ID A0A0V1NN22_9BILA Unreviewed; 1060 AA.
AC A0A0V1NN22;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Protein Hook-like protein 3 {ECO:0000313|EMBL:KRZ85396.1};
GN ORFNames=T08_6828 {ECO:0000313|EMBL:KRZ85396.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ85396.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ85396.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ85396.1};
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:KRZ85396.1}.
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DR EMBL; JYDM01000144; KRZ85396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NN22; -.
DR STRING; 92180.A0A0V1NN22; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IEA:InterPro.
DR CDD; cd22211; HkD_SF; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR019339; CIR_N_dom.
DR InterPro; IPR008636; Hook_C.
DR InterPro; IPR043936; HOOK_N.
DR InterPro; IPR039875; LENG1-like.
DR PANTHER; PTHR22093; LEUKOCYTE RECEPTOR CLUSTER LRC MEMBER 1; 1.
DR PANTHER; PTHR22093:SF0; LEUKOCYTE RECEPTOR CLUSTER MEMBER 1; 1.
DR Pfam; PF05622; HOOK; 2.
DR Pfam; PF19047; HOOK_N; 1.
DR SMART; SM01083; Cir_N; 1.
DR SUPFAM; SSF116907; Hook domain; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT DOMAIN 823..859
FT /note="CBF1-interacting co-repressor CIR N-terminal"
FT /evidence="ECO:0000259|SMART:SM01083"
FT REGION 1003..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 193..456
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 625..659
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1003..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1060 AA; 122397 MW; 5669CE2134B5815F CRC64;
MQFFKMSSDS TNVEHDYDCL LKWMMSLQAN VTHIELNELT SGRAFIDALR VIDSNYFNDA
WMEVFKDANY EEREWRLRAN VLRKILKSVL KYNEEICNNV ISKNILPNVM VIARDGSKEE
IIKFIRIVVA AAVNGPGRDG MIKNVFDLEK SVQHTLMLTI QGWIFIPFFM AKLEFEGDNS
GELEVECKSA VLLENNSASL ADLSLRCEQM EKQMKHLTAE RDSYVQEIDK LKHQLSLVCK
RNEDSENERQ REISELKIQI ETLRDSLDES ESARDQMATE YDELLRQVQH SQMMKENSDN
AEKVRKLVDE VDELRARVAE ADALGDYVAT LEKKLGSVQF LLDLYIEVVG DLKAQIKALE
ELESNNLKLS VDFEEEQRKS HTYKLEAGVY KRQAQSLEQR LEEAVEKSLQ LEKEKQLIAD
RLAVLDQEHD RTLWERNQLS SRVEELRKRL QADENSGKSS PRAEIDVDIE SKIALAGDAP
MEIKHMLFKL KHENRILTET LTKEREQQKK CFDQASEEKC RLQSIIGDLE GKLSSLLIAC
AVNDRDNSGK SNCENVDPQQ DVEEVCRLKG KISRLYECVA DKEREIVNLK TAHTETLEKA
RQVIYHLDVA VKMNADDSNY TVADVEAMKA RLVQNEATIE DLKEENNRQQ IMFEQEERLI
TTAFYELVTH QFGFGLSDLL FSCFARGATA FLFQNQYRRP WQSDALNQAW QMHRKASEDR
LAACLSDPVT FLAEQRKIVC TKPSSSSFLS TASNYAFSSS VNPSSSALFH KILLIRVVVL
AVIGIGYHLV TDVFTFIWSH PRVPASSHCL LKNEKMNILP KKRWHVRTKD NVAKVRRDIA
QAEVEERQRL ARVQLAEQEA RTRFLISKVE HLIPKEQNNV VTVDQSDASG HVNLFADFEF
QESTNFGLNR EAEQEKRLLK EKEERRIGLL KYLGEGSSEY TKKLAWWQQV PDRHRTKPAD
SNDVHSSLDV VDVKRGQVNN NHKRKKKMML SVDELRRKRL NREREERLKA EKLKRKHENN
LHERDGGGVD NQQAESAADD NVKPKYSNQF NPIIAKQNRK
//