ID E5ACY3_LEPMJ Unreviewed; 1502 AA.
AC E5ACY3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=SMC hinge domain-containing protein {ECO:0000259|SMART:SM00968};
GN ORFNames=LEMA_P011220.1 {ECO:0000313|EMBL:CBY02335.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBY02335.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; FP929139; CBY02335.1; -; Genomic_DNA.
DR RefSeq; XP_003845814.1; XM_003845766.1.
DR STRING; 985895.E5ACY3; -.
DR EnsemblFungi; CBY02335; CBY02335; LEMA_P011220.1.
DR GeneID; 13286530; -.
DR eggNOG; KOG0964; Eukaryota.
DR HOGENOM; CLU_001042_5_0_1; -.
DR InParanoid; E5ACY3; -.
DR OMA; DQHQSMR; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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; 1.20.1060.20; -; 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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 813..925
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 934..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 484..546
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 642..669
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 704..787
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1343..1366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1502 AA; 170242 MW; B1CE010BD37D6BAD CRC64;
MASKVSDWIE FLTSRYVHIL MAISGAAPSL SSSPSPPANS HCFNIEISSQ RQHVGAWYED
IIRDNLKSEL LNKCTKKKSS DARGEICKKK AVEFSVTEDK IPEERRKDLQ AAFIDQIADA
YMIATTGKNC YLFDRKSTIR LFCSKVCIAQ VPRRHPPDRR GRVMAMEKRL HPMKVNIKFQ
GITDQGVFDC VHVTDAVDRN TRDNHIGPLK NAMRLQEVNV VVGCLSREVK VSCLNEECNT
AVFLQTCRSR LPDFTRLEGG QAGAIELLKA NTTPPRHDLN DFDAIALLHL SRLQSYPTLR
CFKSYKDQMQ IEPFSPKCNV IVGRNGSGKS NFFAAVRFVL GDDYHSLQRE ERQALLHEGS
GSAVMSAYVE VIFDNSEDRF QTGKPEFFLR RTIGAKKDEY SVNRKNATKA EVMQILESAG
FSRSNPYYIV PQGRVTALTN MKDSERLKLL KEISGSNVYE TRRADSIRLL AETDSKCSNI
DSVVASINER LDELEGEKEE LEAWSRNDRE RRSLMYTLKS REEADLEELL SKIDRLESEG
REIKESNEAA FVQNEADIAQ IDTDINKQRG DLELLAEDRA QSEQARKAAA LQKAKIELEL
KSLQDNQSVS QKMKKQRDAS VKALQKEIAT RKAELDRLVP KYNEQMEEEK ALRSQLLEVE
GQLKRLEEKQ GRTVSYTNKK QRDDALRAQI AEVNTNLSQR KAVLMQTNEE ITQLEIDINQ
YEKQIDELKS SIANEGDRSV DLAAKVQQAK DAQKAINDEQ TNLYREQNKV NRDLSSVQSE
LRTAENTFSR LLDHGTSRGL ESLRRYQAEG PLPGVHGTVA DLLEIDERYR SAAEAAAEGA
LFNVVVDNDT VSSRLIDRLI KDKGGRLTFI PLNRIHVPDM QIPTTGDMQP LLPKLKYDDR
YAAAVKHVFG KIVVCPDLSA CKSNATKYNV RAYTPDGDNA SRKGQYRGGY HDPSKSKIRA
YQKVSQLRAQ YEELRQRRQD IDRDLERKRQ QLTAAASEVR RREHEKNRGD NSYGPMRDEL
RAKQRALQET RDALAKKQTT ASELQSAINE LGAQQSDWEA EIASKFEKNL SSDEEQMLVT
LTSTVRDLRR QYARSKEART LLQSQKVEAE LDLNENLQPG LDSLLAQQGG PSGSTTQSAQ
LREQERALEA VNQTIQALDE QIGETDAQIE EIRAKLGELE ALRSEKESNN RQLAKAIEKQ
ELQMSKKDSD RNRHTARLAE VRRDIREIGT LPEDVHRKYA RWDTTKVTKE LTKANQALKN
FAHVNKKAFE QYENFTRQRR TLTDRRAELD TSRKSIENLI DVLDQRKDEA IARTFRQVAQ
AFHEVFQQLV PIGQGRLIIN RKSDRDVRGQ ASDDEDSEEE TQAKKGSKVA EYTGVSIAVS
FNSKHDEQQK IGQLSGGQKS LCALALIFAI QKCDPAPFYL FDEIDANLDA QYRTAVAQML
KKLSGQGGEN QSGGGQFICT TFRPEMVLVA DRCYGVSYSN KTSSIDVVER EVALDFVDGM
QK
//
