ID A0A1X7R7L7_9SACH Unreviewed; 1447 AA.
AC A0A1X7R7L7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=KASA_0K03421G {ECO:0000313|EMBL:SMN21657.1};
OS Kazachstania saulgeensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1789683 {ECO:0000313|EMBL:SMN21657.1, ECO:0000313|Proteomes:UP000196158};
RN [1] {ECO:0000313|EMBL:SMN21657.1, ECO:0000313|Proteomes:UP000196158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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}.
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DR EMBL; FXLY01000008; SMN21657.1; -; Genomic_DNA.
DR STRING; 1789683.A0A1X7R7L7; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000196158; Unassembled WGS sequence.
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; 1.10.287.1490; -; 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 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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000196158}.
FT DOMAIN 694..807
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 412..663
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 859..1086
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1447 AA; 166058 MW; D507AAD9A686A489 CRC64;
MSDSPLSKKQ RRDLGDKTPE PATLPNVTPT HSQTSESFLN DENDEDNDVM PSNISYSKSR
TPRKLVIGST DNRFAFSQPL NSNPASSLQV PTLQPPLTQQ SRSGRKIKTY SQSPPRSPGR
SQGRSPTRKL ELIQLSPIKN SRVELQKLYS AHNLKLKKEG RLYINKLVLN DFKSYAGRQV
VGPFSTSFSA IVGPNGSGKS NVIDSMLFVF GFRANKMRQD RLADLIHKSE KYPNLPSCSI
EVHFQYVNDL PDGSTKIDTE KGDLVITRRA FKNNSSKYYI NNKESNYKTV TELLKQEGID
LDHKRFLILQ GEVENISQMK AKAEKDNDDG LLEYLEDIIG TTKYKPLIEQ NATEMESLND
ICIEKENRFE IVDRDKTALE KDKDAALEYL EKEKQLTLAR SKRLQVQILE SNVKLKNSLE
KVSELNSQLE IEKEKFESQQ QQISSLVQSH DLMNQELNKL ASEEKTINKD KRENKTKEVS
LEEMLKSLSH KKRKAEKSLK TTREKIKECE TQLRNFGEES IEDEETLQNL NRELEEEKVK
LENIKISLKE KTSDISKDIT KYENELEPWK VKMQEKTLQI QLMESEISVL QEMQINLEND
IANTKSEINL KTQAIDENQK MNENLADEQQ VLKKEILVGE RECKTAKEKL KDMQIVLNTQ
RQRATEARFA LSSVQNKNKV FAALSRLQKS GRISGFYGRL GDLGIIPKKY DIAISTACPR
LDDIVVETVE CGQQCIEYLR KNKLGYARFI LLDKLRNLNT NPIQTPNDVP RLFDLIQPQQ
EKFIQAFYSV LRDTLVAKDL NQANNVAYGK RRYRVVTLDG QLIDISGTMS GGGNQVSRGL
MKLGDKSTVQ MAMCTAEDVQ KIETELNERE KNFKVANDTY HEMEMELTRL KDKEPQVELE
ISKLSLDLDS LKSEIQLLNK SLEQKLTSYA AAQNNNDEVD NAQRKLDDLR KEFSDLESQT
KTTQEKLQKL REKIMEIGGI NLQLQNSKVT SLLERIDTTQ RKLKKKKSEI KKKGNETKKL
NKTLESTATD LRTCEAEITK LETQLLETKE NISELDNSLE GLLNKKEDMN DKIKDVKEKI
SEFELDHNQY QSFKLEVENK LEKLTKLVHY VKKEIKEFDK DLNNLAIRDV TQILQQLEEE
KSETTSPEKN GISTHGDEVL PEHNPSNNSS NAPTNVIERT EIHIDDIEEN EDEEDDKCTE
DAMDVDSEQG EISKGIQRLN DAELQNIDKD ILDQEIFALD EYLNTTNANI DILEEYVKRL
IEYRNRKNDL NSAIQRRDKI GKILEDLKTK RYDEFMEGFS IISMTLKEMY QMITMGGNAE
LELVDSLDPF SEGVTFSVMP PRKSWRNITN LSGGEKTLSS LALVFALHKY KPTPLYVMDE
IDAALDFRNV SIVANYIKES TKNAQFVVIS LRNNMFELAQ QLVGIYKRDN MTKSVTLQNE
DIFEEST
//
