ID A0A3Q3F6H8_9LABR Unreviewed; 794 AA.
AC A0A3Q3F6H8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Gephyrin {ECO:0000313|Ensembl:ENSLBEP00000014467.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000014467.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000014467.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC {ECO:0000256|ARBA:ARBA00008339}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589}.
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DR AlphaFoldDB; A0A3Q3F6H8; -.
DR STRING; 56723.ENSLBEP00000014467; -.
DR Ensembl; ENSLBET00000015326.1; ENSLBEP00000014467.1; ENSLBEG00000011164.1.
DR GeneTree; ENSGT00390000016577; -.
DR InParanoid; A0A3Q3F6H8; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0072579; P:glycine receptor clustering; IEA:Ensembl.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00887; MoeA; 1.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 2.
DR Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005111; MoeA_C_domain_IV.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR NCBIfam; TIGR00177; molyb_syn; 2.
DR PANTHER; PTHR10192:SF32; GEPHYRIN B ISOFORM X1; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 2.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 2.
DR SUPFAM; SSF63867; MoeA C-terminal domain-like; 1.
DR SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 2.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT DOMAIN 18..165
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 560..703
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 180..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 86392 MW; E02ABAE86751C8B8 CRC64;
MASDGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGVNLK DLVHDPSLLG GMISAYKIVP
DEIDEIKETL VDWCDEKELN LILTTGGTGF APRDVTPEAT KEVIEREAPG MSLAMLMGSL
NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAVVKVKEAA
DELEDLPSPP PPLSPPPNSS PRRQTEDKGV QCEDEDEEKK DSGVASTEDS SSSHITAASI
AAKIPDSIIS RGVQVLPRDT ASLSTTPSES PRAQATSRLS TASCPTPKAR LPSCSSTLSI
AEASRREFRA HLDEVITLKS RYSTLDQLQC RLEGLKDDRR RTFSSRVQSR CSSKENILRS
SHSAVDITKV ARRHRMSPFP LTSMDKAFIT VLEMTAVLGT EIINYRDGMG RVLAQDVYAK
DNLPPFPASV KDGYAVRAAD GPGDRFIIGE SQAGEQPTHT VMPGQVMRVT TGAPIPCGAD
AVVQVEDTEL LRESEDGTEE LEVRILVQAR PGQDIRPIGH DIKRGECVLA KGTHMGPSEI
GLLATVGVTE VEVQKFPVVA VMSTGNELLN PEDDLHPGKI RDSNRSTLLA TIQEHGYPTI
NLGIVGDNPD DLLNALNEGI SRADVIITSG GVSMGEKDYL KQVLDIDLHA QIHFGRVFMK
PGLPTTFATL DMDGARKLIF ALPGNPVSAV VTCNLFVIPA LRKMQGILDP RPTIIKARLS
CDVKLDPRPE YHRCILTWHH QEPLPWAQST GNQVSSRLMS MRSANGLLML PPKTEQYVEL
HKGEVVDVMV IGRL
//
