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Database: UniProt
Entry: E3QHU0_COLGM
LinkDB: E3QHU0_COLGM
Original site: E3QHU0_COLGM 
ID   E3QHU0_COLGM            Unreviewed;      1549 AA.
AC   E3QHU0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=GLRG_05572 {ECO:0000313|EMBL:EFQ30428.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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}.
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DR   EMBL; GG697349; EFQ30428.1; -; Genomic_DNA.
DR   RefSeq; XP_008094448.1; XM_008096257.1.
DR   STRING; 645133.E3QHU0; -.
DR   EnsemblFungi; EFQ30428; EFQ30428; GLRG_05572.
DR   GeneID; 24410937; -.
DR   VEuPathDB; FungiDB:GLRG_05572; -.
DR   eggNOG; KOG0996; Eukaryota.
DR   HOGENOM; CLU_001042_4_1_1; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000008782; 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   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; 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|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008782}.
FT   DOMAIN          798..911
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1144..1172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1228..1303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          466..493
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          575..651
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1314..1375
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        9..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1250..1275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1276..1290
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1549 AA;  172925 MW;  9BAC26478B8F3C6D CRC64;
     MSTRPRRATR RQAIVDSSDD DDEIANVTKR ESSEEEFAPE PSKSPVRRPT RARKTKSAAP
     AAAAPAAPTT TTAPRRRGRP KRNAEPAPSE APSTLEASTV LEEPSTVHEP SIAEQDAVTE
     EPSEEPSAVE EPSTLEAPTT LDVAPSIEPT EVFDPDQTVT KTEPQSSPRS PRKSVASRAS
     TKSASPSAIS KKKPSATPEP SRRQAEPLAD ITAASVNEQT STPDDTQTPF KPVRAMDTVL
     EKPMDIVLKS RNLAVPVVED TTPKPRLVIS YLILTNFKSY AGRQEVGPFH GSFSSVVGPN
     GSGKSNVIDS LLFVFGFRAS KMRQGKLSAL IHNSAQHPNL DYCEVAVHFR EVMDQPGGGH
     EVIPDSDLII SRKAFKNNSS SYYINGKTSN FTSVTTLLRD RGIDLDHKRF LILQGEVESI
     AQMKPKAANE HDDGLLEYLE DIIGTSKYKA PIEESAAEVE TLNEICMEKS GRVQHVEKEK
     NSLEDKKNKA LAYIRDENEL TIKKSALYQL YIGECNDNLA VTGEAISQMQ AQLDDELEKH
     HGSEKVIKEL QKAYSRGNKE FEVQAKETEA LVKEMAKFEQ ERVKFDEKKK FLNDKQRKLE
     KTIANAEKSA VEAEETITQC TQEIEDRAKE IASLEVRVQE EEVELAAIRD SLKGKTQKFS
     DQIAAKQKSL EPWKEKINQK QSAIAVAQSE MNILEEKANA GSVAISETEA KIAAIEDART
     AKAKELKQCQ AEKAALEEEA KEVEQELARF NAHEPKIRSK VSNARQKADE ARSSLSKTQT
     QGNVLTALMR MRESGRIDGF HGRLGNLGAI DQKYDVAIST ACGALDNFVT DTVEAGQQCI
     EHLRKTNLGR GNFMCLDKLR VRDMKPIQTP ENAPRLFDLV NPKEEKFRPA FYHALQDTLV
     ANDLAQANRI AYGAKRWRVV TLAGELIDKS GTMSGGGSTV KRGLMSSKLV AETSKEQVAK
     LEEDRDVLEE KYNDFQEQQR QLETRLRELN EQIPMLDTKM QKITLEIDSA ARNLADAHRR
     IKELSKEHQP SASDDKRIAA LRKEIAKLEK EVEKLHDETS GVEEEIKALQ DKIMEVGGEK
     LRLQRANVDS LKEEIVSQNE ETSNAEVRKV KAEKQKTKLE RDHAKATKEI EAAIRDLEKL
     DHEIENQGER AESLQSQVEE AEEGLADKKR ELSSLKAELD EKTTELNATR AIEIEMRNKL
     EENQKTLAEN QKRLMYWNDK LSKLTLQNVD DLTGTSSSAP KPRAPAPAPV RGEEGDESEG
     DGDRTVTQDA VDGDDSRQSE VEEDDEEPEQ PERPSSQPQE LPVYTPDELA DMSKEKLKGE
     IAALEEKTQN VNVDLGVLAE YRRRVEEHAA RSSDLQSAVD QRDAAKKRCD ELRRLRLEGF
     MEGFSTISLR LKEMYQMITM GGNAELELVD SLDPFSEGIL FSVMPPKKSW KNISNLSGGE
     KTLSSLALVF ALHHYKPTPL YVMDEIDAAL DFRNVSIVAN YIKERTKNAQ FIVISLRNNM
     FELAARLVGV YKVNHMTKSV TIENQDYIVR RGGQQGQTQT ATQQTTMAR
//
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