ID W7I3L7_9PEZI Unreviewed; 1202 AA.
AC W7I3L7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=DRE_03729 {ECO:0000313|EMBL:EWC46967.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC46967.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC46967.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC46967.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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; KI966413; EWC46967.1; -; Genomic_DNA.
DR AlphaFoldDB; W7I3L7; -.
DR HOGENOM; CLU_001042_5_0_1; -.
DR Proteomes; UP000024837; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR CDD; cd03272; ABC_SMC3_euk; 1.
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; IPR041741; SMC3_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 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 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:UP000024837}.
FT DOMAIN 522..634
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 286..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 186..220
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 399..475
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 680..777
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 823..930
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 978..1005
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 286..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 138123 MW; 5F07CC393CF6F305 CRC64;
MHIKQIIIQG FKSYKDQTVI EPFSPKHNVI VGRNGSGKSN FFAAIRFVLS DAYTQMGREE
RQALLHEGSG QAVMSAYVEI IFDNSDERFL TGKEEVVIRR TIGLKKDEYS LDRKSATKTD
VMNLLESAGF SRSNPYYIVP QGRVTTLTNM KDPERLTLLK EIAGTQVYEQ RRAESLKIMD
ETSMKRDKID ELLKYIEERL DELEEEKEEL RGYQENDREK RCLEYTILHR EQLEINSAVD
QIEEGRARGA ENNDDALEKF REREKEIEQL IKQLSKVKQE ISLRKTEKKQ LDQERREHLK
SNAQLDLAVR EYTDNQASRD QSRQKHKQEM NRLQSEIASH QKELEKLLPE YNARKADEAK
VRNELDQARA IQNRLHAKQG RNANFSSKKE RDTYLKGDIA QINANLTRRQ TARENLEKAI
TSVEEKIQAL EAELQQTRSM RDNRAAAVNE LQDKLRGAET NWDKLNDQRK TLLREDNRVS
TTLGALWDDL KRAESSLSHM MDRDTSRGLQ SMRAIRAERN MTGVYGTIAD LCQVEDVYRT
AVEVTAGNSL FHVVVDNDRT ASELVEAIAQ RGPGRITIMP LNRIRNRPVS YPDAVDAIPM
LEKMSYDKKY HKAFDHVFGK TIICPDLHIA SQYARSHGLS AIDLEGKSSD KRGALSGGYY
DTQRSRLNAV RQVNDCQEAY ENAFQQSREV KDQIKKLDQE INQAQGNVNQ AEFQLNRLEK
QFHGIPELLQ QKTSQLSRLR DDLRKMELDR DNSDVELARL NEQLAAHKTE LASEFKKNLS
SDEEQSLSQA LDTIQKLGKA LADVSTKRAD VEQMKTNLES MLHENLEVRL DQLKATSEEG
ESESTGGIAQ GRRITDLQAD LKRIKKATSS VEQKLQEIED SIEKYSAEIV KLEKAIASRQ
SEQEQEATNI EKYQKRIEKS MAKRSMLVEN AAEVQRKIRD LGVLPDEAFE KYTKFKSDTL
VNKLKKVHEN LKKFSHVNKK AFEQYNNFTK QRDTLRKRRE ELDESQGSIE DLIQVLDQRK
DEAIERTFRQ VSKNFAEIFE KLVPLGRGRL VIQRKADSRN RREEEDSDDE GGRSSVENYL
GVGISVSFNS KHDEQQKIQQ LSGGQKSLCA LALVFAIQQC DPAPFYLFDE IDANLDAQYR
TAVAQMVKNL STQGGQFICT TFRREMVLTA DQHYGVTFLN KMSSIDLVSK DEALAFVDGQ
KQ
//
