ID A0A179F7U2_METCM Unreviewed; 1634 AA.
AC A0A179F7U2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=VFPPC_02231 {ECO:0000313|EMBL:OAQ61233.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ61233.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ61233.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ61233.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ61233.1}.
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DR EMBL; LSBJ02000001; OAQ61233.1; -; Genomic_DNA.
DR RefSeq; XP_018139042.1; XM_018281915.1.
DR STRING; 1380566.A0A179F7U2; -.
DR GeneID; 28845909; -.
DR KEGG; pchm:VFPPC_02231; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000078397; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 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:UP000078397};
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 117..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 737..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 871..894
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 925..943
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 975..1002
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1022..1040
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1081..1104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1124..1142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1309..1332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1352..1370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1411..1434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1512..1531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1569..1585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..89
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 36..83
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1634 AA; 180616 MW; 05BAD8D6C10A3A94 CRC64;
MNDPVHTPQR RELFPSIPED RSKSSSQQPD AALAICRICR GEGTSAEPLF YPCKCSGSIK
YVHQDCLMEW LSHSQKKYCE LCKTSFRFTK LYAPDMPQSL PVHIFLEHMA KYLVRNVLLW
LRAVVTISVW VCWLPYFMRV VWAFMFWVSD EGLGAGPFIS SPPSPSAAIP LDPTGITTAG
HSQIFSPQSC SLNEQVVFIN SKVGSQSPTL LSDVGFLRNL TRSSTVNRTV ITVVEGQIIT
VLVIVCFILV ILVRDYVVQQ QPEINMRAAF ADQENNNPPA PVQQPLEPEL DHDNPPESDG
LGSDDETLDA GAQVNDPFEI NLDRHADIDE PTHSPAPADM DETMEFEPRI PDFATELRDP
QDAISGDLEV EGLDDRASVI DYLRVYRLAG GNLEKILQIV EEEGLEDKLR YWVDVTRRSI
REREVTEDSS GPSNFQANSQ NKIPMSPILD LNEFGAVDQP AQTSDRQGAA QDRSKGKERE
WLPMSPDLSP SPTTPKSNVA SGPSRPRARS DGPEPNNTTN PLANNSWTFN SLPTADEEDQ
ESTDQGHDSV LPSTMPIQID DSGMSGLNEG PDDALHSDHD DDAASVNHDS DSSHVGRDEP
AVPEPEQRGL VGRVANFMWG DLDQRQVVDE DQHEAAINGA AVAGEEGAAE DPWIDVAIAE
PADANGEINA GEVDAAAAAA GMDAEAMEDL EDFEGVMELL GMRGPIAGLF QNAIFCAVLV
SVTIFTCIFI PYNIGRFSVW IIANPILLVR MLMGLSKVIQ DAAMMVGGFG SWCALNIIDM
FTGIIGGAMG AQVVSARKAS WGLWTGAGTR VVEYALMEFP LTASEVQNFS AISHDALNTV
KGNIGWVLGQ ADHGLKALAG PDFTALVDGR FVAAASIIIQ SSISSIISWV SVLFDPSSWV
IDLGEVATKA PVDAGLAYWS GLDRFWAILV GYMTVFAVGA LYLKRGSPFS RGDMMQAWEA
GVIDSLHQAS GIMKVILIIS IEMLVFPLYC GLLLDGALLP LFEDTTFKSR ILFTCNYPLT
SIFVHWFVGT GYMFHFALFV SMCRKIMRPG VLYFIRDPDD PEFHPVRDVL ERNLTTQLRK
ILFSAFVYGA LVIVCLGGVV WGLYYTMPGV LPIHYSSNEP VLEFPVDLLF YNFLMPLAVK
FFKPSDGLHA MYTWWFRKCA RGLRLTYFLF GERRIDEEGI LQLSSETKSK VPPHKWLLLE
LDENNTVIPK TWRDTFDGGD AKPNPSISRQ EMKDMRHKKA HLVNTGQLEK TGRFVRAPAS
DRVKIPKGQK VFLTVSERNH RKDGKDDTGL YKSPQYQLVY VPPNFRARVF LFILFIWLFA
AVTGVGFTIA PLVLGRTMFK TLIPAHIRTN DIYAFSIGIY VLGSLAYGLF RLRQLSAKFR
EWTGKLRNEI TSGNSSKRAF SGMAHGAKLS YAYFFLLIVF PLMVSMLLEL YVIIPLHTYM
NPPTQQQGMA PYPGKDGESG RHTVRIIQSW TLGLLYLNLA TRLITSLFPD TRVAIAVRTV
MRRGYFKPDV EVLTRAFIVP CIVVSTLATF GPPTTARLLL RFGLVSPAQL MGASAGAPNT
ANLSLIFRYS YPAAAVAAVL VRYAVGMTRV FNRWTAGVRD EAYLIGERLH NFGAATAGSR
KARKAWGAAG GGRL
//