UniProt: A0A3L8SGV3

Database: UniProt
Entry: A0A3L8SGV3_CHLGU

LinkDB:  A0A3L8SGV3_CHLGU 
Original site:  A0A3L8SGV3_CHLGU

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (5)   
   Pfam (3)   
   PROSITE (3)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (21)   

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ID   A0A3L8SGV3_CHLGU        Unreviewed;      1100 AA.
AC   A0A3L8SGV3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE            EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
GN   ORFNames=DV515_00007694 {ECO:0000313|EMBL:RLW01824.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW01824.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLW01824.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLW01824.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLW01824.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-
CC         (R)-S-oxide-[F-actin] + NADP(+); Xref=Rhea:RHEA:51308, Rhea:RHEA-
CC         COMP:12953, Rhea:RHEA-COMP:12956, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16044,
CC         ChEBI:CHEBI:45764, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.14.13.225; Evidence={ECO:0000256|ARBA:ARBA00001591};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the Mical family.
CC       {ECO:0000256|ARBA:ARBA00008223}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLW01824.1}.
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DR   EMBL; QUSF01000021; RLW01824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8SGV3; -.
DR   STRING; 44316.ENSEGOP00005007773; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   CDD; cd21251; CH_MICAL3; 1.
DR   CDD; cd09439; LIM_Mical; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR23167:SF51; [F-ACTIN]-MONOOXYGENASE MICAL3; 1.
DR   PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF00412; LIM; 1.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00132; LIM; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          480..586
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          913..975
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   REGION          618..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          981..1016
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..665
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..720
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..771
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1100 AA;  124610 MW;  7DFAA841D824A7A9 CRC64;
     MEESKNEKVN QAHVLFDRFV QASTCKGTLK AFQELCDYLE LKPKDYRSFY HKLKSKLNYW
     KAKALWAKLD KRGSHKDYKK GKACANTKCL IIGAGPCGLR TAIDLSFLGA KVVVIEKRDA
     FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGSIDHISIR IGWRALVHPK THPVSEYEFE
     VIIGGDGRRN TLEGFRRKEF RGKLAIAITA NFINRNTTAE AKVEEISGVA FIFNQKFFQD
     LRDATGIDLE NIVYYKDDTH YFVMTAKKQS LLDKGVIRHD HADTEVLLSR ENVDQEALLN
     YAREAADFST NQQLPSLDFA INHYGQPDVA MFDFTCMYAS ENAALVREQN GHQLLVALVG
     DSLLEPFWPM GTGIARGFLA AMDSAWMVRS WSLGASPLEV LAERESIYRL LPQTTPENVS
     KNFSHYSIDP ATRYPNINVN FLRPQQVRHL YNTGDLKDIH LEIENFVNSR TPKLTRNESV
     ARSSKLLSWC QRQTDGYAGV NVTDLTMSWK SGLALCAIIH RYRPDLIDFD SLDEHDVEKN
     NQLAFDIAEK EFGISPIMTG KEMASVGEPD KLSMVMYLTQ FYEMFKDTIP SSDSQELNAE
     EKAALIASTK SPISFLSKLG QSISRKRTPK DKKEKELDGA GKRRKTSQSE DEDLPRSYRE
     ERPTLVSALT ERRIDAAIGN QNKVKSMATQ LLAKFEENAP VPSSNLRRQQ PVLPYQERVH
     SQPSSRREQG RLAPIPQWKQ MRHKERSRTC PKKVIMLSSS TPSSSPSYPR QQRFREPGAG
     CPGEQRSRQE RRPPRLFSHD QVPMSVEQRA CQLAALLESR RALRHQPETE PSRRFFVDQW
     ELSLSLRSSN RPSSPSSDSL RQKYIKMYTG GVSSLAEQIA NQLQRKEPPK TLLDKKELGS
     LKKEFPQNLG GSDVCYFCRK RVYVMERLSA EGKFFHRSCF KCEYCATTLR LSSYAYDIED
     GKFYCKPHYC YRVSGYAQRK RPAVGPLSGK DTKGPLQDAM ASDGSGRANS IPTSAERAPG
     SSASFFSRVV QYSLGLVGRV RVVSQRLHST VSSIGHHVAQ NPLDSFFMCQ LLAFGVPFLY
     VQSEVLGQIL GEFCGQPADQ
//

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