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Database: UniProt
Entry: A0A0V1PDV6_9BILA
LinkDB: A0A0V1PDV6_9BILA
Original site: A0A0V1PDV6_9BILA 
ID   A0A0V1PDV6_9BILA        Unreviewed;      1400 AA.
AC   A0A0V1PDV6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Pre-mRNA branch site protein p14 {ECO:0000313|EMBL:KRZ94447.1};
GN   Name=Sf3b14 {ECO:0000313|EMBL:KRZ94447.1};
GN   ORFNames=T08_16120 {ECO:0000313|EMBL:KRZ94447.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ94447.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ94447.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ94447.1};
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:KRZ94447.1}.
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DR   EMBL; JYDM01000018; KRZ94447.1; -; Genomic_DNA.
DR   STRING; 92180.A0A0V1PDV6; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd12241; RRM_SF3B14; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.170.140.10; Chitin binding domain; 4.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034150; SF3B6_RRM.
DR   PANTHER; PTHR23301; CHITIN BINDING PERITROPHIN-A; 1.
DR   PANTHER; PTHR23301:SF109; PROTEIN CBG16847; 1.
DR   Pfam; PF01607; CBM_14; 5.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00494; ChtBD2; 11.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 8.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50940; CHIT_BIND_II; 7.
DR   PROSITE; PS50102; RRM; 1.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}.
FT   DOMAIN          17..92
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          148..207
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          725..779
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          789..847
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          1028..1085
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          1196..1253
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          1272..1329
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          1342..1400
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
SQ   SEQUENCE   1400 AA;  158728 MW;  A475A600C58BE3BC CRC64;
     MAMGRKANVR LPPEVNRILY VKNLPYKITG EEMYDIFGKY GAIRQIRVGN TPETRGTAFV
     VYEDIFDAKN ACDHLSGFNV CNRYLVVLYY QANKAYLRMD TEKSKKELER VKAKYGLGVE
     TEFLRKINFI ENNQFYKYSA FYRVDFVEFN CSSLSSGNFA DLNEICCAYY YTCNNGEAKR
     TLCPDGLYYD KKSKTCKDKE EIAECNLCYL NKNENVPLSA CSSEYIFCHN TIPIRQWCFA
     NEIFDIRTRL CTSRDRASGC LPNEFQFKNV HGLDNLCSEY DRQFKQVKEI QSCLPFFIEC
     SNDNVRIMQC REFGTVFDDF YKTCIPKDLS FTCSGLDAKV NLLNSKEEKS GCPEKMFKRK
     RRMIFQSDYA MHPLYGSILK KTNNSQTISI HPNGALEDFD LTKAVVNDNE RDRLKKGILF
     GNENSHLYLD TDNLHFPSFQ SFNDKADDTL SNTDNNVRKL GCLKNLQQKN GYRFVPSNSD
     DEIFSADLHA KMANADLADA QFPSRSQLGN DWDNKDILVA PKTDLNEICE MIRKSCESEQ
     PDSSGYGNSL TDETNDKRRE KCNVEVTKCL QSLKSDNSTL FQQYHFPFRK LLNELCKNGD
     VKFAVAPCSR FYVHCIEGAY GLKSCLENTS YNAQAGQCMP CTVSTVSATV VTTSETIKCV
     GNFEILKDGL YEERACDHKT EHSSRKVFGQ RCVCQSGYLR LASESGSLCV SENYCRMHKV
     AMTENKFCSG SKADFSSLVD CNEVYYRCQR NRTNFSFCNQ GQVFDLAKGR CVMRQLCSRK
     MKPILTHLND LCIGRKDGAY SLITNLSYPT FYMCTYEMIV FSSCERGSLF DWSRKICMPM
     KIQDCTDGIQ PKGHFEAGYS ICWGGMIYET ACSDGMVLKE VTDHGKIGYV CVEKKDFSNQ
     GYPKSCYGKS DGFYLNLTSE TYFFCANHFA TYLNGENNFS FDCTESKSSA DNESISCEIS
     YKLTNLTSFI KRLKAEQSQS FEVAPCEANY FTKKNSAMIL EKCAAGEVFV SLFQRCMKMS
     TDGRCTRRIL CNGKMDAIYP ILPCHATYYI CFGGYRYEEN CPPGKVFSMH HQSCVAFLDD
     PSCHWNSSSL LLPAKHCSEF GNCQPVYQNC IIEGQIMNIT CGDGNVYDIS LKQCVRKTHC
     SMESYTTTTT ASSSFSAGTS HASISPLVVG STVDFETSPI VDSTESVDVG KSFVITNACK
     NKPNGSYPIK GNCKQFLSCS NEISYVMECP ANTVYNAKIA NCGHPEDVPD CQSYIVNEKL
     TRDVSRAASW MKTFCADKAD GYYRHFNRCD QFIQCLKRRK IILSCTKGLV FNPTMKVCDL
     PRRVPECNII LNNLVEKESA PDDYCKGIEH GAFTKDPNNC GRFYRCVHGK AHRFDCPPNL
     VFNPKLNTCD WLSNVSGCAV
//
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