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
//