ID A0A0D2WPF9_CAPO3 Unreviewed; 1382 AA.
AC A0A0D2WPF9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Peregrin {ECO:0008006|Google:ProtNLM};
GN ORFNames=CAOG_008705 {ECO:0000313|EMBL:KJE92538.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE92538.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KE346364; KJE92538.1; -; Genomic_DNA.
DR STRING; 595528.A0A0D2WPF9; -.
DR EnsemblProtists; KJE92538; KJE92538; CAOG_008705.
DR eggNOG; KOG0955; Eukaryota.
DR InParanoid; A0A0D2WPF9; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15670; ePHD_BRPF; 1.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR CDD; cd05839; PWWP_BRPF; 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; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 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.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 337..387
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 391..506
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 1002..1064
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1152..1216
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 270..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..645
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1382 AA; 153195 MW; 190CA2B14C673212 CRC64;
MFGQCSQHQP KPHLSLFCVC FVSCILFHAS IPSLYCVLLA QHFVGLVLFV LSATMKAPAT
PKAVSAAAGM QSKTLTPAAT SKILAPIQTP SLSRLPSTAS SSSAPVPVVP MAMDVTIDGV
ATQTDTAVPL ALITDVEADT LFGEQWRQPA GTGTLNLDPQ ARLLTAKVKE LAHSAAEVAA
EALRQHPTPS RRVQVSREVG WFKAPVATPD QDQDCSCSIE YDMDDEDEQW LTQLNAYRRQ
YGLVTLDPSL FEVLMDRLEK ESHFLTTPGA ASFAKPAATS SSRAKRAVTS DDEDERSEDD
LSEIVQRNAR LMQQRTRSGP SESQDSDGEP LDENDDDAVC CVCLGPSPAP GNEIIFCDSC
NMAVHQNCYG VPYIPEGQWV CRRCIVSPSK PVDCVLCPNK GGAFKQTVDG RWAHIVCAML
VPETVLGNTV YLEPIDGVQH IPKARWTLKC YLCGKRTGAC IQCHKPNCYT SFHATCAQRA
GLHLHFAHLH SDEEDEEEET PSDRRRSQHV SSSARKRRNS FLAEQDNFAF CDLHTSKPGS
SSSKEEASSD SDSESVQPDS DQDDEENDDD DNENQGDDID IEDTDNESDD DDESLSGDDD
DDEDDDDEDE DDEDLEDEDE DEHSDDESED SANETENDID DADDEQDVFS QKAQQRARKQ
QAQKKQNASS AVSRSQGARK PAPADDFKRR AMLRRTRRLL NASQEVSSTS HATISPQAVS
HIVRDYVPAT ITDKAALLAC LVRYWRLKRD SRNGMPLLRR LQVYRPVHEK STDVANSSVA
ASKSAPQPTA SKAKNPAQWN KAMNDAKRAV ATAAAELAEA EAASNYNIDE DDEIRYTLPR
RGRPPKGVHF LPRTPVRQAR MYEQVRLAAA ERARIANDKL SALQNHSMAT ESDDDADSVS
TVSTRHSSSQ RASAVASDAE DEQGQDSQES DALTLELLDF QRLRHDLERV RLLIELVRKR
EKFHKEKLLL EARIWEYKHF PVQIALRQAI KLMLEADTNG WYSTPVNTKV VWDYLRVIKQ
PIDLGTIQRK VENFGYFTVD EFEKDVQLLI SNARTYNTPD SAYHSEAVAL WYRCAAVLQE
ARECVKDLQA LPSDLSLLSD PLYALQQELE RRRLQAEQQN NPSHESRKRR LSLTSVPPPF
SPASPPVPED LLYRVVWAKA KGFPWYPGEI VDRNDPFSSV SEAARVIPQS VVDLHHENES
SILVCFFDKK RSWLWIAPDQ IACLGVDSQV DKIKLASCHK SSMRSSIKEA FEVAKKMQVD
LPTPKNSPPV YDSATASQSS SASVLRPIKP VAPPQASSSP TSVQPVESET PRKRTLRQSN
NSVSSATDSA AAVPWFATQI AAGTPPRKKL RPETLTSGNA CPRDPGCKKF AGHIGRCLFK
EA
//
