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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377 2300 DSSEIPGALWHIYAGKDVDKIREFLQKVSKEQGLEVLPEHDPVRDQGWYVNRRLRQRLLEEyGVRACTLVQFLGDAIVLP 2379
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94

                           90       100
                   ....*....|....*....|
gi 1958756377 2380 AGTLHQVQNFHSCIQVTEDF 2399
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114

Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato virus X resistance protein (RX) confers resistance against potato virus X. It is a member of a family of resistance proteins with a domain architecture that includes an N-terminal coiled-coil domain (modeled here), a nucleotide-binding domain, and leucine-rich repeats (CC-NB-LRR). These intracellular resistance proteins recognize pathogen effector proteins and will subsequently trigger a response that may be as severe as localized cell death. The N-terminal coiled-coil domain of RX has been shown to interact with RanGAP2, which is a necessary co-factor in the resistance response.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377  126 AVEFLIDKQVDFLTEESAFQLY-QDDIDSLKPEL-------RD---NPQLHAEVKVWVKE 174
Cdd:cd14798      4 AVSFLLEKLGELLEQEADLLSGvKEEIESLKDELesmqaflKDadaKQDEDEELKDWVKQ 63

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377 2300 DSSEIPGALWHIYAGKDVDKIREFLQKVSKEQGLEVLPEHDPVRDQGWYVNRRLRQRLLEEyGVRACTLVQFLGDAIVLP 2379
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94

                           90       100
                   ....*....|....*....|
gi 1958756377 2380 AGTLHQVQNFHSCIQVTEDF 2399
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114

Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato virus X resistance protein (RX) confers resistance against potato virus X. It is a member of a family of resistance proteins with a domain architecture that includes an N-terminal coiled-coil domain (modeled here), a nucleotide-binding domain, and leucine-rich repeats (CC-NB-LRR). These intracellular resistance proteins recognize pathogen effector proteins and will subsequently trigger a response that may be as severe as localized cell death. The N-terminal coiled-coil domain of RX has been shown to interact with RanGAP2, which is a necessary co-factor in the resistance response.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377  126 AVEFLIDKQVDFLTEESAFQLY-QDDIDSLKPEL-------RD---NPQLHAEVKVWVKE 174
Cdd:cd14798      4 AVSFLLEKLGELLEQEADLLSGvKEEIESLKDELesmqaflKDadaKQDEDEELKDWVKQ 63

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377 2300 DSSEIPGALWHIYAGKDVDKIREFLQKVSKEQGLEVLPEHDPVRDQGWYVNRRLRQRLLEEyGVRACTLVQFLGDAIVLP 2379
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94

                           90       100
                   ....*....|....*....|
gi 1958756377 2380 AGTLHQVQNFHSCIQVTEDF 2399
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114

Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato virus X resistance protein (RX) confers resistance against potato virus X. It is a member of a family of resistance proteins with a domain architecture that includes an N-terminal coiled-coil domain (modeled here), a nucleotide-binding domain, and leucine-rich repeats (CC-NB-LRR). These intracellular resistance proteins recognize pathogen effector proteins and will subsequently trigger a response that may be as severe as localized cell death. The N-terminal coiled-coil domain of RX has been shown to interact with RanGAP2, which is a necessary co-factor in the resistance response.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377  126 AVEFLIDKQVDFLTEESAFQLY-QDDIDSLKPEL-------RD---NPQLHAEVKVWVKE 174
Cdd:cd14798      4 AVSFLLEKLGELLEQEADLLSGvKEEIESLKDELesmqaflKDadaKQDEDEELKDWVKQ 63