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
//