ID A0A3B0JI91_DROGU Unreviewed; 3039 AA.
AC A0A3B0JI91;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 28-JUN-2023, entry version 20.
DE RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
GN ORFNames=DGUA_6G005313 {ECO:0000313|EMBL:SPP80433.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP80433.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Mical family.
CC {ECO:0000256|ARBA:ARBA00008223}.
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DR EMBL; OUUW01000005; SPP80433.1; -; Genomic_DNA.
DR STRING; 7266.A0A3B0JI91; -.
DR OMA; RIMSAKQ; -.
DR Proteomes; UP000268350; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF54; [F-ACTIN]-MONOOXYGENASE MICAL; 1.
DR PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00412; LIM; 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; PS50023; LIM_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 572..679
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1089..1153
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 781..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1642..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1820..1866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2035..2119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2169..2193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2216..2281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2320..2399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2454..2554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2573..2647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2746..2788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2801..2857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2911..3023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1257
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1643..1664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1823..1840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2176..2193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2216..2234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2240..2256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2258..2280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2325..2370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2532..2548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2573..2588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2589..2625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2626..2642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2808..2857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2911..2926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2930..3000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3039 AA; 339811 MW; 932795DF88F01352 CRC64;
MREIYAPYLN TEIMSRQHQR HHQTQQQQQQ LQLQQQQQQL TVQQQQQQQL LMAEHAAAAE
AAELFDLLCV ATTMRQILAL HRAMCEAVGL RPSPLNDFYP KLKAKVRSWK AAALWKKFDA
RAAHRVYGKG TACSGTRVLV IGAGPCGLRT AIEAQLLGAK VVVLEKRDRI SRNNVLHLWP
FVITDLRNLG AKKFYGKFCA GSIDHISIRQ LQCMLLKVAL LLGVEIHEGV SFEHALEPSG
DVNGWRAAVT PADHPVSHYE FDVLIGADGK RNMLDFRRKE FRGKLAIAIT ANFINKKTEA
EAKAEEISGV AFIFNQAFFK ELYGKTGIDL ENIVYYKDET HYFVMTAKKH SLIDKGVIIE
DMADPAELLA GPNVDTQKLH DYAREAAEFS TQYQMPNLEF AVNHYGKPDV AMFDFTSMFA
AEMSCRVIVR KGCRLLQCLV GDSLLEPFWP TGSGCARGFL SSMDAAYAIK LWSNPQNSTL
GVLAQRESIY RLLNQTTPDT LQRDISAYTV DPATRYPNLN RESVNSWQVK HLVDTDDPSV
LEQTFMDTQS AALHTAHVET PGRRKRRSGD SLPQGATLLR WIAAQLHSHQ FVPELKEPSD
VLRNGRVLCG LISRYRPDLI DFAATKEMSP LECNELAFAV LERELNVKRI MSAKQSLELT
DIESRLWLNY LDQICELFRG EIPHIKHPKM DFSDLRQKHR IHHTHAPPDF SKLLQIKSKA
KSPMQDAVDV PTTVQRRSVL EEERAKRQRR HEQLLNIGGV TATGGAAAAG GAGAAISVGT
SAGGSNLHAG QNETPRRSKK RRQTSDKTAN IEERQQRLQN IEENRQEWMS KRRQQRYHQT
QNFYKSLQLL QAGKLLREGE DGVAEDGSAF EDYSIFLYRQ QAPIFNDRVK DLERKLLFPD
RERGDIPSAM PRSAADEQFS DRIKSMEQRM TGRGGLGGDK KPKDLMRAIG KIDSTDWNVR
EIEKKIELSK KTEIHGPKGR EKVPKWSKEQ FQARQHKMSK PQRQDSLEAE KFKDIDQTIK
NLDKQLKEGH NLDVGERGRN KVASIAGQFV RKDETNSDEA TNTVVQSNAV IPKSSSKVAL
AFKKQAASEK CRFCRQTVYL MEKTTVEGLV LHRNCLKCHH CHTNLRLGGY AFDRDDPQGR
FYCTQHFRLP PKPLPQRSNK ARKSAASVQA ASPAVAAAAT VERMDIGQEG SPTRDQVDLL
ETTLQADAMS DDEANVIDEH EWSGRNFLPE SNNDSQSELS SSDESDTESD SEVYEEADDS
PFGAQTLQLA SDWIGKQYCG ESDDTTDSYD SSDGIADDGK DDTEGEDFKK ARELRREEVR
LQPLPANLPT DTETEKLQLN VEQDKENVER SSLRSANSFE SARSQPPTPT RVEMEQLERH
APRKFSSEID AISEKLYHMT NMVKMNKDLE LLAKENLVKS DILRKLTLKE KWLAENAAIA
AGMTNTQKAQ AAAPVAAPPA AAAPLKPKSQ FEEKYEKLQS MAEAKPKPKP VIDFSLDELK
PRKPNFEERP KELLQKPGKN LKSPRSSANV SRSSSLKSNA STGSPRVKKK EDETKMNIEG
ILGTIKKLQR QQSNSKQQQE EEDMDMDVDM EVAEDLQGKK ELNSKLKEIQ ASSFAGTMDH
IRSQLAMPTV SAQADPASVD LSKYFPNQKS EKSAALNTNK NQKTLKDVDL AKYFPSSPAP
QRRTVETVAD RLKKSQTEAS LAKLQTQTQS KTAKEGDEKP KEREREKPVP PKRQASLNTF
SLREHQMDGA LDLTKKKASP VKVAKATICK QAVGGTATAT AATAQATGKG KIKIIKKIVP
KGTKAKKAAA AQEAAAAAAK ALEKQPPKDE AERILDEILG GDGEVRSPSS EYQRLFQDEK
SPSDLSDNID RILEESGLDL ELGLPRRSSK KLQKTKSLSE ADFELKPSAS SQLTGVQNIL
KRFESMSSVA SSTHNSDEQA AFKLRRMEST TSNLSSLTRS RESLASLDSM SDLERTMDHL
RNEWRNEATN FLQKKRDKFY AQKEVEQQEK KAAAADPLRD LPVQYRDSKL AKFFGLATRK
SPEKRRSPIK KIKATTTSAK KKSPSPKKSP KVAAKANSSL EELAKIGGAR QAKQQAAKKS
SQKVMPPPKA PLKPATPVPD DFEVLDLLEK ATEAKELVER SKTKSPAVIE VAKEVSLPVA
AAPLPVEDIK NLPKTGCDKS LNSSRRGSQS SLVLSRRQSL DIALTEQLQQ DALEALSSLE
KEQQEQQQEA QNFDELFQDM VVEPEPEEEP NDEDLDADSL CTTISKSPSA QPVTVVKRGS
SEDQSIEKLF GHFSDEMLVQ VEFDSNDELV GITPTVAIIP ASSSEERDYL DKLESLERDE
EPTREATDRF QTEDKNVSND ELDGSHFPMR PQRRAKSSSS SSEPALPAKL EAKLAKLDPE
DMAPSVQDLL QQVYVKPQDV EMNAVDQGTA LKFPSLVIDE DVADVADAAE EHKEKELEVA
ASQSGSLLDV QVPKVAKSKE NSLDWDMEKL PASPMPRRRL PQSQPAASKE SSLEWDMEKL
PNSPMPPRRN KVRNASPSSS SINLLNNLPS DGDEELAQRR LIEDFERERR QALIRRDESF
EATAAEQRRR DSLQSSNSNS NSSSKRSLPP PKTSSSSCSS VARRGDTARS ETKHEGTPPM
FKKLELDNES SCLTTPLDST TTCSTRRSSF AFIELQDNKP VIVPMPRKLK LPKLAEPKFV
PEPVASDEPV PEVFQGRAWP KVQIEGVSAD VDSDPELDDE AAKQLLPDYL RSDSPPAAAF
KNRKWPDGKT IFDQNQTTNG QADDHDDEED ILGKYLEARR RVSKHKPRSQ SPQPFKPLSS
SSRQSSKSYS DLKKGPSLQS LSARSSQDTD TTHSTATTVA TVARPVSSYV NYDDASTRAL
LDRSKRLHNR KREFVNERVV ERNPYMREVI RSTDRRASEE DLASYRPRHY ASPTTGSSSS
RFPSTVMRHN YSDYLSPSSN HTSDYLSSSS SSHRRPYSTL NISTTGSSYY PSTAATPRSS
HLSDLFKPRR RSPVSSYGRS SDYGLTASKE SRRLNYYLY
//
