ID A0A1S3SAX2_SALSA Unreviewed; 810 AA.
AC A0A1S3SAX2;
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-like isoform X1 {ECO:0000313|RefSeq:XP_014061499.1};
GN Name=LOC106608213 {ECO:0000313|RefSeq:XP_014061499.1};
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_014061499.1};
RN [1] {ECO:0000313|RefSeq:XP_014061499.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014061499.1};
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}.
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DR RefSeq; XP_014061499.1; XM_014206024.1.
DR AlphaFoldDB; A0A1S3SAX2; -.
DR KEGG; sasa:106608213; -.
DR OrthoDB; 275356at2759; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000087266; Chromosome ssa06.
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; 1.
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.
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..719
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 255..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"
FT COMPBIAS 262..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 88171 MW; 4C79618B3E3F68A8 CRC64;
MASDGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVHDPSLLG GSISAYKIVP
DEIDQIKETL VDWCDEKELN LILTTGGTGF APRDVTPEAT KEVIEREAPG MSLAMLMGSL
NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAVVKMKEAV
DELEDLPSPP PPLSPPPNSS PRRQTEDKGV QCEEEDDDKK DSGVASTEDS SSSHITAASI
AAKVTNGEIP DSIISRGVQV LPRDTGSLST TPSESPRAQA TSRLSTASCP TPKARLPSCS
STLSIAEASR REFRAHLDEV ITLKSRYSTL DQLQCRLEGL KDDRRSHRTF SSRVQSRCSS
KENILRSSHS AVDITKVARR HRMSPFPLTS MDKAFITVLE MTAVLGTEII NYRDGMGRVL
AQEVYAKDNL PPFPASVKDG YAVRAADGPG DRFIIGESQA GEQPTHTVMP GQVMRVTTGA
PIPCGADAVV QVEDTELLRE SEDGTEELEV RILVQARPGQ DIRPIGHDIK RGECVLSKGT
HMGPSEIGLL ATVGVTEVEV QKFPVVAVMS TGNELLNPED DLHPGKIRDS NRSTLLATIQ
EHGYPTINLG IVGDKPHSPD DLLNALNEGI SRADVIITSG GVSMGEKVCE QIDYLKQVLD
IDLHAQIHFG RVFMKPGLPT TFATLDMDGV RKLIFALPGS NPVSAVVTCN LFVIPALRKM
QGILDPRPTI IKARLSCDVK LDPRPEYHRC ILTWHHQEPL PWAQSTGNQV SSRLMSMRSA
NGLLMLPPKT EQYVELHKGE VVDVMVIGRL
//
