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Database: UniProt
Entry: A0A194VFU0_9PEZI
LinkDB: A0A194VFU0_9PEZI
Original site: A0A194VFU0_9PEZI 
ID   A0A194VFU0_9PEZI        Unreviewed;      1199 AA.
AC   A0A194VFU0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=VP1G_10002 {ECO:0000313|EMBL:KUI62875.1};
OS   Valsa mali var. pyri (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI62875.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) 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}.
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DR   EMBL; KN714840; KUI62875.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194VFU0; -.
DR   STRING; 694573.A0A194VFU0; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000078576; 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; 1.20.1060.20; -; 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:UP000078576}.
FT   DOMAIN          523..635
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1050..1072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          187..217
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          261..504
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          674..808
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          872..920
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          954..981
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1050..1064
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1199 AA;  136771 MW;  6E5190BB7EC5700D CRC64;
     MYIKQIIIQG FKSYKEQTII EPFSPGTNVI VGRNGSGKSN FFAAIRFVLS DAYSNLSREE
     RAALLHEGSG SAVATAYVEI IFDNEDRRFQ TIDKDDVAIR RTIGHKKDEY SVDKKVWAKK
     EVMQLLDTAG FSRTQPFYIV PQGRVTALTN MKEKERLNLL KEIAGTHLYE DKRAESLKIM
     IETNNKREKI DELLAYIKER LSELEEEKEE LRGFQNSDRE RRCLEYAYYY QQQTHFEEAL
     EELGVAMKDG GENDTEQRVA FSKGEKAIAE MESNLSSLQQ QLNLLKIDRR QLEEDRREVA
     KARGKAELKV KNLAESQSAR DQAKRQHDAE LDAVREEIKA KEAELNNLTP ELEKRKKTEA
     EAKLALDTAE NRRMRLLNKQ TRSSQFKNRG ERDAYLQKEI DDLNLTIAKQ KANFIDAEEE
     VKSVTASINN LENSVADLRG QLENWGGGRQ SLIDQVAQAQ ELLDNLNEER KKLRREDDKL
     DTVLAKVREE KDRAERELSH AMDHATAKGL ATLRQLAREK DISGAYGTLA ELMEVPEAYR
     IAVEQTAGSS LFHYVVDNEK TASMLATELY KRHGGRITFM PLAQLKPRRV NMPRASDIVP
     LINKIDYDPQ FENAFQQVFG KTVVTNNLQI GGQYARSHNV DAITSDGDTI NKRGVISGGY
     IDTRRSRLEA VAAVNQWRDK YDEILTQVED TRRQMEQKDQ EITRALGELQ KRESQLRRAD
     GGLEPLKIEL RSKLSQLERE REHLDAAISR RDQVDRNMHE FGANLEAMEA ELASDFKKAL
     SSHEEQELES LADQAQNLQK QWNEAAKARR ELSTRKQILE TDLRQNLRLK EDQLSSLAFE
     NSTAADGGSS YGDSQKELKK IQKATASIGK KIEQNEAQAE DLSSQISEVN SAMETKQQEL
     QELARHIERH QKRIEKSAQK KHLLTGQIEE MAKSIRDLGV LPDEAFTKYI KLKSAEITKR
     LKNVNEKLKK YKHVNKKAFE QYNSFTTQQE QLLKRREELD ASQASIEELI AHLDERKDEA
     VQRTFKQVSK EFSEIFERLV PAGRGGLVIE RRADKRHGNP EDSDEQEGDG VENYTGVGIK
     VSFNSKMDEQ QKIQQLSGGQ KSLCALCLIF ALQRTESSPF VIFDEVDANL DAQYRTAVAG
     LLQSLSKEAG TQFICTTFRP EIVQVADKCY GVTFRNKSSG IGCYDTEDAL EFVDGQAPR
//
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