ID A0A068RFF6_9FUNG Unreviewed; 617 AA.
AC A0A068RFF6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptide-n-(N-acetyl-beta-glucosaminyl)asparagine amidase-like {ECO:0000313|EMBL:CDH48440.1};
GN ORFNames=LCOR_00221.1 {ECO:0000313|EMBL:CDH48440.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH48440.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH48440.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000256|ARBA:ARBA00009390}.
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:CDH48440.1}.
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DR EMBL; CBTN010000001; CDH48440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068RFF6; -.
DR STRING; 1263082.A0A068RFF6; -.
DR VEuPathDB; FungiDB:LCOR_00221.1; -.
DR OrthoDB; 5051at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01951; lectin_L-type; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.10.620.30; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR PANTHER; PTHR12143; PEPTIDE N-GLYCANASE PNGASE -RELATED; 1.
DR PANTHER; PTHR12143:SF19; PEPTIDE-N(4)-(N-ACETYL-BETA-GLUCOSAMINYL)ASPARAGINE AMIDASE; 1.
DR Pfam; PF18483; Bact_lectin; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 184..239
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 494..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 69583 MW; F514120EB4168AA7 CRC64;
MEPDEISAIT TRLTAQWFGF LQQRASGQPS QRSFTQSLGP MFDMSNALGS GGGQDNKFLE
ELKTYGQRVL QYEDKELLEK AMDHIPIHRL YEEAERAVEN GDDPESSLDD QVIIRLLHWF
KHDFFTWVND PPCDYCGSDK TVPQGTAEPN EQDKRYGARI VELYRCTTCN NITRFARYND
AGKLLETRRG RCGEWANCFT LCCRAVGSEA RLVYDKTDHV WTEVYSEFKG RWVHCDSGEE
AYDQPLLYSE GWGKKLNYCI AFSAEEAFDV TKRYTRNWPE VLKRRVLVDE QRLQKFLDDM
TAEKQKYLDD DRKQLLKERR KKEEKELEDA VKRTDVKDSE KLGRKTGSIE WRRARGEDGG
LVNSMMASCI RERDLATSAI NTVGSASIRS SSGTEEEIRL TTADPDQCGA AYCQEPIDVT
QSLVLDIEFS FKITNKEGKP AYGGADGFAF VIQSAGPTVI GQGGCELGYG GIKNSVAIEF
DTYQSGSFIQ KKKKKDSDRC DDPSGNHISI HAVKPPLPNS AHQKNSLGYT SRIPAMNSGA
WLHARIRLFI GRGLIEVALK ESVTEEDYVP VLTKDNLELA AYLGDQAWIG FTASTGGLAQ
NHDIQLKQVT LLRSKNE
//
