ID A0A3B3CT99_ORYME Unreviewed; 794 AA.
AC A0A3B3CT99;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Gephyrin {ECO:0000313|Ensembl:ENSOMEP00000021058.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000021058.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000021058.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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 AlphaFoldDB; A0A3B3CT99; -.
DR Ensembl; ENSOMET00000030655.1; ENSOMEP00000021058.1; ENSOMEG00000023025.1.
DR GeneTree; ENSGT00390000016577; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000261560; Unplaced.
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: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}.
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 181..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..288
FT /note="Disordered"
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; 86418 MW; 52FBBF6F1AE61B6B CRC64;
MASDGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVHDPSLLG GMITAYKIVP
DEIDEIKETL VDWCDEKELN LILTTGGTGF APRDVTPEAT KEVIEREAPG MSLAMLMGSL
NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAVVKVKEAA
DDLEDLPSPP PPLSPPLNSS PRRQTEDKGV QCEEEDEEKK DSGVASTEDS SSSHITAASI
AAKIPDSIIS RGVQVLPRDA ASLSTTPSES PRAQATSRLS TASCPTPKAR LPSCSSTLSI
AEASRREFRA HLDEVITLKS RYSTLDQLQC RLEGLKDDRR RTFSSRVQSR CSSKENILRS
SHSAVDITKV ARRHRMSPFP LTSMDKAFIT VLEMTAVLST 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 DIDGARKLIF ALPGNPVSAV VTCNLFVIPA LRKMQGILDP RPTIIKARLS
CDVKLDPRPE YHRCILTWHH QEPLPWAQST GNQVSSRLMS MRSANGLLML PPKTEQYVEL
HKGEVVDVMV IGRL
//
