ID A0A093YU29_9PEZI Unreviewed; 1868 AA.
AC A0A093YU29;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=V492_06136 {ECO:0000313|EMBL:KFY08546.1};
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:KFY08546.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY08546.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY08546.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KFY08546.1}.
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DR EMBL; JPJU01002213; KFY08546.1; -; Genomic_DNA.
DR STRING; 1420902.A0A093YU29; -.
DR HOGENOM; CLU_001266_0_0_1; -.
DR Proteomes; UP000029299; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF63570; PABC (PABP) domain; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000029299};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 995..1016
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1224..1242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1274..1301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1321..1339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1386..1414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1420..1441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1574..1597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1617..1635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1674..1697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1717..1735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1758..1785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1805..1826
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..95
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 42..89
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 540..617
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..883
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1868 AA; 207447 MW; 2E41BC0619E2A10E CRC64;
MDTNLVVGSA KDDEARKPDI MNDPEYATNT DGDDGTGDQD TCRICRGEAT AQEPLFYPCK
CSGSIKFVHQ DCLMEWLGHS QKKHCELCKT PFRFTKLYAP NMPRTLPLPV FIKHLAVHIL
KNIATWMRMC LVTVVWLVGL PWMMRHIWGL LFWFADGGWS FKHTQISRNV PELLRNSSEA
LAVNEKLASL AANGTSLATP LLGYPTTKPI MWEALVKLYE LVVSHRYNMS LPEPSIMGVF
NSIYNTMGLR EYGLPGNISN RTTDAMLLDP YPVFNQAVVV KHPSLLSDVY FLNNLTRSNW
LNRLIVTCLE GQIITVVVVV CFILIFLIRE WVVQQQPGIN MGAGFNAEFA NPERLPQDPA
ENLRNAERGD VAAIDRIIHD FEAIQDVIDR RAEERGEPVP PRGRRRLENN ANRGFADDST
AAARNFEQQG ARTPDDEGDV PNEALLAELP TSISQIDATE FIALWRRADG DADQILRLME
EEGLGDRLKY WKNALEALRQ GDAESGVVGS RRIGGIPNKR LQPEIREERG ESSRKGDGPE
SRPEKERLLT MDPAQQEQHI GNILYPKLKV IIPELAGKVT GMLLELHPFE LLDLVDDDDA
LFAKMDEALI VYNRFLMEED NEPILTNEKG KDQLLKELVL RKARMMNVER AEKVADIFLE
MDIEDLLSII GDDATFKTRT EEVFAFYELH LTQMKKVFPS RKAKDKYLAE HPEFLPPKIT
PSTPRAGPAE DPTTHTSHSR PRSVSDGAQR APSSLARDYW DFDGLPDSQE QDTSMDTEAQ
AQEPSGDRST TANGLDADDE SMMARASEQD HHPTTQYGVD SGIDVAEGSR RQNIGGREQP
DEPATPVDGT AVATPHGDDA PPHGDDAPPL ENPPPPPGQP RNPPEGIMGH LTDWLWGDVD
GAAYEVEGDD EHVVDDIEAE EPFVPRNRRE ALDHAVDIGA IDLDDPRDLL AAVIDNQAEE
ADPNDPNELD DAEDFDGIME LIGMHGPLTS LIQNALFGAV LISLTVALGV WLPYNVGKLT
LLLTANPIST IKLPLKLVFK AAAVVQDLTL VLIGYISYAL IRIVSIVMSS FTIKPNKLLL
STSDTANLAL NSLKFAYSAG ERVTGGFIGA MAQIPDSEIP AFSAASHESL IQIQSLFSKV
LGFITGSSLA QAVTSSTAPE SLPTFETSQF KEAAAAVGQS IVAWLSALPA TLAKSETWVI
RLNAHPRAEP IDLALSYWDG TDRAYAIIAG YAAFIFLGAA YVRKGSPFSS SQTGKDWEST
IIDVLNQAGG VMKVILIISI EMLVFPLYCG MLLDAATLPL FENATVASRA MFAITSPLTS
VFVHWFVGTC YMFHFALFVS MCRKILRSGV LYFIRDPDDP TFHPVRDVLE RNVGTQLRKI
TFSATVYGAL VMVCLGGVVW GLSFAFIGVL PITWSSNEPV LEFPVDLLFY NFLMPVAVKY
FKPSDAVQAM YTWWFRRCAR LLRLTWFLLD ERMNDEEGYF PQWSLHYSWK RIRGDDLFKD
DEPHPEIPFV KNGRYVRTPD SDMVRIPKSR NAFLEVNDKN ERTDGEPDPE EGLHGTKSKL
FKMVYAPPWF RTRIAGFIVL LWLFAAITGC SLTLIPLVFG RWVFNAILPS EVKKNDIYAF
SMGINILGGL VYCLINLRPG LSALHTAAVS NARAPAAILR KLGAVSLRTI RLSYAYGAFV
FLLPTLAAAL VEFYLLIPLH TYFAPGSRHT IRFVQSWTLG LLFINLARRG ILWYADSRPA
AALRAVVRKG MLDPDVRLAT RAFIAPLTLI AVLGLAAPMV CAWTVNALGL FGSSDEARTR
VYRYAFPAMT AAFAQVQGLA AAAEVVRGWR MSIRDEVYLI GERLHNFGES RRKGSAGVGI
PSMGRIET
//
