ID A0A151NPY7_ALLMI Unreviewed; 952 AA.
AC A0A151NPY7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Lysine-specific demethylase 7A isoform A {ECO:0000313|EMBL:KYO38897.1};
GN Name=KDM7A {ECO:0000313|EMBL:KYO38897.1};
GN ORFNames=Y1Q_0013065 {ECO:0000313|EMBL:KYO38897.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO38897.1};
RN [1] {ECO:0000313|EMBL:KYO38897.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO38897.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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:KYO38897.1}.
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DR EMBL; AKHW03002424; KYO38897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151NPY7; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15642; PHD_PHF8; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 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 PANTHER; PTHR23123:SF11; HISTONE LYSINE DEMETHYLASE PHF8; 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 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KYO38897.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:KYO38897.1};
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 199..355
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 61..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..534
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..644
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..874
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 952 AA; 104632 MW; 67822DE5B2A4EA8B CRC64;
MASVPVYCLC RLPYDVTRFM IECDACQDWF HGSCVGVEED MAAEIDLYHC PNCQVLHGPS
VMKRRRGPQR QPDGTLGRDA GRAVRTGSAQ FIKELRSRTF PSADEILLRP SGSQLTVEYL
EENSFSVPIL VAKKDGLGMT LPPPTFTAHD IEHYVGADKE IDVIDVARQA GCRMRLGDFV
DYFCGAARDK VLNVISLEFS DTRLSNLVET PRLVRKLSWV ENLWPGEAVF ERPSVQKYCL
LGARGSYTDW HVDCGGTSVW YHVLRGEKIF YLVRPTLANL ALFETWSSSS SQSETFFGDQ
ADRCYRCPLR QGQTLFIPTG WIHAVLTPVD CLAFGGNFLH SLNIEMQLKA YEIERRLSTA
DLFRFPNFET ICWYVGKHLL DTFRGLRENR RHPATYLLHG AKALATAFRS WTRKEVLAEH
EDEIPSTVRP AQLIKDLAKE IRLAEDLLQQ SLGKGGSPFG VGRGPPLATL SAPLPARWAD
PTSQDGAKEG GRKGALPGPP QHLELPDAPG SEEGDPPSSS LEETDPESEP PEADDGDLVL
ANGRTPRTKR TQASRRWQPR SCSPPSPPGL DLDSEEDLQI DEAPPPHERQ ALGFPQRLPK
FPRKLPRAKP CSDPNRVREP GEVEFDIEED YTTEEEEEGA ELEDPEGGAS AAGLLDLLKA
SRQVGGADYD ALSTQEAIQG MLRMANLPGA GPAPSTASLQ AWWAGGGPER GPPKRPPRHP
PKRPASRSSE SEDEAPSPDE HDSLGACFKD AEYIYPSLES DEDDPALKSL PKKKKSTDDA
PWSPKARVTP TLPRQARPVR EGTRVASVET GLAAAAAKLA QQEHQRLQRR RNLAGAQHRT
PSPQDTEPEP EPEPEAEPAP PEPPPVPIPT PPVPASLADH EYTVRPGGLG PMLPARPSPP
MAPGVFLSQR RAPAGTPAAL PCQGKRPKKG LATAKQRLGR ILKIHRNGKL LL
//
