ID A0A2C9WA05_MANES Unreviewed; 1471 AA.
AC A0A2C9WA05;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN ORFNames=MANES_03G178900 {ECO:0000313|EMBL:OAY55770.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY55770.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY55770.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY55770.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM004389; OAY55770.1; -; Genomic_DNA.
DR STRING; 3983.A0A2C9WA05; -.
DR EnsemblPlants; OAY55770; OAY55770; MANES_03G178900.
DR Gramene; OAY55770; OAY55770; MANES_03G178900.
DR OMA; DGNLHDQ; -.
DR OrthoDB; 318797at2759; -.
DR Proteomes; UP000091857; Chromosome lg3.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd04301; NAT_SF; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR032308; TDBD.
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; PTHR46309; PHD FINGER PROTEIN 12; 1.
DR PANTHER; PTHR46309:SF1; PHD FINGER PROTEIN 12; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF16135; TDBD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 733..778
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1471 AA; 162405 MW; C07053C41B245AB5 CRC64;
MEEGRRSGDP SGAMVKNRSS SGCLIVRKKG NDGMGGVGSS GSRKVLASKK EKKRARMDMS
DSGSSDELLM PSRRRVAAET LRVCNGLSLY DKGIVEENDI GRKRSRGEKI RINDVDMIDR
NGDDFSERKR NKLDVFEFDE YDGNDGEMIR RNRFDEDGME GRRIFGSMMA GRSGNEREYE
TGSSRHPVVD RRKSSYFERT SGLNRADHGG REGAPSSMSF YRDKYDKDEP IRVQGKNGVL
KVMVNKKKVD GSLKSYDRLE AEEKRKGAKM KNTVRRNDLI RSSLYPESKS ADKGSSFAGT
LKKPMNMLRS SSARNGKVRD RDSEDSDSSL KLGLKDMEAR KSLRTPLPTK NHKGPEVDSE
DSDTSTKLGL KNAEAHKTMK RASNDGEISP CNQLQSAKIG KVKRGTGTEK QKLREHIRGM
LLNAGWTIDY RPRRNRDYLD AVYINPTGTA YWSIIKAYDA LLKQLNDEEE EAKSKADGCP
FTPLSDEVLS QLTRKTRKKM EKEMKRKQRN ESDNARETAA RRSSSSRHDE ESMDSGSHEE
KLSSFIKQSG KSLKSRTNGN SFLNVNTKGQ SSTRHLHDDM EKIPSGSSSH QGRKSRKLGR
CTLLVRNSNE GLNSESGGFV PYAGKRTLLS WLIDCGTVQL SQKVRYMNRR RTKVMLEGWV
NRDGIHCGCC SKILTVSKFE IHAGSKLRQP FQNIYLDSGV SVLECQIDAW NRQESIEHIG
FHSVDIDGDD PNDDTCGLCG DGGDLICCDG CPSTFHQSCL DIQMLPPGDW HCPNCTCKFC
GVASENIYQE DEATVCELQA CSMCAKKYHK TCVLGMDALS VDSNSSFTCF CGNTCRELFE
QLQKNLGVKH ELEAGYSWSL IHRTDIDLDI SPQGLPQRVE SNSKLAIALS VMDECFLPIV
DRRSGINLIN NVLYNCGSNF NRLNYSGFYA AILERGDEII SAASIRFHGT QLAEMPFIGT
RHTYRRQGMC RRLFCAIESA LRSLKVQKLI IPAISELTNT WTGVFGFTTL DEPLKQEVKS
INMLVFPGID MLQKQLFDQE NIDGNKSTSS GDEGMECKDG QHIQPEVAVK SDIDSSAMHD
DLNECDNGGL ECASGTNDEV AASNSGSECM GIPLNDVSVI SSSLDASLEP KNPVLLKETV
NADSDSGDQL DETALEKKSL CVSDTSHYDL DKMENKADSN FPAGDNTQSC SEGDASPMNS
DSRCLGVSLD DTSVMSSSLV ASNDLKNSVS IERNTCADFE SGDKLAELTS DRKRLIISDV
SGDRQEENKP ELASLVKENI QYCEEGNVGD AHGLNLNETT SGEHKISISI EEAKSVVYQL
ENEFSELASQ GEHHFDLGAN HSAVDMETKP LVDSLIKTRS QSSTEDVHTV NTDVACIESV
PPTTDSTVDN SNGKVDEGSV VSVSASNGAN GNSMQVNFEP NDEIACEGGS KLDVASEAVS
ETKQCEVRSP HAPADDFRTD MREGKTESCS V
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