ID A0A0V1HPD3_9BILA Unreviewed; 1137 AA.
AC A0A0V1HPD3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Ankyrin repeat and FYVE domain-containing protein 1 {ECO:0000313|EMBL:KRZ12606.1};
GN Name=Ankfy1 {ECO:0000313|EMBL:KRZ12606.1};
GN ORFNames=T11_408 {ECO:0000313|EMBL:KRZ12606.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ12606.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ12606.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ12606.1};
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:KRZ12606.1}.
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DR EMBL; JYDP01000039; KRZ12606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HPD3; -.
DR STRING; 268475.A0A0V1HPD3; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15728; FYVE_ANFY1; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR049764; ANFY1_FYVE.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24118:SF99; CHARON; 1.
DR PANTHER; PTHR24118; POTE ANKYRIN DOMAIN; 1.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00248; ANK; 21.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 3.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 7.
DR PROSITE; PS50088; ANK_REPEAT; 12.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 77..139
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REPEAT 265..297
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 445..477
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 478..510
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 555..587
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 621..653
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 654..686
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 736..768
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 769..802
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 837..869
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 872..904
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 905..937
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 938..971
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1071..1131
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT COILED 14..48
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1137 AA; 125967 MW; 11B74606860E3242 CRC64;
MATLNDSTDE AKTLVQMEQM LSSLREEYRK VQNSLIECEQ KYETLQASVD FDELPEKSFA
RRLVMNTREL FESEIFSDLT VMLDGHEVPC HRYVLAARSD CWNFSAMANM TALNFDNISY
NIGYILLKWI YTDEVDHRLD EVMLIELMQV AKRFKLSQLI ERCERLLIAC VDEKNCIELY
KHAYELNAPR LMESAASKIY SFRNEMSPDR FDILPGVLLH ELLESKFKYP LHEAILLQRK
DAVDLCLADK GPKLCNRLNE LMNVHGDCPL ALALASRQEA TCRTLIDHGA DVDAKSRNGD
TLLLYFLKKQ DYWACEFLLQ HAARLDCIDP VGGGNLLHVL AACKAESATD KEILNTLIQR
FLSSGISAIN STDSHLNTPL HLSIIHDNMA LFNGLMKIQQ LDLEILNREG LPALWYALAK
NDAEFQYASA LVSRGANFNA IRPRSGDTLL NLCVIDGLLE AAIYLIKKGA SVDVPNAKGE
TALYLASSSG LDQLVQILLN SGANPNVQTK ENRDTPLHVA IRRIYTHVID SLLGEKAGSN
GCRRVPLLFE IYNSNDDSAL SLAISLGFYS VADKLIDFGA DVNAKMPDGR SLLLRFISNG
TVEGALYLIK KGCCPTAVES NSPAPLFLAI EHGVTSVVSA LCQCGADLAA KNANGDSPLW
YALCSNHESI ADILVEHGAD VDCWSTGPNG CMQTMLHRAI DENDERIACY LIKNKCDVNA
IRKEGPCGSG HSEAVEKQTP LHMAATWGLL DVVSALIAYG ASINAQDSEG KTPLHLAVIN
QHLAITERLL QSHHIDLNMP DKAGLTPFAW AVQGKADQIC VAILKRNPQV ALQVDSAGYN
VLHNAIKKQD FELFLFLLSV RVDVNVRTQD SERLSPLHIA CRVGNDLIIR NLLCAGSRIN
DTTSSKQTAL HIAAQNDKAL VCSILLENQI DATALDNEGN NALHVAVQYG SMECIQTLLT
ESNINPFLTN SKGYGILHLL GLFGKENAAS ILVSIMCIIP DYPIEMPDPD GNTLLLFAFM
NENYLLCREA IRAGACVGVC NRHFVSIFNY PMPSPKLLFR ILDQLDHEPK WAEGDSCSEC
KVKFGITTRK HHCRHCGRLL CTKCSEHFLP ILKYDIPKPV RVCNVCYDVL TSGVSQN
//
