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Database: UniProt
Entry: K7FR32_PELSI
LinkDB: K7FR32_PELSI
Original site: K7FR32_PELSI 
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
//
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