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Database: UniProt
Entry: H2SXA8_TAKRU
LinkDB: H2SXA8_TAKRU
Original site: H2SXA8_TAKRU 
ID   H2SXA8_TAKRU            Unreviewed;      1162 AA.
AC   H2SXA8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Structural maintenance of chromosomes 3 {ECO:0000313|Ensembl:ENSTRUP00000017046.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000017046.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000017046.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000017046.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005917}.
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DR   AlphaFoldDB; H2SXA8; -.
DR   Ensembl; ENSTRUT00000017119.3; ENSTRUP00000017046.3; ENSTRUG00000006942.3.
DR   eggNOG; KOG0964; Eukaryota.
DR   GeneTree; ENSGT00580000081628; -.
DR   HOGENOM; CLU_001042_5_0_1; -.
DR   InParanoid; H2SXA8; -.
DR   OMA; DQHQSMR; -.
DR   TreeFam; TF105602; -.
DR   Proteomes; UP000005226; Chromosome 17.
DR   GO; GO:0005694; C:chromosome; 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:0051276; P:chromosome organization; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 2.
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:ARBA00023306};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT   DOMAIN          475..588
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          188..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1004..1035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          344..448
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          620..798
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          907..934
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1012..1035
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1162 AA;  135119 MW;  0F3E2BE8071E2E27 CRC64;
     MPFTFVALSP QEGTGPRVIS AFVEIIFDNS DNRLPIDKEE VSLRRVIGAK KDQYFLDKKM
     VTKNDVMNLL ESAGFSRSNP YYIVKQGKIN QMATAPDSQR LKLLREVAGT RVYDERKEES
     ISLMKETEGK REKINELLKY IEERLHTLED EKEELAQYQK WDKMRRALEY TIYNQELNET
     RAKLDELSSK RETCGDKSRQ LRDAQQDARD KVEETERVVR ELKSKISAMK EEKEQLSAER
     QEQIKQRTKL ELKAKDLQDE LAGNSEQRKR LLKERQKLLE KIEEKQKELQ ETEPKFSMVK
     EKEERGISRL AQATQERTDL YAKQGRGSQF TSKEDRDKWI KKELKSLDQA INDKKRQIAA
     IHKDLEDTET NKEKNLEQYT KLDQDLNEVK TRVEELDKKY YEVKNRKDEL QSERNYLWRE
     ENAEQQALAA KREDLEKKQQ LLRAATGKAI LNGIDSINKV LEHFRRKGIN QHVISGYHGI
     VMNNFECDPA FYTCVEVTAG TRLFYHIVET DEVSTKILME FNKMNLPGEV TFLPLTKLDV
     RDTAYPETND AIPMISKLRY NTNFDKAFKH VFGKTLICRS MEVSTQLARA FTMDCITLEG
     DQVSHRGALT GGYYDTRKSR LELQKDMRKA EEELGELEAK LNENLRRNIE RINNEIDQLM
     NQMQQIETQQ RKFKASRDSI LSEMKMLKEK RQQSEKTFMP KQRSLQSLEA SLHAMESTRE
     SLKAELGTDL LSQLSLEDQR RVDDLNDEIR QLQQDNRQLL NERIKLEGIM TRVETYLNEN
     LRKRLDQVEQ ELNELRETEG GTVLTATTSE LDGINKRVKD TLARSDDLDT LIDKTEGEIK
     EHIRSMDRWK NIEKEQNDAI NHDTKELEKM TNRQGMLLKK KEECMKKIRE LGSLPQEAFE
     KYQTLTLKQL FRKLEQCNTE LKKYSHVNKK ALDQFVNFSE QKEKLIKRQE ELDRGYKSIM
     ELMNVLELRK YEAIQLTFKQ VSKNFSEVFQ KLVPGGKATL VMKKGDAEGS QSQDEGESGV
     DSERGSSSQS SVPSVDQFTG VGIRVSFTGK QGEMREMQQL SGGQKSLVAL ALIFAIQKCD
     PAPFYLFDEI DQALDAQHRK AVSDMIVELA GHAQFITTTF RPELLESADK FYGVKFRNKV
     SHIDVITAEQ AKDFVEDDTT HG
//
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