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Database: UniProt
Entry: A0A2D0RNZ6_ICTPU
LinkDB: A0A2D0RNZ6_ICTPU
Original site: A0A2D0RNZ6_ICTPU 
ID   A0A2D0RNZ6_ICTPU        Unreviewed;       807 AA.
AC   A0A2D0RNZ6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Gephyrin isoform X3 {ECO:0000313|RefSeq:XP_017332228.1};
GN   Name=LOC108270253 {ECO:0000313|RefSeq:XP_017332228.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017332228.1};
RN   [1] {ECO:0000313|RefSeq:XP_017332228.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017332228.1};
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_017332228.1; XM_017476739.3.
DR   AlphaFoldDB; A0A2D0RNZ6; -.
DR   Ensembl; ENSIPUT00000020536; ENSIPUP00000019684; ENSIPUG00000013063.
DR   GeneID; 108270253; -.
DR   OrthoDB; 275356at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000221080; Chromosome 9.
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}.
FT   DOMAIN          18..165
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   DOMAIN          539..716
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          183..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..329
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   807 AA;  87388 MW;  95A4E1A49113BA81 CRC64;
     MASDGMSLTN HDHQIRVGIL TVSDSCFRNL ADDRSGFNLK DLVHDPSLLG GIVSAYKIVP
     DERDFIKETL VDWCDEKELN LILTTGGTGF APRDVTPEAT REVIEREAPG MALAMLMGSL
     NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAIVKVKEVH
     NALEDLPSPP PPLSPPPVTS PHKQTEDKGI QCEEEEEEKK DSGVASTEDS GSSHITAAAI
     AAKSVFHPTH AVVMAKGGQP LTCFVPPTTL PSHFTCSCGD QIPDAIISRG VQVLPRDTAS
     LSTTPSESPR AQQSRLSTAS CPTPKVQSRC GSKENILRSS HSAVDITKVA QRHRMSPFPL
     TSMDKAFITV LEMTPVLGTE IINYRDGMGR VLAQDVYAKD NLPPFPASVK DGYAVRAADG
     PGDRFLIGES QAGEQPTRTV MPGQVMRVTT GAPIPCGADA VVQVEDTELL QESEDGTEEL
     EVRILVQARP GQDIRPIGHD LKRGECVLAK GTHMGPSEIG LLATVGITEV EVHKFPVVAV
     MSTGNELLNP EDDLHPGKIR DSNRSTLLAT IQEHGYPTIN LGIVGDNPDD LLNALNEGIS
     HADVIITSGG VSMGEKDYLK QVLDIDLHAQ IHFGRVFMKP GLPTTFATLD LDGARKLIFA
     LPGNFSYRDT GVTLLEAMPM SDSEASRLPV SPPPRRSNPV SAVVTCNLFV IPALRKMQGI
     LDPRPTIIKA RLSCDVKLDP RPEYHRCILT WHHQEPLPWA QSTGNQMSSR LMSMRSANGL
     LMLPPKTEQY VELHKGEVVD VMVIGRL
//
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