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Database: UniProt
Entry: A0A226NFS9_CALSU
LinkDB: A0A226NFS9_CALSU
Original site: A0A226NFS9_CALSU 
ID   A0A226NFS9_CALSU        Unreviewed;      1227 AA.
AC   A0A226NFS9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Peregrin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASZ78_000675 {ECO:0000313|EMBL:OXB66250.1};
OS   Callipepla squamata (Scaled quail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC   Callipepla.
OX   NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB66250.1, ECO:0000313|Proteomes:UP000198323};
RN   [1] {ECO:0000313|EMBL:OXB66250.1, ECO:0000313|Proteomes:UP000198323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texas {ECO:0000313|EMBL:OXB66250.1,
RC   ECO:0000313|Proteomes:UP000198323};
RC   TISSUE=Leg muscle {ECO:0000313|EMBL:OXB66250.1};
RA   Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA   Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA   Decker J.E., Seabury C.M.;
RT   "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT   of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT   Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT   Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OXB66250.1}.
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DR   EMBL; MCFN01000068; OXB66250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226NFS9; -.
DR   STRING; 9009.A0A226NFS9; -.
DR   Proteomes; UP000198323; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd05512; Bromo_brd1_like; 1.
DR   CDD; cd15701; ePHD_BRPF1; 1.
DR   CDD; cd15676; PHD_BRPF1; 1.
DR   CDD; cd20156; PWWP_BRPF1; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR042008; BRPF1_PHD.
DR   InterPro; IPR049583; BRPF1_PWWP.
DR   InterPro; IPR019542; Enhancer_polycomb-like_N.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR042061; Peregrin_ePHD.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR013087; Znf_C2H2_type.
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:SF85; PEREGRIN; 1.
DR   PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF10513; EPL1; 1.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198323};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          21..52
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          283..333
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          337..458
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          653..729
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          1098..1181
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   REGION          43..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..993
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1008..1072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..179
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..851
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..898
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1008..1064
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1227 AA;  138746 MW;  828535E550C54367 CRC64;
     MGVDFDVKTF CHNLRATKPP YECPVGSCRK IYKSYSGIEY HLYHYDHDNP PPPQQPPLRK
     HKKKGRQGRA GAADKQSPNP SEASQSPGRE VMTYAQAQRM VEVDLHGRVH RISIFDNLDV
     VSEDEEAADE APENGGGGKE NGESQAAAAA AAAPKSAKQK SKEKRKDSNH HHHHHHNASA
     GAAPKLPEVV YRELEQDTPD APPRPTSYYR YIEKSAEELD EEVEYDMDEE DYIWLDIMNE
     RRKTEGVSPI PQEIFEYLMD RLEKESYFES HNKGDPNALV DEDAVCCICN DGECQNSNVI
     LFCDMCNLAV HQECYGVPYI PEGQWLCRRC LQSPSRAVDC ALCPNKGGAF KQTDDGRWAH
     VVCALWIPEV CFANTVFLEP IDSIEHIPPA RWKLTCYICK QRGSGACIQC HKANCYTAFH
     VTCAQQAGLY MKMEPVRETG ANGTSFSVRK TAYCDIHTPP GSVRRLPALS HSEGEEEDEE
     EEEEGKSWSS EKVKKAKAKS RIKMKKARKI LAEKRAAAPV VSVPCIPPHR LSKITNRLTI
     QRKSQFMQRL HSYWTLKRQS RNGVPLLRRL QTHLQSQRNC DQRDTEDKNW ALKEQLKSWQ
     RLRHDLERAR LLVELIRKRE KLKRETIKVQ QVALEMQLTP FLILLRKTLE HLQEKDTGNI
     FSEPVPLSEV TEIYEVPDYL DHIKKPMDFQ TMKQNLEAYR YLNFDDFEED FNLIINNCLK
     YNAKDTIFYR AAVRLREQGG VVLRQARRQA EKMGIDFETG MHFPHCVTVE EAQVQDIEDE
     DMRLLLSENQ KHLPLEEQLK ILLERLDEVN AGKQSIGRSR RAKMIKKEIT VLRRKLAHPR
     DLGRDGLERH SSSARGVLQS HNPCEKDLQT DSAAEESSSQ ETGKGLGPNS SSTPAHEVGR
     RTSVLFSKKN PKTAGPPKRP GRPPKNRDSQ IAPGHGNSPI GPPQLPIMGS SQRQRKRGRS
     PRPSSSSDSD SDKSTEDAPM DLPANGFSSG NQPVKKSFLV YRNDCNLPRS SSDSESSSSS
     SSSAASDRTS TTPSKQGRGK PSFSRVNFPE DSSEDTSGTE NESYSVGAGR GVGHSMVRKG
     IGRGAGWLSE DEDSSLDALD LVWAKCRGYP SYPALIIDPK MPREGMFHHG VPIPVPPLEV
     LKLGEQMTQE AREHLYLVLF FDNKRTWQWL PRTKLVPLGV NQDLDKEKML EGRKSNIRKS
     VQIAYHRAMQ HRNKVQGEQS SDSSESD
//
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