ID K7FR32_PELSI Unreviewed; 1295 AA.
AC K7FR32;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=SMC4 {ECO:0000313|Ensembl:ENSPSIP00000010492.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000010492.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000010492.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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DR EMBL; AGCU01089798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01089799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01089800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01089801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01089802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01089803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01089804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01089805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01089806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006123501.1; XM_006123439.2.
DR STRING; 13735.ENSPSIP00000010492; -.
DR Ensembl; ENSPSIT00000010545.1; ENSPSIP00000010492.1; ENSPSIG00000009523.1.
DR GeneID; 102455971; -.
DR KEGG; pss:102455971; -.
DR CTD; 10051; -.
DR eggNOG; KOG0996; Eukaryota.
DR GeneTree; ENSGT00900000141094; -.
DR HOGENOM; CLU_001042_4_1_1; -.
DR OMA; CPALDNM; -.
DR OrthoDB; 231904at2759; -.
DR TreeFam; TF101158; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0000796; C:condensin complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0051383; P:kinetochore organization; IEA:Ensembl.
DR GO; GO:0010032; P:meiotic chromosome condensation; IEA:Ensembl.
DR GO; GO:0045132; P:meiotic chromosome segregation; IEA:Ensembl.
DR GO; GO:0007076; P:mitotic chromosome condensation; IEA:Ensembl.
DR GO; GO:1905821; P:positive regulation of chromosome condensation; IEA:Ensembl.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IEA:Ensembl.
DR GO; GO:1905820; P:positive regulation of chromosome separation; IEA:Ensembl.
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.
DR SUPFAM; SSF57997; Tropomyosin; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267}.
FT DOMAIN 612..727
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 540..595
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 768..1009
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1295 AA; 147633 MW; 38E5170587AE37FE CRC64;
MPSKSTKTST AARQKGKEPL EEPTSDMEVG KEADTSLSEA SQQADSNGNG ELDNRSLEEI
LSSISPPPPP AMTNEAGAPR LMITHIVNQN FKSYAGEQIL GPFHKRFSCI IGPNGSGKSN
VIDSMLFVFG YRAQKIRSKK LSVLIHNSDE HKNIQSCTVE VHFQKIIDKE GDDYEVIPNS
NFCVSRTAYR DNSSVYHISG KKKTFKDVGI LLRSHGIDLD HNRFLILQGE VEQIAMMKPK
GQNEHDEGML EYLEDLIGSG RLKDPIQVLC RRVEMLNEQR GEKLNRVKMV EKEKDALEGE
RNKAIEFLSL ENKMFKEKNR ICQYYIYDLQ NRITDMETQK RKIHEDTKDV NVKSSKLADE
MKVKSNALKD VEKKLNKITK FIEENKEKFT QLDLQDVTVR EKLKHAKSKA KKLQKQLEKD
KEKVEQFKSV PGNSETAISK ATSKKEVLEK EKEREEEKLK EVMDSLKQET QGLQEEKEGK
EKELMEFSKT VNEARSKMDV AQSELDIYLS HHNTAVSQLN KAKEALKTAS GTLKERTVGI
KELNTKLPQA EQELKEKEKE LEKLGREEMD IKKLVRELRQ KVEEAKSSLA INRSRGKVLD
ALLQQKKSGK IPGIYGRLGD LGAIDEKYDV AISSSCGALD YIVVDTIDTA QKCVNFLKNQ
GIGVATFIGL DKMTVWENNM NTIQTPENTP RLFDMVKVKD EMIRQAFYFA LRDTLVANNL
DQAIRVAFQR NRRWRVVTLQ GQIIEQSGTM SGGGHNIMKG RMGSSVVVEM SEEEANKMES
QLQKDSIKAM QCQEERGQLE EAVAKLHLSV QQMRNTLEKY TASIQSLSEQ EVHLKVQVKE
LEANVIAAAP DKNKQKHLEK NLNTFKKDYE TVAEKASKVE NEVKRLHNLI IEINNHKLKA
QQDKLDKINK EIDECSSAIT KAQVAIKTAD RNLKKSEESV LRTEKEIGDN EKEMKELIEE
LTILEEKATE VMNNCKQAEE SLPEVQEEHR SLLQKIKAIQ EDEHALQKEA LNIRLKIEQI
DSHIGEHQSK IKYWQREISK ILLHPVEDKL SEELPVLNQE ELEAIKDPDI ITNQIALLEA
QCHEMKPNLG AIAEYNKKEE LYLKRVTELD EITNERDNFR LAYEDLRKQR LNEFMAGFNV
ITNKLKENYQ MLTLGGDAEL ELVDSLDPFS EGIMFSVRPP KKSWKKIFNL SGGEKTLSSL
ALVFALHHYK PTPLYFMDEI DAALDFKNVS IVAFYIYEQT KNAQFIIISL RNNMFEIADR
LIGIYKTHNT TKSVATNPKI IGSKGLAEIG SVGCC
//