ID A0A024GI91_9STRA Unreviewed; 1364 AA.
AC A0A024GI91;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=BN9_069870 {ECO:0000313|EMBL:CCI46058.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI46058.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI46058.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI46058.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) 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. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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:CCI46058.1}.
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DR EMBL; CAIX01000115; CCI46058.1; -; Genomic_DNA.
DR STRING; 65357.A0A024GI91; -.
DR InParanoid; A0A024GI91; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000053237; 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; 1.10.287.1490; -; 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; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF172; 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; 2.
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|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT DOMAIN 586..705
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 311..461
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 518..545
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 924..1014
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1099..1162
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1364 AA; 156505 MW; 92542123CD874813 CRC64;
MNDKQDEHVA DVEMEPETPP ECPSPSNVPL SSSKRLIITR MQLENFKSYA GFIEIGPFHN
NFSAVVGPNG SGKSNVIDAL LFVFGKRASK LRLKKISELI HRSEQFPNLE TASVSVYFHE
IIERDANESD ESAEIIPNSE FYVTRTASRN CNSKYFVDGA LSSYTKVTNL LREKGIDLDH
NRFLILQGEV EQIAMMKSKG NVSTSSSSGG TSNNASEEGL LEYLEDIIGS NKYIHPIEEA
WEVLEKLNDR RSQKLNRVRV SEQEKEHLKG PRTEALAYLR KERELYAKEN ILYQLYIHST
AVKRVECEKT MEETQTKFKA QEESIHSLRK DLEKVEEKYQ SEKNECDLIV TQLDDIKTKF
ANLEKEDVVL REELKCSKEK MNDLQKSEKK EIKLLADLTE KHKKQEEQIP LTENELEVLQ
SKLKKEEGKV EKLMEVHKNE TNELRHRMEE LQHQMEPLQT KTNQLRSVID TTATEIQLIQ
QPLERAQKAL ETNVTAMNVA EENATRYQSS QKSMRKRESE LQKCIEEAKD DLHRFQKQEE
ELYHEYRIAR SKAEEIGNAM SSRSSRNRML TALLDASKPG KPLADAGLLG RLGDLGAIDS
KYDVAVSTAC SALNNMVVET TRGAQQCVDY LRRNNLGRAT FIILQQLEYM HRQSLRAFQE
PKSTPKVSRL FDLVRFQEEK YRVAFYFALR DTLVASDLDQ ATSIAYQGKQ CRYRVVTLDG
QLVELSGAMS GGGNRARSGG MSSSLPLSNA SQEECNQLER NAAAAHERLC KLRDDKAALE
HSLDQWCQEL ENIQNEIPKV TLSLQAVEKQ IQDFKHQKVT LEKELERVTS SQKNVKKSVK
DLETKKTSKI EALREVQEQI RVHEDQVDDI KEQILQIGGV KAQQAHVKVK EMTDKIDAKV
SQLTKLRVES KSGGKHCEKL RLSLEKQRSD QSELTLKMEQ LRERCAQVEE IGVKIVEEKE
KLQLQVEEKQ NVCRKTERNV SKMQKQVEKL TNSEIDLQNE LDNTRQTLEE HVRQEKYWKS
KLASVQATFI LEQEQYANVF DGNDDPAGNE VLAKKVTKCL KRQERKSETD SDEETEELKE
TSVLQLPILT AHELASFTQE ELQFDMALLT QQRDALKENV NMQALIEYQE KVQELQTRTS
ELEEATSNRD EKRLELERLQ RKRLDDFMKG FGVITLKLKE MYQMITLGGD AELELVDSLD
PFSEGVVFSV RPFKKSWKPI SNLSGGEKTL ASLALVFALH HYKPTPLYVM DEIDAALDYR
NVSIVGNYIK ERTRNAQFII ISLRNNMFEL ADRLVGIYKT DNTTKTVTIN PKAYQQPLSP
TESNEMESQN KEENGRKDGD KVKRQRTRSN KSDTTIALGD RTNR
//
