ID A0A094AQ07_9PEZI Unreviewed; 1880 AA.
AC A0A094AQ07;
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=V493_02386 {ECO:0000313|EMBL:KFY29398.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY29398.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY29398.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
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:KFY29398.1}.
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DR EMBL; JPJV01000929; KFY29398.1; -; Genomic_DNA.
DR STRING; 1420906.A0A094AQ07; -.
DR HOGENOM; CLU_001266_0_0_1; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000029327; 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; 2.
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:UP000029327};
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 1009..1030
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1238..1256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1288..1315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1335..1353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1400..1428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1434..1455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1588..1611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1631..1649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1688..1711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1723..1741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1772..1799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1819..1840
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 544..621
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..893
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1880 AA; 208594 MW; 2B185EE0DB144F19 CRC64;
MDANLEVGTA KDNETRNPDI MNDPEYATNF DGDDGMGDQD TCRICRGEAT AQEPLFYPCK
CSGSIKFVHQ DCLMEWLGHS QKKHCELCKT PFRFTKLYAA NMPRTLPLPV FVKHLAVHIL
KNIATWLRMC LVTVVWLVGL PWMMRHIWGL LFWFADGGWS FKHTQLSGHI PGQLRNSSEA
LAVDEKLASL AANGTSPASP LLGYPTTTPI MWEALTKLYE LVVSHRYNMS LPEPSVMGVF
NSIYSTMGLR EFGLPSNISN RTNGAMLLEP FPHFNQAIVV KHPSLLSEVF FLNNLTRSNW
VNRLIVTCLE GQIITVVVVV CFILIFLIRE WVVQQQPGIN MGAGFNAEFA NPERHPQDPI
DNLRNAERGD VAAIDRIIHD FEAIQDVIDR RAEERGEPVP ARARRRMGVF DANNANRGLA
EDASAAARNR DRQDPRTSDD EEDVADENLL AELPTSLGQI DAAEFIALWR RADGDADQIL
RLMEEEGLGN RLKYWKNALE ALRQGDAESG VVGSRRIGEI TNKNPGPESS QDMGESSRTR
DGPESRPEKS RLLIIDPAQQ ERQIGNTLYL KLKNLIPELA GKVTGMLLEL DTSELLDLVD
DDDALHAKMD QALIVYNRYL IEGDNEPILT NEKGKDQLLK SLVLRKAKMM HVERAEKVAD
IFLEMDFEDL LNIIEDDASF KTRTEEVFAF YELHLTQMRK VFPSQKAKEK YIAEHPGFMP
PKITPSSAES SKDGPAEPRK SHFTGPEKAP SALAMDYWDF DGLIPEPDTQ EQHTSTGSRA
QSQESSIERS TTSNGLNTDN ESEEVHASEQ DRHSTMQDDL VAGVDDAEET GGQSSGDGEQ
SDELTTPPDA TGVATPQGDD VSPPDTTGVA TPQGDDLPPL ENPPTPPGPG NEQQRNPPAG
IMGHVTDWLW GGVDGTAYEV EGDDEHVVHD IEAEEPFVPR NRREALDHAI DIGALNIDDP
RDLVAAVIDN QAEEMDPNDP NELDDGEDFD GIMELIGMHG PLMSLIQNAL FGAVLISLTV
ALGVWLPYNV GKLTLLLTAN PISTIKLPLK LVFKAAAVVQ DLTLVVIGYI SYALIRIVSI
LMSAFTIKPN SLFLSTSDTA NLALNSLKFA YSAGERVTGG FIGAMAQIPD SEIPAFSAAS
HESLIQIQSL FSKILGFVTG SSLAQAVTSN TGFESLPTFE TSHFKEAVTA VGQSIIACLS
ALPSTLAKSE TWVIRLNAHP REEPIDLALS YWDGTDRAYA IIAGYAAFIF LGAAYVRKGS
PFSSSQTGKD WESTIIDILN QAGGVMKVIL IISIEMLVFP LYCGMLLDAA TLPLFENATV
ASRAMFAITS PLTSIFVHWF VGTCYMFHFA LFVSMCRKIL RSGVLYFIRD PDDPTFHPVR
DVLERNVGTQ LRKITFSATV YGALVMVCLG GVVWGLSFAF IGVLPITWSS NEPVLEFPVD
LLFYNFLMPV AVKYFKPSDA VQAMYSWWFR RCARLLRLTW FLLDERMNDE EGYFPQWSLR
YSWKRMQGDD LFKDGKPNPE IPFVKNGRYV RTPDSDMVRI PKSRNAFLEV NENNQRIDGE
SDPEEGLHGT NSKLFKMVYA PPWFRTRIAG FIFLLWLFAA VTGCSLTLIP LVFGRWVFNA
ILPSEVKKND IYAFSMGINI LGGLVYCLIN LRPGVAALHS AVLANARAPA TILRKFLSLS
FHTLRLSYAY GAFVFLLPTL AAALVEFYFL IPLHTYFAPG SRHTIRFVQS WTLGLLFINL
ARRGILWYED SRPAAALRAV VRRGMLDPDV RLATRAFIAP LTLIALLGLA APMACAWIVN
ALGLLGSSEE AKTRVYRYAF PAMTAAFALV QGLAAAAEVV RGWRMSIRDE VYLIGERLHN
FGESRRKGSV GIPSMGRIET
//
