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CAZyme Information: MGYG000000042_00935

You are here: Home > Sequence: MGYG000000042_00935

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Phocaeicola sp900066445
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900066445
CAZyme ID MGYG000000042_00935
CAZy Family PL35
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
593 MGYG000000042_2|CGC8 68393.1 7.241
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000042 3613218 Isolate United Kingdom Europe
Gene Location Start: 337139;  End: 338920  Strand: +

Full Sequence      Download help

MFRFIFLFIF  VCFVNNLFPI  ESHPRLLLKR  DEENRIKMMI  IEHEQMKTVH  DYIIKYSDKT60
IGESPVNRIK  QGKRLLAVSR  IALQRIYFLS  YSYRMTKNIK  YAERAKQELL  AVCNFQDWNP120
SHYLDVGEMA  MAVAIGYDWL  YDYLSENVKM  KLRKAIVEKA  FNTAEIGGFY  DRTNNWNQVC180
NAGLVLAALA  IYEEEKEKSD  YIIDKAVKTV  PLAMESYSPD  GIYPEGFSYW  GYGTGFQVTM240
LAAMESALGT  DFGLSDNYGF  LKSPYFMLYM  TAPSGWCYNF  CDSGRKIDLN  QAMYWFASKN300
KDTSLLWYEC  YYLKRLNKYT  GNDIDRLLPN  ILIFSKDIDL  ANLKEPKGKF  FSGKGIKPVF360
IYRSGWSNKT  DSYLGVVAGS  PSIPHGHMDS  GSFVYEKKGE  RWAIDLGLQS  YYTLEKEGVD420
LWNSSQNGQR  WDVFRLGNTG  HTTITINGKK  HLVTGNPEFI  ETYQKSDYKG  AKIDMTSLYG480
DDVNNVLRSV  YLDRNDDLNI  IDEIQTNDNN  AEIMWTMVTS  AQAKIIKDNI  IELSKNGKKM540
RFHVEAPIDI  NLKIWDNKPV  HHYDQDNPGT  VRVGFTADLS  SNDIFKFKVT  VKE593

Enzyme Prediction      help

No EC number prediction in MGYG000000042_00935.

CAZyme Signature Domains help

Created with Snap295988118148177207237266296326355385415444474504533563370547PL35
Family Start End Evalue family coverage
PL35 370 547 1.7e-60 0.9776536312849162

CDD Domains      download full data without filtering help

Created with Snap29598811814817720723726629632635538541544447450453356322275DUF496286251LANC_like86249LanC_like
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam16332 DUF4962 1.57e-07 22 275 136 406
Domain of unknown function (DUF4962). This family consists of uncharacterized proteins around 870 residues in length and is mainly found in various Bacteroides species. The function of this protein is unknown.
pfam05147 LANC_like 2.14e-05 86 251 15 181
Lanthionine synthetase C-like protein. Lanthionines are thioether bridges that are putatively generated by dehydration of Ser and Thr residues followed by addition of cysteine residues within the peptide. This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 (P40 seven-transmembrane-domain protein) and LANCL2 (testes-specific adriamycin sensitivity protein) are thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs. Lanthionines are found in lantibiotics, which are peptide-derived, post-translationally modified antimicrobials produced by several bacterial strains. This region contains seven internal repeats.
cd04434 LanC_like 0.004 86 249 8 175
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.

CAZyme Hits      help

Created with Snap29598811814817720723726629632635538541544447450453356315582QBN17882.1|PL3520589QNL40059.1|PL3520589QRQ54739.1|PL3520589QIU93528.1|PL3520589ALJ47853.1|PL35
Hit ID E-Value Query Start Query End Hit Start Hit End
QBN17882.1 3.35e-227 15 582 32 606
QNL40059.1 6.09e-219 20 589 28 598
QRQ54739.1 2.82e-217 20 589 28 598
QIU93528.1 2.82e-217 20 589 28 598
ALJ47853.1 2.82e-217 20 589 28 598

PDB Hits      download full data without filtering help

Created with Snap2959881181481772072372662963263553854154444745045335631295633A0O_A1292893AFL_A194712FUQ_A194713E80_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3A0O_A 3.27e-09 129 563 259 717
Crystalstructure of alginate lyase from Agrobacterium tumefaciens C58 [Agrobacterium fabrum str. C58],3A0O_B Crystal structure of alginate lyase from Agrobacterium tumefaciens C58 [Agrobacterium fabrum str. C58]
3AFL_A 3.90e-08 129 289 259 423
Crystalstructure of exotype alginate lyase Atu3025 H531A complexed with alginate trisaccharide [Agrobacterium fabrum str. C58]
2FUQ_A 1.81e-06 19 471 19 446
ChainA, heparinase II protein [Pedobacter heparinus],2FUQ_B Chain B, heparinase II protein [Pedobacter heparinus]
3E80_A 1.82e-06 19 471 21 448
Structureof Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus],3E80_B Structure of Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus],3E80_C Structure of Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000404 0.998969 0.000181 0.000139 0.000143 0.000148

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000042_00935.