ID A0A094FK54_9PEZI Unreviewed; 1432 AA.
AC A0A094FK54;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=V498_05652 {ECO:0000313|EMBL:KFY91146.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY91146.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY91146.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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:KFY91146.1}.
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DR EMBL; JPKA01001326; KFY91146.1; -; Genomic_DNA.
DR HOGENOM; CLU_005075_0_0_1; -.
DR Proteomes; UP000029270; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20343; BRcat_RBR_HHARI-like; 1.
DR CDD; cd17303; PIPKc_PIP5K_yeast_like; 1.
DR CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR CDD; cd16625; RING-HC_RBR_HEL2-like; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR023610; PInositol-4/5-P-5/4-kinase.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23086:SF8; PHOSPHATIDYLINOSITOL 5-PHOSPHATE 4-KINASE, ISOFORM A; 1.
DR PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1.
DR Pfam; PF21235; ARI1_UBAl; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00330; PIPKc; 1.
DR SMART; SM00184; RING; 3.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Kinase {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 436..852
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT DOMAIN 1048..1262
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1052..1100
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 52..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..951
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1432 AA; 162627 MW; B1436F380E108342 CRC64;
MCWSLGQPYG VAEERLTEPC QYDIQFPEGI VITTTHCYIE GREGDNRLKT SLASDDEPHR
GRQVATVGPQ PSPYVPTVVK PGTNTLYPRL ASFQTPSGAN EMPSFHSDEL NNRTLDDPFF
QTLNDTRQSQ ENAALKNWPL QQPIVRTNYE TTPPRTPTDS LESMNDEITP PDNGGMYNDT
GLNAVPNGRS ARNSWEDRLV RNTGALSING GMAGIPENGK KSPEPHNRSS KSLSTERNSF
GLANGGPLQP QSAASEVVNG AQSANGHNES YKRLSPHPST YNPQSTGPLT YSSSLVGTMK
HLDSPPTTQN AKHRLSPDYH IRTPTTGPPT VASGSAQSAV GPPQLKQRVP KIGPPRASTD
ETAIASGRFS PIAASNVRRG SLSINRRNTQ SIHSNIPHED IAQDEDALRW AEAIRQKRAS
KRKRRDEEDE DRVVVGTKVD QNHVNWVTAY NMLTGIRFTV SRTNAKLDRE LTDSDFNARH
KFSFDITGNE LTPSAKYDFK FKDYAPWVFR RLRANFKIDP ADYLMSLTSK YILSELGSPG
KSGSFFYFSR DYKYIIKTIH HAEHKLLRKI LKDYYHHVEQ NPNTLLSQFY GLHRVKVPYG
GKIHFVVMNN LFPAHRDIHQ TFDLKGSTVG RDYTEDNVVN NPRATLKDLN WLRRNYHLEF
GPEKKNTFLE QMEQDVHLLQ KLKIMDYSML VGIHDVGKGN QENLRDKTLR VFQPGGDTSP
DDIVPSNPIL TRTPSKLETA RKAQELRKII KQEKPIPMGE STTRMPDQME ENTSKRDFTF
YSDDGGFRAT HEDNSPGEEI YYLGIIDLLT HYGTVKRLEN FWKGLSHDKQ QISPIPPVPY
GDRFIKFVTD ITKSREEVRE EAVREETIRE ETVREGTVRE ETVQEEIEEA REFGNSLPPS
KRIASALSPP ATTASMADSD EYMSAFSSED DILQDESDNE SGDDFGFDEP EPDLEISQKE
SPREKRRPFE VTYKVYHPDD IQRQQDELID EVNMILDLKK EDAAIILRHF RWNKERLIED
YMDRPKKVLE DAGLGPSTEG PPTLQVIPGF VCDICCEDET GLLTFAMKCG HRYCVDCYRH
YLSQKIKEEG EAAHIQCPQD GCKRIMDSKS MDLLVASDLN NRYHELLTRT YVEDKNALKW
CPAPDCVNAV ECKINKRDLD KVVPTVACDC GYRFCFGCIL TDHQPAPCDL VKRWLKKCAD
DSETANWISA NTKECPKCNS TIEKNGGCNH MTCRKCKHEF CWMCMGLWSE HGTSWYNCNR
FEEGSGSDAR DAMAKSRVSL ERYLHYYNRY ANHEQSAKLD KDIATKTEKK MVQLQSASGL
SWIEVQYLNL ASQALQTCRQ TLKWTYAFAF YLARNNLTEM FEDNQKDLEM AVENLSEMFE
KPVGELADAN LRVDIMDKTS YCNKRRVILL ADTAENLANG VWSFNGDYNG TD
//
