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Conserved domains on  [gi|1169016401|ref|XP_020459796|]
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M-phase inducer phosphatase 2 isoform X2 [Monopterus albus]

Protein Classification

M-inducer_phosp and Cdc25 domain-containing protein( domain architecture ID 10535130)

M-inducer_phosp and Cdc25 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 110-384 5.34e-112

M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer phosphatases (EC:3.1.3.48), which also contain the pfam00581 domain. These proteins are involved in the control of mitosis.


:

Pssm-ID: 461962  Cd Length: 269  Bit Score: 335.18  E-value: 5.34e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 110 MDPLSPMDAVEVDDTFEKAIQQSSRVVSEKMAIRRNNSLPLQLLGFSPALK-GQETDSHRYgifgqQPSQItatSSQHSN 188
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVVNLKMPIRRINSLPQRLLGSSPALKrSQSLDSDIY-----QPEQL---SSQGEN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 189 KENMPEeGFEFKKPTKPVSRSRIRSFTSRQPKDAFACRLSSAPALMLSSPPPIQQLDFYDSSPVFlKSSSLTSSLNDDDD 268
Cdd:pfam06617  73 KENVPE-GFEFKKPTKPASRSRLRSFNSGTAKDAFAQRPNSAPALMLSSPPPKMQELEGDSSPVF-LRRSSLTSSLNDEE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 269 DDGFLDVLDDNTENDSGMPMGMASLLTAPLVAEE------SPVIRYRPRNLFRSPSMPSPVSRSSVKRPDCPGDENTPVR 342
Cdd:pfam06617 151 DDGFLEILDGDLENDEEVPSGMASLLTAPLVTDEigerptSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVK 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1169016401 343 VKRRRSLAGTQVTSQEQNHESPRMgclLLQRSKSFCQTEIDK 384
Cdd:pfam06617 231 VKRRRSVAGTQVEAEEQEPESPRS---LLQRSKSLCHQEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 415-534 1.18e-59

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


:

Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 193.97  E-value: 1.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 415 LKYITPDMMSAALNGQFNHLVEQVIVIDCRYPYEFEGGHIKGALNLHQEDQVEDFLLQTPIVPScPEKRVVIIFHCEFSS 494
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVAS-KKKRRVLIFHCEFSS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1169016401 495 ERGPRMCRFIRERDRA--VNDYPKLHYPELYILKGGYKDFFP 534
Cdd:cd01530    80 KRGPRMARHLRNLDRElnSNRYPLLYYPEIYILEGGYKNFFE 121
 
Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 110-384 5.34e-112

M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer phosphatases (EC:3.1.3.48), which also contain the pfam00581 domain. These proteins are involved in the control of mitosis.


Pssm-ID: 461962  Cd Length: 269  Bit Score: 335.18  E-value: 5.34e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 110 MDPLSPMDAVEVDDTFEKAIQQSSRVVSEKMAIRRNNSLPLQLLGFSPALK-GQETDSHRYgifgqQPSQItatSSQHSN 188
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVVNLKMPIRRINSLPQRLLGSSPALKrSQSLDSDIY-----QPEQL---SSQGEN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 189 KENMPEeGFEFKKPTKPVSRSRIRSFTSRQPKDAFACRLSSAPALMLSSPPPIQQLDFYDSSPVFlKSSSLTSSLNDDDD 268
Cdd:pfam06617  73 KENVPE-GFEFKKPTKPASRSRLRSFNSGTAKDAFAQRPNSAPALMLSSPPPKMQELEGDSSPVF-LRRSSLTSSLNDEE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 269 DDGFLDVLDDNTENDSGMPMGMASLLTAPLVAEE------SPVIRYRPRNLFRSPSMPSPVSRSSVKRPDCPGDENTPVR 342
Cdd:pfam06617 151 DDGFLEILDGDLENDEEVPSGMASLLTAPLVTDEigerptSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVK 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1169016401 343 VKRRRSLAGTQVTSQEQNHESPRMgclLLQRSKSFCQTEIDK 384
Cdd:pfam06617 231 VKRRRSVAGTQVEAEEQEPESPRS---LLQRSKSLCHQEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 415-534 1.18e-59

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 193.97  E-value: 1.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 415 LKYITPDMMSAALNGQFNHLVEQVIVIDCRYPYEFEGGHIKGALNLHQEDQVEDFLLQTPIVPScPEKRVVIIFHCEFSS 494
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVAS-KKKRRVLIFHCEFSS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1169016401 495 ERGPRMCRFIRERDRA--VNDYPKLHYPELYILKGGYKDFFP 534
Cdd:cd01530    80 KRGPRMARHLRNLDRElnSNRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
302-567 3.24e-36

Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 140.56  E-value: 3.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 302 ESPVIRYRPRNLFRSPSMPSP------VSRSSVKRPDCPGDENTPVRVKRRRSLAGTQVTSQEQNHESPRMGCLllqrsK 375
Cdd:COG5105   146 WSSSENIEFEDPGHDPFVDNSdnskmnHLRGSGKQPKCREKIAFAVWTSLQGMRGFSRAGPAPAAENSHLIDFF-----K 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 376 SFcqteidkvldiENGCNeligdFTKPFilpTVEGKHQDLKYITPDMMSAALNGQFNHLVEQVIVIDCRYPYEFEGGHIK 455
Cdd:COG5105   221 SF-----------SNGEV-----FPLPT---LGPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHII 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 456 GALNLHQEDQVEDFLLQTPIVpscpeKRVVIIFHCEFSSERGPRMCRFIRERDRAVN--DYPKLHYPELYILKGGYKDFF 533
Cdd:COG5105   282 NAVNISSTKKLGLLFRHKPLT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNpdHYPLLTYPEVYILEGGYKKFY 356

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1169016401 534 PHFQSQCEPQSYRPMNHGD-----------FKEDLRKFRSKSRTL 567
Cdd:COG5105   357 SNYPDLCDPKGYVTMNNAEldyrclykmdkFRRNKKFFATKNNSF 401
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 436-533 2.15e-17

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 77.50  E-value: 2.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401  436 EQVIVIDCRYPYEFEGGHIKGALNLHQEDQVEDFLLQTPIVPSCPEKR------VVIIFHCeFSSERGPRMCRFIRERDr 509
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRlgldkdKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....
gi 1169016401  510 avndypklhYPELYILKGGYKDFF 533
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWS 95
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 436-532 1.42e-10

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 57.88  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 436 EQVIVIDCRYPYEFEGGHIKGALNLH----QEDQVEDFLLQTPIVPSCPEKRvvIIFHCEfSSERGPRMCRFIRerdrav 511
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPlsslSLPPLPLLELLEKLLELLKDKP--IVVYCN-SGNRAAAAAALLK------ 74

                          90       100
                  ....*....|....*....|.
gi 1169016401 512 ndypKLHYPELYILKGGYKDF 532
Cdd:pfam00581  75 ----ALGYKNVYVLDGGFEAW 91
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 414-531 1.90e-09

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 55.36  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 414 DLKYITPDMMSAALNGqfnhlvEQVIVIDCRYPYEFEGGHIKGALNLHQeDQVEDFLLQTPivpscPEKRVViiFHCEfS 493
Cdd:COG0607     2 SVKEISPAELAELLES------EDAVLLDVREPEEFAAGHIPGAINIPL-GELAERLDELP-----KDKPIV--VYCA-S 66

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1169016401 494 SERGPRMCRFIRerdravndypKLHYPELYILKGGYKD 531
Cdd:COG0607    67 GGRSAQAAALLR----------RAGYTNVYNLAGGIEA 94
 
Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 110-384 5.34e-112

M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer phosphatases (EC:3.1.3.48), which also contain the pfam00581 domain. These proteins are involved in the control of mitosis.


Pssm-ID: 461962  Cd Length: 269  Bit Score: 335.18  E-value: 5.34e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 110 MDPLSPMDAVEVDDTFEKAIQQSSRVVSEKMAIRRNNSLPLQLLGFSPALK-GQETDSHRYgifgqQPSQItatSSQHSN 188
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVVNLKMPIRRINSLPQRLLGSSPALKrSQSLDSDIY-----QPEQL---SSQGEN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 189 KENMPEeGFEFKKPTKPVSRSRIRSFTSRQPKDAFACRLSSAPALMLSSPPPIQQLDFYDSSPVFlKSSSLTSSLNDDDD 268
Cdd:pfam06617  73 KENVPE-GFEFKKPTKPASRSRLRSFNSGTAKDAFAQRPNSAPALMLSSPPPKMQELEGDSSPVF-LRRSSLTSSLNDEE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 269 DDGFLDVLDDNTENDSGMPMGMASLLTAPLVAEE------SPVIRYRPRNLFRSPSMPSPVSRSSVKRPDCPGDENTPVR 342
Cdd:pfam06617 151 DDGFLEILDGDLENDEEVPSGMASLLTAPLVTDEigerptSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVK 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1169016401 343 VKRRRSLAGTQVTSQEQNHESPRMgclLLQRSKSFCQTEIDK 384
Cdd:pfam06617 231 VKRRRSVAGTQVEAEEQEPESPRS---LLQRSKSLCHQEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 415-534 1.18e-59

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 193.97  E-value: 1.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 415 LKYITPDMMSAALNGQFNHLVEQVIVIDCRYPYEFEGGHIKGALNLHQEDQVEDFLLQTPIVPScPEKRVVIIFHCEFSS 494
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVAS-KKKRRVLIFHCEFSS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1169016401 495 ERGPRMCRFIRERDRA--VNDYPKLHYPELYILKGGYKDFFP 534
Cdd:cd01530    80 KRGPRMARHLRNLDRElnSNRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
302-567 3.24e-36

Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 140.56  E-value: 3.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 302 ESPVIRYRPRNLFRSPSMPSP------VSRSSVKRPDCPGDENTPVRVKRRRSLAGTQVTSQEQNHESPRMGCLllqrsK 375
Cdd:COG5105   146 WSSSENIEFEDPGHDPFVDNSdnskmnHLRGSGKQPKCREKIAFAVWTSLQGMRGFSRAGPAPAAENSHLIDFF-----K 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 376 SFcqteidkvldiENGCNeligdFTKPFilpTVEGKHQDLKYITPDMMSAALNGQFNHLVEQVIVIDCRYPYEFEGGHIK 455
Cdd:COG5105   221 SF-----------SNGEV-----FPLPT---LGPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHII 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 456 GALNLHQEDQVEDFLLQTPIVpscpeKRVVIIFHCEFSSERGPRMCRFIRERDRAVN--DYPKLHYPELYILKGGYKDFF 533
Cdd:COG5105   282 NAVNISSTKKLGLLFRHKPLT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNpdHYPLLTYPEVYILEGGYKKFY 356

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1169016401 534 PHFQSQCEPQSYRPMNHGD-----------FKEDLRKFRSKSRTL 567
Cdd:COG5105   357 SNYPDLCDPKGYVTMNNAEldyrclykmdkFRRNKKFFATKNNSF 401
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 415-534 4.29e-33

Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR).


Pssm-ID: 238720 [Multi-domain]  Cd Length: 113  Bit Score: 122.51  E-value: 4.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 415 LKYITPDMMSAALNGQFNHLVEQVIVIDCRYPyEFEGGHIKGALNLHQEDqVEDFLLQTPIVPScPEKRVVIIFHCEFSS 494
Cdd:cd01443     1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQS-CYQTLPQVYALFS-LAGVKLAIFYCGSSQ 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1169016401 495 ERGPRMCRFIRERDRAVNDYpklhYPELYILKGGYKDFFP 534
Cdd:cd01443    78 GRGPRAARWFADYLRKVGES----LPKSYILTGGIKAWYH 113
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 436-533 2.15e-17

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 77.50  E-value: 2.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401  436 EQVIVIDCRYPYEFEGGHIKGALNLHQEDQVEDFLLQTPIVPSCPEKR------VVIIFHCeFSSERGPRMCRFIRERDr 509
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRlgldkdKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....
gi 1169016401  510 avndypklhYPELYILKGGYKDFF 533
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWS 95
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 415-529 2.99e-11

Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.


Pssm-ID: 238789 [Multi-domain]  Cd Length: 113  Bit Score: 60.51  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 415 LKYITPdmmsAALNGQFNHLVEQVIVIDCRyPYEFEGGHIKGALN------LHQEDQVEDFLLQTpivpscpeKRVVIIF 488
Cdd:cd01531     1 VSYISP----AQLKGWIRNGRPPFQVVDVR-DEDYAGGHIKGSWHypstrfKAQLNQLVQLLSGS--------KKDTVVF 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1169016401 489 HCEFSSERGP----RMCRFIRERDRAVNDypklhyPELYILKGGY 529
Cdd:cd01531    68 HCALSQVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGGF 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 436-530 3.19e-11

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 59.62  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 436 EQVIVIDCRYPYEFEGGHIKGALNLHqedqVEDFLLQTPIVPSCPEKRvvIIFHCEfSSERGPRMCRFIRerdravndyp 515
Cdd:cd00158     9 EDAVLLDVREPEEYAAGHIPGAINIP----LSELEERAALLELDKDKP--IVVYCR-SGNRSARAAKLLR---------- 71

                          90
                  ....*....|....*
gi 1169016401 516 KLHYPELYILKGGYK 530
Cdd:cd00158    72 KAGGTNVYNLEGGML 86
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 436-532 1.42e-10

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 57.88  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 436 EQVIVIDCRYPYEFEGGHIKGALNLH----QEDQVEDFLLQTPIVPSCPEKRvvIIFHCEfSSERGPRMCRFIRerdrav 511
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPlsslSLPPLPLLELLEKLLELLKDKP--IVVYCN-SGNRAAAAAALLK------ 74

                          90       100
                  ....*....|....*....|.
gi 1169016401 512 ndypKLHYPELYILKGGYKDF 532
Cdd:pfam00581  75 ----ALGYKNVYVLDGGFEAW 91
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 414-531 1.90e-09

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 55.36  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 414 DLKYITPDMMSAALNGqfnhlvEQVIVIDCRYPYEFEGGHIKGALNLHQeDQVEDFLLQTPivpscPEKRVViiFHCEfS 493
Cdd:COG0607     2 SVKEISPAELAELLES------EDAVLLDVREPEEFAAGHIPGAINIPL-GELAERLDELP-----KDKPIV--VYCA-S 66

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1169016401 494 SERGPRMCRFIRerdravndypKLHYPELYILKGGYKD 531
Cdd:COG0607    67 GGRSAQAAALLR----------RAGYTNVYNLAGGIEA 94
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 422-536 5.10e-03

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 37.65  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169016401 422 MMSAALNGQFNHLVEQVIVIDCRYPYEFEGGHIKGALNLH---------QEDQVedfLLQtpIVPSCPEKRVV------- 485
Cdd:cd01446     2 IDCAWLAALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCcptilrrrlQGGKI---LLQ--QLLSCPEDRDRlrrgesl 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169016401 486 -IIFHCEFSSERGPR------------MCRFIRERDRAvndypklhypelYILKGGYKDF---FPHF 536
Cdd:cd01446    77 aVVVYDESSSDRERLredstaesvlgkLLRKLQEGCSV------------YLLKGGFEQFsseFPEL 131
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 430-459 5.71e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 36.79  E-value: 5.71e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1169016401 430 QFNHLVEQ--VIVIDCRYPYEFEGGHIKGALN 459
Cdd:cd01518     8 EWNELLEDpeVVLLDVRNDYEYDIGHFKGAVN 39
 
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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