ID A0A0V1MYK6_9BILA Unreviewed; 1069 AA.
AC A0A0V1MYK6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=E3 ubiquitin-protein ligase synoviolin B {ECO:0000313|EMBL:KRZ76829.1};
GN Name=Nob1 {ECO:0000313|EMBL:KRZ76829.1};
GN ORFNames=T10_760 {ECO:0000313|EMBL:KRZ76829.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ76829.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ76829.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ76829.1};
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 -!- 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:KRZ76829.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDO01000025; KRZ76829.1; -; Genomic_DNA.
DR EMBL; JYDO01000025; KRZ76831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1MYK6; -.
DR STRING; 268474.A0A0V1MYK6; -.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09876; PIN_Nob1-like; 1.
DR CDD; cd16479; RING-H2_synoviolin; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 6.20.210.10; Nin one binding (NOB1), Zn-ribbon-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039907; NOB1.
DR InterPro; IPR036283; NOB1_Zf-like_sf.
DR InterPro; IPR014881; NOB1_Zn-bd.
DR InterPro; IPR033411; Ribonuclease_PIN.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12814; RNA-BINDING PROTEIN NOB1; 1.
DR PANTHER; PTHR12814:SF2; RNA-BINDING PROTEIN NOB1; 1.
DR Pfam; PF08772; NOB1_Zn_bind; 1.
DR Pfam; PF17146; PIN_6; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF144206; NOB1 zinc finger-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
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 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 342..381
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 396..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 120497 MW; 24C55205B435129C CRC64;
MVLIRCITTG IYLYLSITFQ IADVKLAAVF IICEFVSLTP RKWFFILANT MQVRYGHLLV
FSLLLTAAVV LNAFHQRKQF YPSMVYLSKS NASVTALYIQ AFVLVSLVGK LFQMIFFGSL
HRFEQEHIAD RAMFAVTETC LAFTIFRDDF SPRFVAQFTQ LFFFKCFHWM AEERIDYMER
SPVITTLFCA RVMGLIAILS AVDSYHISHA YFTTLQKGAT PQIVFGFEYA ILLTVVFHIA
VKYVLHRVDL RQPHPWENKA VYLLYFELVI VFLRVLLYAI FICVTMQLHT FPLFSIRPMY
LALKTLKKAI MDAILSQRAI RNMNSLYPDV TAEDLSRGDC VCIICREDIT ERAKKLPCNH
IFHISCLRSW FQRQQTCPIC RLNVLQLRQT ERQQQQQQPQ QQQQQQQAAN IAGTSTTAAG
TSTTAANQIP APNFTNMNMP AWFAGLPAGI IPPPAPGVGD GTPSSINPTV FAGFTGNGNT
SATLPMPIMP PFFPFTQAFP TPPDFTGLSD EEVRRMEGNE RTAVEARIRC LRNIQTLLDG
AVVLMQQYTS LMSAMDLKYS EKRTVNTEET EHKKETNSKT EEVNAKTVNI DELVEKPSTS
AAAIAGTSSG DAQNELRQRR LQHYEKSTKA VHLCIYLYNN FCKYNQSSLC TGLNFFTTFA
IFSLINKSPR SFGGTKAGFI CILMTEMQLQ VEHLVVDTVG FVKADDLRKY GKNIYTIQDV
LNEIRDSNTR KKLSVLPYDL KTVIPDGKAI QFVTEFAKKT GDYPSLSVTD VKLIAAVYTM
ELEHVGSEHI IQEPKVQKTS SVGGQKCEEG KGLPGFYMPS KKKQSDCNDL EEAVRKIDIH
DNSTSEEENS FSESDSEYED EIRDTSNLSG WITPENFSST VDSANDTVPV ACLTADFAIQ
NVLLHMGLKV VSVDGMLIKQ LKTYILRCFS CFHTTSKMMK KFCPNCGNAT LKRLAISVDE
NGCTVFHFSR RKVISVRGSK FSIPAPKGGK HANNLILCED QPVSQNRLSR KARQNLDVFD
PDYIAGHSPF SLNDITSRSA LLGIRAIHRP PRRNPNTYSL GRKRGGKKR
//