ADCD_DICDI
ID ADCD_DICDI Reviewed; 785 AA.
AC Q54LD5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Arrestin domain-containing protein D;
GN Name=adcD; ORFNames=DDB_G0286693;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; AAFI02000089; EAL64102.1; -; Genomic_DNA.
DR RefSeq; XP_637626.1; XM_632534.1.
DR AlphaFoldDB; Q54LD5; -.
DR SMR; Q54LD5; -.
DR STRING; 44689.DDB0267090; -.
DR PaxDb; Q54LD5; -.
DR EnsemblProtists; EAL64102; EAL64102; DDB_G0286693.
DR GeneID; 8625767; -.
DR KEGG; ddi:DDB_G0286693; -.
DR dictyBase; DDB_G0286693; adcD.
DR eggNOG; KOG1818; Eukaryota.
DR HOGENOM; CLU_357327_0_0_1; -.
DR InParanoid; Q54LD5; -.
DR OMA; YSKGREW; -.
DR PRO; PR:Q54LD5; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.640; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011021; Arrestin-like_N.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00339; Arrestin_N; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..785
FT /note="Arrestin domain-containing protein D"
FT /id="PRO_0000363157"
FT ZN_FING 682..742
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT ZN_FING 688..738
FT /note="RING-type; degenerate"
FT REGION 29..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 688
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 691
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 704
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 707
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 712
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 715
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 734
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 737
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 785 AA; 88552 MW; 64C4E4A739C975D5 CRC64;
MTTLLNNHHN NNSLPIQISQ QHVLINSNQN ESNQPSSLFN SISPQKKLSP TLNSTSIPPP
PPSSSSKYPL ELSEKGQICN LKINLDKSYF TNGETISGKV NILLTERQCI KRVKLQLCGY
EKIFQHAQHS NNTYQTFKFY SGNLNIPPLN VNIETTSLNS LPISNSENNS PILLPTTTST
QNSTLSPTLL SSNLNSKSST TTTTTTGMMS SVSSLSSSFS QQLTTPIHEF ESGVYEYPFS
FQLPKYLAPS LNYIGYLSIF YLVHCKVDYS KGREWKDQKV MKSSELWISG INKQYQDYLL
YNKTHFTSHK LAHYLNWLSF GTNTNSNNSN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNQ
PSTITNNNIN NNNNIGISNN YKSNPIEMAI CLRENNCYIG SKATFFIQLK NPLNLKINSI
RVELFQQISF IKTLSNSNSS SSGGSSNKNN NGGGIGNDRI SNIQKSNKKS SGSHRYHYRN
NSSDHNIDKT KVSQTQILLH NYDCRELFKN QTTTSSSSSQ EILCSTNLQI LIPFKIEDDQ
VFPTTRGFLS TVKHFFIISI PSISNFKLKI PVHLWQRFDD NNFTTISNNI HSLPFHTSNS
FGNIRNSYSS SGSGSGSGSS NSNSNHSSSN YLNEQEENLD EQQQQNYDDE FYDDEDDEDN
DRFKLNPPKE WKVLWLPKWK DESSITNCNL CDNTFTIIRR THHCRACGGV FCEACSNQKV
CLYGFGVNNK VRICLMCFDA VKAESSNSIY GSNINSSILP FKNGLPLQNV FSKKKVYKPP
YLVHL
