ID A0A0V1PAT2_9BILA Unreviewed; 944 AA.
AC A0A0V1PAT2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=RING finger protein nhl-1 {ECO:0000313|EMBL:KRZ93312.1};
GN Name=nhl-1 {ECO:0000313|EMBL:KRZ93312.1};
GN ORFNames=T08_2918 {ECO:0000313|EMBL:KRZ93312.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ93312.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ93312.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ93312.1};
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:KRZ93312.1}.
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DR EMBL; JYDM01000026; KRZ93312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PAT2; -.
DR STRING; 92180.A0A0V1PAT2; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd14954; NHL_TRIM71_like; 1.
DR CDD; cd16524; RING-HC_NHL-1-like; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR PANTHER; PTHR24104:SF8; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51125; NHL; 6.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}; Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 53..95
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 139..182
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 670..712
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 716..759
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 763..806
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 812..853
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 857..900
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 906..944
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 374..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..224
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 374..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 108049 MW; 58A2F0FB2D358B3E CRC64;
MESNPCESSC NCKKQTKVDM EENIGILHHQ TSSSKQQPDW VNPLEKIEEL LTCAICLDRY
KHPKVLPCQH SFCLEPCLDG LIDVIRRTVK CPECRIEHLV PPDGARGFPT NYTLVGFLEI
HLQATEQSTS ELEAYIRSYN MERCKICDEK AALRLCSHCN KKICQECQNN HVEMMKRDLN
RLMNQVKRVA GRITDWTDCI IRATENLNLQ ADSLKEEIRE CLRRLYKEVK KREEVLLAEV
DTYCSIEKRI LKSVQAAFDF ESNNINEAVA RVESYQKGER NMTLDVLVRY KQMFFDGLEH
LRSFTPDVDA LCNKRLRFAV NTSTASLASM IAHFGEIQVC HFMTNISLQN SDIMVPRFLR
VDLESDELNF EKRERSTALR HHEEQPLEGK KTSMLTEESN KTGRKANRLS TYKPSEVYES
HRQSERVHVD ICEAFASSPW QFGIHEPDPD QPTCSNVAYV DYKRPKIRTQ SSDDPDDELN
TRVANIRRDF ESRRRQLDQQ IHTIVHQGNS VKSSQPTSIV DDRINELNTD EEMDIQQIPI
QVFTSTIASC SWPAVVVVDD EADSSPEEIL DDHHQNVASA DNNNAASTSL SLFNDDDERK
AKRRSFVSDD KSDNKRDLNE SNRRWSNKIP PTTSMKQAPF SCDKIPVKRY TYTNNAPKNN
YARKGRMIVK FGEKGDSLGQ FNWPRGIALS SNGREVIVCD SSNHRLQVFD LHGHFLRSYG
KYGNGSGEFD SPAGVAVNHC NQLIVSDRYN HRLQILDPNG RSVRILGCHG QNNGRFNNPW
GLTIGSHGII YVCDRDNHRV QVLQSDGSFY AKFGELGSRE GQFQHPHFIV ANHHDQLIVS
DTSNHRIQVF DQNGQFQFAF GSEGHHEGQF KYPKGVAIDD QEFIFVADSG NSRVQIFYPD
GRFFAQFGSW GNGDGELRSL EDLKVTSDGF IIVTDRENHR VQIF
//
