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
//