ID A0A2K1IZ24_PHYPA Unreviewed; 747 AA.
AC A0A2K1IZ24;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aspartyl aminopeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHYPA_024351 {ECO:0000313|EMBL:PNR34534.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR34534.1};
RN [1] {ECO:0000313|EMBL:PNR34534.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c19_20030V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR34534.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c19_20030V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c19_20030V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-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 M18 family.
CC {ECO:0000256|ARBA:ARBA00008290}.
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DR EMBL; ABEU02000019; PNR34534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1IZ24; -.
DR STRING; 3218.A0A2K1IZ24; -.
DR PaxDb; 3218-PP1S414_2V6-1; -.
DR EnsemblPlants; Pp3c19_20030V3.1; Pp3c19_20030V3.1; Pp3c19_20030.
DR EnsemblPlants; Pp3c19_20030V3.2; Pp3c19_20030V3.2; Pp3c19_20030.
DR EnsemblPlants; Pp3c19_20030V3.3; Pp3c19_20030V3.3; Pp3c19_20030.
DR Gramene; Pp3c19_20030V3.1; Pp3c19_20030V3.1; Pp3c19_20030.
DR Gramene; Pp3c19_20030V3.2; Pp3c19_20030V3.2; Pp3c19_20030.
DR Gramene; Pp3c19_20030V3.3; Pp3c19_20030V3.3; Pp3c19_20030.
DR InParanoid; A0A2K1IZ24; -.
DR OMA; EAECINC; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000006727; Chromosome 19.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF15; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
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 Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT REGION 150..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 82824 MW; A6221110436362B0 CRC64;
MDEVSRTPSF LIDIELWQKF NLELRAACHW CTHHHTTTPA EAAKQLERGE GWPRDWISRK
VKNSTRQFGG LFICPAPDCA GHSNAKGERR RRWFCRFCIN RHLSVDLKNF FQFDEVQGKW
IQIPDLFCWH CQARSGEAEC INCPQKHTKR AKRAKENPLP PTRSLLGPPG HTNVAGVVSV
LLAAAGDGDY DGVSSEGRGG PTNEAHSMDE SNFGVGETHV RLGLPMHASP VSDFRYGPPP
LHQQHQQQPP PPRAFFSEKG LVCRESQSSV VPHLLDYVNN SCTPFHATAE TRNHLLSSGF
QEISECEEWA VQPGGRYFFT RNMCSIYAFA VGHKYKPGNG FHVVAAHTDS PCPKLKPVSY
SAKGGFLHVR VQPYGAGVWQ TWFDRDLSIA GRVLIRRKDG ELVNELVRVR RPILRIPTVA
KILDRGLAAD ASKADAEVNL APILAMQIES ELAMSCDSES SMAMEHNDHG SHVYPQPTTA
HHPLLIQVLA DELKCDVSEV ADFDLSVYDT QPGCVGGARD DFVFAGRLDN LTSTFCALWA
LLDTCADSSS LVDESCVRMI ALFDSGELGG TDSVQAAGPS TLLQAMTRIT RWLARGSDSE
GVVERAMRRS LIVTADMVDG MHPSQVCPPG QEESFHQPKL RDGLVLKQDA GNSNDIMTLF
LFREVAKRSS IPIQNFPVSR EIGCCSTVSS ILAAGYGLRL IDCGVPLLSM HSVREMCSTE
DIDTTFRHFR AFFQHFTSMD EQPRVDV
//
