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Database: UniProt
Entry: A0A1Y1S654_9MICR
LinkDB: A0A1Y1S654_9MICR
Original site: A0A1Y1S654_9MICR 
ID   A0A1Y1S654_9MICR        Unreviewed;      1091 AA.
AC   A0A1Y1S654;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=SMC1A {ECO:0000313|EMBL:ORD93890.1};
GN   Name=SMC1A {ECO:0000313|EMBL:ORD93890.1};
GN   ORFNames=ECANGB1_1408 {ECO:0000313|EMBL:ORD93890.1};
OS   Enterospora canceri.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC   Enterospora.
OX   NCBI_TaxID=1081671 {ECO:0000313|EMBL:ORD93890.1, ECO:0000313|Proteomes:UP000192639};
RN   [1] {ECO:0000313|EMBL:ORD93890.1, ECO:0000313|Proteomes:UP000192639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB1 {ECO:0000313|EMBL:ORD93890.1,
RC   ECO:0000313|Proteomes:UP000192639};
RX   PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA   Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA   Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA   Stentiford G.D., Williams B.A.;
RT   "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT   within Enterocytozoonidae microsporidia.";
RL   Environ. Microbiol. 19:2077-2089(2017).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORD93890.1}.
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DR   EMBL; LWDP01000041; ORD93890.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1S654; -.
DR   VEuPathDB; MicrosporidiaDB:ECANGB1_1408; -.
DR   Proteomes; UP000192639; 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; 1.20.1060.20; -; 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: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; 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   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192639}.
FT   DOMAIN          469..582
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          172..209
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          248..310
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          340..440
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          617..700
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          728..761
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1091 AA;  127618 MW;  870BC8593A8AEEFE CRC64;
     MQLEKIELRN FKSYSGNYTV GPFDKFTCIV GPNGSGKSNI LDGITFATNV SINFLRVKRA
     AELVSNGFTE CEVKLHITSS EKHRVFSRSY SCINQTYTYK INEKVVQSAI YTKELEKINI
     FAKIRNFIIY QGVLLNENVD LFNVIEKISN SVMYKDEYEK LKANHLACSK LLQQKHEKKK
     DIMNDMNEMN EAKDKERRFL KNMQEQEELT KKCYVLETKI KENELKKLGV EFDDISKRMC
     SLKEDSEYKR VKEDVSDMKK QVAKEYKEFY EIDTEIKCIR EAGNKETGEL EELEKEKTLL
     QKSIEKLRSP IDYEEYCCDE EDKRQQFEDD LFVAMEEYNK ETAEEQKEEC KLTLDNYERI
     SRKEELLNEI KKFNEKKNKM EKENKSVEQN NKLKKEAKIK IDKILEELRE KATPEALNQL
     QKLEEDMKKR ESELNQFTKE ILIHKAKFNI SKNEIFVSGV IENLKAINGG VYGKISKLIQ
     PTQECYEVPV SVLIAKYDNT VVVENEKTAI ECINYLKETK SCKLTFLCLD RFTSTGYRNG
     AYGEICMDPM DCVAYENRYV GIVEHIFKDK AIITTENIEE FQNNFKAICT TNGSYYQRSG
     LITGGSNKIN KYEENLVEEL SAKRTRVLNE IKGIKNKKES FTGINIYMDK IRELEKKKET
     YTFEKETNIE IAMEKELERL KVVNEELSNL NVLLQDYEMA KQFIRETFRV KEKKTLAPIL
     NKIGVETYEE YKAKIQDEEK RIDLTENLKN IETKIANLTT NDNDNDKTES EDKYVQIFNL
     NKKQVEIQNK LEQSKQILRM KNATYTESTR KIDDLNKKMM NNTLTRTKYA EEIKDLIGFC
     VLETNLQNED EITNEYNKIA ITGVNIINLL NDLKSSKYKV QQELQANVPL GLMQNDTLQS
     KYLKFNREYE FAKNAAQQAK AHFNEIAVHR KRLFDQYFET LQRQINSVYK KLAYSLEFDT
     EIHEVGKVVL EGDPFAAKNA IKFYVMPPNK GYTEFRDLSG GEKSLAILSF IFAIQKVPPF
     YVLDEVDTAL DRDNVQRLAN FITNETNGVE DEKQFLVISL KDYFFKNAES LVGVYKDQTE
     NRSKILTYKF V
//
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