ID A0A1S8W7W8_9FUNG Unreviewed; 2241 AA.
AC A0A1S8W7W8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=BSLG_00623 {ECO:0000313|EMBL:OON10575.1};
OS Batrachochytrium salamandrivorans.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON10575.1, ECO:0000313|Proteomes:UP000189906};
RN [1] {ECO:0000313|EMBL:OON10575.1, ECO:0000313|Proteomes:UP000189906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS {ECO:0000313|EMBL:OON10575.1,
RC ECO:0000313|Proteomes:UP000189906};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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:OON10575.1}.
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DR EMBL; LYON01000048; OON10575.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:BSLG_00623; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000189906; Unassembled WGS sequence.
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: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; 3.30.1390.10; -; 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; 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; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000189906};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
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 124..196
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 124..196
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 90..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1899..1937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1325
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2241 AA; 248384 MW; B62B5C544A9232EC CRC64;
MAYLDYDEVE QEYLQMQIRM AELPPAHAQV PLGANPQLYT FLHYAPFMYD LKLPLTGAVR
KTILAVVWYH MSMGSRSVFE DLVGSPSSIV VPTDDDTAGR QGLDTPSDDE DHLPLEYQPS
QRGKACGHVF DRGEGIYRCR TCALDDTCVF CVRCYDATTH EGHDTTMSIA VGSGGCCDCG
DPEAWRIPIV CKYHSIDTTD SQSLDGLADH DSDLDHTTTA EPDIAKASTP ASNAFRETII
TLLEFAICNL SKSSENPRFT GDVNVIQSRH PPDVVMGEDR TMYFSCILWN DESHSFQEVI
DQVTEATNCT DAFARNVAVT VDKRGRFPIR TSDSLQLLVA VASIISKISL TVSIRPTRDI
FREEIAGVLI NWLKTVCRFV LSSQTVNGVK SESVEQLVRT IICEELCNPL LTDLEEFNSA
SPLISELSTP SNLTATRAQR SRIHYFLTLD SRLWKDVRNS LRELYIGTLI VSGDVFKKSM
AIHFVNSYLE VSRCYLFHDR EIDLSIMNFT VQIFTVPSIA NYLIHHTLLL PYMFSLLKAH
FLSDVLPDEY PLKTKYYDAI QKAKVDFRPI YPTLRFDGEA VRNKRHAHLL FDARYVLSSH
NVRNGGSVNN VLVASSPDGS ASVLLRFLDL CLVWQGINPQ IRSLHNHIEY ETDDWLHAFN
HSINILQVVR SFANCFDSVS SDTAAATLLN AMSETRDTLL KWTLHRHVEY TKSWQTMQIS
IAGVMRRRAT VRDGFHLVTL VQGHPCRVPD FHVAFQPISF HKCLHWLLAS FVKNNAVLLQ
HTTDHKKRLA IVHAVFDIAV ESPSVSVESS LADSTHILDL HEMARILSVE DRMALIFDFP
LRSIVFASQI KSGVWVRNGY NIREQAKHYK DAVMREAYDH DMLLLQYAAV CLGPDKLLSM
LVDRYGLVSW FQGHTVSQDT SHYESSQILS FVQDLLQVII IVLTERSSAA AVSPTDELRR
EMIHYLAVHR SGTAYSELSR RVADSLMDAA ADSAGTMNDR NTLVASAASF DALLSSVAHF
KFPDGASDHG LYELKDEMYA QVDQWFWHYT SNEREDLNDV LRKRLEKKRA LSRQGGREAS
FEDEAVRRPK LLKIEPCTGF DRLSSVIHSP IFNQILFYSL WNVTRTAAES GQEPASNETI
LSEAIHLLVV SFEILEMEED SVNSGVVGHT PHDTGFIHHA ISSRLLIPVR KGAATRPTTL
LELILSLVDR ANEDDIKEQA PRLRYLVQRF EAIGGPVVTL TLSGWRDKSH WDLGKPVLPG
SGSIEKQSGL SGSSEALTEL EQRKLAAKTR QANIMAQFAQ AQQSFMANFG DDMDDMDDAE
DQSDFEDRDE AAHSGKDTLD RPDHRAWRFA TGTCIVCQED AVAGGKMYGM LCLLRHTTVR
RQILFSDAAN VAKVLAASPS SFDVESDPAV KIDSKGVHCY NNASGKRPMD PAVAHTGLGA
SSSSTGATTS PSQTLPFSGS SSQPCPLKRV SFEGVTATSC GHLMHFSCFN TYTNSITARQ
LSQPTRNHPE DQDANEFMCP LCKSLGNAVL PVVWSSRHET VNWRGSDVPE RGTGDANDRQ
LLGSLRLWLV DSGFMHVKNS QDTEMESKSS FSDGHTGGPL IDASRTISDL GAEVALDELE
TSGMSSTSVM SLTDSLTQAF VDHTALAPAA LTFKSSSDTA RLHELHVIYT RNVYNALNGL
FEGGGVSEST GSLPFKTDMG VEMLTSTRMC ELLATTIASL DILGRASPTS WTPGVPRAAL
ADSLLNVGVL DTMSSQMLMC LRILSEAALG ATFYTKCTQT ALVEFGDRYL TSFFGDHGIK
GLYPKPLEED LSHVHPPVLL RDGFSHLVVL SMSVIPARVA TRSKDESEVF QWIRVLWIFE
LVRCVVSVVE SILLYGDAWI MDPRVLSAAA AAASSHPVRS VYSDDPVPIN ESNPEAGQST
RSSEPEHTDG GDNDDDELKY GGLCHLIRVV LSEMKLMPDA RTYVHKSIRA DIVLALFERT
GLVFVRRCAV LLYARFGLVP PGGISGFGFD LVQPDQDHVG GLESDRGFNA AACLGGSELE
RLCKYLDLPS AATLASLPII HDRVFGHMVL HWVHDFGRSM ANHFGVVWST EAPRRLERER
QRAVGATRTL LSSISTDVLA PPSAPHVSLD LPLVFELANL PLRLATLFEE SRRKVCKRCG
TIPLDPALCV LCGMILCSQS YCCSDEDHGE CNQHIQECGG SIGIFLLIKQ AMMILLLPNG
KGTFMDLPYL DAHGEVDPQL R
//
