ID A0A093H177_DRYPU Unreviewed; 930 AA.
AC A0A093H177;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Dystrophin-related protein 2 {ECO:0000313|EMBL:KFV73145.1};
DE Flags: Fragment;
GN ORFNames=N307_12507 {ECO:0000313|EMBL:KFV73145.1};
OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV73145.1, ECO:0000313|Proteomes:UP000053875};
RN [1] {ECO:0000313|EMBL:KFV73145.1, ECO:0000313|Proteomes:UP000053875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV73145.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL217074; KFV73145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093H177; -.
DR STRING; 118200.A0A093H177; -.
DR Proteomes; UP000053875; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16248; EFh_DRP-2; 1.
DR CDD; cd00176; SPEC; 1.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 2.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12268:SF16; DYSTROPHIN-RELATED PROTEIN 2; 1.
DR PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 1.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00150; SPEC; 2.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 2.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053875};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 340..373
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 593..649
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 731..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 755..849
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 855..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 930
FT /evidence="ECO:0000313|EMBL:KFV73145.1"
SQ SEQUENCE 930 AA; 104920 MW; F5591B2158AB7238 CRC64;
MQEWPYVLPR CPEWHAPGPV QHASAAHPLS QVDVSQDGAG PSCITPRALS SAAGPQAPLE
MNLCWNEIKK KSHSLRARLE AFSDHSGKLQ VPLQEIIDWL GQKDEELSAQ LPLRGDVLLV
QQEKEMHAAF MEEVKSRGPY IYSVLESAQA FLSQHPFEEL EEPTSEGKDA SPRHRIQNLS
RFVWKQANVA SELWEKLTAR CVDQHRHIER TLEQLLEIKG AMEELSTTLD QAESVRETWE
PIGDLFIDSL PEHIQSTKLF KEELSPMKDG VKVVNDLAHQ LAISDVHLSM ENSRTLEQIN
TRWKQLQVGR RQSQALQIYH RQGDAGEGLW SDLYASLLAA SVQVPWERAI SPNKVPYYIN
HQAQTTCWDH PKMTELYQTL ADLNNIKFSA YRTAMKLRRV QKALRLDMVT LTTALEIFNE
HNLQPSDRAM DVVEVIHCLT ALYERLEEER GILVNVPLCV DMSLNWLLNV FDSGRSGKMR
ALSFKTGIAC LCGTEVKEKF QYLFSQVANA GGLCDQRHLG VLLHEAIQVP RQLGEVAAFG
GSNVEPSIRS CFRFSNGKST IEASQFLEWA NLEPQSMVWL AVLHRVTMAE QVKHQTKCSV
CRQCPIKGFR YRSLKQFNVD ICQTCFLTGR ASKGNKLHYP IMEYYTPVRR WAGLEGSHLT
SGPHQWQQQG GAAPKWISCM VLLPSTVSLA LSQSVSLSSR LAEMESQNCS FFSDSLSPDD
SLDEDQYLLR HSSPITDREP GGNQQVPGSL NMDDKGDLER ILAHLEDENR ILQGELRRLK
WQHDEAVESP TLATGSPESV QDPHNDELLA EARILRQHKS RLETRMQILE DHNKQLESQL
HRLRELLLQP PAESEGNGSA VSSLASTLHQ SEGSQAKENE HNTPDTEAAD EVEAKTQEVS
VCLEDIMEKL RSAFPNSRGT RVKSPSMASY
//
