ID A0A2P5A0E2_9HYPO Unreviewed; 1699 AA.
AC A0A2P5A0E2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-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=TGAM01_v201385 {ECO:0000313|EMBL:PON30019.1};
OS Trichoderma gamsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=398673 {ECO:0000313|EMBL:PON30019.1, ECO:0000313|Proteomes:UP000054821};
RN [1] {ECO:0000313|EMBL:PON30019.1, ECO:0000313|Proteomes:UP000054821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6085 {ECO:0000313|EMBL:PON30019.1,
RC ECO:0000313|Proteomes:UP000054821};
RX PubMed=26893428;
RA Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL Genome Announc. 4:e01747-15(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:PON30019.1}.
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DR EMBL; JPDN02000003; PON30019.1; -; Genomic_DNA.
DR RefSeq; XP_018662013.1; XM_018804745.1.
DR STRING; 398673.A0A2P5A0E2; -.
DR GeneID; 29984828; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000054821; 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; 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:UP000054821};
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 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 782..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 994..1012
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1044..1071
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1091..1109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1150..1173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1193..1211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1385..1408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1428..1446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1485..1510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1588..1611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..82
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 29..76
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 324..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1699 AA; 188242 MW; 63AF61272C9C422E CRC64;
MEDAASDAGP TAQQQRYDDR PNAAAIEICR ICRGEGTEEE PLFHPCKCSG SIKHVHQDCL
MEWLSHSQKK YCELCKTPFR FTKLYAPDMP QSLPVHVFAK HMASHLLSNL LVWLRAAVAI
SVWVFWLPYF MRAVWSFMFW ISDEGLGGSI ISRINETNNT MSAIPPSLLA IGTCPASPLL
ATTTTSAAEV EAVVGQLEGK DVSDYFVRFL LNSFTSPLLA SDGELGYAAN ASAALNNASQ
VATATTLLSN VGFLGNLTRN ASLNRAIVSV LEGQIITILV IISFILIILV RDYVVQQQPE
INMRAAFAAP ENDFQVPEPG EIIQQENLPP ANPHPTDSDD ETLEDSDQVG DQDWQRVPPG
RLAPAGEEAL TPDSSNHSTP DHDSFPTSST NTSLQNDQLH SHAHEDANED DVAEEPSGLA
DYQRIYGRAN GDLQDVVRIV EEEGLQEKLK YWVESTRRSA STTENTTYEH ATDEADQEHP
EHEIDSDHDT LQSSSNWKGK APWSPTQADA DTSGPSDAPE DDLFGVASRP RSKSEGLQGQ
FSVNPLANNS WSFDALPVDD KPDELFQSLP AIQEQFAQDF NGDEPSGGSS RQSRDSGDED
DSHLNRDAYR RLPDIEIYQR HPPRELQQPL PDLNEREQRL DDGIDPQPPH ANGAAEEIAV
NGGDVPAAGF ADKVADFMWG NMDDLDPPAG PRALIVAAHR AALDDMAAEE AVERAAGQEA
AAGNNNREDL WVDVPAEPNG DDGEGIAADD NAAPLDPEAI EDMEDFEGVM ELIGMRGPIA
GLFQNAIFCA VLVSVTIFAC IFIPYNIGRV SVWLLASPMR VVRLLFELSK LLQDATFLVG
GLGSWCALNF VDIFAAVMGG SVKAHIVSAR KMSWALWTGA GSRICTFLFK DFFPMSATEI
HNFSAVSHDA LNIVKGNVVS VFSNISGSLT TVNSVGFDKM MATTVTLLSS TFETAVKVSS
LLTKPSSWVI DLSLAEEWPS LDPQLTYWSS LDRFWAILAG YTTMFLIGAL YLKKGSPFSR
NAIVHAWETG VIESLQQASG IMKVILIISI EMLVFPLYCG LLLDAALLPL FENTTFTSRI
IFTCRYPMTS IFVHWFVGTG YMFHFALFVS MCRKIMRPGV LYFIRDPDDP EFHPVRDVLE
RNLTTQLRKI LFSAFVYGAL VIVCLGGIVW GLAFAMPSAL PIHYSSNEPV LEFPVDLLFY
NFLMPLAVKF FKPSDALHTM YTWWFRRCAR ALRLTYFLFG ERRVDEEGVL HLPAETPAGR
IPHMGYLLEL SHAENAPAEN AKIVPKTWRD TFEGGDSKPT TRMSSSERKA HRHKKAHLVD
SHQLDKDGKF IRAPASDRIK IPKGQQVFLT VSERNHRKDG RADDDIYSSD QYLQVYIPPN
FRTRIFTFIL LIWLFASVTG VGFTIIPLVL GRKIFKELIP DYIRTNDIYA FSIGVFLLGS
AAYAIARQHA IREKIRKWIR EAERDILEGE VAGRMTRIAI HTAKLFYAYT VLLVVFPLLT
SALMELYVAI PLHTYMYPPT AVSLKDEGAN RHTVRVIQSW VLGLLYLKLG SRMITSLFPD
SRASAAVRNI IRRRWWLRPN VRLLTRGFVI PGLLISGVAI CGPPMVAGFI IRHTGLAGGS
APEDAAAAVT ATVIYRQSYP IAACAAILAK HAVGFVKVTN RWTASVRDEA YLIGERLHNF
GSRTSSSQKT KVRARRVNA
//
