ID B6H8S6_PENRW Unreviewed; 363 AA.
AC B6H8S6;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Pc16g06100 protein {ECO:0000313|EMBL:CAP93280.1};
GN ORFNames=Pc16g06100 {ECO:0000313|EMBL:CAP93280.1}, PCH_Pc16g06100
GN {ECO:0000313|EMBL:CAP93280.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP93280.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP93280.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; AM920431; CAP93280.1; -; Genomic_DNA.
DR RefSeq; XP_002560946.1; XM_002560900.1.
DR AlphaFoldDB; B6H8S6; -.
DR GeneID; 8314411; -.
DR KEGG; pcs:Pc16g06100; -.
DR VEuPathDB; FungiDB:PCH_Pc16g06100; -.
DR eggNOG; ENOG502RB81; Eukaryota.
DR HOGENOM; CLU_039268_2_1_1; -.
DR OMA; RWDLVFN; -.
DR OrthoDB; 3626832at2759; -.
DR BioCyc; PCHR:PC16G06100-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c16.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT DOMAIN 123..353
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 363 AA; 39683 MW; 6AC6B2BA403FD99F CRC64;
MNGARTPCLN IALVCEKKSA YLSHGYSEEQ CAALPHRGEI DAVMAALERL GHHVTLVSGI
EALVQLLAAG KHNGWDLVFN MAQGFHGSAR ESQVPALLEA YQVPYTFSDA ATMALCQNKQ
VTKTILDRHM IPNAPFSVIP MLDVVADFPK GFAALPPYPL FVKPVTEGSS KGIDGFNKVK
EPADLKPAVW ELVRKFPGQD ILVESFLSGR EFTVSILGTG PHSRVIGIRE HIWRTSPEHS
NTNGYHSDGS LDFASRDSKS SKGEKMLLYN DSHDMDEPQI KATCQVALQT WKVFNCRDGG
RVDIRFDSDE PGSTPNVLEV NPIAGLLPGH SPLPATAKMN GLSFEELLSE IIGSVCERSQ
YKN
//
