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Conserved domains on  [gi|2499600563|ref|WP_280959705|]
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deaminase [Archaeoglobus profundus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
12-86 4.37e-42

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 148.45  E-value: 4.37e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499600563  12 SRPSWDEYFMELALVVAKRSTCLRQKVGAIIIKDKRILATGYNGAPSGMAHCLDIGCLREKLSVPSGERQELCLT 86
Cdd:COG2131     4 ERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLREKLGIPSGERGECCRT 78
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
502-578 1.59e-40

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 144.21  E-value: 1.59e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499600563 502 CRGLHAEQNAIIQAAKFGICIDGATMYTTHCPCITCAKMIINAGIKKVVYGKEYADKRGLELLKEAGVEVVYLPIEK 578
Cdd:COG2131    76 CRTVHAEQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKELLKEAGVEVRQLELEE 152
Hop super family cl34242
Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, ...
 256-502 1.50e-24

Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, transposons];


The actual alignment was detected with superfamily member COG1372:

Pssm-ID: 440983 [Multi-domain]  Cd Length: 866  Bit Score: 108.83  E-value: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 256 NWVNGG--SPRGYVIVRNGMLHSGDSPSKDipaeiEINKDTMWLFGIYLAEGCTSGNQIAFGLNVEEsEIVERIENVMRE 333
Cdd:COG1372   177 GWKEAGelKPGDRVAVPRHLPSFGEEELPD-----SLDEELAYLLGLLLGDGSLSKRGAGRFTNADE-ELLEDVAEAAEE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 334 TFNLKPNIYT----RKQSTLVRYSSKILATIFERL--FGGNAYTKRIPAELMRVKPKLQSYMLRGWLEGDGY--DNSVDV 405
Cdd:COG1372   251 LFGRADEGPRvearRATVYEVRVSSKPLAELLEELglFGKRSGEKRIPDFVFRLSREQIRAFLRGLFDADGSvsNRGGRI 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 406 RGVTASKTLALQMYQICLRLNMLPTLDSSPPRKGVKSVMYRLRI---------------------------------NKN 452
Cdd:COG1372   331 RLSTTSRRLAEQVQLLLLRLGIVSRIYERRRPDGKGRTAYRLRIsggdnlrrfaerigfgssrkqerlaellaalrrRKD 410

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2499600563 453 PKLKTRYIKNGKLYTPVSYVKM-------------DFY-----------EGKVYNLEVEEDKSFVTESFIVHNC 502
Cdd:COG1372   411 DLVRARELANGRRLSRERLRRLaledealealadsDVYwdevvsiepvgEEDVYDLTVPGTHNFVANGIVVHNS 484
Hint cd00081
Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins ...
 84-232 2.46e-10

Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins and undergo protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In protein splicing an intervening polypeptide sequence - the intein - is excised from a protein, and the flanking polypeptide sequences - the exteins - are joined by a peptide bond. In addition to the autocatalytic splicing domain, many inteins contain an inserted endonuclease domain, which plays a role in spreading inteins. Hedgehog proteins are a major class of intercellular signaling molecules, which control inductive interactions during animal development. The mature signaling forms of hedgehog proteins are the N-terminal fragments, which are covalently linked to cholesterol at their C-termini. This modification is the result of an autoprocessing step catalyzed by the C-terminal fragments, which are aligned here.


:

Pssm-ID: 238035 [Multi-domain]  Cd Length: 136  Bit Score: 58.82  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  84 CLTPDVEILT-DRGFVRISDI--KVGDKVLTH----RNRYQKVVKVISRDYKGEICVVKPMGLLPIRLTPEHEVLavkTV 156
Cdd:cd00081     1 CFTGDTLVLLeDGGRKKIEELveKKGDKVLALdetgKLVFSKVLKVLRRDYEKKFYKIKTESGREITLTPDHLLF---VL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499600563 157 KCIDGKtickescqsilrerckrffesyeedWIPAILLNKGDLVVFGFDTTVENLKSldlskyIENPPKVYYDVVR 232
Cdd:cd00081    78 EDGELK-------------------------WVFASDLKPGDYVLVPVLEKVKEIEE------IEYTGGVYDLTVE 122
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
12-86 4.37e-42

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 148.45  E-value: 4.37e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499600563  12 SRPSWDEYFMELALVVAKRSTCLRQKVGAIIIKDKRILATGYNGAPSGMAHCLDIGCLREKLSVPSGERQELCLT 86
Cdd:COG2131     4 ERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLREKLGIPSGERGECCRT 78
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
502-578 1.59e-40

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 144.21  E-value: 1.59e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499600563 502 CRGLHAEQNAIIQAAKFGICIDGATMYTTHCPCITCAKMIINAGIKKVVYGKEYADKRGLELLKEAGVEVVYLPIEK 578
Cdd:COG2131    76 CRTVHAEQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKELLKEAGVEVRQLELEE 152
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 500-565 4.88e-31

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 117.38  E-value: 4.88e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499600563 500 HNCRGLHAEQNAIIQAAKFGICIDGATMYTTHCPCITCAKMIINAGIKKVVYGKEYAD--KRGLELLK 565
Cdd:cd01286    64 KCCRTVHAEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDddPAAAELLE 131
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 17-86 4.30e-29

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 111.98  E-value: 4.30e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  17 DEYFMELALVVAKRSTCLRQKVGAIIIKDKRILATGYNGAPSGMAHCLDIGCLREKLsvPSGERQELCLT 86
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERDDL--PSGEDQKCCRT 68
Hop COG1372
Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, ...
 256-502 1.50e-24

Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, transposons];


Pssm-ID: 440983 [Multi-domain]  Cd Length: 866  Bit Score: 108.83  E-value: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 256 NWVNGG--SPRGYVIVRNGMLHSGDSPSKDipaeiEINKDTMWLFGIYLAEGCTSGNQIAFGLNVEEsEIVERIENVMRE 333
Cdd:COG1372   177 GWKEAGelKPGDRVAVPRHLPSFGEEELPD-----SLDEELAYLLGLLLGDGSLSKRGAGRFTNADE-ELLEDVAEAAEE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 334 TFNLKPNIYT----RKQSTLVRYSSKILATIFERL--FGGNAYTKRIPAELMRVKPKLQSYMLRGWLEGDGY--DNSVDV 405
Cdd:COG1372   251 LFGRADEGPRvearRATVYEVRVSSKPLAELLEELglFGKRSGEKRIPDFVFRLSREQIRAFLRGLFDADGSvsNRGGRI 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 406 RGVTASKTLALQMYQICLRLNMLPTLDSSPPRKGVKSVMYRLRI---------------------------------NKN 452
Cdd:COG1372   331 RLSTTSRRLAEQVQLLLLRLGIVSRIYERRRPDGKGRTAYRLRIsggdnlrrfaerigfgssrkqerlaellaalrrRKD 410

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2499600563 453 PKLKTRYIKNGKLYTPVSYVKM-------------DFY-----------EGKVYNLEVEEDKSFVTESFIVHNC 502
Cdd:COG1372   411 DLVRARELANGRRLSRERLRRLaledealealadsDVYwdevvsiepvgEEDVYDLTVPGTHNFVANGIVVHNS 484
cd PHA02588
deoxycytidylate deaminase; Provisional
 501-579 1.61e-22

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 94.44  E-value: 1.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 501 NCRGLHAEQNAIIQAAKFGICIDGATMYTTHCPCITCAKMIINAGIKKVVYGKEYaDKRG---LELLKEAGVEVVYLPIE 577
Cdd:PHA02588   78 SKNEIHAELNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKY-DRNGpgwDDILRKSGIEVIQIPKE 156


                  ..
gi 2499600563 578 KL 579
Cdd:PHA02588  157 EL 158
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
503-552 1.07e-18

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 81.19  E-value: 1.07e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2499600563 503 RGLHAEQNAIIQAAKFGICID--GATMYTTHCPCITCAKMIINAGIKKVVYG 552
Cdd:pfam00383  49 PTIHAERNAIRQAGKRGEGVRleGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 13-69 1.57e-18

ComE operon protein 2; This protein is found in the ComE operon for "late competence" as characterized in B. subtilis. Proteins in this family contain homology to a cytidine/deoxycytidine deaminase domain family (pfam00383), and may carry out this activity.


Pssm-ID: 131622 [Multi-domain]  Cd Length: 151  Bit Score: 82.60  E-value: 1.57e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499600563  13 RPSWDEYFMELALVVAKRSTCLRQKVGAIIIKDKRILATGYNGAPSGMAHCLDIGCL 69
Cdd:TIGR02571   2 RIKWDQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCY 58
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 445-567 5.59e-15

anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria from phage infections by depleting deoxycytidine triphosphate (dCTP), which are important for the replication of viruses. The anti-phage dCTP deaminases have an N-terminal kinase and a C-terminal dCTP deaminase domains, however, the housekeeping dCTP deaminases usually do not have the N-terminal kinase.


Pssm-ID: 468954 [Multi-domain]  Cd Length: 435  Bit Score: 77.21  E-value: 5.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 445 YRLRINKNPKLKTRYIKNgkLYTPVSYVKMDFYEGKVYNLEVEED---KSFVTESFIVHNcRGLHAEQNAIIQAAKFGIC 521
Cdd:NF041025  278 YSLGYDRNDEEKRKIIED--ILKRLADAGSESLKKKGRNASECFKlilKKSRIKDLIEFG-RAVHAEMNAILSAARLGGS 354

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2499600563 522 IDGATMYTTHCPCITCAKMIINAGIKKVVYGKEYADKRGLELLKEA 567
Cdd:NF041025  355 TKGGTLYTTTFPCHNCAKHIVAAGIKRVVYIEPYPKSLALELHSDS 400
cd PHA02588
deoxycytidylate deaminase; Provisional
 20-65 9.12e-13

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 66.70  E-value: 9.12e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2499600563  20 FMELALVVAKRSTCLRQKVGAIIIKDKRILATGYNGAPSGMAHCLD 65
Cdd:PHA02588    6 YLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCD 51
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
16-84 6.58e-11

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 59.24  E-value: 6.58e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499600563  16 WDEYFMELALVVAKRS-TCLRQKVGAIIIK-DKRILATGYNGAPSGMAHCL--DIGCLREKLSVPSGERQELC 84
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKkDGEIIATGYNGENAGYDPTIhaERNAIRQAGKRGEGVRLEGA 73
Hint cd00081
Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins ...
 84-232 2.46e-10

Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins and undergo protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In protein splicing an intervening polypeptide sequence - the intein - is excised from a protein, and the flanking polypeptide sequences - the exteins - are joined by a peptide bond. In addition to the autocatalytic splicing domain, many inteins contain an inserted endonuclease domain, which plays a role in spreading inteins. Hedgehog proteins are a major class of intercellular signaling molecules, which control inductive interactions during animal development. The mature signaling forms of hedgehog proteins are the N-terminal fragments, which are covalently linked to cholesterol at their C-termini. This modification is the result of an autoprocessing step catalyzed by the C-terminal fragments, which are aligned here.


Pssm-ID: 238035 [Multi-domain]  Cd Length: 136  Bit Score: 58.82  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  84 CLTPDVEILT-DRGFVRISDI--KVGDKVLTH----RNRYQKVVKVISRDYKGEICVVKPMGLLPIRLTPEHEVLavkTV 156
Cdd:cd00081     1 CFTGDTLVLLeDGGRKKIEELveKKGDKVLALdetgKLVFSKVLKVLRRDYEKKFYKIKTESGREITLTPDHLLF---VL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499600563 157 KCIDGKtickescqsilrerckrffesyeedWIPAILLNKGDLVVFGFDTTVENLKSldlskyIENPPKVYYDVVR 232
Cdd:cd00081    78 EDGELK-------------------------WVFASDLKPGDYVLVPVLEKVKEIEE------IEYTGGVYDLTVE 122
PRK08332 PRK08332
vitamin B12-dependent ribonucleotide reductase;
290-502 4.12e-10

vitamin B12-dependent ribonucleotide reductase;


Pssm-ID: 181392 [Multi-domain]  Cd Length: 1740  Bit Score: 62.86  E-value: 4.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  290 INKDTMWLFGIYLAEGCTSGN--QIAFGLNVE-ESEIVERIENVMRETFNLKPNIYtrkqstlvRYSSKILATI------ 360
Cdd:PRK08332  1056 IGEDLAFVLGWFIGDGYLNVNdkRAWFYFNAEkEEEIAWKIREILAKHFGIKAEPH--------RYGNQIKLGVrgeayr 1127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  361 -FERLFGGNayTKRIPAELMRVKPKLQSYMLRGWLEGDGY-DNSVDVRGVTASKTLALQMYQICLRLNMLPTLDSSP--- 435
Cdd:PRK08332  1128 wLESIVKTN--EKRVPEIVYRLKPREIAAFLRGLFSADGYvDNDMAIRLTSKSRELLRDVQDLLLLFGILSKIYERPyks 1205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  436 -----PRKGVKSV-----MYRLRIN----------------KNPKLKTRYIKNGKLYTPVSYVKMdFYEGKVYNLEVEED 489
Cdd:PRK08332  1206 efkytTKDGEERTyraegYYELVIAnysrklfaekigfegyKMEKLSLQKTKIDEPIVTVESVEV-LGEEIVYDFTVPEH 1284

                          250
                   ....*....|...
gi 2499600563  490 KSFVTESFIVHNC 502
Cdd:PRK08332  1285 HSYISNGFMSHNC 1297
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 506-571 4.54e-09

riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 273015 [Multi-domain]  Cd Length: 344  Bit Score: 58.30  E-value: 4.54e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499600563 506 HAEQNAIIQAakfGICIDGATMYTTHCPCI------TCAKMIINAGIKKVVYGKEYADK----RGLELLKEAGVEV 571
Cdd:TIGR00326  44 HAEVHALRQA---GENAKGATAYVTLEPCShqgrtpPCAEAIIEAGIKKVVVSMQDPNPlvagRGAERLKQAGIEV 116
HintN smart00306
Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. ...
 83-152 2.87e-08

Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. Domain has been split to accommodate large insertions of endonucleases.


Pssm-ID: 197642 [Multi-domain]  Cd Length: 100  Bit Score: 51.50  E-value: 2.87e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499600563   83 LCLTPDVEILTDR-GFVRISDIKVGDKVLTHRN-----RYQKVVKVISRDYKGEICVVKPMGLLPIRLTPEHEVLA 152
Cdd:smart00306   1 GCFPGDTLVLTEDgGIKKIEELEEGDKVLALDEgtlkySPVKVFLVREPKGEKKFYRIKTENGREITLTPDHLLLV 76
Intein_splicing pfam14890
Intein splicing domain; Inteins are segments of protein which excise themselves from a ...
 118-501 1.57e-07

Intein splicing domain; Inteins are segments of protein which excise themselves from a precursor protein and mediate the rejoining of the remainder of the precursor (the extein). Most inteins consist of a splicing domain which is split into two segments by a homing endonuclease domain. This domain represents the splicing domain.


Pssm-ID: 434290 [Multi-domain]  Cd Length: 378  Bit Score: 53.62  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 118 KVVKVISRDYKGEICVVKPMGLLPIRLTPEHEVLAV----KTVKCIDGktickescqsilrerckrffesyeedwipail 193
Cdd:pfam14890  37 SVKHAWKLGYKGPLYEITLSNGRKIKATPDHKFFVIrdnlGWVKRADE-------------------------------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 194 LNKGDLVVFGFDTTVENLKSLDLSKYIENPPKVYYdVVRAKNSGKTYSYIEKVYGISrsvawNWVNGGSPRGYVIVRNGM 273
Cdd:pfam14890  85 LKEGDYIAVPRKLPSSGLPNMELLELLLWLGILGH-LIEITGDGCILKRHYIVYTEK-----YKYTREIPLKELIEWIEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 274 LHSGDSPSKDIPAEIEInkdtmwlfgIYLAeGCTSGNQIAFGLNVEESEIVERIEnvmretfnlkpniytrkqstlvrys 353
Cdd:pfam14890 159 ELFGDVINPRIKPERKF---------WYQV-GLVAGDGLTHDKKNPIAKWLESLE------------------------- 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 354 skilatiferLFGGNAYTKRIPAELMRVKPKLQSYMLRGWLEGDGYDNSVDVRGVTASKTLALQmYQICLRLNMLPTLDS 433
Cdd:pfam14890 204 ----------IFGLLSYNKFIPEFVFSLPKGAIASFIRGYFDTDGCISKRNPGIYLSSTSERLA-EDVQLLLLSLGINAR 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 434 SPPRKGVKSVMYRLRINKNPKLKTRYIKNGK--------------------------------------LYTPVSYVKMD 475
Cdd:pfam14890 273 LSKINGKGRNVYHVLITGKSSLEKFKEKIGAylqikkekleeilnkykqsnaessevkdflewlinsdvYWDKVKSIEVL 352

                         410       420
                  ....*....|....*....|....*.
gi 2499600563 476 FYEGKVYNLEVEEDKSFVTESFIVHN 501
Cdd:pfam14890 353 DEEEYVYDLTVEGYHNFVANGIIVHN 378
Hint_2 pfam13403
Hint domain; This domain is found in inteins.
 84-146 1.76e-06

Hint domain; This domain is found in inteins.


Pssm-ID: 433179 [Multi-domain]  Cd Length: 147  Bit Score: 48.01  E-value: 1.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499600563  84 CLTPDVEILTDRGFVRISDIKVGDKVLTHRNRYQKVVKVISRDYKGEICVVKPmGLLPIRLTP 146
Cdd:pfam13403   2 CFAPGTLIATPRGEVPVETLRPGDLVVTRDGGAQPVRWIGRRTLSLADLPAPP-ALRPVRIRA 63
intein_Cterm TIGR01443
intein C-terminal splicing region; This model represents the well-conserved C-terminal region ...
 480-500 3.21e-03

intein C-terminal splicing region; This model represents the well-conserved C-terminal region of a large number of inteins. It is based on interated search results, starting with a curated collection of intein N-terminal splicing regions from InBase, the New England Biolabs Intein Database, as presented on its web site. Inteins are regions encoded within proteins from which they remove themselves after translation in a self-splicing reaction, leaving the remainder of the coding region to form a complete, functional protein as if the intein were never there. Proteins with inteins include RecA, GyrA, ribonucleotide reductase, and others. Most inteins have a central region with putative endonuclease activity.


Pssm-ID: 213622 [Multi-domain]  Cd Length: 21  Bit Score: 35.09  E-value: 3.21e-03
                          10        20
                  ....*....|....*....|.
gi 2499600563 480 KVYNLEVEEDKSFVTESFIVH 500
Cdd:TIGR01443   1 YVYDLTVEGNHNFIANGIVVH 21
HintC smart00305
Hint (Hedgehog/Intein) domain C-terminal region; Hedgehog/Intein domain, C-terminal region. ...
 480-507 5.35e-03

Hint (Hedgehog/Intein) domain C-terminal region; Hedgehog/Intein domain, C-terminal region. Domain has been split to accommodate large insertions of endonucleases.


Pssm-ID: 197641  Cd Length: 46  Bit Score: 35.23  E-value: 5.35e-03
                           10        20
                   ....*....|....*....|....*...
gi 2499600563  480 KVYNLEVEEDKSFVTESFIVHNCRGLHA 507
Cdd:smart00305  19 GVYDPTVTENHNFIANGILVHNCAEIET 46
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
12-86 4.37e-42

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 148.45  E-value: 4.37e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499600563  12 SRPSWDEYFMELALVVAKRSTCLRQKVGAIIIKDKRILATGYNGAPSGMAHCLDIGCLREKLSVPSGERQELCLT 86
Cdd:COG2131     4 ERPSWDEYFMEIAKLVALRSTCLRRQVGAVIVKDKRILATGYNGAPSGLPHCDEVGCLREKLGIPSGERGECCRT 78
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
502-578 1.59e-40

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 144.21  E-value: 1.59e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499600563 502 CRGLHAEQNAIIQAAKFGICIDGATMYTTHCPCITCAKMIINAGIKKVVYGKEYADKRGLELLKEAGVEVVYLPIEK 578
Cdd:COG2131    76 CRTVHAEQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDYPDELAKELLKEAGVEVRQLELEE 152
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 500-565 4.88e-31

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 117.38  E-value: 4.88e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499600563 500 HNCRGLHAEQNAIIQAAKFGICIDGATMYTTHCPCITCAKMIINAGIKKVVYGKEYAD--KRGLELLK 565
Cdd:cd01286    64 KCCRTVHAEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDddPAAAELLE 131
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 17-86 4.30e-29

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 111.98  E-value: 4.30e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  17 DEYFMELALVVAKRSTCLRQKVGAIIIKDKRILATGYNGAPSGMAHCLDIGCLREKLsvPSGERQELCLT 86
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIISTGYNGSPSGLPHCAEVGCERDDL--PSGEDQKCCRT 68
Hop COG1372
Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, ...
 256-502 1.50e-24

Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, transposons];


Pssm-ID: 440983 [Multi-domain]  Cd Length: 866  Bit Score: 108.83  E-value: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 256 NWVNGG--SPRGYVIVRNGMLHSGDSPSKDipaeiEINKDTMWLFGIYLAEGCTSGNQIAFGLNVEEsEIVERIENVMRE 333
Cdd:COG1372   177 GWKEAGelKPGDRVAVPRHLPSFGEEELPD-----SLDEELAYLLGLLLGDGSLSKRGAGRFTNADE-ELLEDVAEAAEE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 334 TFNLKPNIYT----RKQSTLVRYSSKILATIFERL--FGGNAYTKRIPAELMRVKPKLQSYMLRGWLEGDGY--DNSVDV 405
Cdd:COG1372   251 LFGRADEGPRvearRATVYEVRVSSKPLAELLEELglFGKRSGEKRIPDFVFRLSREQIRAFLRGLFDADGSvsNRGGRI 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 406 RGVTASKTLALQMYQICLRLNMLPTLDSSPPRKGVKSVMYRLRI---------------------------------NKN 452
Cdd:COG1372   331 RLSTTSRRLAEQVQLLLLRLGIVSRIYERRRPDGKGRTAYRLRIsggdnlrrfaerigfgssrkqerlaellaalrrRKD 410

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2499600563 453 PKLKTRYIKNGKLYTPVSYVKM-------------DFY-----------EGKVYNLEVEEDKSFVTESFIVHNC 502
Cdd:COG1372   411 DLVRARELANGRRLSRERLRRLaledealealadsDVYwdevvsiepvgEEDVYDLTVPGTHNFVANGIVVHNS 484
cd PHA02588
deoxycytidylate deaminase; Provisional
 501-579 1.61e-22

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 94.44  E-value: 1.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 501 NCRGLHAEQNAIIQAAKFGICIDGATMYTTHCPCITCAKMIINAGIKKVVYGKEYaDKRG---LELLKEAGVEVVYLPIE 577
Cdd:PHA02588   78 SKNEIHAELNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKY-DRNGpgwDDILRKSGIEVIQIPKE 156


                  ..
gi 2499600563 578 KL 579
Cdd:PHA02588  157 EL 158
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
503-552 1.07e-18

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 81.19  E-value: 1.07e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2499600563 503 RGLHAEQNAIIQAAKFGICID--GATMYTTHCPCITCAKMIINAGIKKVVYG 552
Cdd:pfam00383  49 PTIHAERNAIRQAGKRGEGVRleGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
ComEB TIGR02571
ComE operon protein 2; This protein is found in the ComE operon for "late competence" as ...
 13-69 1.57e-18

ComE operon protein 2; This protein is found in the ComE operon for "late competence" as characterized in B. subtilis. Proteins in this family contain homology to a cytidine/deoxycytidine deaminase domain family (pfam00383), and may carry out this activity.


Pssm-ID: 131622 [Multi-domain]  Cd Length: 151  Bit Score: 82.60  E-value: 1.57e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499600563  13 RPSWDEYFMELALVVAKRSTCLRQKVGAIIIKDKRILATGYNGAPSGMAHCLDIGCL 69
Cdd:TIGR02571   2 RIKWDQYFMAQSHLLALRSTCTRLSVGATIVRDKRIIAGGYNGSVAGGVHCIDEGCY 58
antiphage_deaminase NF041025
anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria ...
 445-567 5.59e-15

anti-phage dCTP deaminase; It has been shown that proteins of this family prevented bacteria from phage infections by depleting deoxycytidine triphosphate (dCTP), which are important for the replication of viruses. The anti-phage dCTP deaminases have an N-terminal kinase and a C-terminal dCTP deaminase domains, however, the housekeeping dCTP deaminases usually do not have the N-terminal kinase.


Pssm-ID: 468954 [Multi-domain]  Cd Length: 435  Bit Score: 77.21  E-value: 5.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 445 YRLRINKNPKLKTRYIKNgkLYTPVSYVKMDFYEGKVYNLEVEED---KSFVTESFIVHNcRGLHAEQNAIIQAAKFGIC 521
Cdd:NF041025  278 YSLGYDRNDEEKRKIIED--ILKRLADAGSESLKKKGRNASECFKlilKKSRIKDLIEFG-RAVHAEMNAILSAARLGGS 354

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2499600563 522 IDGATMYTTHCPCITCAKMIINAGIKKVVYGKEYADKRGLELLKEA 567
Cdd:NF041025  355 TKGGTLYTTTFPCHNCAKHIVAAGIKRVVYIEPYPKSLALELHSDS 400
cd PHA02588
deoxycytidylate deaminase; Provisional
 20-65 9.12e-13

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 66.70  E-value: 9.12e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2499600563  20 FMELALVVAKRSTCLRQKVGAIIIKDKRILATGYNGAPSGMAHCLD 65
Cdd:PHA02588    6 YLQIAYLVSQESKCVSWKVGAVIEKNGRIISTGYNGTPAGGVNCCD 51
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 506-557 5.02e-12

MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems.


Pssm-ID: 433953 [Multi-domain]  Cd Length: 144  Bit Score: 63.70  E-value: 5.02e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2499600563 506 HAEQNAIIQAAKFGICI--DGATMYTTHCPCITCAKMIINAGIKKVVYGKEYAD 557
Cdd:pfam14437  52 HAEILAIQQAAKKLGSWrlDDATLYVTLEPCPMCAGAIVQAGLKSLVYGAGNPK 105
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 506-572 5.14e-12

Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and metabolism]; Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439887 [Multi-domain]  Cd Length: 311  Bit Score: 67.01  E-value: 5.14e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499600563 506 HAEQNAIIQAakfGICIDGATMYTTHCPCI----T--CAKMIINAGIKKVVYGKE----YADKRGLELLKEAGVEVV 572
Cdd:COG0117    47 HAEVNALAQA---GEAARGATLYVTLEPCShhgrTppCADALIEAGIKRVVIAMLdpnpLVAGKGIARLRAAGIEVE 120
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
16-84 6.58e-11

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 59.24  E-value: 6.58e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499600563  16 WDEYFMELALVVAKRS-TCLRQKVGAIIIK-DKRILATGYNGAPSGMAHCL--DIGCLREKLSVPSGERQELC 84
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKkDGEIIATGYNGENAGYDPTIhaERNAIRQAGKRGEGVRLEGA 73
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 506-568 1.82e-10

Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD (Diaminohydroxyphosphoribosylaminopyrimidine deaminase) catalyzes the deamination of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, which is an intermediate step in the biosynthesis of riboflavin.The ribG gene of Bacillus subtilis and the ribD gene of E. coli are bifunctional and contain this deaminase domain and a reductase domain which catalyzes the subsequent reduction of the ribosyl side chain.


Pssm-ID: 238611 [Multi-domain]  Cd Length: 115  Bit Score: 58.40  E-value: 1.82e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499600563 506 HAEQNAIIQAAKfgICIDGATMYTTHCPCI------TCAKMIINAGIKKVVYG----KEYADKRGLELLKEAG 568
Cdd:cd01284    45 HAEVNALASAGE--KLARGATLYVTLEPCShhgktpPCVDAIIEAGIKRVVVGvrdpNPLVAGKGAERLRAAG 115
Hint cd00081
Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins ...
 84-232 2.46e-10

Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins and undergo protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In protein splicing an intervening polypeptide sequence - the intein - is excised from a protein, and the flanking polypeptide sequences - the exteins - are joined by a peptide bond. In addition to the autocatalytic splicing domain, many inteins contain an inserted endonuclease domain, which plays a role in spreading inteins. Hedgehog proteins are a major class of intercellular signaling molecules, which control inductive interactions during animal development. The mature signaling forms of hedgehog proteins are the N-terminal fragments, which are covalently linked to cholesterol at their C-termini. This modification is the result of an autoprocessing step catalyzed by the C-terminal fragments, which are aligned here.


Pssm-ID: 238035 [Multi-domain]  Cd Length: 136  Bit Score: 58.82  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  84 CLTPDVEILT-DRGFVRISDI--KVGDKVLTH----RNRYQKVVKVISRDYKGEICVVKPMGLLPIRLTPEHEVLavkTV 156
Cdd:cd00081     1 CFTGDTLVLLeDGGRKKIEELveKKGDKVLALdetgKLVFSKVLKVLRRDYEKKFYKIKTESGREITLTPDHLLF---VL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499600563 157 KCIDGKtickescqsilrerckrffesyeedWIPAILLNKGDLVVFGFDTTVENLKSldlskyIENPPKVYYDVVR 232
Cdd:cd00081    78 EDGELK-------------------------WVFASDLKPGDYVLVPVLEKVKEIEE------IEYTGGVYDLTVE 122
PRK08332 PRK08332
vitamin B12-dependent ribonucleotide reductase;
290-502 4.12e-10

vitamin B12-dependent ribonucleotide reductase;


Pssm-ID: 181392 [Multi-domain]  Cd Length: 1740  Bit Score: 62.86  E-value: 4.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  290 INKDTMWLFGIYLAEGCTSGN--QIAFGLNVE-ESEIVERIENVMRETFNLKPNIYtrkqstlvRYSSKILATI------ 360
Cdd:PRK08332  1056 IGEDLAFVLGWFIGDGYLNVNdkRAWFYFNAEkEEEIAWKIREILAKHFGIKAEPH--------RYGNQIKLGVrgeayr 1127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  361 -FERLFGGNayTKRIPAELMRVKPKLQSYMLRGWLEGDGY-DNSVDVRGVTASKTLALQMYQICLRLNMLPTLDSSP--- 435
Cdd:PRK08332  1128 wLESIVKTN--EKRVPEIVYRLKPREIAAFLRGLFSADGYvDNDMAIRLTSKSRELLRDVQDLLLLFGILSKIYERPyks 1205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  436 -----PRKGVKSV-----MYRLRIN----------------KNPKLKTRYIKNGKLYTPVSYVKMdFYEGKVYNLEVEED 489
Cdd:PRK08332  1206 efkytTKDGEERTyraegYYELVIAnysrklfaekigfegyKMEKLSLQKTKIDEPIVTVESVEV-LGEEIVYDFTVPEH 1284

                          250
                   ....*....|...
gi 2499600563  490 KSFVTESFIVHNC 502
Cdd:PRK08332  1285 HSYISNGFMSHNC 1297
PRK14715 PRK14715
DNA-directed DNA polymerase II large subunit;
297-492 9.01e-10

DNA-directed DNA polymerase II large subunit;


Pssm-ID: 237799 [Multi-domain]  Cd Length: 1627  Bit Score: 61.78  E-value: 9.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  297 LFGIYLAEG----CTSGNQIAFglNVEESEIVERIENVMRETFNLKPNIYTRKQSTLVrySSKILATIFERLF--GGNAY 370
Cdd:PRK14715  1123 VIGYYLAEGyareSKSVYQINF--SNAEEEVREDIKKALREAFGDGFGIYERGGKVTV--GSRILYLLFTEVLkaGKNAH 1198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  371 TKRIPAELMRVKPKLQSYMLRGWLEGDGYDNSVDVRGV--TASKTL-----ALQMYQICLRLNMlpTLDSSPPRKGVKSV 443
Cdd:PRK14715  1199 SKRVPSFVFKLPKEKVKLMLSAYFEGDGSALKTVPRVVvySANKKLledidTLLLAKFGIRGYW--TADKNANRGGARVR 1276

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2499600563  444 MYRL-RINKNPKLKTRYIKNGKLYTPVSYVKMDFYEGKVYNL-EVEEDKSF 492
Cdd:PRK14715  1277 KYHEeRGTEAPKSKVYALNIAGEYYDRFFEEIGFVSERKQSIyELHKNKVR 1327
eubact_ribD TIGR00326
riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in ...
 506-571 4.54e-09

riboflavin biosynthesis protein RibD; This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 273015 [Multi-domain]  Cd Length: 344  Bit Score: 58.30  E-value: 4.54e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499600563 506 HAEQNAIIQAakfGICIDGATMYTTHCPCI------TCAKMIINAGIKKVVYGKEYADK----RGLELLKEAGVEV 571
Cdd:TIGR00326  44 HAEVHALRQA---GENAKGATAYVTLEPCShqgrtpPCAEAIIEAGIKKVVVSMQDPNPlvagRGAERLKQAGIEV 116
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 500-552 8.38e-09

Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.


Pssm-ID: 238612 [Multi-domain]  Cd Length: 109  Bit Score: 53.39  E-value: 8.38e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2499600563 500 HNCRG------LHAEQNAIIQAAK-FGICI-DGATMYTTHCPCITCAKMIINAGIKKVVYG 552
Cdd:cd01285    35 HNRVEqdgdptAHAEIVAIRNAARrLGSYLlSGCTLYTTLEPCPMCAGALLWARIKRVVYG 95
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 506-560 1.31e-08

tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification


Pssm-ID: 440355 [Multi-domain]  Cd Length: 148  Bit Score: 53.97  E-value: 1.31e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499600563 506 HAEQNAIIQAAKF--GICIDGATMYTTHCPCITCAKMIINAGIKKVVYGkEYADKRG 560
Cdd:COG0590    53 HAEILAIRAAARKlgNWRLSGCTLYVTLEPCPMCAGAIVWARIGRVVYG-ASDPKAG 108
HintN smart00306
Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. ...
 83-152 2.87e-08

Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. Domain has been split to accommodate large insertions of endonucleases.


Pssm-ID: 197642 [Multi-domain]  Cd Length: 100  Bit Score: 51.50  E-value: 2.87e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499600563   83 LCLTPDVEILTDR-GFVRISDIKVGDKVLTHRN-----RYQKVVKVISRDYKGEICVVKPMGLLPIRLTPEHEVLA 152
Cdd:smart00306   1 GCFPGDTLVLTEDgGIKKIEELEEGDKVLALDEgtlkySPVKVFLVREPKGEKKFYRIKTENGREITLTPDHLLLV 76
Intein_splicing pfam14890
Intein splicing domain; Inteins are segments of protein which excise themselves from a ...
 118-501 1.57e-07

Intein splicing domain; Inteins are segments of protein which excise themselves from a precursor protein and mediate the rejoining of the remainder of the precursor (the extein). Most inteins consist of a splicing domain which is split into two segments by a homing endonuclease domain. This domain represents the splicing domain.


Pssm-ID: 434290 [Multi-domain]  Cd Length: 378  Bit Score: 53.62  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 118 KVVKVISRDYKGEICVVKPMGLLPIRLTPEHEVLAV----KTVKCIDGktickescqsilrerckrffesyeedwipail 193
Cdd:pfam14890  37 SVKHAWKLGYKGPLYEITLSNGRKIKATPDHKFFVIrdnlGWVKRADE-------------------------------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 194 LNKGDLVVFGFDTTVENLKSLDLSKYIENPPKVYYdVVRAKNSGKTYSYIEKVYGISrsvawNWVNGGSPRGYVIVRNGM 273
Cdd:pfam14890  85 LKEGDYIAVPRKLPSSGLPNMELLELLLWLGILGH-LIEITGDGCILKRHYIVYTEK-----YKYTREIPLKELIEWIEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 274 LHSGDSPSKDIPAEIEInkdtmwlfgIYLAeGCTSGNQIAFGLNVEESEIVERIEnvmretfnlkpniytrkqstlvrys 353
Cdd:pfam14890 159 ELFGDVINPRIKPERKF---------WYQV-GLVAGDGLTHDKKNPIAKWLESLE------------------------- 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 354 skilatiferLFGGNAYTKRIPAELMRVKPKLQSYMLRGWLEGDGYDNSVDVRGVTASKTLALQmYQICLRLNMLPTLDS 433
Cdd:pfam14890 204 ----------IFGLLSYNKFIPEFVFSLPKGAIASFIRGYFDTDGCISKRNPGIYLSSTSERLA-EDVQLLLLSLGINAR 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 434 SPPRKGVKSVMYRLRINKNPKLKTRYIKNGK--------------------------------------LYTPVSYVKMD 475
Cdd:pfam14890 273 LSKINGKGRNVYHVLITGKSSLEKFKEKIGAylqikkekleeilnkykqsnaessevkdflewlinsdvYWDKVKSIEVL 352

                         410       420
                  ....*....|....*....|....*.
gi 2499600563 476 FYEGKVYNLEVEEDKSFVTESFIVHN 501
Cdd:pfam14890 353 DEEEYVYDLTVEGYHNFVANGIIVHN 378
Hint_2 pfam13403
Hint domain; This domain is found in inteins.
 84-146 1.76e-06

Hint domain; This domain is found in inteins.


Pssm-ID: 433179 [Multi-domain]  Cd Length: 147  Bit Score: 48.01  E-value: 1.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499600563  84 CLTPDVEILTDRGFVRISDIKVGDKVLTHRNRYQKVVKVISRDYKGEICVVKPmGLLPIRLTP 146
Cdd:pfam13403   2 CFAPGTLIATPRGEVPVETLRPGDLVVTRDGGAQPVRWIGRRTLSLADLPAPP-ALRPVRIRA 63
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 505-550 1.96e-06

Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine deaminases, nucleoside deaminases, deoxycytidylate deaminases and riboflavin deaminases. Also included are the apoBec family of mRNA editing enzymes. All members are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate.


Pssm-ID: 238406 [Multi-domain]  Cd Length: 96  Bit Score: 46.39  E-value: 1.96e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2499600563 505 LHAEQNAIIQAAKFGiCIDGATMYTTHCPCITCAKMIINAGIKKVV 550
Cdd:cd00786    48 NHAERTALFNAGSEG-DTKGQMLYVALSPCGACAQLIIELGIKDVI 92
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 17-54 1.02e-04

tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification


Pssm-ID: 440355 [Multi-domain]  Cd Length: 148  Bit Score: 42.80  E-value: 1.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2499600563  17 DEYFMELALVVAKRStcLRQK---VGAIIIKDKRILATGYN 54
Cdd:COG0590     4 DEEFMRRALELARKA--VAEGevpVGAVLVKDGEIIARGHN 42
PRK14898 PRK14898
DNA-directed RNA polymerase subunit A''; Provisional
 281-441 2.09e-04

DNA-directed RNA polymerase subunit A''; Provisional


Pssm-ID: 237854 [Multi-domain]  Cd Length: 858  Bit Score: 44.50  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 281 SKDIPAEIEINKDTMWLFGIYLAEGCTSGNQIAFGlNVEEsEIVERIENvMRETFNLKPNIYTRKQSTLVRYSSKILATI 360
Cdd:PRK14898  232 TVGLPETFPLDEETGYFVGAYLAEGSLTDHYVSIS-NVDE-TFQNRVRA-FAERFDLSVNEYENDSGFATGYDIRLNGTV 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 361 ---FERLFGGNAYTKRIPAELMRVKPKLQSYMLRGWLEGDGY--DNSVDVRGVTASKTLALQMYQICLRLNMLPTLDSSP 435
Cdd:PRK14898  309 lsdFLRNFCTDDGEKKIPDFAFGANKEFVRGLLQGYFDGDGNvgTNKKAIRISSTSKELIDGISLLLARFDIYATKGTQK 388


                  ....*.
gi 2499600563 436 PRKGVK 441
Cdd:PRK14898  389 DSFTLR 394
ribD PRK10786
bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6- ...
 489-571 2.89e-03

bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD;


Pssm-ID: 182729 [Multi-domain]  Cd Length: 367  Bit Score: 40.13  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563 489 DKSFVTESFivHNCRG-LHAEQNAIIQAakfGICIDGATMYTTHCPCI------TCAKMIINAGIKKVVYGKEYADK--- 558
Cdd:PRK10786   34 DGEIVGEGY--HQRAGePHAEVHALRMA---GEKAKGATAYVTLEPCShhgrtpPCCDALIAAGVARVVAAMQDPNPqva 108

                          90
                  ....*....|....
gi 2499600563 559 -RGLELLKEAGVEV 571
Cdd:PRK10786  109 gRGLYRLQQAGIDV 122
intein_Cterm TIGR01443
intein C-terminal splicing region; This model represents the well-conserved C-terminal region ...
 480-500 3.21e-03

intein C-terminal splicing region; This model represents the well-conserved C-terminal region of a large number of inteins. It is based on interated search results, starting with a curated collection of intein N-terminal splicing regions from InBase, the New England Biolabs Intein Database, as presented on its web site. Inteins are regions encoded within proteins from which they remove themselves after translation in a self-splicing reaction, leaving the remainder of the coding region to form a complete, functional protein as if the intein were never there. Proteins with inteins include RecA, GyrA, ribonucleotide reductase, and others. Most inteins have a central region with putative endonuclease activity.


Pssm-ID: 213622 [Multi-domain]  Cd Length: 21  Bit Score: 35.09  E-value: 3.21e-03
                          10        20
                  ....*....|....*....|.
gi 2499600563 480 KVYNLEVEEDKSFVTESFIVH 500
Cdd:TIGR01443   1 YVYDLTVEGNHNFIANGIVVH 21
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 290-483 3.50e-03

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 40.39  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  290 INKDTMWLFGIYLAEGCTSGNQIAFgLNVEESeIVERIENVMRETFNLKPNIYTRKQSTLVRYSSKILATIFERL-FGGN 368
Cdd:PRK14698   389 LDEELAEFLGYLIADGTLKPRTVAI-YNNDES-LLKRANELAMELFGIEGKIVKERTVKALLIHSKALVDFFKKLgIPGN 466

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499600563  369 --AYTKRIPAELMRVKPKLQSYMLRGWLEGDGY--DNSVDVRGVTASKTLALQMYQICLRLNMLPTLDssppRKGVKS-V 443
Cdd:PRK14698   467 kkARTWKVPKELLISEPEVVKAFIKAYIACDGYydEEKGEIEIVTASEEAAYGFSYLLAKLGIYAIIR----EKIIGDkE 542

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2499600563  444 MYRLRINKNPKLKTRYIKN-GKLYTPVSYVKMDFYEgkVYN 483
Cdd:PRK14698   543 YYRVVISGEANLEKLGIEReARGYTSIDIVPVDVEE--IYE 581
HintC smart00305
Hint (Hedgehog/Intein) domain C-terminal region; Hedgehog/Intein domain, C-terminal region. ...
 480-507 5.35e-03

Hint (Hedgehog/Intein) domain C-terminal region; Hedgehog/Intein domain, C-terminal region. Domain has been split to accommodate large insertions of endonucleases.


Pssm-ID: 197641  Cd Length: 46  Bit Score: 35.23  E-value: 5.35e-03
                           10        20
                   ....*....|....*....|....*...
gi 2499600563  480 KVYNLEVEEDKSFVTESFIVHNCRGLHA 507
Cdd:smart00305  19 GVYDPTVTENHNFIANGILVHNCAEIET 46
 
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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