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Database: UniProt
Entry: A0A4D9EU31_9SAUR
LinkDB: A0A4D9EU31_9SAUR
Original site: A0A4D9EU31_9SAUR 
ID   A0A4D9EU31_9SAUR        Unreviewed;       942 AA.
AC   A0A4D9EU31;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=DBH-like monooxygenase protein 1 {ECO:0000313|EMBL:TFK09670.1};
GN   ORFNames=DR999_PMT07242 {ECO:0000313|EMBL:TFK09670.1};
OS   Platysternon megacephalum (big-headed turtle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Platysternidae; Platysternon.
OX   NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK09670.1, ECO:0000313|Proteomes:UP000297703};
RN   [1] {ECO:0000313|EMBL:TFK09670.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK09670.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK09670.1};
RA   Gong S.;
RT   "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TFK09670.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK09670.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK09670.1};
RA   Gong S.;
RT   "The genome sequence of big-headed turtle.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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:TFK09670.1}.
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DR   EMBL; QXTE01000050; TFK09670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4D9EU31; -.
DR   STRING; 55544.A0A4D9EU31; -.
DR   Proteomes; UP000297703; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   CDD; cd15674; ePHD_PHF14; 1.
DR   CDD; cd15561; PHD1_PHF14; 1.
DR   CDD; cd15562; PHD2_PHF14; 1.
DR   CDD; cd15563; PHD3_PHF14; 1.
DR   Gene3D; 2.30.30.1150; -; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13793:SF150; PHD FINGER PROTEIN 14; 1.
DR   PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00249; PHD; 4.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 3.
DR   PROSITE; PS50016; ZF_PHD_2; 3.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Monooxygenase {ECO:0000313|EMBL:TFK09670.1};
KW   Oxidoreductase {ECO:0000313|EMBL:TFK09670.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000297703};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          275..336
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          338..455
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          681..735
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          824..877
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          21..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          876..942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          586..634
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        25..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..75
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..215
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..818
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..908
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        911..942
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   942 AA;  106116 MW;  7C4F4A9301666953 CRC64;
     MDRSSKRRQV KPLAASLLEA LDYDSSDDSD FKVGDASDSE GSGRGSEDAS KDSGEGSCSE
     SEENVLEEEL AEEVKVEEEQ QPKTSAGETM LTTEKEVIKT EIKEQEEEDE KPKKKKEKEK
     EKATESDAAV DEQTNEPKKW NLRRNRPLLD FVSMEELNEM DDYDSEDDND WRPTAGKKKG
     KTALRKEGSD GDNEDEEDGS GSDEDDNDEE GNEDNSSTAS DGGSKKKKNK VLSRNSADDE
     ELTNDSLALS QSKSNEDSLI LEKSQNWTSQ KMDHILICCV CLGDNSEDAD EIIQCDNCGI
     TVHEGCYGVD GESDSIMSSA SENSTEPWFC DACKCGVSPS CELCPNQDGI FKETDAGRWV
     HIVCALYVPG VAFGDIDKLR PVTLTEMNYS KYGAKECSFC EDPRFARTGV CISCDAGMCR
     AYFHVTCAQK EGLLSEAAAE EDIADPFFAY CKQHADRLDR KWKRKNYLAL QSYCKMSLQE
     REKQLSPEAQ ARINARLQQY RAKAELARTT RPQAWVPREK LPRPLTSSAS AIRKLMRKAE
     LMGISTDIFP VDTSDTSSSV DGRRKHKQPA LTADFVNYYL ERNMRMIQIQ ENMAEQKNIK
     DKLENEQEKL HVEYNKLCES LEELQNMNGK LRNEGQGIWT LLGRIIGQKL NIPAILRAPK
     ERKPSKKEGG TQKTSTLPAV LYSCGICKKN HDQHLLLLCD TCKLHYHLGC LDPPLTRMPR
     KTKNSYWQCS ECDQAGSSDM EADIAMETLP DGTKRSRRQI KEPVKFVPQD VPPEPKKIPI
     RNTRTRGRKR SFVPEEEKPE ERIPRERRQR QSLLQKKPKS EDLRTECATC KGTGDNENLV
     RCDECRLCYH FGCLEPPLKK SPKQTGYGWI CQECDSTSSK DSEPSNEVVS EAPGNVVPST
     SRSSSEELVA VAQKHPEEED ENEAKEENPS QDLNMEQKNS KK
//
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