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Database: UniProt
Entry: A0A6J3R1G8_TURTR
LinkDB: A0A6J3R1G8_TURTR
Original site: A0A6J3R1G8_TURTR 
ID   A0A6J3R1G8_TURTR        Unreviewed;      1033 AA.
AC   A0A6J3R1G8;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Protein AF-10 isoform X5 {ECO:0000313|RefSeq:XP_033708319.1};
GN   Name=MLLT10 {ECO:0000313|RefSeq:XP_033708319.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_033708319.1};
RN   [1] {ECO:0000313|RefSeq:XP_033708319.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_033708319.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_033708319.1; XM_033852428.1.
DR   AlphaFoldDB; A0A6J3R1G8; -.
DR   Proteomes; UP000245320; Chromosome 2.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd20901; CC_AF10; 1.
DR   CDD; cd15708; ePHD_AF10; 1.
DR   CDD; cd15574; PHD_AF10_AF17; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR049773; AF10-like_CC.
DR   InterPro; IPR049781; AF10/AF17_PHD.
DR   InterPro; IPR049775; AF10_ePHD.
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; PHD FINGER PROTEINS; 1.
DR   PANTHER; PTHR13793:SF93; PROTEIN AF-10; 1.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          22..74
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          79..198
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          134..197
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          207..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          709..746
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        306..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1033 AA;  109053 MW;  7BFCEE2E95EBB65C CRC64;
     MVSSDRPVSL EDEVSHSMKE MIGGCCVCSD ERGWAENPLV YCDGHGCSVA VHQACYGIVQ
     VPTGPWFCRK CESQERAARV RCELCPHKDG ALKRTDNGGW AHVVCALYIP EVQFANVSTM
     EPIVLQSVPH DRYNKTCYIC DEQGRESKAA TGACMTCNKH GCRQAFHVTC AQFAGLLCEE
     EGNGADNVQY CGYCKYHFSK LKYKEKDKHK QKHKKQPEPS PALVPSLTVT TEKTYTSTSS
     NSISGSLKRL EDTAARFTNA NFQEVSAHTT SAKDVSEARG SEGKGKKSSA HSSGQRGRKP
     GGRNPGTTVS AASPFQQGSF SGTPGSVKSS SGSSVQSPQD FLSFTDSDLR NDSYTHSQQS
     SSTKDVHKGE SGSQEGGVNS FSSIIGLPST SAVIPQPKNF ENSPGDLGNS SLPTAGYKRA
     QTSGIEEETV KEKKRKGNKQ SKHGPGRPKG NKSQENVSHL SVSSASPTSS VASAAGSVTS
     SSLQKSPTPL RNGSVQSLSV GSSPLGSEIS MQYRHDGACP TTTFSELLNA IHNGIYSSSD
     VAVSFPNVAS GSGSSTPVSS SHLPQQPSGH LQQVGALSPS AGSSAPSAVA TTQANTLAGS
     SLSQASSHIY GNRINPNSSM AALIAQSENN QTDQELGDNS RSLGGRGSSP RGSLSPRSPV
     SSLQIRYDQP GNSSLENLPP VAASIEQLLE RQWSEGQQFL LEQGTPSDIL GMLKSLHQLQ
     VENRRLEEQI KNLTAKKERL QLLNAQLSVP FPTITTNPSP SHQMHAFSAQ NAPTTDSLNS
     SKSPHLGNSF LPDNSLPVLN QDLTSSGQST SSSSALSTPP PAGQSPAQQG SGLSGVQQVN
     GVTVGALASG MQTVTSTIPA VPGVGGIIGA LPGNQLAING IVGALNGVIQ TPVTISQNPT
     PLTHTTVPPN AAHPMPTTLT NSASGLGLLS DQQRQIFLHQ QQFQQLLNSQ QLTPEQHQAL
     LYQLVQQHHQ PDLQQLQIPA PTQMPINNLL AGTQAPPLHP ATTNPFLTIH GDNASQKVTR
     LSDKTGPVAQ EKS
//
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