ID A0A3Q3AA81_KRYMA Unreviewed; 1070 AA.
AC A0A3Q3AA81;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=PHD finger protein 2 {ECO:0000313|Ensembl:ENSKMAP00000007964.1};
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:ENSKMAP00000007964.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000007964.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000256|ARBA:ARBA00006942}.
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DR RefSeq; XP_017295779.1; XM_017440290.1.
DR AlphaFoldDB; A0A3Q3AA81; -.
DR STRING; 37003.ENSKMAP00000007964; -.
DR Ensembl; ENSKMAT00000008089.1; ENSKMAP00000007964.1; ENSKMAG00000005943.1.
DR GeneID; 108250417; -.
DR KEGG; kmr:108250417; -.
DR CTD; 5253; -.
DR GeneTree; ENSGT00940000158148; -.
DR OMA; KDIVHTQ; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd15554; PHD_PHF2_like; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
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; PTHR23123:SF14; LYSINE-SPECIFIC DEMETHYLASE PHF2; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 5..56
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 197..353
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 444..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 120107 MW; D790E9FD41E66FC6 CRC64;
MATVPVYCIC RLPYDVTQFM IECDACKDWF HGSCVGVDED DAPDIDIYHC PNCEKTHGKS
TLKKKKNWSK YDTGQSTDMR AVQNGSQVFI KELRSRTFPS ADDIVVKLSG SQLSIDYLEE
NGFSEPILVQ KKDGLGMSMP APTFYISDVE NYVGPDDSVD VVDVTKQTDS KMKLKEFVDY
YYSTNRKKVL NVINLEFSDT RMSTIVESPQ IVRQLSWVEN YWPDDALLGK PKVTKYCLIC
VKDSYTDFHI ECGGASVWHH ILKGEKIFFL IKPTSANLSL YERWRSSSNH SEMFFADQVD
KCYKCTLKQG QTLFIPSGWI NAILTPVDCL AFSGHFVHNL SVEMQMRAYE IEKRLKVKTL
TPFPNFETAC WYVGRHFLER FRSLHKANKQ PAPYLIHGAK IINGAFRAWT KKQALLEHED
ELPENMKPSQ LIKDLAKEIR LSENATKTIK SEPSIKVPAE EPPSIQSELE EPASPEHISS
PSREKSRKKI SKSPKIPKAP KPPKVPKVKE GEKKKAKKTK ELSPPPKPSS FAALESHAKN
ILSKMEQPKK TKAVKNVMSL PEKEISKHNN MGKFEMREQN KNKNEAKWKY KNSKPDSLLK
MEEECKFDRT ALSGNKDRFS FIMSHRKMSS SKILKPQTNS SVFGSLQNLK DDKTKPVRDE
YEYVSDEGEL KIDEFPIRRK KNTVKRDLSF LSEIREPLQP PKKTRLQPSV TKSMDSSDEE
TLHIDTEAKP EVKSRNSKVK KKSGSAAGIL DLLQASKQVG GIDYTTNSQP PASPSTQEAI
QGMLSMANLS SSESLQQSWS NNQSKNNSQS KNNSHSSQVC KKSSGGAGSK RPTKRLPKKP
RKSSSIESLD YDDEQDHMDA CFKDSDYVYP SLESEEDNPV FKSRSKKRKS SDDTPYSPTA
RVGPSVPRQE RPARDGARVA SIETGLAAAA AKLSHQEEQQ KTKKKKKSTK KKAIVTDEPS
TISQDSSSPD HNVDSQDGSL TDNEVNTGTV KFPGGLQPMA PGIFLSQKRP SVSSSNNSTN
SSSTNNSSMA KGDRTGSADA KAKRLKKGMA TAKQRLGKIL KIHRNGKLLL
//
