ID   A0A0N5A320_PARTI        Unreviewed;      1231 AA.
AC   A0A0N5A320;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   03-MAY-2023, entry version 25.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001603000.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001603000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005597}.
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DR   AlphaFoldDB; A0A0N5A320; -.
DR   STRING; 131310.A0A0N5A320; -.
DR   WBParaSite; PTRK_0001603000.1; PTRK_0001603000.1; PTRK_0001603000.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0008278; C:cohesin complex; 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:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR   CDD; cd03275; ABC_SMC1_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; IPR028468; Smc1_ABC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR18937:SF12; 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; 2.
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|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719}.
FT   DOMAIN          511..631
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          161..222
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          263..294
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          319..353
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          398..495
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          676..780
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          805..900
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1031..1072
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1231 AA;  142322 MW;  ABB9CC54CB27009E CRC64;
     MGRLVRLEIE NFKSYKGKVT IGPFKEFTAI IGPNGSGKSN LMDAISFVLG EKAINLRVKK
     LTDLIHGMTH GQPAANKCFV EMHFDIGRGK IKVFSRGVVG GSSEYRINGE HVTPQLYAAE
     MEKQNIFIKA KNFLVYQGAV ESIAMKNPKE RCQLFEEISR SNELVAEYNK LKEEMLKSEE
     LAQNNMHRRK NIAQEKKEAR AEKEEAEKYR SKQNELANLN QQLYLMKLQY VEKHTKKATA
     DVIEKRKEVE EIRNKRDESN SGITSAQKTA KLVAREVRKL EQEANDVLRQ LENERPKFLK
     TKNEVVHVKG KLNYQENAFE SMTKSAEQQK QNIIDIENRI NEINREKEEC LNKMKSDSQS
     MNLNMNESDL NEYKALKMEA GKRNAKLSLR LEDLFQEYES LLTLLSHEKR KLASYEERCK
     IKQELVDRHE ILISNNEEQL KTHLNNIEEE KKNVELLEKE LGTANKRIEE VRTSLDAVAR
     QLNDAQGDSA ESERNRRKNE AFENLKRIFA DRVYGRLVDL CQPSHKKFKL AVTKILSKQM
     MNIVCDTEET ARECITYLKE QRYQTETFLP LDSLSVGPLN ERIRNFPESK GIKLVYDVLQ
     ISNVANVKKA VQFVCGNALV CETLDDARKM AFGNDSSGER YKAVSFDGTL FMENGMMSSG
     KQELRMKAKK WDEVAMKKLR EQYSQLQDEY HSLQKIKKRE MDLDMKIKHI QQLESRVIAT
     KEEINKLKTT DKQNVQQQLE FAQNELNMQR PRIEEISERI ESKKESIANL EKKKDGIIDE
     VFHSFCTRLN IPDIRRYEER EMRFHEEMQT KLKEFDNQLD KWKSELEFLV RDDKAGKAKE
     AEIKIVDLSK QLKSLEKKQL FEENKIKEIE KKYDDLLELG KQKQVDLESA EQALAVAKKE
     ASYVDKEINA VEKVIMQLEA VVSAEKIQRH DLLLECRLKN IDLPLINGSL TELVSEEDGM
     DEQEMSSQLA SSQKASQRMI HSQDWIEVDY TNLSKEYKNV KDESTLKKFT EKILKDISDI
     EHTLSKLNAP NSKALERMEQ VKEREAESTE ECEQARKRSR KARDAFEKLK AERIKRFHTV
     FEPVSQKIDE IYKMLSGNES AQAFLGADNL EEPYLEGISY NCVAPGKRFR PMDHLSGGEK
     TIAALALLFA IHSRNPSPFF VLDEIDAALD NSNIAKVVNY ITERSKKDFQ VVVISLKEEM
     FQHADALIGI YSKPEKCTTS GVLTIDLSET S
//