ID A0A2H3T3F4_FUSOX Unreviewed; 1664 AA.
AC A0A2H3T3F4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=FRV6_07164 {ECO:0000313|EMBL:SCO82951.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO82951.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) 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}.
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DR EMBL; FMJY01000004; SCO82951.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOC1_g10009442; -.
DR VEuPathDB; FungiDB:FOC4_g10010740; -.
DR VEuPathDB; FungiDB:FOIG_05400; -.
DR VEuPathDB; FungiDB:FOMG_04637; -.
DR VEuPathDB; FungiDB:FOXG_02373; -.
DR VEuPathDB; FungiDB:FOZG_04813; -.
DR VEuPathDB; FungiDB:HZS61_010262; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000219369; Unassembled WGS sequence.
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; 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; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 871..894
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 958..976
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1035
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1055..1073
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1114..1137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1157..1175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1343..1366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1386..1404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1444..1468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..86
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1664 AA; 183476 MW; 47DF696E1887194D CRC64;
MEDPTSIAKA KSLHRTSTRS DDLLQPQDNP SICRICRGEG TPEEPLFYPC KCSGSIKYVH
QDCLMEWLSH SQKKYCELCK TSFRFTKLYA PDMPQSLPVH IFIGHMARYF FQNVLVWLRA
AMAISVWLCW LPYFMRSVWS FMFWVSDEGF GNTSMMARSN DTASSTANSL RGMSPSALDF
ETCPASPLFV ATTTPASVAN TLLDGLSEQN ISDFFARMMS IWGVAVKSDR PESTNATSSG
SMSIPPTLLG EVAFLNNLTR NPTVNRTIIS ILEGQIITVL VIVCFILVIL VRDYVVQQQP
EMNLRPAFPA PENPVPQQEP MLVRPEDVEE LQGPDESDDE TLDTGDPFTT ANDVAFAAQV
QADGRLRRRT NSELMVPPGL IETGPSEAGP VESQTPTDAG ISEERASVYD YLRIYRQADG
DARKILELIH EEGLENKLSY WVDVTRRALH DEDDSPLLGI GTDPYTSRER AGSFGSTVAS
SSRKAYTPGS DDFPTPMDIP GESSSSKGKE KEILPPLPDQ TSETSFAASP SRPRAVSDGP
QLHDSVNPLA NNSWSFEGLP VDTQEEGASS GLPNASEAAL FGSKNHEQLR QDVAASALPD
LRENENEPAR RVERTGTFGT PEPHALEQPP VAAVQENGRP AGLVGRVTDF MWGDLDEQQR
AVPDANAADP VVAQQDDTDG WETELDEVHQ DGPPPDAAAA EEPEEPEDLG DAPGAGLDQE
AMEDLEDFEG VMELIGMRGP VAGLFQNAIF CAVLVSVTIF ACIFVPYNFG RVSVWVVANP
MRLVRLIFEF SKLLQDAAVM AAGFGLWVAI NMIDMFTGLI GGPVGAQVLT ARKASWSLWT
NAGSRVLDYT FMDLPMSAAE MQNFSAISHS ALLAVKGNIG ALFTIISKVV GFIFSGRIVT
SSVSVDSIKS AAAVAWPKIT ALSSALLKPN SWVVNLGEPD GPLNVNPELA HWSGLDRFWA
IAAGYATLFF FGALYLKRGS PFSRGHMLQA WEAGIIDTLH QASGIMKVIM IISIEMLVFP
LYCGLLLDGA LLPLFENTTF KSRLLFTYNY PLTSVFVHWF VGTGYMFHFA LFVSMCRKIM
RQGVLYFIRD PDDPEFHPVR DVLERNLTTQ LRKILFSAFV YGALVIVCLG GVVWGLFYAI
PGVLPVHYSS NEPVLEFPVD LLFYNFLMPL AVSFFKPGDG LHAMYTWWFR TCARGLRLTY
FLFGERRIDE EGSLRLGNAL RDQQLPWYKT LFLELNDRYH VVPKTWTDFF DGGDAKPRAP
LNNSEIRSLT RHKNHLKTAN QLVESGHFVR APASDRVKIP KGKRVFLDVD EHGRRNDGQE
DTDLYASNQY QMVYIPPHFR ARVFLFILFI WIFAAVTGVG FTIIPLVFGR RMFKMLIPQH
IRTNDIYAFS IGVYLLGSAA YLVFHARSVW AKIQDGVSAA RASLTAGNLE RRAAAVLLRG
VRLLYAYSFL LVVFPLLISG LLELYLAIPL HTYMYPPTAA SIQAAREGGP EASRHTVRVI
QAWTLGLLYL KLGARMITSM FPDTRLAVAV RTVLRGGWAN PDIGVLTRAF VLPGLAIAGA
AIFGPPALTS ALIKYNIIPG IDAGESEVAE AARIAITYRH SYPAVALAAL LVKNTIGLVK
VFNGWTARIR DEAYLIGERL HNFGAAAAGA GRVRGAWRAG GARL
//
