGNAEL ELVDSLDPFS EGVLFSVMPP
     KKSWRNISNL SGGEKTLSSL ALVFALHKYK PTPLYVMDEI DAALDFRNVS IVANYIKERT
     KNAQFIVISL RNNMFELAQQ LVGIYKNKNM TKSVALRNKD LIDRN
//