ID I4YHP8_WALMC Unreviewed; 934 AA.
AC I4YHP8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EIM23490.1};
GN ORFNames=WALSEDRAFT_59229 {ECO:0000313|EMBL:EIM23490.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM23490.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM23490.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000256|ARBA:ARBA00008593}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH668224; EIM23490.1; -; Genomic_DNA.
DR RefSeq; XP_006956168.1; XM_006956106.1.
DR AlphaFoldDB; I4YHP8; -.
DR GeneID; 18473235; -.
DR KEGG; wse:WALSEDRAFT_59229; -.
DR eggNOG; KOG2277; Eukaryota.
DR HOGENOM; CLU_313565_0_0_1; -.
DR InParanoid; I4YHP8; -.
DR OMA; MQETETH; -.
DR OrthoDB; 170176at2759; -.
DR Proteomes; UP000005242; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR CDD; cd05402; NT_PAP_TUTase; 1.
DR Gene3D; 1.10.1410.10; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR PANTHER; PTHR12271:SF138; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005242};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..78
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 245..312
FT /note="PAP-associated"
FT /evidence="ECO:0000259|Pfam:PF03828"
FT REGION 366..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 102328 MW; 249D9F1B00EF1A6C CRC64;
MREALSQDLT GCLFSFILPL LPTAEEYAIK EQTRLLLEKL IDRVSPGARL IAFGSMANGF
ALRNSDMDLQ CILDPASEPL SSSELTTIVG ELIRHETNFH VKPLPKARIP IIKLTLAPTP
ALPYGIACDI GFGGQLALEN TRLLLGYASI DPPRLRTLVL FIKVWSKRRK INSAYRGTLS
SYGFTLLVIF FLAHVKRPPV LPNLQRIPPL RPVSPESASY EGRNIYFFDD VALLRQEWSS
ANTQSVGELL WEFFRFYAKD FNYTHDVISI RTEGGILSKD AKGWVQDLEV DGASEFARDR
NRLCIEDPFD TTYNVARTVT ADGLYTIRGE FMRASRMLQT VGKTDILPSQ VLVDLCEERE
EALVPAPFSA GNRTPRPLTN PSLGPTLGPS LHPPPSLQPP PIVQTHSHNT HMTQTASQQS
YSPTQSQSSI FPSRKVSDQI SSPPATFNRR RQSSSHAQAL SIALNVAQNE RMRNAHEEHL
MYQHPQSHTK PLGSAFWEAE NLVSDESTRT EQSSSIPRRA SSGANVGPTW LSRLHERKYA
PKHHLKATIP NVSGPYADAT TQAEIGWPPV PIPAPLRHSP RLANAALHSR ASSSAAAVAA
AATTANSVNA SPSQLIQKQI AANNSDMKIR VPTFVTNGAG QQIRITPSTF TQPSESGTPT
NSPPLSTTST LSAPVTSTAQ PSRNGEEKEQ TVGLGLGFPP FPLAQRYTFG QNTFVASESL
TTSALTLAAD VRVPPPRMSA RRWLKLQKQA TARNTQTPSK ATTTTATTPS TTTGRKLPTR
SRSVPSTPRV SNKTSRISSR EFEKSVGGGR TYSRIIPNAT LPLLDDKAGD ATNVDEDTPP
FKPNLTTGLE EGFPALSNNN SQGQFKTSSS LNNLYSASLQ ASRKKQQQQQ QSHKEKRRSA
SVGSETSKNK SNNSKKKSNK DKQHQRNNSS QSTK
//
