ID A0A182XLV4_ANOQN Unreviewed; 1350 AA.
AC A0A182XLV4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=MYND-type domain-containing protein {ECO:0000259|PROSITE:PS50865};
OS Anopheles quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA010849-PA, ECO:0000313|Proteomes:UP000076407};
RN [1] {ECO:0000313|Proteomes:UP000076407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AQUA010849-PA}
RP IDENTIFICATION.
RC STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA010849-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EnsemblMetazoa; AQUA010849-RA; AQUA010849-PA; AQUA010849.
DR VEuPathDB; VectorBase:AQUA010849; -.
DR Proteomes; UP000076407; Unassembled WGS sequence.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03860; M14_CP_A-B_like; 2.
DR CDD; cd20071; SET_SMYD; 1.
DR Gene3D; 1.10.220.160; -; 1.
DR Gene3D; 6.10.140.2220; -; 2.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 2.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR11705:SF60; FI16720P1; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 2.
DR Pfam; PF02244; Propep_M14; 2.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 2.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 2.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 2.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 2.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1350
FT /note="MYND-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008143184"
FT DOMAIN 838..874
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
SQ SEQUENCE 1350 AA; 151679 MW; 98DD4D27F287E98D CRC64;
MVACGQVLAC WTLLALLAGV SADPARYDHF RLYRLLIETP AQVEMLQQLE KQSDSYAFIG
HARQPNQNLT IMVAPHKIAE ITELLQRYEL QGSILLYNMQ ELIDREKATI KPKGTRPEEF
GWQFYHHLDT INEWLRWQAG RHPELQLLEL GASYENRSLY GVKLGTNPAN SGVFVECGIH
AREWISPASC TFVLNELLTS DRPDVRRLAD RFNWIIFPVV NPDGYRYTFE GDRLWRKNTQ
PYGVCRGVDL NRNFASDWNG PGASSDPCRY DFAGGSAASE PETRALVEFL ERHVAQWRIR
TYFSVHSFSQ LVMFPYGYKV DRVPNYDDLV AIGRKGVDAI ERAHGARYVS GAMIETIYPS
SGDSVDWVYS ALGVPVAYTF ELRGPPDSTN MFVLPAEEII PTAEELLAAF IAMLGCKPRS
RRTRPDARIL SSVAGKMSGA AAADGAARYD HYRLYRVELA TDEQVQLFQQ LEAKSDSCTF
YGHARQPGQQ LTIMVSASKV ADFEDLLVLH AVSGRVLERN MQQLIEREAA TVQPASTDPS
QMDWEHYFQL ETIYAWMELL AERFPGAVST LDIGTSYEGR PIRGVKLSRR PGNKAIVVEG
GIHAREWISP ATATFLLHEL LTSEDPTVRE LGTAYDWFFF PIVNPDGYRF TFTGDRLWRK
NRKPYGLCRG VDLNRNFDSN WGGVGSSDDP CSYDFSGSGP FSEPEAVALA DFVRNNVGPA
RIRTYIALHS YSQLLMFPYG HTADRVPNYD HLRSITEKGI AALTAVSGTS YRGGSKYETI
YPSSGGSIDW AYRPGGVPVS LTFELRGPPD STDMFILPAD QIRPVGKETL AAFVAIVQEA
ARLAAQRCAG CQQVGYCGRD HQRADWKAQH RDQCRRFKVV RNDRLGRHLV ATKHIKQGEI
IYRDEPYAVG PKIANVPLCL GCNRNLMAGW DATRGLDRFH ECCRCGWPLC GPGCEEAAQH
RPECSVLAGS GYRPNIRPNP SNPEQRESAY CVIVPLRVLL LERIAPERYA TVQGFESHLD
ERLASPLYGV LRSNLVPFLR QVLRLQQYSE QTVLQLSAIL DTNCYEIRLP EQHVKVRGLY
PLGAMLSHDC RPNTKHYFDD RLHMVLVATV DIPAGGVIHA SYTQPLLGTV QRRLALRQAK
CFDCCCERCA DPTEYGTSAS GFRCPNCRRT PSLVLAAEPT NYRTVWRCQN RRCAYHERPD
QYVARCERMQ QELLALDRTE PAGYEEFLAR HATTLHPWNA YMLQAKYALT QLLGSARPAK
APPSEAAARR TVELCRDLLA VAERLEPGYS TFRAKLLLEL GSALATLHAL GVLSDPERQE
WRTTRAELEC IAKTDPTVDV SSVGKENGSS
//
