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Database: UniProt
Entry: A0A094F5M3_9PEZI
LinkDB: A0A094F5M3_9PEZI
Original site: A0A094F5M3_9PEZI 
ID   A0A094F5M3_9PEZI        Unreviewed;       766 AA.
AC   A0A094F5M3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY86094.1};
GN   ORFNames=V498_07602 {ECO:0000313|EMBL:KFY86094.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY86094.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY86094.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the oligopeptide OPT transporter family.
CC       {ECO:0000256|ARBA:ARBA00008807}.
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:KFY86094.1}.
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DR   EMBL; JPKA01002133; KFY86094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094F5M3; -.
DR   HOGENOM; CLU_017375_6_0_1; -.
DR   Proteomes; UP000029270; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035673; F:oligopeptide transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049482; ANM3-like_C2H2_Zf.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR004813; OPT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11006:SF116; PROTEIN METHYLTRANSFERASE; 1.
DR   Pfam; PF21137; ANM3_C2H2_Zf; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   Pfam; PF03169; OPT; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01015};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01015};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        637..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        697..722
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        742..760
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..132
FT                   /note="Protein arginine N-methyltransferase 3-like C2H2
FT                   zinc finger"
FT                   /evidence="ECO:0000259|Pfam:PF21137"
FT   DOMAIN          260..357
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13649"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          160..187
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        35..53
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  85969 MW;  AF7D7AE850AD8BD1 CRC64;
     MENATDLAAS QGPKPADMSA ATRSPSHSGS DTSDIDLNEE EEEGWEDAEP QEEQDQIVSL
     FDDKVFTDVP SMLAHCKEKY GFDFLEIRNK FSLDFYGTIK LVNYIRTAVQ NGQTTLPDVA
     KADFEDDKFM MPVLQDDALL FNLDDLPPAS KQGDEPIADE RNLLVRVAEL EEELRKTQFQ
     FEDYRSVVKK TLTDRWNDNS TDQSTAAPGP SAEKRDDDSH YFTSYSYNDI HETMLKDTVR
     TDAYRDFIYQ HKHLFKGKVV LDVGCGTGIL SLFCAKAGAS RVIAVDNSDI IDKARENIFN
     NGFADTITCL RGKVEEVTLP VDKVDIIVSE WMGYCLLYEA MLDSVIWARD KYLKPDGLMV
     PSHMNMWVAP VSDAEYVADH FSFWRDVYGF DMKAMMAGIR EDAQVLHMPG STICGDAYPF
     LQLSLHTTTG KDLVFTRPWK TTFTNDIDRL DGFDIWFDTF FMPTGGDAVP LDARAEDWTK
     QEQKGIAFTT GPFGKETHWR QGVMFIDHEG EKSSRSFAKG DTLEGSLEYA VPDDNSRALD
     VKFSWASGPD KETTAQTWKM RAGLSNAIAE KLLFPLNPQN TTKMAPDRGR TIEPAYQTIS
     TSDNPVIDDE LDDRGMQNRR SEELDFLAQH GHEPQNFTLR GILVGLGVGL VICFSNMYFG
     LQTGWISSMS MPSSLIGFAF FKTLSKHLDI PFTPVENVLV QTVAGSMGTM PLGCGFVGVM
     PALNYLLKPE EGGPLFLSLW KLILWSLGLC FFGVVFAVPL RRQVNH
//
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