ID A0A151MRK9_ALLMI Unreviewed; 1671 AA.
AC A0A151MRK9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Peregrin {ECO:0008006|Google:ProtNLM};
GN ORFNames=Y1Q_0007749 {ECO:0000313|EMBL:KYO27176.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO27176.1};
RN [1] {ECO:0000313|EMBL:KYO27176.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO27176.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- SIMILARITY: Belongs to the copine family.
CC {ECO:0000256|ARBA:ARBA00009048}.
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:KYO27176.1}.
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DR EMBL; AKHW03005292; KYO27176.1; -; Genomic_DNA.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05512; Bromo_brd1_like; 1.
DR CDD; cd04048; C2A_Copine; 1.
DR CDD; cd04047; C2B_Copine; 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; 2.60.40.150; C2 domain; 2.
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; IPR018359; Bromodomain_CS.
DR InterPro; IPR042008; BRPF1_PHD.
DR InterPro; IPR049583; BRPF1_PWWP.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037768; C2B_Copine.
DR InterPro; IPR045052; Copine.
DR InterPro; IPR010734; Copine_C.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR042061; Peregrin_ePHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
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; PTHR10857; COPINE; 1.
DR PANTHER; PTHR10857:SF112; COPINE-9; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF07002; Copine; 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; SM00239; C2; 2.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50004; C2; 2.
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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
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 1..97
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 107..245
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 481..512
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 732..782
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 786..907
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 1102..1172
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1542..1625
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 504..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1671 AA; 188781 MW; 742D80C70C707B84 CRC64;
MDTFSKSDPV VVLYVQGTGD KDWREFGRTE VIDNTLNPDF VRKFVLDYYF EEKQNLRFDV
YNVDSRSCNI YKHLKPALSL SAAWRRDPQK DFLGQAFVAL GEVIGSRRGR LEKALTGVPG
KKCGTIMVLA EELSNCRDVV TMQLCANKLD KKDFFGKSDP FLVFYRSNED GTFTICHKTE
VVKNTLNPVW QPFTIPVRAL CNGDYDRTVK IDVYDWDRDG SHDFIGEFAT SYRELSRAQS
QFTVYEVLNP RKKCKKKKYV NSGTVTLLSF SVESEFTFVD YIRGGTQLNF TVAIDFTASN
GIPSQPTSLH YMSPYQLSAY AMALKAVGEI IQDYDSDKLF PAYGFGAKVP PDGRISHQFP
LNNNLEDPNC TGIEGVLEAY FQSLRTVQLY GPTNFAPVIN QVARSAAQVT DGSQYHVLLI
ITDGVISDML QTKEAIVSAS ALPMSIIIVG VGPAEFEAAA MGVDFDVKTF CHNLRATKPP
YECPVGTCRK IYKSYSGIEY HLYHYDHDNP PPPQHAPLRK HKKKGRQARA ANKQSPSPSE
TSQSPGREVM TYAQAQRMVE VDLHGRVHRI SIFDNLDVVS EDEEAPEEAP ESGSNKENAE
APAAAPKAAK HKNKEKRKDS NHHHHSAAAG ATPKLPEAVY RELEQDTPDA PPRPTSYYRY
IEKSAEELDE EVEYDMDEED YIWLDIMNER RKTEGVSPIP QEIFEYLMDR LEKESYFESH
NKGDPNALVD EDAVCCICND GECQNSNVIL FCDMCNLAVH QECYGVPYIP EGQWLCRRCL
QSPSRAVDCA LCPNKGGAFK QTDDGRWAHV VCALWIPEVC FANTVFLEPI DSIEHIPPAR
WKLTCYICKQ RGSGACIQCH KANCYTAFHV TCAQQAGLYM KMEPVRETGA NGTSFSVRKT
AYCDIHTPPG SMRRLPALSH SEGEEEDEEE EEEGKGWSSE KVKKAKAKSR IKMKKARKIL
AEKRAAAPVV SVPCIPPHRL SKITNRLTIQ RKSQFMQRLH SYWTLKRQSR NGVPLLRRLQ
THLQSQRNCD QRDTEDKNWA LKEQLKSWQR LRHDLERARL LVELIRKREK LKRETIKVQQ
VALEMQLTPF LILLRKTLEQ LQEKDTGNIF SEPVPLSEVP DYLDHIKKPM DFQTMKQNLE
AYRYLNFDDF EEDFNLIINN CLKYNAKDTI FYRAAIRLRE QGGAVLRQAR RQADKMGIDF
ETGMHFPHCM PVDDAQCMGI EDEDARLLLT ENQKHLPLEE QLKILVERLD EVNTGKQSIG
RSRRAKMIKK EITILRRKLA HPRELGREVM DRHGGSARGI LQPHNPCEKD TQTDSAAEES
SSQETGKGLG PNSSSTPAHE VGRRTSVLFS KKNPKTAGPP KRPGRPPKNR ESQLVPGHGS
SPIGPPQLPI MGGSQRQRKR VRKSPHQSSS SDSDSDKSAE EPPMDLPANG FSSGNQPVKK
SFLVYRNDCN LPRSSSDSES SSSSSSSAAS DRTSTTPSKQ GRGKPSFSRV NFPEDSSEDT
SGTENESYSV STGRGVGHSM VRKSIGRGAG WLSEDEDSSL DALDLVWAKC RGYPSYPALI
IDPKMPREGM FHHGVPIPVP PLEVLKLGEQ MTQEAREHLY LVLFFDNKRT WQWLPRTKLV
PLGVNQDLDK EKMLEGRKSN IRKSVQIAYH RAMQHRNKVQ GEQSSDSSES D
//
