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Conserved domains on  [gi|1932547762|gb|KAF9099974|]
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DNA break repair nuclease [Mortierella sp. GBA35]

Protein Classification

DNA cross-link repair protein( domain architecture ID 10888615)

DNA cross-link repair protein similar to Arabidopsis thaliana SNM1, which is involved in the repair of DNA lesions formed by oxidative stress

Gene Ontology:  GO:0006974|GO:0005634
PubMed:  12177301

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 303-464 8.17e-95

SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


:

Pssm-ID: 293831  Cd Length: 160  Bit Score: 291.37  E-value: 8.17e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 303 AGGNFKPKAPRPCPFYKKMPDTGFTVDAFCYGKVEGCEAYFLSHFHSDHYGGLTSSWNHGPIYCSSITANLVISRLKVDE 382
Cdd:cd16273     1 KSSKKKPKRKKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHGPIYCSEITANLVKLKLKVDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 383 QYVRRLPMYEPTVVQG-VTVRLMDANHCPGSVLFVFDLHNpKRRYLHTGDFRAAPDMCIDPILRQPQnvPIDILYLDTTY 461
Cdd:cd16273    81 EYIVVLPMNTPVEIDGdVSVTLLDANHCPGAVMFLFELPD-GRRILHTGDFRANPEMLEHPLLLGKR--RIDTVYLDTTY 157


                  ...
gi 1932547762 462 SNP 464
Cdd:cd16273   158 CNP 160
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 591-717 3.28e-29

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


:

Pssm-ID: 429512  Cd Length: 108  Bit Score: 111.98  E-value: 3.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 591 PELMDMLTSDRHEAQVHLLHMGSDmSPEALQDYLDSLAPTFVRLIAVRPTGWTFtgtkkftpadngstdlpNPAKPATSL 670
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMPKL-SYEALLDYLTARKDHFDSVLAIRPTGWTY-----------------RPPKTEVSD 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1932547762 671 ELRPSYTSPtVKIYPVPYSEHSSFSELAGFCRSLNILKVIPTVGVGS 717
Cdd:pfam07522  63 RIGPSIRGR-ITIYGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVGG 108
 
Name Accession Description Interval E-value
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 303-464 8.17e-95

SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293831  Cd Length: 160  Bit Score: 291.37  E-value: 8.17e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 303 AGGNFKPKAPRPCPFYKKMPDTGFTVDAFCYGKVEGCEAYFLSHFHSDHYGGLTSSWNHGPIYCSSITANLVISRLKVDE 382
Cdd:cd16273     1 KSSKKKPKRKKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHGPIYCSEITANLVKLKLKVDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 383 QYVRRLPMYEPTVVQG-VTVRLMDANHCPGSVLFVFDLHNpKRRYLHTGDFRAAPDMCIDPILRQPQnvPIDILYLDTTY 461
Cdd:cd16273    81 EYIVVLPMNTPVEIDGdVSVTLLDANHCPGAVMFLFELPD-GRRILHTGDFRANPEMLEHPLLLGKR--RIDTVYLDTTY 157


                  ...
gi 1932547762 462 SNP 464
Cdd:cd16273   158 CNP 160
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 591-717 3.28e-29

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


Pssm-ID: 429512  Cd Length: 108  Bit Score: 111.98  E-value: 3.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 591 PELMDMLTSDRHEAQVHLLHMGSDmSPEALQDYLDSLAPTFVRLIAVRPTGWTFtgtkkftpadngstdlpNPAKPATSL 670
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMPKL-SYEALLDYLTARKDHFDSVLAIRPTGWTY-----------------RPPKTEVSD 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1932547762 671 ELRPSYTSPtVKIYPVPYSEHSSFSELAGFCRSLNILKVIPTVGVGS 717
Cdd:pfam07522  63 RIGPSIRGR-ITIYGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVGG 108
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 343-477 5.16e-13

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 71.37  E-value: 5.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 343 FLSHFHSDHYGG---LTSSWNHGPIYCSSITANLVISRL----KVDEQYVRRLPMY------------------EPTVVQ 397
Cdd:COG1236    55 VLTHAHLDHSGAlplLVKEGFRGPIYATPATADLARILLgdsaKIQEEEAEAEPLYteedaeralelfqtvdygEPFEIG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 398 GVTVRLMDANHCPGSVLFVFDLHNpkRRYLHTGDFRAAPdmciDPILRQPQNVP-IDILYLDTTYSNPRYtfPPQDVVIR 476
Cdd:COG1236   135 GVRVTFHPAGHILGSAQVELEVGG--KRIVFSGDYGRED----DPLLAPPEPVPpADVLITESTYGDRLH--PPREEVEA 206


                  .
gi 1932547762 477 E 477
Cdd:COG1236   207 E 207
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 343-439 2.51e-08

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 54.10  E-value: 2.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762  343 FLSHFHSDHYGGLTS--SWNHGPIYCSSITANLVISRLKVDEQYVRRLPMYEPTVV--QGVTVRLMD--------ANHCP 410
Cdd:smart00849  40 ILTHGHPDHIGGLPEllEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTlkDGDELDLGGgelevihtPGHTP 119

                           90       100
                   ....*....|....*....|....*....
gi 1932547762  411 GSVLFVFdlhnPKRRYLHTGDFRAAPDMC 439
Cdd:smart00849 120 GSIVLYL----PEGKILFTGDLLFAGGDG 144
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 343-482 6.46e-04

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 41.53  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 343 FLSHFHSDHYGGLTS--SWNHGPIYCS-----SITANLVISRLKVdEQYVRRLPM--YEPTVV--QGVTVRLMDANH--- 408
Cdd:pfam12706  33 LLTHDHYDHLAGLLDlrEGRPRPLYAPlgvlaHLRRNFPYLFLLE-HYGVRVHEIdwGESFTVgdGGLTVTATPARHgsp 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 409 -----CPGSVL-FVFDlhNPKRRYLHTGDFRAAPDMcIDPILRqpqnvPIDILYLDTTYSNPRYTFPPQDVVIRETARLI 482
Cdd:pfam12706 112 rgldpNPGDTLgFRIE--GPGKRVYYAGDTGYFPDE-IGERLG-----GADLLLLDGGAWRDDEMIHMGHMTPEEAVEAA 183
 
Name Accession Description Interval E-value
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 303-464 8.17e-95

SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293831  Cd Length: 160  Bit Score: 291.37  E-value: 8.17e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 303 AGGNFKPKAPRPCPFYKKMPDTGFTVDAFCYGKVEGCEAYFLSHFHSDHYGGLTSSWNHGPIYCSSITANLVISRLKVDE 382
Cdd:cd16273     1 KSSKKKPKRKKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHGPIYCSEITANLVKLKLKVDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 383 QYVRRLPMYEPTVVQG-VTVRLMDANHCPGSVLFVFDLHNpKRRYLHTGDFRAAPDMCIDPILRQPQnvPIDILYLDTTY 461
Cdd:cd16273    81 EYIVVLPMNTPVEIDGdVSVTLLDANHCPGAVMFLFELPD-GRRILHTGDFRANPEMLEHPLLLGKR--RIDTVYLDTTY 157


                  ...
gi 1932547762 462 SNP 464
Cdd:cd16273   158 CNP 160
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 306-464 1.90e-67

5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293856 [Multi-domain]  Cd Length: 157  Bit Score: 219.31  E-value: 1.90e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 306 NFKPKAPRPCPFYKKMPDTGFTVDAFCYGKVEGCEAYFLSHFHSDHYGGLTSSWNHgPIYCSSITANLVISRLKVDEQYV 385
Cdd:cd16298     4 NGEGKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKF-PIYCSKITGNLVKSKLKVEEQYI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1932547762 386 RRLPMYEPTVVQGVTVRLMDANHCPGSVLFVFDLHNpKRRYLHTGDFRAAPDMCIDPILrqpQNVPIDILYLDTTYSNP 464
Cdd:cd16298    83 NVLPMNTECIVNGVKVVLLDANHCPGAVMILFRLPS-GTLVLHTGDFRADPSMERYPEL---IGQKIHTLYLDTTYCSP 157
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 591-717 3.28e-29

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


Pssm-ID: 429512  Cd Length: 108  Bit Score: 111.98  E-value: 3.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 591 PELMDMLTSDRHEAQVHLLHMGSDmSPEALQDYLDSLAPTFVRLIAVRPTGWTFtgtkkftpadngstdlpNPAKPATSL 670
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMPKL-SYEALLDYLTARKDHFDSVLAIRPTGWTY-----------------RPPKTEVSD 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1932547762 671 ELRPSYTSPtVKIYPVPYSEHSSFSELAGFCRSLNILKVIPTVGVGS 717
Cdd:pfam07522  63 RIGPSIRGR-ITIYGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVGG 108
artemis-SNM1C-like_MBL-fold cd16297
artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease ...
 327-464 4.21e-14

artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Inactivation of Artemis causes severe combined immunodeficiency (SCID). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293855  Cd Length: 171  Bit Score: 71.00  E-value: 4.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 327 TVDAFCYGKVEGcEAYFLSHFHSDHYGGLtsswnHGP-------------IYCSSITANLVIS--RLKVDEQYVRRLPMY 391
Cdd:cd16297    15 SIDRFDRENLRA-RAYFLSHCHKDHMKGL-----RAPglkrrlkaslkvkLYCSPVTKELLLTnpKYAFWENHIVSLEID 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 392 EPTVV----------QGVTVRLMDANHCPGSVLFVFDLHNPKrrYLHTGDFR-AAPDMCIDPILRQPQNVP-IDILYLDT 459
Cdd:cd16297    89 TPTQIslvdeatgekEDVVVTLLPAGHCPGSVMFLFQGNNGT--VLYTGDFRlAVGEAARMELLHSGDRVKdIQSVYLDT 166


                  ....*
gi 1932547762 460 TYSNP 464
Cdd:cd16297   167 TFCDP 171
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 343-477 5.16e-13

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 71.37  E-value: 5.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 343 FLSHFHSDHYGG---LTSSWNHGPIYCSSITANLVISRL----KVDEQYVRRLPMY------------------EPTVVQ 397
Cdd:COG1236    55 VLTHAHLDHSGAlplLVKEGFRGPIYATPATADLARILLgdsaKIQEEEAEAEPLYteedaeralelfqtvdygEPFEIG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 398 GVTVRLMDANHCPGSVLFVFDLHNpkRRYLHTGDFRAAPdmciDPILRQPQNVP-IDILYLDTTYSNPRYtfPPQDVVIR 476
Cdd:COG1236   135 GVRVTFHPAGHILGSAQVELEVGG--KRIVFSGDYGRED----DPLLAPPEPVPpADVLITESTYGDRLH--PPREEVEA 206


                  .
gi 1932547762 477 E 477
Cdd:COG1236   207 E 207
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 343-439 2.51e-08

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 54.10  E-value: 2.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762  343 FLSHFHSDHYGGLTS--SWNHGPIYCSSITANLVISRLKVDEQYVRRLPMYEPTVV--QGVTVRLMD--------ANHCP 410
Cdd:smart00849  40 ILTHGHPDHIGGLPEllEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTlkDGDELDLGGgelevihtPGHTP 119

                           90       100
                   ....*....|....*....|....*....
gi 1932547762  411 GSVLFVFdlhnPKRRYLHTGDFRAAPDMC 439
Cdd:smart00849 120 GSIVLYL----PEGKILFTGDLLFAGGDG 144
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 335-433 1.02e-07

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 53.56  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 335 KVEGCeayFLSHFHSDHYGGLTSSWNHG--PIYCSSITANLVISRLK----VDEQYVRRLPMYEPTVVQGVTVRLMDANH 408
Cdd:cd07714    55 KIKGI---FITHGHEDHIGALPYLLPELnvPIYATPLTLALIKKKLEefklIKKVKLNEIKPGERIKLGDFEVEFFRVTH 131

                          90       100
                  ....*....|....*....|....*.
gi 1932547762 409 C-PGSVLFVFdlHNPKRRYLHTGDFR 433
Cdd:cd07714   132 SiPDSVGLAI--KTPEGTIVHTGDFK 155
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 343-455 1.12e-07

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 52.85  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 343 FLSHFHSDHYGG---LTSSWNHGPIYCSSITANLV---------ISRLKVDE----------------QYVRRLPMYEPT 394
Cdd:cd16295    56 ILTHAHLDHSGRlplLVKEGFRGPIYATPATKDLAelllldsakIQEEEAEHppaeplyteedvekalKHFRPVEYGEPF 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1932547762 395 -VVQGVTVRLMDANHCPGSVLFVFDLHNPKrRYLHTGDFRAAPdmciDPILRQPQNVP-IDIL 455
Cdd:cd16295   136 eIGPGVKVTFYDAGHILGSASVELEIGGGK-RILFSGDLGRKN----TPLLRDPAPPPeADYL 193
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 339-434 2.97e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 48.76  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 339 CEAYFLSHFHSDHYgGLTSSWNHG-PIYCSSITANL--VISRLKVDEQYVRR----LPMYEPTVVqG---VTVRLMDanH 408
Cdd:cd07732    76 VDAVLLSHAHLDHY-GLLNYLRPDiPVYMGEATKRIlkALLPFFGEGDPVPRnirvFESGKSFTI-GdftVTPYLVD--H 151

                          90       100
                  ....*....|....*....|....*..
gi 1932547762 409 -CPGSVLFVfdLHNPKRRYLHTGDFRA 434
Cdd:cd07732   152 sAPGAYAFL--IEAPGKRIFYTGDFRF 176
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 343-464 4.68e-06

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 48.74  E-value: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 343 FLSHFHSDHYGGLTS-----SWNHGPIYCSSITANLVISRLKVDEQY------VRRLPMYEPTVVQGVTVRLMDANH-CP 410
Cdd:COG1235    73 LLTHEHADHIAGLDDlrpryGPNPIPVYATPGTLEALERRFPYLFAPypgkleFHEIEPGEPFEIGGLTVTPFPVPHdAG 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1932547762 411 GSVLFVFDlhNPKRRYLHTGDFRAAPdmciDPILRQPQNVpiDILYLDTTYSNP 464
Cdd:COG1235   153 DPVGYRIE--DGGKKLAYATDTGYIP----EEVLELLRGA--DLLILDATYDDP 198
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
340-463 1.46e-05

Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 47.11  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 340 EAYFLSHFHSDHYGGLT----SSWNHG-----PIYCSSITANlVISRLKVDEQYVRRLPM----YEPTVV---QGVTVRL 403
Cdd:COG1234    54 DAIFITHLHGDHIAGLPgllsTRSLAGrekplTIYGPPGTKE-FLEALLKASGTDLDFPLefheIEPGEVfeiGGFTVTA 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 404 MDANHCPGSVLFVFDLhnPKRRYLHTGDfrAAPDmciDPILRQPQNVpiDILYLDTTYSN 463
Cdd:COG1234   133 FPLDHPVPAYGYRFEE--PGRSLVYSGD--TRPC---EALVELAKGA--DLLIHEATFLD 183
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
340-442 2.22e-05

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 47.75  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 340 EAYFLSHFHSDHYGGLTSSWNHG--PIYCSSITANLVisRLKVDEQ----YVRRLPMYEPTVVQ--GVTVRLMDANH-CP 410
Cdd:COG0595    65 KGIVLTHGHEDHIGALPYLLKELnvPVYGTPLTLALL--EAKLKEHgllkKVKLHVVKPGDRIKfgPFKVEFFRVTHsIP 142

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1932547762 411 GSVLFVFdlHNPKRRYLHTGDFRaapdmcIDP 442
Cdd:COG0595   143 DSLGLAI--RTPAGTIVHTGDFK------FDQ 166
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 323-432 5.75e-05

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 44.58  E-value: 5.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 323 DTGF----TVDAFCYGKVEGCEAYFLSHFHSDHYGGLT--SSWNHGPIYCSSITANLVisrLKVDEQYVRRLPMYEPTVV 396
Cdd:cd06262    26 DPGAgaleKILEAIEELGLKIKAILLTHGHFDHIGGLAelKEAPGAPVYIHEADAELL---EDPELNLAFFGGGPLPPPE 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1932547762 397 QGVTV----RLMDAN----------HCPGSVLFVFdlhnPKRRYLHTGDF 432
Cdd:cd06262   103 PDILLedgdTIELGGlelevihtpgHTPGSVCFYI----EEEGVLFTGDT 148
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 343-431 9.67e-05

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 44.30  E-value: 9.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 343 FLSHFHSDHYGG---LTSSWNhGPIYCSSITANLVISRlkvDEQYVRRLPMYEPTV---------VQGVTVRLMDAN-HC 409
Cdd:COG0491    56 LLTHLHPDHVGGlaaLAEAFG-APVYAHAAEAEALEAP---AAGALFGREPVPPDRtledgdtleLGGPGLEVIHTPgHT 131

                          90       100
                  ....*....|....*....|..
gi 1932547762 410 PGSVLFVFdlhnPKRRYLHTGD 431
Cdd:COG0491   132 PGHVSFYV----PDEKVLFTGD 149
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 343-482 6.46e-04

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 41.53  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 343 FLSHFHSDHYGGLTS--SWNHGPIYCS-----SITANLVISRLKVdEQYVRRLPM--YEPTVV--QGVTVRLMDANH--- 408
Cdd:pfam12706  33 LLTHDHYDHLAGLLDlrEGRPRPLYAPlgvlaHLRRNFPYLFLLE-HYGVRVHEIdwGESFTVgdGGLTVTATPARHgsp 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 409 -----CPGSVL-FVFDlhNPKRRYLHTGDFRAAPDMcIDPILRqpqnvPIDILYLDTTYSNPRYTFPPQDVVIRETARLI 482
Cdd:pfam12706 112 rgldpNPGDTLgFRIE--GPGKRVYYAGDTGYFPDE-IGERLG-----GADLLLLDGGAWRDDEMIHMGHMTPEEAVEAA 183
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
343-437 2.04e-03

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 40.04  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 343 FLSHFHSDHYGG---LTSSWNHGPIYCSSITANLVISRLKVDEQYVRRLPMYEPTVVQGVTVRLMDANHCPGSVLFVFDL 419
Cdd:pfam00753  48 ILTHGHFDHIGGlgeLAEATDVPVIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHG 127

                          90       100
                  ....*....|....*....|....*...
gi 1932547762 420 HNP----------KRRYLHTGDFRAAPD 437
Cdd:pfam00753 128 PGHgpghvvvyygGGKVLFTGDLLFAGE 155
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 343-455 2.76e-03

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 40.23  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 343 FLSHFHSDHYGGLTS---SWNHGPIYCSSITANLVISRLKVDEQYVRRLPMYEPTV-----VQGVTVRLM---------- 404
Cdd:COG2333    57 VLTHPDADHIGGLAAvleAFPVGRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAgdtwqLGGVRFEVLwppedllegs 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1932547762 405 DANHcpGSVlfVFDLHNPKRRYLHTGDfraAPDMCIDPILRQPQNVPIDIL 455
Cdd:COG2333   137 DENN--NSL--VLRLTYGGFSFLLTGD---AEAEAEAALLARGPDLKADVL 180
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 336-498 4.02e-03

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 39.52  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 336 VEGCEAYFLSHFHSDHYGGLTSSW---NHGPIYCSSITANLvISRLKVDEqyVRRLPMYEPTVVQGVTVRLMDANHCPGS 412
Cdd:COG2220    46 LPKIDAVLVTHDHYDHLDDATLRAlkrTGATVVAPLGVAAW-LRAWGFPR--VTELDWGESVELGGLTVTAVPARHSSGR 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 413 VL--------FVFDLhnPKRRYLHTGDFRAAPDMciDPILRQpqnVPIDILYLDTtySNPRYTFPPQDVVirETARLIci 484
Cdd:COG2220   123 PDrngglwvgFVIET--DGKTIYHAGDTGYFPEM--KEIGER---FPIDVALLPI--GAYPFTMGPEEAA--EAARDL-- 189

                         170
                  ....*....|....
gi 1932547762 485 evgiktdQPEVVAP 498
Cdd:COG2220   190 -------KPKVVIP 196
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 345-425 4.28e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 345 SHFHSDHYGGlTSSWN-HGPIYCSS-ITANLVISRLKvdeqyvRRLPMyePTV---------VQGVTVRLM--DANHCPG 411
Cdd:cd16276    52 SHNHADHIGG-ASIFKdEGATIIAHeATAELLKRNPD------PKRPV--PTVtfddeytleVGGQTLELSyfGPNHGPG 122

                          90       100
                  ....*....|....*....|...
gi 1932547762 412 S---------VLFVFDLHNPKRR 425
Cdd:cd16276   123 NiviylpkqkVLMAVDLINPGWV 145
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 343-431 5.46e-03

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 38.40  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 343 FLSHFHSDHYGGLTS---SWNHGPiycssITANLVISRLKVDEQYVRRLPMYEPTVVQ--------------------GV 399
Cdd:cd16272    55 FLSHFHLDHIGGLPTllfARRYGG-----RKKPLTIYGPKGIKEFLEKLLNFPVEILPlgfpleieeleeggevlelgDL 129

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1932547762 400 TVRLMDANHCPGSVLFVFDLHNPKRRYlhTGD 431
Cdd:cd16272   130 KVEAFPVKHSVESLGYRIEAEGKSIVY--SGD 159
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 343-418 6.06e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 38.61  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932547762 343 FLSHFHSDHYGGLT--SSWN-----HGPIYCSSITANLVISRLKVDEQY----------VRRLPMYEPTVVQGVTVRLMD 405
Cdd:cd16279    71 LLTHAHADHIHGLDdlRPFNrlqqrPIPVYASEETLDDLKRRFPYFFAAtggggvpkldLHIIEPDEPFTIGGLEITPLP 150

                          90
                  ....*....|....
gi 1932547762 406 ANHCPGSVL-FVFD 418
Cdd:cd16279   151 VLHGKLPSLgFRFG 164
 
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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