ID A0A1S3MBX8_SALSA Unreviewed; 802 AA.
AC A0A1S3MBX8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Gephyrin isoform X6 {ECO:0000313|RefSeq:XP_014000461.1};
GN Name=LOC106571666 {ECO:0000313|RefSeq:XP_014000461.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014000461.1};
RN [1] {ECO:0000313|RefSeq:XP_014000461.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014000461.1};
RG RefSeq;
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}.
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 RefSeq; XP_014000461.1; XM_014144986.1.
DR AlphaFoldDB; A0A1S3MBX8; -.
DR GeneID; 106571666; -.
DR OrthoDB; 275356at2759; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000087266; Chromosome ssa15.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 18..165
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 567..711
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 182..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..293
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 802 AA; 87320 MW; 1AC67BD6545B952C CRC64;
MASDGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVHDPSLLG GFISAYKIVP
DEIDEIKETL VDWCDEKELN LILTTGGTGF APRDVTPEAT REVIEREAPG MSLAMLMGSL
NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAVVKVKEAV
DELEDLPSPP PPLSPPPNSS PRRQTEDKGV QCEEEDDEKK DSGVASTEDS SSSHITAASI
AAKVTNGEIP DSIISRGVQV LPRDTASLST TPSESPRAQA TSRLSTASCP TPKARLPSCS
STLSIAEASR REFRAHLDEV ITLKSRYSTL DQLQCRLEGL KDDRRSHRTF SSRVQSRCSS
KENILRSSHS AVDITKVARR HRMSPFPLTS MDKAFITVLE MTAILGTEII NYRDGMGRVL
AQDVYAKDNL PPFPASVKDG YAVRAADGPG DRFIIGESQA GEQPTHTVMP GQVMRVTTGA
PIPCGADAVV QVEDTELLRE SEDGTEELEV RILVQARPGQ DIRPIGHDIK RGECVLSKGT
HMGPSEIGLL ATVGVTEVEV QKFPVVAVMS TGNELLNPED DLHPGKIRDS NRSTLLATIQ
EHGYPTINLG IVGDNPDDLL NALNEGISRA DVIITSGGVS MGEKDYLKQV LDIDLHAQIH
FGRVFMKPGL PTTFATLDMD GARKLIFALP GSNPVSAVVT CNLFVIPALR KMQGILDPRP
TIIKARLSCD VKLDPRPEYH RCILTWHHQE PLPWAQSTGN QVSSRLMSMR SANGLLMLPP
KTEQYVELHK GEVVDVMVIG RL
//
