ID   A0A183S7E3_SCHSO        Unreviewed;      1495 AA.
AC   A0A183S7E3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=SSLN_LOCUS141 {ECO:0000313|EMBL:VDL83054.1};
OS   Schistocephalus solidus (Tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX   NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0000014901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SSLN_0000014901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL83054.1, ECO:0000313|Proteomes:UP000275846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NST_G2 {ECO:0000313|EMBL:VDL83054.1,
RC   ECO:0000313|Proteomes:UP000275846};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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; UYSU01000074; VDL83054.1; -; Genomic_DNA.
DR   STRING; 70667.A0A183S7E3; -.
DR   WBParaSite; SSLN_0000014901-mRNA-1; SSLN_0000014901-mRNA-1; SSLN_0000014901.
DR   Proteomes; UP000050788; Unplaced.
DR   Proteomes; UP000275846; 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:0051276; P:chromosome organization; IEA:InterPro.
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; 2.
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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275846}.
FT   DOMAIN          667..778
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          471..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1107..1150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          221..409
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          837..910
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          938..1071
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        471..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1131..1150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1495 AA;  167538 MW;  072A5784145569DB CRC64;
     MEQPMSIPVY TDEELLSNCP PVEIPPPEIP LHLADNTGSR LLISKIVCEN FKSYGGKRIL
     GPFHKNFTCI IGPNGSGKSN VIDALLFVFG FRASKVRSKK LSSLIHNSDR LPSVDFCQVS
     VYFQRIIDTG QGVVTGSEFV VSRKAFKDNS NAYYINESRA GFRDVTSLLR QHGIDLDHNR
     FLILQGEVEQ ISLMKPKAAT EYETGFLEYL EKPLAILADR IERLKDIRLE KLARVKAVEK
     EKNELEVVRD EAMAYLRLMN KVIRVKNVIF QQNQKRDLKH EAELKQQLTS VDAELEILTA
     RLKELNSQLT ALRADREAQN RQASCLQERH RDAKERFARF EAEDSRVRDE HAHLKSQGKK
     TLKALQAERK KLEEIRSLPG EAEGRRITLQ NQLAELEKAK TLHENTYKET MAILAQETEP
     LRKKVEAAEA ALAPIQKVAD EAASRLALAQ QELDLAMSAY RREEERVAKA REGAAAARHR
     LAERESQVLK TEQQLERGST SSANSGRRRS KTGSADACLR EALQTSSTEL AEVRVKEAVL
     AEEVGKLRST LSEAKSSFQA RQNACLLYSL FCFELYRLTC EGGEGRWFIA TSERWRRIRC
     IRRPFLLYNF SFILHFLSIL FPYAYSSLFT TIFPRNLNSF GFRQQADNSR NRVLSSLLTA
     AKEGKLTGIL GRLGDLGVIP QRCDVAVSTA CGALDHIVVQ TMEEAQKALV GFYHFPKGLD
     KMKRWELESA KPFKGPTASA QRLFDLVEVS DPSLKPCFYF GLRNTLVAET LDVATDWAFK
     HPVRFRVVTL QGQLIETSGA MTGGGGRQLS GRMTTDVSKA KQARRSLSEA VLTEEGLSAK
     ERQLATKEAE LGQLRSKREW LEEKVTHLQR QVTDAERNIA KWQAEIVRLR EEAEALTREA
     EQAEKRAANA GPSKAEREKL EANVAALSNE NIKRAAKAEK LREEVDDLKT KLMEAGTARL
     ATVRSRVALV EKKIKEVTDQ FTKLEVEIKT AHRNEAKTQS KIEALEKEVE SLKEKLTENE
     AQLVEIETTA KTCMTEFQTI QQEITALSEE REKVNAQIGE VETELAAAKK DEGVVQRKAE
     DLRSQVKDSA ARARAWQMKL RSLRLNKVDD DDEEEEEKKE ADADVADAET DLSQSLASGA
     GSQSQDNSQR DPLAFLESSK DTKLPTYTDE QLAEMNINEA ELKKLEAQIA SMSPNMAAIQ
     QYRSKVDLYL SRVAELDHVT DLRNEQLRQE AEAKGTRLSE FMAGFNVITT RLKEMYQLLT
     QGGDAELELI DSLDPFSEGI VFSVRPPKKT WKSIANLSGG EKTLSSLALV FALHHFKPTP
     LYVMDEIDAA LDFKNVSIVG NYVMERTKDA QFVIISLRNN MFELADRLVG IYKTHNITKS
     ISVDCHVLAQ RLNQAVSKVR GHQSKQQQQR WPLTTTAATS SLPVPPCVGV LGSQPVVTDG
     TVVGATAETS VLLGPRGDIV GSKAENEPSN EIEAQLAGVV KDEGTDSDTP IIELY
//