ID A0A2N3NCJ5_9PEZI Unreviewed; 1311 AA.
AC A0A2N3NCJ5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=jhhlp_001936 {ECO:0000313|EMBL:PKS10186.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS10186.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS10186.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS10186.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(2017).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:PKS10186.1}.
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DR EMBL; NLAX01000008; PKS10186.1; -; Genomic_DNA.
DR STRING; 41688.A0A2N3NCJ5; -.
DR VEuPathDB; FungiDB:jhhlp_001936; -.
DR InParanoid; A0A2N3NCJ5; -.
DR OrthoDB; 852805at2759; -.
DR Proteomes; UP000233524; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF211; PALP DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233524};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 16..72
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 95..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1311 AA; 144991 MW; 425EE405980ABD07 CRC64;
MDIPRPGLDL EKELTCSICT ELLYQPLTLL DCLHTFCGAC LKDWFSFQAV SAEDAPTPPA
PGTPIFTCPS CRSSVRDTRH NATVATLLDM YLKANPDKDR SDGEKQEISA KYRPGQNVLP
RINTTKSPEQ LRAEEEDRRL MEEVRAMSLR EAGVESSLVP TSRRRRGESR SREASRDSRQ
ARRATESSAR PRGEEGRTRS RHPPDSNRPS GEERRRRRSE SRRRPEEGAE TRRRPDEAVE
ARTRQIEHQS SIRSLIGSAN MSERDIEREI EEFARQIQEE GILDGLDLDN IDLERDDELS
RRITEAYRRR QRDRARQQDS ARESSRRNTA AADARPELNP PETQRPREED RSVNRRRNST
GASMHSEDRS RSQQGVNHLE VQPEPRHRRR TASSSRTSTA PIAASPAIAV ATRSQTDLST
TQASLSTAAN PRSAFTEGRS SSSPVVAAGN STPVEGSHLS FASRVPLHTQ SVIGPPDLPS
PTRLQRPHRP AELALLNQSG HSSPASSPIS PSIKRPPLVF PEPSLNCSRC NKQGIEYNVH
YNCGVCAGGN WNICLDCYRG GKGCLHWFGF GYAALTKWEK VRRENPNLEP FHVLTASRYT
QPKTTPVRGE DGRFHTTEDP MQRLQSGTFC DRCSAWSNGC YWRCGTCNHG DWGFCNNCVN
QGRCCSHPLL PYIYQPPSTH NTPPASPRPP KLPHNTMLFA GSSSAGLSNF QSLTFVTRCD
LCQDPIPPSQ SRYHCFECVS SVEPDTQPGD YDVCMTCYSN LVRDRQISAE NGPNGWRRCL
AGHRMVVMTF QESVAGQRRY IVRDLVGGRR LWSRPVEGTS EVVTWCWEQA GQTLGRLVTT
DVSATAPTME SGVDGLVPAQ TFPPEGGVGM VAKARWGWLP IQGRQAEDEL YFPRNAEIRE
VEDVNGDWYF GSYMGDVGTF PAPPAAPTSL AMSQFPVMLR QNVLRRGVRT FATAIPPRDP
SARTIAVSKA QGVSNGLTEA IGNTPLIRLN HLSKETGCNV LGKAEFMNPG GSIKDRAALY
VVLDAEERGL LRPGGTVVEG TAGNTGIGLA HVCRSRGYKL VIYMPNTQSQ GKIDLLRLLG
AEVHPVPAVA FDNEMNYNHQ ARRHAESLDN AVWTNQFDNI ANRRAHIETT GPEIWTQTEG
KVDAFTCSTG TAGTFAGVTR YLKTVSDGRV KAFLADPPGS VLHSYISSGG KLTERSGSSI
TEGIGQGRVT DNLAQDIDLV DGSLHISDEK SINMVYRCLD EEGLYLGASS ALNVVAAKEV
AEKLGEGHTV VTVLADGAYR YADRLFSRKW LESKNLLGAI PKHLEKYIVL P
//
