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Conserved domains on  [gi|996646465|gb|KXH65443|]
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cupin [Colletotrichum nymphaeae SA-01]

Protein Classification

cupin domain-containing protein( domain architecture ID 10008056)

cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold

CATH:  2.60.120.10
Gene Ontology:  GO:0046872
PubMed:  19478949|14697267|9573603
SCOP:  3001825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
36-125 3.57e-16

Uncharacterized conserved protein, cupin superfamily [Function unknown];


:

Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 70.05  E-value: 3.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  36 TDNRVGCMTLELPPATSGPPMHWHRFHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTFSNPSEtDPAEFFMTS 115
Cdd:COG3837   24 GLTRLGVNLITLPPGASSSPYHAHSAEEEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGD-EPARYLVVG 102

                         90
                 ....*....|
gi 996646465 116 TPGYYMDYFR 125
Cdd:COG3837  103 TRAPYPDSFD 112
 
Name Accession Description Interval E-value
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
36-125 3.57e-16

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 70.05  E-value: 3.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  36 TDNRVGCMTLELPPATSGPPMHWHRFHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTFSNPSEtDPAEFFMTS 115
Cdd:COG3837   24 GLTRLGVNLITLPPGASSSPYHAHSAEEEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGD-EPARYLVVG 102

                         90
                 ....*....|
gi 996646465 116 TPGYYMDYFR 125
Cdd:COG3837  103 TRAPYPDSFD 112
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 25-127 3.01e-11

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 57.16  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  25 MTIYIfeDGTNTDNRVGCMTLELPPAtSGPPMHWHRFHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTFSNps 104
Cdd:cd02215   19 FTVLA--TGESTGGAFTLVTTEGPKG-DAIPPHYHKRHHETFYVLEGRLQLWLDGESRLLTPGDFASVPPGTIHAYRM-- 93

                         90       100
                 ....*....|....*....|...
gi 996646465 105 ETDPAEFFMTSTPGYYMDYFRMM 127
Cdd:cd02215   94 LSPDTRFLGVITPGGFERFFRAL 116
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 43-113 1.61e-10

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 53.80  E-value: 1.61e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 996646465   43 MTLELPPATSGPPmHWHRFHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTFSNPSETdPAEFFM 113
Cdd:pfam07883   1 GLVTLPPGESSPP-HRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDE-PARLLD 69
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 55-119 1.61e-05

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 42.27  E-value: 1.61e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 996646465    55 PMHWHRFHDECFFVTKGTIR--FSTPEGNV----DAEEGQLMVVPPRAIHTFSNpSETDPAEF--FMTSTPGY 119
Cdd:smart00835  44 PPHYHPRATELLYVVRGEGRvgVVDPNGNKvydaRLREGDVFVVPQGHPHFQVN-SGDENLEFvaFNTNDPNR 115
 
Name Accession Description Interval E-value
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
36-125 3.57e-16

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 70.05  E-value: 3.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  36 TDNRVGCMTLELPPATSGPPMHWHRFHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTFSNPSEtDPAEFFMTS 115
Cdd:COG3837   24 GLTRLGVNLITLPPGASSSPYHAHSAEEEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGD-EPARYLVVG 102

                         90
                 ....*....|
gi 996646465 116 TPGYYMDYFR 125
Cdd:COG3837  103 TRAPYPDSFD 112
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
21-119 3.40e-12

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 59.38  E-value: 3.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  21 KLGPMTIYIFEDGTNTDNRVGCMTLELPPATSgPPMHWHRFHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTF 100
Cdd:COG0662    8 ELKAIGWGSYEVLGEGGERLSVKRITVPPGAE-LSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRL 86

                         90
                 ....*....|....*....
gi 996646465 101 SNPSETdPAEFFMTSTPGY 119
Cdd:COG0662   87 RNPGDE-PLELLEVQAPAY 104
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 25-127 3.01e-11

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 57.16  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  25 MTIYIfeDGTNTDNRVGCMTLELPPAtSGPPMHWHRFHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTFSNps 104
Cdd:cd02215   19 FTVLA--TGESTGGAFTLVTTEGPKG-DAIPPHYHKRHHETFYVLEGRLQLWLDGESRLLTPGDFASVPPGTIHAYRM-- 93

                         90       100
                 ....*....|....*....|...
gi 996646465 105 ETDPAEFFMTSTPGYYMDYFRMM 127
Cdd:cd02215   94 LSPDTRFLGVITPGGFERFFRAL 116
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 43-113 1.61e-10

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 53.80  E-value: 1.61e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 996646465   43 MTLELPPATSGPPmHWHRFHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTFSNPSETdPAEFFM 113
Cdd:pfam07883   1 GLVTLPPGESSPP-HRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDE-PARLLD 69
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 43-107 1.66e-10

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 54.03  E-value: 1.66e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 996646465  43 MTLELPPATSGPPmHWHRFHDECFFVTKGTIRFSTPEGN-VDAEEGQLMVVPPRAIHTFSNPSETD 107
Cdd:cd02208    2 SVVTLPPGTSSPP-HWHPEQDEIFYVLSGEGELTLDDGEtVELKAGDIVLIPPGVPHSFVNTSDEP 66
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
35-118 1.31e-09

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 52.54  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  35 NTDNRVGCMTLELPPATSGPPmHWHRfHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTFSNPSETdPAEFFMT 114
Cdd:COG1917   18 DGEDELEVVRVTFEPGARTPW-HSHP-GEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDE-PAVLLVV 94


                 ....
gi 996646465 115 STPG 118
Cdd:COG1917   95 FSPG 98
cupin_RemF-like cd06979
Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is ...
 24-117 1.34e-06

Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is a manganese-containing polyketide cyclase present in bacteria that is involved in the biosynthesis of resistomycin, the aromatic pentacyclic metabolite in Streptomyces resistomycificus. Structure of this enzyme shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold that forms a homodimer. It contains an unusual octahedral zinc-binding site in a large hydrophobic pocket that may represent the active site. The zinc ion, coordinated to four histidine side chains and two water molecules, could act as a Lewis acid in the aldol condensation reaction catalyzed by RemF, reminiscent of class II aldolases.


Pssm-ID: 380384 [Multi-domain]  Cd Length: 93  Bit Score: 44.38  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  24 PMTIYIFEDGTNTDNRVGCMTLELPPATSGPPMHWHRFHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTFSNp 103
Cdd:cd06979    1 TTELRFLDTKDGTADRFDLFEFEVSPNAGMPPPHYHEDWEETIYGLEGSVTLTLPGKTVEVGPGDSIFIPRGEVHGFVN- 79

                         90
                 ....*....|....
gi 996646465 104 SETDPAEFFMTSTP 117
Cdd:cd06979   80 RSGGPTCRLCVLAP 93
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 55-119 1.61e-05

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 42.27  E-value: 1.61e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 996646465    55 PMHWHRFHDECFFVTKGTIR--FSTPEGNV----DAEEGQLMVVPPRAIHTFSNpSETDPAEF--FMTSTPGY 119
Cdd:smart00835  44 PPHYHPRATELLYVVRGEGRvgVVDPNGNKvydaRLREGDVFVVPQGHPHFQVN-SGDENLEFvaFNTNDPNR 115
cupin_CucA-like cd20291
soluble periplasm cuproprotein CucA and related proteins, cupin domain; This family includes ...
 33-125 1.87e-05

soluble periplasm cuproprotein CucA and related proteins, cupin domain; This family includes bacterial proteins homologous to a soluble periplasm protein, CucA, found in the periplasm of the cyanobacterium Synechocystis where it shows some Cu2+-dependent quercetin dioxygenase activity. Studies show that a copper-trafficking pathway enables Cu2+ occupancy of CucA to accumulate in the periplasm, and this involves two copper transporters (CtaA and PacS) and a metallochaperone (Atx1). CucA belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380425  Cd Length: 201  Bit Score: 42.71  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  33 GTNTDNRVGCMTLELPPAtSGPPMHWHRFHDECFFVTKG--TIRFST---PEGN--------------VDAEEGQLMVVP 93
Cdd:cd20291   19 GETTGGGYLIAKATIPPG-GGPPPHIHHYTDEWFYAPEGgfELFMGTntyPDLDkvpgdnapkdtlysIPMEPGQLFYGP 97

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 996646465  94 PRAIHTFSNPSETdPAEFFMTSTP----GYYMDYFR 125
Cdd:cd20291   98 RNHVHGFVNTTDK-TLPLQFVWTPdtpdGGIREYFQ 132
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 57-96 6.92e-05

Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380355 [Multi-domain]  Cd Length: 94  Bit Score: 39.73  E-value: 6.92e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 996646465  57 HWHRfH---DECFFVTKGTIRFSTPEGNVDAEEGQLMVVP------PRA 96
Cdd:cd02226   36 VWHK-HddeDELFLVLEGELTIDFRDRDVTLGPGEFFVVPkgvehrPVA 83
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 57-131 7.86e-05

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 40.65  E-value: 7.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  57 HWHRFHDECFFVTKGTIRFST--PEGNVD---AEEGQLMVVPPRAIHTFSNPSEtDPAE---FFMTSTP--GYYMDYFRM 126
Cdd:cd20306   50 HWHPNANELGYVISGEARVSIldPTGSLDtftVKPGQVVFIPQGWLHWIENVGD-EEAHlliFFNHETPedIGLSDSLRA 128


                 ....*
gi 996646465 127 MAKGV 131
Cdd:cd20306  129 TPPEV 133
RmlC COG4101
Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];
42-118 2.12e-04

Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];


Pssm-ID: 443277  Cd Length: 146  Bit Score: 39.18  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  42 CM-TLELPPATSGPPmHWHRFHDECFFVTKGTIRFSTPEG---NVDAEEGQLMVVPPRAIHTFSNPSETDPAEFFMTSTP 117
Cdd:COG4101   47 WMgLVTIPPGARAKA-HHHGEHETAIYVLSGRAETRYGERlehRVVTEPGDFIFIPPGVPHQEINLSDTEPAVAVIARTD 125


                 .
gi 996646465 118 G 118
Cdd:COG4101  126 P 126
cupin_BLR2406-like cd02210
Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain; This family includes ...
 42-111 4.63e-04

Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLR2406, a Bradyrhizobium japonicum protein of unknown function with a cupin beta barrel domain. Proteins in this subfamily appear to align closest to RmlC carbohydrate epimerase which is involved in dTDP-L-rhamnose production, and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380340 [Multi-domain]  Cd Length: 98  Bit Score: 37.50  E-value: 4.63e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 996646465  42 CM-TLELPPATSGPPmHWHRFHDECFFVTKGTIRFSTPEG---NVDAEEGQLMVVPPRAIHTFSNPSETDPAEF 111
Cdd:cd02210   12 WMgVVTIPPGARTGA-HHHGEHETAIYVLSGRAETRYGDRlehRAEAGPGDFIYIPPGVPHQEVNLSDDEPAVA 84
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 55-121 6.57e-04

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 395138  Cd Length: 151  Bit Score: 38.08  E-value: 6.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 996646465   55 PMHWHRFHDECFFVTKGTIR--FSTPEGNV-----DAEEGQLMVVPPRAIHTFSNPSETDPAEFFMTSTPGYYM 121
Cdd:pfam00190  47 PPHWHPNATEILYVLQGRGRvgFVVPGNGNrvfhkVLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGN 120
cupin_BLR7677-like cd02234
Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes ...
 43-112 1.07e-03

Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLR7677, a Bradyrhizobium japonicum protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380362 [Multi-domain]  Cd Length: 103  Bit Score: 36.71  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646465  43 MTLELPPATSGPPmhwHRFHDECF-FVTKGTIRFstpegnvdAEEGQLMVV---------PPRAIHTFS-NPSETDPAEF 111
Cdd:cd02234   22 LLVTYPPGAASPP---HRHPGFVFaYVLEGEVRS--------QVNGGPPRVykagesfyePPGAHHRVSrNASATEPAKL 90


                 .
gi 996646465 112 F 112
Cdd:cd02234   91 L 91
cupin_BF4112 cd06985
Bacteroides fragilis BF4112 and related proteins, cupin domain; This family includes archaeal ...
 47-107 2.05e-03

Bacteroides fragilis BF4112 and related proteins, cupin domain; This family includes archaeal and bacterial proteins homologous to BF4112, a Bacteroides fragilis protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380390 [Multi-domain]  Cd Length: 101  Bit Score: 35.58  E-value: 2.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 996646465  47 LPPATSGPPMHWHRFHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTFSNPSETD 107
Cdd:cd06985   21 LPAGAAVPFVHSHKENEEIYIILKGKGEFQVDGEVFPVKEGSVIRVAPDGKRSWRNTSDEP 81
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 39-72 2.11e-03

Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase with a cupin domain; This family includes proteins similar to sugar phosphate isomerase SPO2919 from Silicibacter pomeroyi and Afe_0303 from Acidithiobacillus ferrooxidans, but are as yet uncharacterized. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380353 [Multi-domain]  Cd Length: 105  Bit Score: 35.93  E-value: 2.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 996646465  39 RVGCMTLELPPATSGPPMHWHRFHDECFFVTKGT 72
Cdd:cd02224   16 QLGVNLERLPPGARSSPRHWHSAEEEFVYVLSGE 49
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 55-112 2.97e-03

Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3.4) catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide (H2O2). It is widespread in fungi and various plant tissues and may play a role in plant signaling and defense. This enzyme has been employed in a widely used assay for detecting urinary oxalate levels. Also, the gene encoding OxOx from barley roots has been expressed in oilseed rape in order to provide a defense against externally supplied oxalic acid. In germin, the predominant protein produced during the early phase of wheat germination, it is believed that H2O2 production is employed as a defense mechanism in response to infection by pathogens. Germin is also a marker of growth onset in cell walls in germinating cereals. The H2O2 produced by OxOx, together with the Ca2+ released by degradation of calcium oxalate, are thought to mediate cell wall cross-linking at high concentrations. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380368  Cd Length: 191  Bit Score: 36.42  E-value: 2.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 996646465  55 PMHWH-RFhDECFFVTKGTIR--FSTPEGNV----DAEEGQLMVVPPRAIHTFSNPSETdPAEFF 112
Cdd:cd02241   84 PPHTHpRA-TELLYVVEGTLYvgFVDENGNRlftkTLNPGDVFVFPQGLIHFQFNPGCE-PAVFV 146
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 57-117 9.27e-03

TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380396 [Multi-domain]  Cd Length: 105  Bit Score: 34.19  E-value: 9.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 996646465  57 HWHRFHDECFFVTKGTIRFSTPEGNVDAEEGQLMVVPPRAIHTFSNPSeTDPAEFFMTSTP 117
Cdd:cd06991   35 HYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLENAG-DEPARLVFHLSP 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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