ID A0A0V1A2L3_9BILA Unreviewed; 2163 AA.
AC A0A0V1A2L3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Protein polybromo-1 {ECO:0000313|EMBL:KRY19126.1};
DE Flags: Fragment;
GN Name=PBRM1 {ECO:0000313|EMBL:KRY19126.1};
GN ORFNames=T12_16907 {ECO:0000313|EMBL:KRY19126.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY19126.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY19126.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY19126.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRY19126.1}.
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DR EMBL; JYDQ01000039; KRY19126.1; -; Genomic_DNA.
DR STRING; 990121.A0A0V1A2L3; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016586; C:RSC-type complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 1.20.920.10; Bromodomain-like; 6.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR037382; Rsc/polybromo.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR16062:SF19; PROTEIN POLYBROMO-1; 1.
DR PANTHER; PTHR16062; SWI/SNF-RELATED; 1.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF00439; Bromodomain; 6.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00439; BAH; 2.
DR SMART; SM00297; BROMO; 6.
DR SMART; SM00398; HMG; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF47370; Bromodomain; 6.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 5.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 49..119
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 188..258
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 339..409
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 503..573
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 667..736
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 953..1079
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1174..1289
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1392..1454
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1473..1501
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1861..2163
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DNA_BIND 1392..1454
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 140..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1673..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1431..1458
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 621..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2163
FT /evidence="ECO:0000313|EMBL:KRY19126.1"
SQ SEQUENCE 2163 AA; 247653 MW; 9E122EC75D15B50A CRC64;
MTSKRAHSSD EVPLAKRLRR SALSSAAEEQ VSKHIRELFT RMRDFVNEDG RHVSRPFFRF
ASKKLTPEYV KIVTNPMDLT LIHEKVKQDE YANVDQFMSD VNLMVENAKN FYKKDSVEYG
DACDLWNMIT EARNKQECNS DSMSEFSNRS IDSSPTPSLS PKRENVNNRT QACLLEKLLC
TVLTAKSEDG LLCEAFKVIP SKEEWPYYYE VIRDPIDLRT ISMKLRRGRY RSVNDLEKDL
NQLCRNAKLF NEPSSSVYRA ANAIRKLVAH RKMELTDSNA KSSNYYHEMK KNSAVIDNFL
REVCAVVEED SDDEQIPLST NAQLKNLYTF LRSCRDELSG QCLVEPFLRC PDRSSFPKYY
EKIAMPISFY AINHKLKVGL YNAVSGMLDD ISLLCSNVKV YFGENSELYK RALKLQLLAF
SKIQDTDTSQ LELSVWKDLE HLAGLDDVPK TESTLHLPAV KLEFNEESAR GKVGRKSFDD
ALAQYREKLL SVYNTVVNYR DQTGRVVALA FMEKPSKKLY PDYYKVIPEP IDLHMIKATI
DSDRYTSSQA LAADFELLFE NARHYNEDYS AIYTDANTLN GVFADAMKHS VITCVSWTHQ
ALLQLITHTC TRKNKLNSSI DRSRRGSYSS DSSGNRVSRK SQNISLGEHE LKLWYIYQAI
KEFRDPNNRT LSSVFLKLPS RTVRNYYEVI RKPIDLQKIC NKLSAKQYDS VEALVSDFAL
MFDNACKFND PDSLIYKDAL TLQRVLIQKA AELRRGEQHS PPIDVQSDVQ ELLNRIFSDV
LNYQDDLGRC LSDSLYEADE EYLIKTKDKD AVTLNIIKKR LEMKWYTRLD RFQQDMLEVF
KRARRLKSVN SQIFEDSVDL QSYFIKVRDE LTKRGDLFYS SAMRFTEKDL ISEIDAMRRR
NASKSNLESE VEDNSINEPK VRRLGSLINA VVDIHHFEAG LSFAVIKGRV DMKSCGEGDV
ELSSVDVGGT VYNVGHFAYV KQQQNNYMPR ILLISRIWKQ PTGAVGIFGN WYYKPSETCH
EVFRTDAYDR VEPSALAGRC HVLFIKTFVN HKPTNFADED VYVCESRYSV VSQEFKKIKV
SMQASWQLSS QGVHLEDRST PCLLLRMPLN LEPHDANNGS LLSSVQQEES TNKQEDNNSS
CLFVADTGRT DVVVAGQKEN LSTVAYEQIQ LNGCWIRLGD CVYIRVSEHE VKVVLVERIW
KSQDDILLHG IPFVSPHQIE HEPTQMFYKK ELFAVEPSET FSGRSVVGRC AVLSLKDYCS
SRPTEVNEAD VFLCDSRAVW NEYGKRVIPD NPERKFKLPT FRLSCEVPED EVAFFKKPMN
AEKEPSPFLM QRAIVYNDLP LPEQKNNNIR FSNSEIAEPS SSTISITATT TTTTTTATTT
VRVDTPSTPK LTSRSKSGYI LFSAVIRKRI MAENPECSFG HISKIVGAEW KKLSEEEKKK
YEEEAQKIAE EREKADQLTG GRLQLLPGQI RVYCCKWRDC DYQFDTVEQL NEHITSMHTS
QIVEGSDNQY VCMWLTCSKY RKEGRPFPSL ARLHRHIKEK HMPQSVKCLF PQNLGKHYIS
MSSSSGLDSA QLAQTSISAF QQQQQQTEQH QYYQQQQYLE QQQQNAVLMS TPTPAHQFSN
VAQTQPIRYA PPGSSINAPS AHVAYDNQTA GGAYPMHYSG QPLSPAVQQA MASSHGGRVR
SPASFSMPAT PTKSSVDPGS ILVRALEKPV EPIQLQPQVL RVSKVVHSKT YLNWARNRSG
RTLTLSGDSS ELKKARKIDT LESIAMDSKK TDAVVQALNI MTKALYCRVD SLRNLWETNY
FCCCTDFALF WTFAMFICWL FQRKKIAVSI LLDVLAQLGW QKMASITSNI SVQIGDVIGN
WKLTKLLGFG TYGYVYEVLN LKNDQLEAMK LEDQNPNQSL KVEILVLRSL NKHNARHCCQ
LLGSGRKDKF SYMVITLVGK TFEDISQVMK EKHGDNGKLD SCSAMYLCMQ ALEGLQDLHT
ICFIHRDVKP QNFAIGVHPN LRNVYMLDFG TVRKYLRSDG KHRRPRAKAG FRGTFNFASV
YALNLDDQSR RDDMWSWMYL LIQMTTGTLP WLDMPPTGNY FAELEQYKTM KNEHIENPAV
LLNGCPEEYY AIFNIIKQMT YYSAPEYEGI YELLKFSMKR ENSLSEDEPL QYEKILNEET
AHK
//
