ID A0A2P4ZPG7_9HYPO Unreviewed; 2315 AA.
AC A0A2P4ZPG7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=TGAM01_v205141 {ECO:0000313|EMBL:PON26197.1};
OS Trichoderma gamsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=398673 {ECO:0000313|EMBL:PON26197.1, ECO:0000313|Proteomes:UP000054821};
RN [1] {ECO:0000313|EMBL:PON26197.1, ECO:0000313|Proteomes:UP000054821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6085 {ECO:0000313|EMBL:PON26197.1,
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 -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000256|RuleBase:RU366018}.
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 ECO:0000256|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UQCR10/QCR9 family.
CC {ECO:0000256|ARBA:ARBA00007856}.
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:PON26197.1}.
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DR EMBL; JPDN02000015; PON26197.1; -; Genomic_DNA.
DR STRING; 398673.A0A2P4ZPG7; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054821; Unassembled WGS sequence.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR CDD; cd16482; RING-H2_UBR1-like; 1.
DR CDD; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 1.20.5.260; Cytochrome b-c1 complex subunit 9; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR008027; QCR9.
DR InterPro; IPR036656; QCR9_sf.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF24; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF05365; UCR_UQCRX_QCR9; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF81514; Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000054821};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 245..317
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 245..317
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 572..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1719..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..597
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2315 AA; 261642 MW; B2B73A7C735D5F82 CRC64;
MVSVPAIQLV RFSCPKLIAH VRSLSPTPST GKLPRRQTND VDSHSNTRLY STLFRKNYTM
LATVFAAGFA WEIGFNSTMD KIWDSNNRGR QWKDIRNKYV EGGEDEDLDH DRTYISEQAF
LLLELKLPKA FPHLALRHSS PAARYCYSSS PYELHHELMT MESPLSTQEQ QLCQLLGGLP
ARYNNRYTEE AARELLSSLF WSLAGGNHEY MRLLFPEGRP SESLKLSDAQ GAVEGAEYTE
AARGKRCGHI FKPGEASYMC RTCGTDETCC LCSRCFDATD HTGHMVRIQI SVGNSGCCDC
GDDEAWKTPL YCTIHSDMAS GPHAKDPKAP PSLPEDLVNS VQMTIGRAFD YICDVISCSP
EQLRQSKTKE SILKDEETSR LQSTYYGSDV TDTEDPTEFA LVLWNDEKHT VDEVRDQVAR
ACRKSRRQAS KDAWDTDAVG RSLLIFSDDV DRLLQMAKIL EAIRVTITIR SARDTFREQM
CGTLVEWLSD ISGCSIGHDN LILRRTICEE TMKPWRKGSA ATHTMGLIDD EEEEDQRMES
RDMLHNVNAR FILALQAAAR ARGGLDVEID VDVGDVDDDD DDDDDDEDDD DNRSFSDDGD
DDVIMVDARD TISELDMTFR PDDISLEDHE ATLAGYPPPP PPPPVPATAP GPAPAETDQN
TRQREGTPSE SDMQEPLIAQ SIHSKANVDI PKTPGKSEKA MPNPGLYWLE TPAAYTRSEI
VLPAEDVFQR VRLDWLLLFD LRMWKRVRND LRALYISTVV QIPEFKRVLA LRFASLYTIL
AQLYLVGDRE PDHSIINLSL QMLTTASITA EVIERGNFLT SLLAILYTFL TTRQVGHPWD
ISPTAVLAFD SGSVTNRRMY HFYQDLKYLF SSQHVQERLR SEPRYLMQFL DLVKLHQGIG
PNVRAVIEHV EYEADSWITA SLVTRQINLQ ARNLAEAFRE CPPDEMRHLM RAIRIAAKAA
IFNSVGGDRL RLKQGEIRDE VRFKTMSDLE FDIEGKSYDV VQFVVEKDSI SFHHGLHYTL
SWLIECGRSL PASKMRALLS FTRQELKSKP RLMAVGPIQI PKKEYSHEDY LMALFDYPLR
VCAWLAQIKA NMWVRNGISL RHQASTYRGV GQRDVSHHRD IFLLQTAMVV CDPARVLASI
IDRFGMENWV KGIFEVFSEA QDDAQHLDVV EDMIHLLIVL LSDRTSLIAP EDQPNSRLLA
MRRDIIHVLC LKPLSFNEIC LKLPEKYQES EEFHQVLDEM ATFKPPEGVS DVGTFELRQE
FIEEIDPYIA HYNKNQREES ELAYRKKMAK KTGQAIDDIV FEPKLRPIPS GLFQHLADFT
GTGVFAQVIY YSLLYVLTSH KITPSVPNTR LETFLQVVLH LILLAIMEDE SVDTEMSGKS
PKSFVHAALT RIARSNFMRE AKDARTIVSL LDMLSTNEDF KAVHPRISLV LKRLKQKRPT
TFNAEFLKLG LPLDRVNTAS PANISVDGER ERRKQAAIDR QARVMAQFQQ QQKSFLETQG
TTIDWGSDLD EEDEETEQTE DRKHNWKYPT GTCILCQEEA DDRRLYGAFA QINESLLFRQ
TDFQDPDLVR EASQTPCNLD RSAEDIRPFG IAQENRKMVE KLNAQGDTFL AERQTIGRGF
KASLSRPGPV ASSCGHMMHY SCFEQYVEAA NRRHTHQIAR HHPENINRHE FVCPLCKALG
NVFVPIVWKG LEESYPGNLQ AEESFEDFLD KQMSSYPFGG SKAREVDDSR LPAIHTPSLP
GSLLQTITQV KPPQNPHWVG KEDLEARSST TPRASGSSSR SAAAAETSEA GANQQLVTTN
ELLLMELLTA YHRIKETLVV NKLDTRYPVD KIQAGEDLHS SDTLVQVVGC TISSVEIEQR
GVEAQPGMTL IEKIPEQVIS HLRILAETTS AYIAMGGRHS LPGGRIESEF IADAEQQHGQ
LFMAQYFGAE AGDARRRLYS YPPLLSMDPF LFLVECSYGL VVAQNVDIMH VVRLCYLAEI
VKVVFHMGRN MPVGLWFGTL ANRETQDPVM NNFADFALAL SKSSVEFQAR SGNDIPDMGE
NRGFQQPGVD TLEGWYSFVK KYALAFLRKS TIFLHVKYGV DFNNHISSTP DADELDRLTE
ALQLPTFDEM CAAMTMDSLT CGWPNTTPAL VTGWVKHQVL WTKGFPDLVP SAMVSHPGIF
ELIGLPRTFD TLIEEAARRR CPTTGKDLTD PVICLFCGDL FCSQGTCCQK LDTDGTKLGG
AQQHMKKCQR NIGVFLNVRK CAIVYLFYRS GSFTPAPYID KYGETDPQLR HGRQLYLNQK
RYDSMIRSTI LKHGVPSLIS RKLEADINNG GWDTL
//
