ID Q5B612_EMENI Unreviewed; 772 AA.
AC Q5B612; C8V5P8;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Glutamate carboxypeptidase, putative (AFU_orthologue AFUA_1G03740) {ECO:0000313|EMBL:CBF74875.1};
GN ORFNames=ANIA_04018 {ECO:0000313|EMBL:CBF74875.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF74875.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; BN001302; CBF74875.1; -; Genomic_DNA.
DR RefSeq; XP_661622.1; XM_656530.1.
DR AlphaFoldDB; Q5B612; -.
DR STRING; 227321.Q5B612; -.
DR EnsemblFungi; CBF74875; CBF74875; ANIA_04018.
DR GeneID; 2873438; -.
DR KEGG; ani:AN4018.2; -.
DR VEuPathDB; FungiDB:AN4018; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_2_0_1; -.
DR InParanoid; Q5B612; -.
DR OMA; LWNVIGT; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08022; M28_PSMA_like; 1.
DR CDD; cd02121; PA_GCPII_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 1.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CBF74875.1};
KW Hydrolase {ECO:0000313|EMBL:CBF74875.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:CBF74875.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 205..276
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 395..581
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 645..772
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 265..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 85634 MW; 99960760AD589B6C CRC64;
MKEKAIMSPS ETTPLLVPVQ VAPQRHRYPH DKLRRACSYS LSLILAVALV LFLFPQALFP
REGGSLWSYL PGAQPYPNTW PSGNGLDQEE LQTLLLGTPS AARAREWSKY YTSGPHLTGK
NLSQALWTKE RWEEFGIADT KIATYDVYLN YPLDHRLALY QGGNISYEAS LEEDVLEEDS
TSGLPDRVPT FHGYSASGNV TASFVFVNFG TYADFEDLVN ANVSLSGKIA IAKYGRVFRG
LKVKRAQELG MVGVVLYDDP QTDGEYTEEN GYKPYPEGPA RNPSAVQRGS TQFLSIGFAP
GDPTTPGYPS KPGCERQDPH HFIPSIPSIP VSNRDVLPLL KALNGHGPKA SDFNEAWQGG
GLAYKGVEYN IGPSPDDLVI NLYNEQEYVT TPLWNVIGVI PGSLPDTIIL GNHRDAWIAG
GAGDPNSGSA VLNEVVRSFG EARRAGWKPL RTIVFASWDG EEYGLLGSTE WVEDHLPWLS
KSNVAYLNVD VAASGTRLAP NASPLLNKLI YEITGLVQSP NQTVPGQTVR DVWDGYIGTM
GSGSDFTAFQ DFAGIPSYDL GFSPSSQDPV YHYHSNYDSF DWMQRFGDPD WLYHEACAKI
WALAAAKLAE TPVLFFNATD YSLGLEEYVD RIRPAADNLP NGLTFDFGPL YEAISRLQKT
AIEFDAYAAD LTSQLTEELP WYLWWKKVRL FFLIHEVNTK YKNIERQFLY QQGLDGRSWF
KHVVFAPGLW TGYAGATYPG IVESLEAGDV ANAAKWQYIV IERVKAATEL LQ
//
