ID A0A1B0CF67_LUTLO Unreviewed; 2801 AA.
AC A0A1B0CF67;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 03-MAY-2023, entry version 33.
DE RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
OS Lutzomyia longipalpis (Sand fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC Lutzomyia; Lutzomyia.
OX NCBI_TaxID=7200 {ECO:0000313|EnsemblMetazoa:LLOJ002987-PA, ECO:0000313|Proteomes:UP000092461};
RN [1] {ECO:0000313|Proteomes:UP000092461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jacobina {ECO:0000313|Proteomes:UP000092461};
RA Richards S., Qu C., Dillon R., Worley K., Scherer S., Batterton M.,
RA Taylor A., Hawes A., Hernandez B., Kovar C., Mandapat C., Pham C., Qu C.,
RA Jing C., Bess C., Bandaranaike D., Ngo D., Ongeri F., Arias F., Lara F.,
RA Weissenberger G., Kamau G., Han H., Shen H., Dinh H., Khalil I., Jones J.,
RA Shafer J., Jayaseelan J., Quiroz J., Blankenburg K., Nguyen L., Jackson L.,
RA Francisco L., Tang L.-Y., Pu L.-L., Perales L., Lorensuhewa L.,
RA Munidasa M., Coyle M., Taylor M., Puazo M., Firestine M., Scheel M.,
RA Javaid M., Wang M., Li M., Tabassum N., Saada N., Osuji N., Aqrawi P.,
RA Fu Q., Thornton R., Raj R., Goodspeed R., Mata R., Najjar R., Gubbala S.,
RA Lee S., Denson S., Patil S., Macmil S., Qi S., Matskevitch T.,
RA Palculict T., Mathew T., Vee V., Velamala V., Korchina V., Cai W., Liu W.,
RA Dai W., Zou X., Zhu Y., Zhang Y., Wu Y.-Q., Xin Y., Nazarath L., Kovar C.,
RA Han Y., Muzny D., Gibbs R.;
RT "Whole Genome Assembly of Lutzomyia longipalpis.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:LLOJ002987-PA}
RP IDENTIFICATION.
RC STRAIN=Jacobina {ECO:0000313|EnsemblMetazoa:LLOJ002987-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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; AJWK01009736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJWK01009737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJWK01009738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJWK01009739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJWK01009740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EnsemblMetazoa; LLOJ002987-RA; LLOJ002987-PA; LLOJ002987.
DR VEuPathDB; VectorBase:LLOJ002987; -.
DR OrthoDB; 5399346at2759; -.
DR Proteomes; UP000092461; 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 GO; GO:0016491; F:oxidoreductase activity; 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; 2.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR003953; FAD-binding_2.
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; PF12130; bMERB_dom; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM01203; DUF3585; 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; PS51848; BMERB; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 611..718
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1074..1138
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 2651..2801
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 789..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1696..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2077..2096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2174..2214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2511..2537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2574..2634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2650..2681
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 794..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1292
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1711..1737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2179..2194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2574..2611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2801 AA; 316089 MW; E1F5BEF9FEA18F70 CRC64;
MDNENAKLAA EMFDHFCSVT TMRQIMGLYR NMMDAVGLRP GPLNDFYPKL KAKIRNWKAQ
ALWKKFDTRA GHRVYNKGTA CNGIRVLVIG AGPCGLRTAI EAQLLGAKVV VVEKRDRISR
NNVLHLWPFV ITDLRNLGAK KFYGKFCAGS IDHISIRQLQ CILLKVALLL GVEVHEGVSF
VKLIEPKDGC GWRAQVSPED HAVSHYEFDA LIGADGKRNT LEGFVRKEFR GKLAIAITAN
FINKRTEAEA KVEEISGVAF IFNQSFFKEL YYRTGIDLEN IVYYKDETHY FVMTAKKMSL
IDKGVIIQDS ADPAELLSPS NVNTDKLLDY AREAAEFSTK YQMPNLEFAV NHYGKPDVAM
FDFTSMFQAE NSSRVCVRKN YRLLQCLVGD SLLEPFWPTG SGCARGFLSS MDAAYAIKLF
ANPRNSCLAV LAQRESLYRL LGQTTPENLN RDIMAYTLDP STRYPNLNKT LVQNYRLLQC
LVGDSLLEPF WPTGSGCARG FLSSMDAAYA IKLFANPRNS CLAVLAQRES LYRLLGQTTP
ENLNRDIMAY TLDPSTRYPN LNKTLVQVQQ VEMLLDADDE TIYQQTFMDT NAISAVPDAP
VRRKRRTGDT TPLGMVLLRW IKSQLKAYEF ANNLTEVAQC FTHGRVLCAL IHRYRPELLD
FSTFGDLPAE QCNAKAFDIL ENDLGIPRVM QASESVNIEK IESKLWLNYL EQICELFRGE
IPHVKHPKLD FAELKEKQRS NIPDFSNLVK SSGKRNVVEV EAINRRITLD EERNKNRSRR
LNYEQMQAVQ AAEGSRRAKK RRSHEKFANV EEQKKRLQDI QNNRMERQSK RRLERARQTE
NFYKSLHMLQ FNSFLRDTDS STPFEDYSLY VYRQQAPDFN DRVKDLERKL LYPDRERGFY
SALARGAPDE KFSNRIKSME SKIVGKNAGL GDKKPKDLLR AIGKIESDDW NVREIEKKIE
QSKKAEVGKS REKVPKWSRE QFLARQSKMS KPIDRQSSID EKFKEIDMTI KSLDKQLKEG
HNLDRGERGR NKVASIAGQF VKKTPGTSAE EKQGSKSLMN SKLGLVLTSQ GVSEICHFCK
QKVYLMEKIA AEGLVLHRSC LKCHHCHTNL RLGGYAFDRD SPDGLFYCNQ HFKLPPKPYK
PVTKRQPSHP KHEEIAAKTS RISPEKVSRA ENIVAMDLLD RGQTPERIEF ENTDAMSDGE
RSLNNIIDEN EWTDRNFGTG TDETDSDLSS SDSSDSETDS DMYEEANDSP IGAETLQLAT
DWIGKQRICS LQDSDGDEFY DSSEDDDVDT QTEGEELARA REIRMQEVKL MPPVYPATDT
ETEVQSDSES SSVEIEPNSA TEISTDSEFD HDPIAKTPPQ IVIDDTYIKR PTRVHIRQGM
IANGLNRQVA KENTAESKVS DLSKIELDIK PLVQVDPSVL ASTNRIPLKN PRPGDYLLNK
APSTEGIASK RSLELKKRYL LGESGSTGLM KSGSTSVLDS TFKNFHSNIS QCQKLLNRGG
ADISPTMQMF LKQQTNRLSG TKEEKKEVES NLINEKINVY GMNNNLKEIA EKRIDEEHVM
PTETINTALV ENKLKDFISC SKSNDPADVP IVDLTNVDLP EEMIRANQEF IEKLECSDDV
ENNKVIEVID LTIEASHPVK FDLGARCEKR DEQVVPESIS SIKSKIEADK SAIDSLLRQR
DMCDVQETTI QVPVLNSWEP KKKPRSDSDV ESDSLSNSSS TSSLEEIPHY ILDSTTSPDT
QINERFVPRL EVRDTTGELM QIDSLMIVDG KYIGDPEDLQ LLEKLPEIPA ASAEVSQPSS
ANECDISCNS ETKRQNDVGR GISEVLRRND SFKFDARNKS KIESLKHLPL NLETKESQSD
LESPIVDRDK TPTANLAPGF IGQSDSETEI TGQVLTETEL SDWTADDAVS ENFVDIEFAL
NSNKGTIKRN KKAKKKAVPP EPPVYHQQLS DGDLETNIMK SFDIDNIEFM DTGSDGCVET
YSTTNKGMLR NRGYVEFVDQ IPEHGSTNRY CPSYRSDTGY SSSSRINLGY AKPESSSSRE
IPGVDYIEQG ACVLSSSSEG ELKTPVNEVT KSVFTDTSSS QVIKTQDSEQ HSSSVNEIED
DSLVLITSQT NTTEDSEALT VVTSPLDSAD KNAVEQSFGE AVKAISKDEY RNTPEEMSYE
DYVRKLQMKI SQISNSRDSI DVKKSKRRSS KGEGDASASE IPSPTSFTPK LSIFDDKIKE
PPTLTKKLEE ITKERAKQKD LIHDLVMDKL QTKKQLNAEK RLNRSRTRQM GCTSGSLALS
GLKSFDIPHC HPVPGEKRTT PSKVFEPLQS PSKVLETAIS SAEKLKDRPL SENVDSKFGA
GIVLPVSPKK LTKTQSFCGY SSRLVSAEND LIAESFKTPI PPPRSGRRID DKTLAHSDKL
RQEARARARL MSNEDLGLSP EEKMQMLRKR YQLDADLDTP NKSDDAKVRE QKLMASKSVS
DISTANSFVA FDKSIDGSDG KSTPRKFFKG AEFTSDSNLV SDVGVVNDKR QWWEEGEPKR
LSDRRSRSKD PERRKSIIQT VSDFFHKKKD SKDAINQINK DKADGVFGLF KLSSKHKEKS
KEKENSPSYS ERSKSEDCLK ADWRNRRSED ELTPPPIPPL PLNYQRSDDE STSVAENREL
KRLKAVSKAS RQAELKRLRI AQEIQREQEE IEVQIKELEA RGVIIEKVLR GEGSFGEYFN
ANDPNGSSDE KYLKELLEIW RKITQLKKRD QELGIREQEL KLEHRHAQLK EQLNMRLSCS
KLDKSSADVA AEGAILNEML EIVAKRAALR PTDGLPTADE I
//
