ID A0A091FS05_9AVES Unreviewed; 891 AA.
AC A0A091FS05;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 25.
DE SubName: Full=Dystrophin-related protein 2 {ECO:0000313|EMBL:KFO71964.1};
DE Flags: Fragment;
GN ORFNames=N303_15148 {ECO:0000313|EMBL:KFO71964.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO71964.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO71964.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO71964.1};
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; KL447292; KFO71964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091FS05; -.
DR STRING; 55661.A0A091FS05; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16248; EFh_DRP-2; 1.
DR CDD; cd00176; SPEC; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 2.
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; 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; PF00569; ZZ; 1.
DR SMART; SM00150; SPEC; 2.
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 PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 571..627
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 18..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 716..810
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 18..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 891
FT /evidence="ECO:0000313|EMBL:KFO71964.1"
SQ SEQUENCE 891 AA; 100945 MW; 6A7D003EEC66842D CRC64;
MQEWPYVPPR CPEWHVTDRA QHSSSAHPLS QVEASQDGAG PSCITPRALS SAIRPQSPLE
MNLCWNEIKK KSHSLRARLE AFSDHSGKLQ VPLQEIIDWL GQKDEELSAQ LPLRGDVLLV
QQEKETHAAF MEEVKSRGPY IYSVLESAQA FLSQHPFEEL EEPASESKDV SPRHRIQNIS
RFVWKQANVA SELWEKLTAR CVDQHRHIER TLEQLLEIKG AMEELSTTLD QAESVRETWE
PIGDLFIDSL PEHIQSTKLF KEELSPMKDG VKVVNDLAHQ LAISDVHLSM ENSRTLEQIN
TRWKQLQVRR SQGQALQIND KQEDAGEGLS VLSFQDINHQ AQTTCWDHPK MMELYQTLAD
LNNIKFSAYR TAMKLRRVQK ALRLDMVTLA TALEIFNEHD LQPSDRAMDV VEVIHCLTAL
YERLEEERGI LVNVPLCVDM SLNWLLNVFD SGRSGKMRAL SFKTGIACLC GTEVKEKFQY
LFSQVANSGG LCDQRQLGVL LHEAIQVPRQ LGEVAAFGGS NVEPSIRSCF RFSNGKPAIE
ASQFLEWANL EPQSMVWLAV LHRVTMAEQV KHQTKCSVCR QCPIKGFRYR SLKQFNVDIC
QTCFLTGRAS KGNKLHYPIM EYYTPVGTCV GRVFTQSWQI PQCLALPMCS LVLLACFPLL
LPCRLQCLCP HRGPRCFSTC CNRDEDQYLL RHSSPITDRE PGGSQQVPGS LNMDDKGELE
RILAHLEDEN RILQGELRRL KWQHDEAVES PTLATGTPES VQDPRNDELL AEARILRQHK
SHLETRMQIL EDHNKQLESQ LHRLRELLLQ PPAESDGNGS PASSLASSPH QSESSQAKEK
EHNTPDTEAA DEVEAKTQEV SVCLEDIMEK LRSAFPNSQG TRVKSPSLAS Y
//
