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Database: UniProt
Entry: A0A0K0DUV3_STRER
LinkDB: A0A0K0DUV3_STRER
Original site: A0A0K0DUV3_STRER 
ID   A0A0K0DUV3_STRER        Unreviewed;      1193 AA.
AC   A0A0K0DUV3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000102100.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000102100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005917}.
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DR   AlphaFoldDB; A0A0K0DUV3; -.
DR   STRING; 6248.A0A0K0DUV3; -.
DR   WBParaSite; SSTP_0000102100.1; SSTP_0000102100.1; SSTP_0000102100.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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   CDD; cd03272; ABC_SMC3_euk; 1.
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; IPR041741; SMC3_ABC_euk.
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; 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|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681}.
FT   DOMAIN          534..647
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          235..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          407..448
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          672..783
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          810..913
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          979..1023
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        235..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1193 AA;  138892 MW;  60BF0A2F173B84C5 CRC64;
     MYIKEICIHN FRSYKDKTVI NDLSKRHNVV VGRNGSGKSN FFFAIQFLLS DDFANLSQDA
     RLNLLHEGAG EKVRSARVDI VFDNSDRRIM SYDINDLKIS REISERKDTF YIDGKIVSRS
     EIVNLMESAG FSKSNPYYIV KQGKIMELAT STDAQRLALI KEVAGTRVYD EKKQDSAKLL
     KENMDKLEKI EETIEFINER LKTLEEESND LREYQKYDKM KRALEYTIYE QEATDSRKKL
     DNLSHEREEL NSQQNEIESS LLQYKQQSMK RETDLRRLEA TFKGVKEERE VLLEEQNVLV
     EKKTNLELCI ADLREEADRE RKNRARAEEE MSSVGRIIND REIELEELEP SYKDVVEREN
     NLLTDIKICE QKRKDLYIRQ GQQDQFRTTE DRDNYLRREC KKMDRYLSEL RERVAESEGL
     IEQDRVETEE IQKNIMSLKL KLDRVMDRMD RLSGDQNQAK AHLEKCTIRQ GEIQREEKNW
     HESMMNLNQE KSQVETDIRR MIPPSLMHGM NSIKKAIEHF KKNNKNGKYD YIINGYYGAL
     VDLIDADDIF YHAIETTAGN SIYYSVVEDD RIASEITSYI NSSNLPGECN FCPLNRIVAK
     PRKLITDPDA KHIMDCMKYD PKFETIIRSF FGQTAVVGSL DVGGRVSRTD NVNCVTLDGD
     KISRRGPLTG GYREMKRSKL ELNNVLRQLN GNEIDMKKRS DEISKRANDA SISTAQAAQA
     LENITEEIKR LRREHHLCNE ELSHKTEALN RMGMNIEPQR QHLQTHKNKI REIEAKKEIL
     QNQIGTPLHS TLTDEEQAML ELLEKDMKER SIIESKKHKI ENELQNYLRR RREKLRCELQ
     DISMEDKKHK LSSTNSELKS TNERLSNIME KINDIDTSLI DYKIQKDNLI KIKEEQQERI
     KILENQLNDV GKRADVVCTK LATIRATNEE VTKKMAELGT LPQDAFKKFQ NLSRKKLDEK
     LTECLVELKK YSNVNKRALD QFLRASQQKE DLVKRVQEQK KSKKAIENLI EVLDNRKNEA
     LNMTFKMVTK HFHTVFQQLI PEGKADLILK LKDDDGPVPS GNELISVDRF VGVKIKCTFR
     GDAESVEMNH LSGGQKTLIA LALIFAIQKC DPAPFYLFDE IDAALDAAHR SSVASMIHEL
     SENAQFITTT FRPQLLEHAE KYYGVRFRNR VSHIDPVTKE QAYDFITDAE KRN
//
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