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Database: UniProt
Entry: A0A015ISC1_RHIIW
LinkDB: A0A015ISC1_RHIIW
Original site: A0A015ISC1_RHIIW 
ID   A0A015ISC1_RHIIW        Unreviewed;      1250 AA.
AC   A0A015ISC1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=RirG_182930 {ECO:0000313|EMBL:EXX60102.1};
OS   Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX60102.1, ECO:0000313|Proteomes:UP000022910};
RN   [1] {ECO:0000313|EMBL:EXX60102.1, ECO:0000313|Proteomes:UP000022910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA   Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA   Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA   Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA   Huang S.;
RT   "Single nucleus genome sequencing reveals high similarity among nuclei of
RT   an endomycorrhizal fungus.";
RL   Submitted (FEB-2014) 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. SMC1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005597}.
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:EXX60102.1}.
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DR   EMBL; JEMT01026043; EXX60102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A015ISC1; -.
DR   STRING; 1432141.A0A015ISC1; -.
DR   HOGENOM; CLU_001042_0_1_1; -.
DR   OMA; SYIRDHT; -.
DR   Proteomes; UP000022910; Unassembled WGS sequence.
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; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022910}.
FT   DOMAIN          526..642
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          968..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          178..229
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          329..370
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          421..497
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          689..942
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1046..1087
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1250 AA;  144615 MW;  92DC87E9B9D302D2 CRC64;
     MGRLDRLELE NFKSYKGLQT IGPFHNFTSV IGPNGAGKSN LMDAISFVLG IKSAQLRSSQ
     LKDLIYRGRA MQDDDEEVTD GMAIEGRTNN PKRAWVMAVY KDDNGNEIKF TRSITTSGAS
     EYKINNKPVT YAKYNSTLEQ QNILVKARNF LVFQGDVEAI ASQSPKDLTR LIEQISGSLE
     LKAEYEQLKV QQERATENSA FNFNKKRGIN SEIQEYQRQK AQAQQFEKLQ AERTQILVDY
     LLWKLFHIQQ NIQGYKGEID EHNDVIRRRQ REQKKFDSEL KEARLEQSKV HKEYFQMEGV
     IKSKEKELEE KRPALLTVEE KIFHSKRKLS QYEQDAERVR KDFDRQTNHV VELQSELDKI
     TRSAEQYEAS LRAGGGSNKR LNAEDMAEYS RKREAANKKT VNEKQRLVNV RRQEKTCRES
     THRLKEKMED LDRRRKQLEE EKLAVSDQKE KVGSYVTQLN ADLEAARKEL EAAVAERNSI
     NQQETQYNRE LQETLNKLTV ASVDQRESER EQKMKECLES LKRVFSGVHG RLLDLFTPSQ
     RKYAVPVSII LGRNMDAIIV DQQKTAIECI QYIREQRLGH ATFIPLDTIV VKPINDKYRS
     FMKGARLAID VITYNDKLER AFQYACGNTL VCDTLEIAKY ICYEKNQQVK AVTLDGTIIH
     KSGLVTGGHS DDILTGAKRV AEKRRADNID ELRRQRDDLL SKLNNLSKSK RRGNFEEQKK
     SEISGLESRL KFSQEELSVI TRKLESINSE LNFIASETNE LQPRWRKAHS DLTNFENQIT
     QLENTIHSIE DTIFEDFCAK IQVANIREYE QRQLQLAQEM AEKRLKFTTL KSRLQNQLKF
     ESEQRKEAED RLNKLEAAIK NDTERLTQLG QEKEQLLRDK KLISDQIAEA QNALNEIKES
     FDEKTDAVNV AKRKLSQITK EIERMMKEIV NKESDIEKLE ADQFSIFRKC KLEEIHLPLE
     RGSLDDIPIK DSRFQDDDEM DIDEDDVLSS NRAGPSSTAT SSGWNVQVDY SSLTDDLKEN
     DGIEIANEFE KKLDEKSAKM EEIAPILKAI ERLDGIEQRL HDTEKEFDSA RREAKTAKDR
     FNNVKQKRCK RFRAAYDHIE KNIDRIYKDL TKSRSFPLGG TAYLSLEDNE EPYLDGVKYH
     AMPPMKRFRD MEQLSGGEKT MAALALLFAI HSYQPSPFFV LDEVDAALDN TNVGKIANYI
     REHASDTFQF IVISLKSTLY EKAQALVGIY RDQEVNSSKT LTLQLDKFQE
//
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