ID A0A093YUD6_9PEZI Unreviewed; 1392 AA.
AC A0A093YUD6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Sm domain-containing protein {ECO:0000259|PROSITE:PS52002};
GN ORFNames=V492_06052 {ECO:0000313|EMBL:KFY08651.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY08651.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY08651.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY08651.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000256|ARBA:ARBA00010304}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY08651.1}.
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DR EMBL; JPJU01002166; KFY08651.1; -; Genomic_DNA.
DR STRING; 1420902.A0A093YUD6; -.
DR HOGENOM; CLU_005260_4_0_1; -.
DR Proteomes; UP000029299; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd01725; LSm2; 1.
DR CDD; cd16273; SNM1A-1C-like_MBL-fold; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR Gene3D; 3.40.50.12650; -; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR InterPro; IPR016654; U6_snRNA_Lsm2.
DR PANTHER; PTHR23240:SF6; DNA CROSS-LINK REPAIR 1A PROTEIN; 1.
DR PANTHER; PTHR23240; DNA CROSS-LINK REPAIR PROTEIN PSO2/SNM1-RELATED; 1.
DR Pfam; PF07522; DRMBL; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS52002; SM; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000029299}.
FT DOMAIN 389..463
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 19..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1392 AA; 153152 MW; D8C4B59223176B7F CRC64;
MLVGSLLFSR PRVLYRTDVM SNGKGKGPAK AAGEPEDSVI SNETTTTSSN SVLDRVAASA
IGLTRNAFGT TNSNEVNDSA TAALATSGKG QGQPSGSGQG SVWAESSQTS RQQPSHGSHQ
PGPQVFRSSH QEQHTASAEA EFSSFLDGID TFGPSTEDGT RPVLEEEDTT TFGSAPAAQI
PGHNSEPYQS SSVKEQESRD GEAVLDILSE RRQEVDYFAP QNIEDEIEEW RLTDDQTAKI
KDIVKELFPS SHVHTGADVS DPLNLQPDTF RSSDMSTWLP DEYAQESYSH FGQVLPQEEA
STLWIEQWEG VLTRYADEVW GGLLPLVREA RDEIEEIKQA EDPAEHRPKA LRRQQLLPTT
AAGLGEHAIL PLCSSLQLPQ QPSIAIKMLF FSFFKTLVDQ EVTVELKNDI QIRGTLKSVD
QYLNIKLDDI SVVEEIKYPH LSSVKNVFIR GSVVRYVHLP GAVVDTQLLE DATRRAPSTL
GPWQLLPCDA MFRKPREDAR SDISLKPSTG RPPTPPDGRS TGRTGSTTAM GGPSSSTKPL
TPRPNTKTNV RRASSQTTKK AFNAKTPAKA NGSILNFFKK VEAEDDGGLF LSGGRYEVSP
TKKGLAVRSP TIDDIDGATY DDLYSAPDDT GRYNESGQST KRRRTSDGRT DSQARRMNTI
VYSEDKQLAT EDLNLPLHAG TDVKAEIPQA CTPPPPDAEN PQPKRIGAFL DDSDSEDDEA
VVGIDVRSRD TAIEGNVALS SEGLLGRSKI VKPEADDESY LFEDTPDVST DQPAGGQIRE
EASYGEYGAF EDMDEYPDIE DEFADGEEFM ERKWMEEQEK FENADESEIN GPLRSDVFGM
PDESSVSKCP ICDSDLGGNT TDEITRHVNA CLDGNPEPPP PATVTKIKAE HGSDRFSKAS
IARSGQANPF QLDAPDPSTS SAFSKLMSSK AEDAAWETAA AAETSAKGKP AYKRVCPFYK
IMPGFYICVD AFRYGAVQGC NAYFLSHFHS DHYIGLTASW CHGPIYCSKV TGNLVKQQLK
VDPKWVVTLE FEDMAEVPNT HGVSVTMIPA NHCPGSSLFL FEKVVGKGPK PKVQRILHCG
DFRACPAHVE HPQLMPDIVD SITGKTRQQK IDVCYLDTTY LNPRYSFPSQ DDVVQSCADI
CVSMSRDKGE LTWERAGKER AGASMAKFVD TGMKSEDAAT QPRGKLLILC GTYSIGKENI
CLGIARALDC KIWAPPRKQK ICAALEDPEL TSRMTTDPHK AQIHMQSLME IRAETLQDYL
NSLKPHFSRI VGFRPSGWNY RPPNSRLVDS PSVAAVLTGE NWRSRYTMAD LQPQRGSTRE
AACFGVPYSE HSSFRELTMF CCALRIEKVV PTVNVGSAAS RAKMKVWIDR WLTERRKKGV
IRFGEGKDMV KW
//
