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Database: UniProt
Entry: V9GC14_9BACL
LinkDB: V9GC14_9BACL
Original site: V9GC14_9BACL 
ID   V9GC14_9BACL            Unreviewed;       448 AA.
AC   V9GC14;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=peptidylamidoglycolate lyase {ECO:0000256|ARBA:ARBA00012343};
DE            EC=4.3.2.5 {ECO:0000256|ARBA:ARBA00012343};
GN   ORFNames=JCM10914_3592 {ECO:0000313|EMBL:GAE07367.1};
OS   Paenibacillus sp. JCM 10914.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE07367.1, ECO:0000313|Proteomes:UP000018028};
RN   [1] {ECO:0000313|EMBL:GAE07367.1, ECO:0000313|Proteomes:UP000018028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE07367.1,
RC   ECO:0000313|Proteomes:UP000018028};
RA   Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA   Hattori M.;
RT   "Draft Genome Sequence of the Alkaliphilic and Xylanolytic Paenibacillus
RT   sp. Strain JCM 10914, Isolated from the Gut of a Soil-Feeding Termite.";
RL   Genome Announc. 2:e01144-13(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:GAE07367.1}.
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DR   EMBL; BAUO01000012; GAE07367.1; -; Genomic_DNA.
DR   RefSeq; WP_023962472.1; NZ_BAZR01000012.1.
DR   AlphaFoldDB; V9GC14; -.
DR   STRING; 1236974.GCA_001315105_03487; -.
DR   OrthoDB; 9799230at2; -.
DR   Proteomes; UP000018028; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR   CDD; cd14955; NHL_like_4; 1.
DR   Gene3D; 2.40.10.500; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR005102; Carbo-bd_X2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR000720; PHM/PAL.
DR   PANTHER; PTHR10680:SF28; DED DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10680; PEPTIDYL-GLYCINE ALPHA-AMIDATING MONOOXYGENASE; 1.
DR   Pfam; PF03442; CBM_X2; 1.
DR   Pfam; PF17170; DUF5128; 1.
DR   Pfam; PF01436; NHL; 2.
DR   PRINTS; PR00790; PAMONOXGNASE.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF101898; NHL repeat; 1.
DR   PROSITE; PS51125; NHL; 5.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018028};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..448
FT                   /note="peptidylamidoglycolate lyase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004776310"
FT   REPEAT          74..117
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          125..165
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          173..212
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          220..259
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          275..304
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   DOMAIN          318..402
FT                   /note="Carbohydrate binding X2"
FT                   /evidence="ECO:0000259|Pfam:PF03442"
SQ   SEQUENCE   448 AA;  49382 MW;  2ADFB397DB860C86 CRC64;
     MRMMFSTMLI MALLLNAYPI VRASGGDEFN PSIYQNQTLI DRPVAIEIDD DGNMYIANYG
     NHQIVKLDSH GNLLTQWGGL GSGNGQFNYP SGVAIDSNAN VYVVDRENHR IQKFDADGTY
     LTEWGRRGAN DGEFRNPANI EIDRNTDIAY VTDRDNHRVQ KFDLNGQFLG KWGGYGNGDG
     EFNRPYGVAI DDSGIVYITE SENHRVQKFD ADGTYISQWG SQGVGNGQFM YPFDIAIDNS
     GYVYVPDAQN NRVQKFDLNG NYISQWGSAG NGSGQFPNSI AIDRDGNVYV TEANNPRIQK
     FDPDGDYLGG WPRSAPSITP QIESFDRNEA GIHYRDITVT LEANDHVLSG ILNGSTTLIE
     GSDYLRVGNM VTITKEYLAT LSIGQSVLTF DFSTGPQLPL TIDISNSTPI PGAPHLQPAI
     AGDEQVSLTW SPVDDATSYN IYQSISLL
//
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