ID A0A0P7BLT8_9HYPO Unreviewed; 1287 AA.
AC A0A0P7BLT8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cysteine synthase {ECO:0000313|EMBL:KPM41549.1};
GN ORFNames=AK830_g5027 {ECO:0000313|EMBL:KPM41549.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM41549.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM41549.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM41549.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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:KPM41549.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKCW01000063; KPM41549.1; -; Genomic_DNA.
DR STRING; 78410.A0A0P7BLT8; -.
DR OrthoDB; 1462937at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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 InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF211; PALP DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 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; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
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 97..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1287 AA; 140863 MW; 4DA37BDCE408C8AB CRC64;
MESPRPGLDL EKELTCSICT ELLYQPLTLL DCLHTFCGAC LKEWFSFQAA TAARSPNPPV
PGAAVFTCPA CRANVRDSRH NATVVTLLDM FVAANPDKDR SPAEKEEMAA KYKPGDQVLP
KLPSSRTAGE RRADDEDRRL VDEVRELSLR DAGVSGSVPP RARRRRDSRS DDGLRTSRDR
SLDSRQRHGE HRPRADEGPR HSADHVYTES ERRNRRSESR QRQIEHQSSI RSLISSADMS
ERDIEREIEA FARQIQEEGL LDGLDLDNID LSRDDELSRR ITEAYRRRQR ERARHEATRR
NNGSGYSSSR YTESTSTDVR LRAPNGSDRP RSRTRPHSRS ASATSQTEER TRPPSSTPSA
ALDVQDSSRR TRRRTASDSR SATTPIFPTI SDTRPAARSS TDLSLRSQTS DPMAPRSSFS
ESRSTSTPAV PGVPPPSTND LGTHAGTSSN LSFASRAPQG APSSGQTSTQ PAATHQDLGQ
GRGNRFSRPA DLAIVHSAVA SPINSPTATS HQRTRSQLFP EPSISCSRCN KPHIEYEVHY
NCVSCYNGQW NICLDCYRAG KGCLYWFGFG HGATAKWEKK RRQADGPVAM PHILTASRYL
PPRSTPGGAD GRKTLSMEDP RKRLETGTFC AKCFAWTNEC YWRCDVCNEG DWGFCNDCVN
QGRSCTHPLL PLVHEATQSP LGRPVSPRSP GRPPTATILH GPNTSIMGAF KPLSFATRCD
VCQDPIPPSQ ARYHCYNCTS SLVPDAAPGD YDICSSCYGN LVARGQISGE NGHSGWRRCF
NGHRMVVVAF TNGKVGQWRY VANDLVGGRS LRSEAPESPE RQAKGLQKWL WQHGDQAVAR
LITKDVSETA PTSDGSTAMS KNFPPDGGVG YKASARWAWY PKTGSDDELL FPRGAEIKEI
EDVNGDWFFG SYMGTRGLFP APVRRLAVAA AKAAEPSAHT IAVSGAQGVA KGLTGAIGNT
PLIRLNKLSE ETGCEILGKA EFMNPGGSVK DRAALYVVKD AEERGLLKPG GTVVEGTAGN
TGIGLAHVCR SRGYKLVIYM PNTQSQGKID LLRLLGAEVY PVPAVAFDNP ENYNHQARRH
AEGLDNAVWT NQFDNTANRR AHIETTGPEI WTQTQGKVDA FTCATGTAGT LAGITRYLKD
VSNGRVKSFL ADPPGSVLHS YITSGGKLTE RSGSSITEGI GQGRITDNLQ PDIDLIDGSL
TIADEKSIEM VYRCLDEEGL YLGASSSLNV VAAKEVAEKL GKGNTVVTVL CDGAYRYADR
LFSRKWLTEK KLLGAIPKHL EKYIVLP
//
