ID W5N9V7_LEPOC Unreviewed; 792 AA.
AC W5N9V7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Gephyrin {ECO:0000313|Ensembl:ENSLOCP00000017416.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000017416.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000017416.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 EMBL; AHAT01022301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01022302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01022303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01022304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01022305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01022306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01022307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01022308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01022309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01022310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N9V7; -.
DR Ensembl; ENSLOCT00000017447.1; ENSLOCP00000017416.1; ENSLOCG00000014136.1.
DR GeneTree; ENSGT00390000016577; -.
DR HOGENOM; CLU_010186_2_2_1; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000014136; Expressed in brain and 13 other cell types or tissues.
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:SF5; GEPHYRIN; 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:UP000018468}.
FT DOMAIN 1..117
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 558..701
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 133..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 86640 MW; 0B457FCE2CC777DC CRC64;
MGGTVSAYKI VPDEIDEIKE TLVDWCDEKE LNLILTTGGT GFAPRDVTPE ATKEVIEREA
PGMALAMLMG SLNVTPLGML SRPVCGIRGK TLIINLPGSK KGSQECFQFI LPALPHAIDL
LRDAIVKVKE VHDELEDLPS PPPPLSPPPT TSPHKQTEDK GVQCEEEEEE KKDSGVASTE
DSSSSHITAA AIAAKKSKPL TNVLHYQFSN HPGPDMHMNN LLECNSHSLY PAKCSYIIPD
SIISRGVQVL PRDTASLSTT PSESPRAQAT SRLSTASCPT PKHQARLPSC SSTYSVSEAA
RREFRAHLDE VITLKSRYST LDQLHYRLEG LKDELRTHRS YDSRVQSRCS SKENILRASH
SAVDITKVAR RHRMSPFPLT SMDKAFITVL EMTPVLSTEI INYRDGMGRV LAQDVYAKDN
LPPFPASVKD GYAVRAADGP GDRFIIGESQ AGEQPTHTVM PGQVMRVTTG APIPCGADAV
VQVEDTELIR ESEDGTEELE VRILVQARPG QDIRPIGHDI KRGECVLAKG THMGPSEIGL
LATVGVTEVE VQKFPVVAVM STGNELLNPE DDLHPGKIRD SNRSTLLATI QEHGYPTINL
GIVGDNPDDL LNALNEGISR ADVIITSGGV SMGEKDYLKQ VLDIDLHAQI HFGRVFMKPG
LPTTFATLDI DGARKLIFAL PGNPVSAVVT CNLFVIPALR KMQGILDPRP TIIKARLSCD
VKLDPRPEYH RCILTWHHQE PLPWAQSTGN QMSSRLMSMR SANGLLMLPP KTEQYVELHK
GEVVDVMVIG RL
//