ID   A0A024UUS3_9STRA        Unreviewed;      1070 AA.
AC   A0A024UUS3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=SMC hinge domain-containing protein {ECO:0000259|SMART:SM00968};
GN   ORFNames=H310_00477 {ECO:0000313|EMBL:ETW10094.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW10094.1};
RN   [1] {ECO:0000313|EMBL:ETW10094.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETW10094.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005597}.
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DR   EMBL; KI913952; ETW10094.1; -; Genomic_DNA.
DR   RefSeq; XP_008861505.1; XM_008863283.1.
DR   AlphaFoldDB; A0A024UUS3; -.
DR   EnsemblFungi; H310_00477-t26_2; H310_00477-t26_2-p1; H310_00477.
DR   EnsemblProtists; ETW10094; ETW10094; H310_00477.
DR   GeneID; 20077527; -.
DR   VEuPathDB; FungiDB:H310_00477; -.
DR   OrthoDB; 231904at2759; -.
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; 1.
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; 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|ARBA:ARBA00023242}.
FT   DOMAIN          522..638
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          177..288
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          342..479
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          681..708
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          798..911
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1039..1066
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1070 AA;  122223 MW;  D279B457AF72F327 CRC64;
     MGRILRLEVN NFKSYGGKQE IGPFARFTAV VGPNGSGKSN LMDAISFVLG VQSRQLRSNQ
     LKDLLHKSGL TLSAETSAHV SLVYDLDQDE QQRIHAKLPG GITSNELTFT RCISEKGIGS
     YRINNHEKSY EEYESTLKDL GILVKARNFL VFQGDVESIA SKSPEQLTRM FELISSSEEL
     KEEYEKCLQE KAIAEENTIF AYQKRKGLAA ERKIVKEQKE EAERYKQRRK DLAKTKQEYY
     LWQVKLVEDD ASDHKDAIVQ LREKVAKLQD KEHELAGVQK EKKKLHATQL KKCRQLDTLV
     ADVTRKLEDV APRTIQLNEQ IKHDKKKLEA ASAKEYTMAK NVQNHEREIL GLRQDIKDLK
     HAQNELDASK DDEELVLKGT QLKEYNRIKE AAQLKTAKLR NELESLRRQQ QADNGRLQAL
     LRDEKEHTDE LSRMNEDHAV AEARLVDIRR VVASSTAEID DTEAELQNAE QFEKSLADKK
     LANKAELDKI HSKLRNVKDG MRQSQADQRK VETLETLTRL FPGVRGRLVD LCKPIQRKYN
     MAVTVATGKY MDALVVTDYK TAGDCIQYLR EQRLESVQFI PLDKIRVTPP NERFRRLGDN
     IKLVVDVIDC DPEFQPAVAY AVSDAIVCDS IEDARDVCFR RNEKVKAVTL NGMVVSKNGS
     MTGGKTYKDT ARSERWDEKE TASLKVKRDE LQAELSALEK ESTGVVRKQT LETKLGSLMN
     RLRYANADIK TTESKLPKIL ARKQECTKIL MQLVPEINKI RGALSARESN LTSLEHQINS
     VEDTMFEGFS QQFGIPSIRE YEEKVVKQQR ERLERRRQLD SHLAKVQAQL QYLEAQDLPS
     EWERVKDVIS KQKRHLKELE SEKKGLQAKT AELEETSTKH VEAATAAHDA LKEIEHELKI
     LMKKRDDHNN IMTGVQKQLA VEETALERFK DKKTEILKRA TMDQVKLPVV GEAATAIDDD
     EIGDSDIDMS SHSIVATGSS EESISLTYQA GDRYADKEIN FSTLEDLHLD TDKMRQDHLV
     KYEQLISTIA GDLERMQPNL KALEKYDEIQ ARISREEEEL EKIKVGLALN
//