ID A0A420J7Z9_9PEZI Unreviewed; 1222 AA.
AC A0A420J7Z9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=GcM3_019007 {ECO:0000313|EMBL:RKF82907.1};
OS Golovinomyces cichoracearum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Golovinomyces.
OX NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF82907.1, ECO:0000313|Proteomes:UP000283383};
RN [1] {ECO:0000313|EMBL:RKF82907.1, ECO:0000313|Proteomes:UP000283383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG3 {ECO:0000313|EMBL:RKF82907.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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:RKF82907.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCBQ01001972; RKF82907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420J7Z9; -.
DR STRING; 62708.A0A420J7Z9; -.
DR Proteomes; UP000283383; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 1.
DR Gene3D; 1.10.287.1490; -; 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 Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000283383}.
FT DOMAIN 502..617
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 36..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..345
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 397..452
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 707..796
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 829..912
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1011..1052
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 36..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1222 AA; 140019 MW; 7941DCED94463EBF CRC64;
MDAISFVLGI KSSHLRSSHL RDLVYRGRVL KTSKVGTEDF GDKDVPDPSD KTDKITESPT
SENIDPKSAW VMAVYEDDAG DKQKWKRTIT NQGVSEYRIN DRVVTAVQYN EALESENILI
KARNFLVFQG DVEAIASQSP KDLTKLIEQI SGSLEYKAEY ERLEEEAKRT AENQLYNLSR
RRGINSEIKQ YQEQKREAEA FQAKANERDL AIITHILWEL YNYQLEMNNS IASIEENRET
LKEYRRRVEK YEKSVEEARQ AQAKVSKDVS RIERTIKKKE REIEGMENNL VPIDEKLEIT
EVEIGKTRKK IESLSNEQEK HNREVLKLQK DLAAVEKAEK ESERKWQEIL KKQGKKLSDE
DFKEYNSLRS QVAAKTAAQK AKLDNYTRQM KTDQVALNSL KVKLTASQVA VDRLQSEVDE
ISERKASTEA DVKETMKQVE SKKKELNQLI SERIRVNQLH TEKEEKLRTV LKEIADADAG
RRKSLREQKI KETVAALKRL YGGVRGRIGD LCKPKQKKYD EAVITALGRD FDSVVVDTEK
TGTECVQYLK DQRANPMTFI PLDNIKVSAP DANLKGLPKA RLTIDTIDFD PSIERAMAYA
CGNSIVCDDL AAAKHICYEK HIHVKAVTLQ GYVIHKAGLM TGGRGPEKGD KRKFDDQDID
KLRAQVTRFQ NEIDALPDPH RRGIAEEALQ NELAGLDQRF LYTKNELAAF EQNLTSKKRQ
LEFEQGQLKE IQPKFNSKEI ALHSIMETVA EAQKEVDQEQ DELFAEFCKR LNYSNIRDYE
AQQGSFEQQN AEERNKFSKH KASLQNQINW LKGQYDDVTR RITVISSRVE SLEAQILTYQ
QDKQKLDEAI NVGRAQITEL EDELHKYKEK YAQKTTKVNQ TRSDLTKQNK KLEEINKEIS
VLEMKAQRKS VERYSLLRRC KLEQISIPLK PGSKKLDSLP IEENSLQTDP EAMDIDEDDA
PSGRKIEDYG IVVDTDRLDE DLTRSSDEET GEKLLQRIND LNAELEKLNP NMRATERLDS
VEIRLKIAER EFENARKSAK KAKEEFELVK EKRCDLFNKA FTHISEQISH VYKDLTRSST
FPLGGQAYLD IEESDTPYYS GIKYHAMPPL KRFRDMEHLS GGEKTMAALA LLFAVHSFQP
SPFFVLDEVD AALDNANVEK IKNYIREHAG PGMQFIVISL KTGLFQGSES LIGVFRDQDA
NSSKTLTLDV SLSFSSEALA ST
//
