ID A0A164LJF3_9CRUS Unreviewed; 893 AA.
AC A0A164LJF3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Retrotransposon gag domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=APZ42_032944 {ECO:0000313|EMBL:KZS04169.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS04169.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS04169.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS04169.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS04169.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) 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:KZS04169.1}.
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DR EMBL; LRGB01003128; KZS04169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164LJF3; -.
DR STRING; 35525.A0A164LJF3; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00303; retropepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR33223; CCHC-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR33223:SF6; TY3_CAPSID DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13975; gag-asp_proteas; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 123..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..339
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 557..584
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 347..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 101402 MW; 8CA71EB266DEC159 CRC64;
MAAIGAGAAA LGAAAPGAAA GAICAVAWFW SIRSSVSVAR SLSSSAVMET LLYCFILSIF
LQLLPATATP PSKKVVTWQI HRLETFTFGG PNETLEEKFL VCASFASCKC STLLSTSLQA
TDIGKPSSNQ EPIAEPSQKK RGKQRSCRDR RARNNQKFEG ERTRLNQKLN TAENQIKQVS
ETAEQLQKEI KVLADRLDKA TTEKINLKKN LLDFTSKNKN LEKELQELQN RVQRQENQTI
IQENRGKEYK KLQVKFIETE DSNDSRLDKD EPGEITKLVG DINELILPTD SGVKSLHYEL
EIKQTNDFEQ KIENLKTQIE HLNKKIIYLE KENQQLKKKV DMGVTQGDEE TSKNTTQKTF
ANTSKKNPKD NDIPTTEQDD EDAKKVNRYF TQPLVKALGE LFSIEDKKAI PIFKGKSTDK
LISEWLRGAE HVARNNEWDD NKKIRFFSDR LKGEAFEWHE NYAEEEGDDL NSQDWKEALI
TRFQDTYDLA TLEKKPKENC RAFVSRLNNL YDTNAENTED FDALCKQLFI SEKILHTKEA
TDDKEMSAVI AEIMHHEKQQ DDKIQLLEQK LSEALSELKF TNTKRESSQE NDVTIAATDQ
YEKGRPRSII TPENQAEKEL SVKTETTAPI AEIKIHQDEE IIILQDTGNP DFHLTNVPHI
GTNTPTGSDV EVEIPKLIRI PVKIFNKEII ALVDTGAATS LVSSKILDTL ECNEYLKQVK
NTNTPIFRMV SGQELKSIGK FEFSVVINDY HIFNHHFYVM NNLNEQCILG LHFLSNNNVK
INTRNRQICH DHFGVEHNFG SNTMPIYSVT FSNAGIHIPL NPIDRGDEDL TQQDYRNLQS
FTKLDFNNKT NQIAKIAENV LNVSDDIQTK IEILLKKHEG LFADQESDLG LAT
//