ID A0A150H1W0_GONPE Unreviewed; 597 AA.
AC A0A150H1W0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXZ56136.1};
GN ORFNames=GPECTOR_1g115 {ECO:0000313|EMBL:KXZ56136.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ56136.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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:KXZ56136.1}.
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DR EMBL; LSYV01000002; KXZ56136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150H1W0; -.
DR STRING; 33097.A0A150H1W0; -.
DR OrthoDB; 2454808at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF15; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT REGION 373..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 60143 MW; DA9EDA2807215116 CRC64;
MAAISSTLLA LCNTGDHIVA SNTIYGGSHA LLKTFLPTKA AISTTFVDIT DLDAVRAALR
ARPTKVLYTE VVSNPTLRVA DLRSLADLAH GSGAVLVVDN TFTPFVVTPR RFGADVVIHS
LTKFVSGASD IIAGAVCGSA AFISSLTDFH AGPCMLLGPT MDPKVASELA LRLPHLALRM
QEHGRRAAAY AARLQALGAA VTYPGLASHP QHGLMAAQAN PGYGSGGLMG IDLGSPARAN
AFMERLQNRH GFGFMAVSLG YFDSLMSLSA ASTSSELSSA DMAASGIGRG YVRLSVGVTG
SLEERWRQLE EAYRFVSQLG PEGAAPFRAV KVRRTPSGAA EQLISWPSFG PGVGLGEEVV
EEAAPTRAAT QVTAAGAANG AATDGEQQRS DGGDGEGVEG PAAGAVLAAA PVAAAAAQGV
PAVFPPVAAG AATAVSAESG NEEAVDVTSG PVAVAATADT AGTPAPEAAS PKAAALLKAS
SPIRSPFVPR LPPHQPSAGG ANYAAVSAGG AAAADVAPGR GAHGVVAGLE FTVHGAGDGP
AVDLTYPAVP AAGRDEKGPG AETRSRETPD AGVQRPVKIR RTGSVEIHYV AVPQAKS
//