ID A0A232F1R2_9HYME Unreviewed; 955 AA.
AC A0A232F1R2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=RAP domain-containing protein {ECO:0000259|SMART:SM00952};
GN ORFNames=TSAR_002060 {ECO:0000313|EMBL:OXU24377.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU24377.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU24377.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU24377.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU24377.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|RuleBase:RU000590}.
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:OXU24377.1}.
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DR EMBL; NNAY01001319; OXU24377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232F1R2; -.
DR STRING; 543379.A0A232F1R2; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IEA:InterPro.
DR CDD; cd01087; Prolidase; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR010622; FAST_Leu-rich.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR InterPro; IPR013584; RAP.
DR PANTHER; PTHR48392; -; 1.
DR PANTHER; PTHR48392:SF2; PEPTIDASE D; 1.
DR Pfam; PF06743; FAST_1; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM00952; RAP; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335}.
FT DOMAIN 580..638
FT /note="RAP"
FT /evidence="ECO:0000259|SMART:SM00952"
SQ SEQUENCE 955 AA; 108695 MW; E8A6B7F4CE539BB9 CRC64;
MFVQEGFDIY ELPIVIKKIS DIHFFCNAKY IDNCPATLCI SQPLKEHKSE EHCNALQNSK
QKISIDADNI PILFDQEVNI SNILNVEQIF KETVNSVSEE KIKALLLDSA IHMDINSRMA
LQCLKKIVNM ERKHRKLMRA SKFIPNRHMM LRQLSEIIIT SQDSGVILEA LSIIIKDKFL
PPNNSYKDIL TNEALIRSTN GDFSIQQLID ITKILSIFRD AKYQDAIDYF WTGIVIKQED
ITAHHLVPLF KLLSYMKRSR IRVQILLEKK LIKNYHKLSA PQMTDILNIF QKSSKSSVVM
ECVSKWANMH LLSISKYDFL EFVESLTTAK FINFTLEKAI EKALDMQKMK SNDHALMLAV
AVYCSTVHLR NICICNRVVK YLEKHSKYLP LDSSVEMIVA LGNLNFEPKS KDDFWHAFEQ
TLDNQFFYLR QEKVMQVLLS CAYINKYFPK CMQKIFSPGF LDNLESQGDA VMAQSLRNQL
YVLDTAMTLE CTTYSGPLLF RSNQLDPVVI DMQIIRTISR IHSQLIKLAG DSKKLSTHVT
LSNLSTTPLY IIDALIHKQS KYTRALELDL IKEKNENTAV IVLLPHHYCW SSRKLIGEQA
MRIRHLRKLG FRVMLLDFNN LCLTYGKVHE LAKYLNRAFK TARVIKTPKE IEVLRYVVKV
SSDAHKSVMR TVRPGLAEFQ AEAAFQHYAY SVGGCRYVSY TCICGSGCNA AILHYGHAGA
PNNKVLKDGD MCLFDMGGNY CGYAADITCS FPANGKFTDD QKIVYNAVLD ARNAVMNAAK
PGVLWTDMHL LANRVMLEAL KKGGLLQGDV GDMIKAGLNA VFQPHGLGHF LGLDVHDVGG
YLPNHPARSK EPGLNKLRTA RPLMAGMVLT IEPGCYFIDW LLDKARENKE QSKFIVWEKL
SRFRGTGGVR IEDDVLITET GTENLTIVPR TVEEIEAWMA PNREKLQLPQ EKLCV
//
