ID A0A0V1L5Q7_9BILA Unreviewed; 1101 AA.
AC A0A0V1L5Q7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Heterogeneous nuclear ribonucleoprotein U-like protein 1 {ECO:0000313|EMBL:KRZ54727.1};
GN Name=Hnrnpul1 {ECO:0000313|EMBL:KRZ54727.1};
GN ORFNames=T02_4299 {ECO:0000313|EMBL:KRZ54727.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ54727.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ54727.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ54727.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ54727.1}.
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DR EMBL; JYDW01000131; KRZ54727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1L5Q7; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16475; RING-H2_RNF121-like; 1.
DR CDD; cd12884; SPRY_hnRNP; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035778; SPRY_hnRNP_U.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12381:SF56; B30.2_SPRY DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR12381; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN U FAMILY MEMBER; 1.
DR Pfam; PF13671; AAA_33; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Ribonucleoprotein {ECO:0000313|EMBL:KRZ54727.1};
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:PRU00175}.
FT TRANSMEM 649..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 680..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 711..744
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 751..768
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 119..316
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 802..851
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 125999 MW; D5A10F38D1F06572 CRC64;
MKLSNENSEC KTIEEEKKDD SSCDTDEVTD AEIESSGSDS DSDNDRASKS EACNGEEKLD
EDAQRRFIEE FILINANLKN NHESDDSETS ETTTVNKNSW KDDEKRIHYL KENSLGDDDE
VTAEFANEFD LENCDETQVF IDPNNRDLNM KVMAKEPFIV LPYNEEGFVH MLASGRATYG
VYYGCVAFEV KILENVDLSG NEYREEENAY ELRLGWTVDT SEMRLGETTY SYAYCSNGKL
ATEKYFENWG CKYSPTDVIT CLVNFSEGTV SFCLNGKLIG IAFRFPVQTF SQRRPLFPAF
TTKNVKFHIN FGQQPEPWFP LPEEYVFIND VPYGNRIRGP LPMKSKEECV VVMMIGLPGC
GKSQWVRDYL SGHPEERWWL LSPSHALEQM SIQGTARFKF HQGRWDIVMG TAAKCYRKLL
QMACKKKRNY IIDATNVFSV ARKRKLAAFR EFQRKAIVIV PSEEEYARRL MHQSKNGTTQ
VPADALLEMK AGFSLPTMRD GQFTDIEFVE LQVKDAERIV ARYNQEGRAL RPPEKRRRGG
GVDCQQDVNF FVEAKHTADS YLQEETVLHT NRYFSNHQQS SNDVNNVSLG KSWNSAPLSS
NPVGIDQQRN EHFYDNYTSE QLKGLDEALQ MKIKHARFLL KHMGHEDKHM LIVCIAFFGV
MIAQYLLFEW KKRYSKSYTR FTLFSMWIIP FALSLWRGFW RFIVSWLAFT IYKWFLFIHK
LCSFLGFFGY VVTVLTLFGI GILLSMKFDD LFNFGILCLF YGIYYGVLNR DLAAICSNTM
AAHIGYYSDE GLPRRTLESD MCAVCGSKIS ANDNERQVEQ LYNLSCGHTF HEFCIRGWCI
VGKNEICPYC REKVNLKEFF TNPWEKTEAV LMYVLDFVRY LVAWNPILNN RSFVMHTLTS
SGRNKLKKGM ESQGVEQSGG TNAASSNCGR DDNDENNEGR TNKSSSAEEN AANSAFECNI
CLETAREAVI SIWSCLHQWF ETRPANPICP VCKSSISKEK VIPLYGRGGS GCDPREKVPP
RPAGQRSESF RTGFPGFNFG GEHAGGFQLS LGIGAFPFTF LTSTFNLGDV RHPHNGNTNN
AIPREEEQFL SRMLFWMALD R
//
