ID A0A3Q3A0J6_KRYMA Unreviewed; 1778 AA.
AC A0A3Q3A0J6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000009678.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000009678.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Mical family.
CC {ECO:0000256|ARBA:ARBA00008223}.
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DR RefSeq; XP_017284412.1; XM_017428923.1.
DR Ensembl; ENSKMAT00000009827.1; ENSKMAP00000009678.1; ENSKMAG00000007101.1.
DR GeneID; 108243470; -.
DR CTD; 569564; -.
DR GeneTree; ENSGT00940000158780; -.
DR OrthoDB; 5399346at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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; 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; IPR022735; bMERB_dom.
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:SF39; [F-ACTIN]-MONOOXYGENASE MICAL2; 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; PF01494; FAD_binding_3; 1.
DR Pfam; PF00412; LIM; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
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); 2.
DR PROSITE; PS51848; BMERB; 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 Coiled coil {ECO:0000256|SAM:Coils}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 516..622
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1119..1181
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1603..1754
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 635..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1704..1731
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 654..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..780
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..922
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..943
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1778 AA; 198964 MW; 6C8F7EBECB175656 CRC64;
MGETEDERTA QASQLFENFV QTSTCKGTLQ AFSILCRQLH LDPLDHSNFY SSLKAAVSSW
KVKALWTKLD KRAQQKVYNQ NKACQGTRCL IIGGGPCGLR TAIELALLGC KVVVIEKRST
FSRNNVLHLW PYTIHDLKAL GAKKFYGKFC AGAIDHISIR QLQLMLLKVS LILGVEIHVN
VEFVKLVEPP EEQTDDSPGW RAEIRPSNHP VSDFEFDVVI GADGRRSTLD GFTRKEFRGK
LAIAITANFV NRNTTAEAKV EEISGVAFIF NQKFFLELKE ETGIDLENIV YYKDNTHYFV
MTAKKQSLLD KGVIINDYIE TERLLASDNV NQEALLSYAR EAADFGTNYQ LPSLDYAINH
YGQPDVAMFD FTCMYASENA ALIREKYGHQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD
TVWMVRGWAQ GKNSLEALAE RESIYRLLPQ TTPENISKNF EQYSIDPATR YPNLNSNCVR
PHQVRHLFID GQQDLSLGGK GGPTRRSVNL FRKESEVRPG RLLTWCQKQT QGYRGVDVTN
LTSSWRNGLA LCALIHRQRP DLIDFDSLNE EDVAGNNQLA FDVAEQEFSI QPVTTGKEMA
ANAEPDKLLM VLYLSKFLEA FRKSSLNIVC KEADENGEEY PSKTNQKLLN LPQPRKRIPR
DEKKLEDDSV NKRRRKGSSY LTELSCHSTP PAGEDGELRE NKVRSMATQL LAKFEENSST
AKIHTKSENP SSPSSSPPLS PSTTPPSSDE EEEKENPRFA KPKDTPPLPP PPPPPHPKWQ
PSVYLRLLEN PGAVVQSTGF FFSPPESSYS HSRSPSPLRS KSPFSAPRSP DSPRSPDSPP
RRFSVSAPDA DPSSDVSEQQ SKNQKLSSGE FSRRSIRERA VLLSSMFHGS NKPSAALFVT
QVESPASSSP SPPPPPPLSV SKSSIPYPAV HPVPDPTVQA GFSPVPPNAP EQKDKIPSPF
LLSYSDSDKP EQSSLPCADS CSSNDETSSP VSSPDESQNS STYCDAERIN GNNWEHKKVH
GNAQELFHDR NIAEKDYLKR AGSCDDECDG RNAPKSVVRS ESCPSGAPSY SKERTVGKVS
SAIDAKAQIL AILYETDHRP NAVPCMGRKE FPAGLGGSDV CHFCSKRVYV MERLSAEGFF
FHRECFRCHV CNCTLRLGGH GFDSQEAKFY CRMHYAQRQS SSHLGRVRRK TEDQSHVKPS
PLDSGIFSSP GRVQPAGGAP SLQPEPLVKG QRLFPEDTEL AVDALEASCT VEEGAAAKGQ
IQDATKGHCN TKQNNRWKRK IRTAFPLILI KHFHLPPDKQ RPETVPEVDC EETVSSENQT
ESKGISKTST DTQNHSKESE KQAEPSAAEK PASDASSSRK RLILTQGEKE KLLNWDEETS
VSHRQEQVRA EADKLQTNSI QNETASQSQT SAFQVLSNAF RRTFSGSANS SGPKTSVPMR
PKRDGPRKRR PVSEGAFRAA ESSTEGRRRT STPGVRWASV SSDPWGAGQD LPSLLQQVSL
KGRRESEGVF SDSIGSLSPK RVDLFSSIRI RKREVSEGEG TEQEVQKEIR TFLSNLRNKT
SSQQNLEEPS SSDEEDESLT SSPKLCPEKL RRKQEKMAAQ QEKREQLKRL HRAQAIQRQL
EEVEEKQRDL EERGVKIEKI IRGEDSPETE ERDEAQLYQA WFQLVLEKNR LARYESELMI
FAQELALEDT QSRLQQDLRQ RMAVEDSEKS ASELQREQEI LAEMMRTVEK RDMLVSVLEE
QRLKEKAEDK DLESLILSKG YEFRWAHGGD SWGPEKLE
//
