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Database: UniProt
Entry: F4WZE8_ACREC
LinkDB: F4WZE8_ACREC
Original site: F4WZE8_ACREC 
ID   F4WZE8_ACREC            Unreviewed;      1334 AA.
AC   F4WZE8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Gephyrin {ECO:0000313|EMBL:EGI60392.1};
GN   ORFNames=G5I_11370 {ECO:0000313|EMBL:EGI60392.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI60392.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; GL888479; EGI60392.1; -; Genomic_DNA.
DR   STRING; 103372.F4WZE8; -.
DR   EnsemblMetazoa; XM_011064343.1; XP_011062645.1; LOC105150946.
DR   eggNOG; KOG2371; Eukaryota.
DR   eggNOG; KOG2548; Eukaryota.
DR   InParanoid; F4WZE8; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
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   InterPro; IPR019147; SWAP_N_domain.
DR   NCBIfam; TIGR00177; molyb_syn; 2.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF09750; DRY_EERY; 1.
DR   Pfam; PF00994; MoCF_biosynth; 2.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   SMART; SM01141; DRY_EERY; 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:UP000007755}.
FT   DOMAIN          50..180
FT                   /note="Suppressor of white apricot N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01141"
FT   DOMAIN          712..855
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   DOMAIN          1088..1231
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          253..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..282
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..462
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..522
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..591
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..717
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1334 AA;  150692 MW;  1A7829BBCECD1BD6 CRC64;
     MSFSVKKTGG RMWHEARKQE KKIRGMLVDY RRRAERRRDY YEKIKSDPTQ FLQLHGRPCK
     IHLDPAIAAA GDSPANMMPW QGNDDNLIDR FDVRAHLDWI PEPVDTIDVD IALTSEDRHI
     NYERYRIIVQ NEFLGVTEEK FLHQIHLEEQ FGSSTKLDAA KDKKKSANNA AIGYNYETEE
     PIPEPVKTID SVISEEKGDD EDSDIDLDIC VDVSQIEPSQ AHEMNLVAQK YGLLGADYFS
     FLTQDFEEAE TLRQARKQEE EKAMYSGRRS RRERRAFREK KMIGRVMSPP SYAARESPEY
     NPYRKSSSKS RSRSASPVNA GQITYITSFG GEEETHGSTS HVSSSNSRKV NYSYLRRRRS
     DSPAFNDRTV SKKISKSRSR SCSRSVSRTK SYRTRDRKRS GSRMRSRRTR SRPRKYTRSR
     TRSRSRRSRT RSKSRSRCRS ISRSRSRSLS RSRSRSRSHL KRSRSSSSSS ISKSRSRSKS
     RNRSHSRDSY RKRRYSLSKS RSKSRSRSKS PSRSRSRSRS QSSCKRSRSD DNKMPALPRY
     YGRRGKSSSL ELELSDNEEK SSPAAPKTPI NTSVNKPKAG LSTNSGGGHK SLKITPQERL
     KKKMQVLLNR QYKADKKAEQ LRIEKMEQQR QDREDEIREM SLKLRRKQRE RRHRYEGHSS
     DTRSSMSRTP SPSRSPRHHT VRRDRRDTDG DRERDRDRDR ERDRRDDRDR MSDTCASGEK
     IDESGPGLKA FISNAKNIFQ GDISCTAIVE DDETSIMKYL IQWSDENKAD VILTTGGTGF
     SERDVTPEAT KKVIHKETPG LSLEMLMSSL KITPMAVLSR AVCGIRHKTL IVNLPGSRKA
     AIECLTAIAP AIPHAVDLIL DNKAKVKDTH NIVQHNITSC SHHASCTNPM SFENVATRLR
     ESSFPMISVA EALHIIRFES TKDVEVEIIN LKDAYGRVLS GESIRSNCDL PPFRASIKDG
     YAVLASDGKG KRTVLCGVKA GTAPALVSLK SGTCVRVNTG APIPDEATAV VQVEDTKLVS
     KSSDGTEEEE IEIMIEPKEG QDIRHIGCDI KKGSLVLNPF TRIGPVEIGL LAACGYKRVA
     VTLLPRIGIL STGDELQQPG EPLKPGQVYD SNRISLISLL KENGFDSLDF GIVTDNTMEM
     ANKIGIALEK VDVLVTTGSV SMGDRDLLKP ILENIFKATI HFGRVNMKPG KPTTFATCTI
     LGKKKFILCL PGNPVSALVT AHLFLLPLVN ELHFDASESI IMQAKLTSSY NLDPRPEYAR
     AILKWNDKET LPMAYSTGNQ ISSKLLNCND ANALLMLPER TAEKEVLNEG DVVPARLISL
     KSPRKRIQIN YTLD
//
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