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Conserved domains on  [gi|220927203|ref|YP_002502505|]
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metal dependent phosphohydrolase [Methylobacterium nodulans ORS 2060]

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List of domain hits

Name Accession Description Interval E-value
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
189-328 1.88e-22

Metal dependent phosphohydrolases with conserved 'HD' motif


:

Pssm-ID: 238032  Cd Length: 145  Bit Score: 91.25  E-value: 1.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 189 GVYQHSLGVAGYAGAFAGLLGFRRHDQERLVRAALLHDVGKARIPLAILNkpsslsaEEMAVMRRHPVIGAALLARQPG- 267
Cdd:cd00077    2 HRFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITE-------EESELEKDHAIVGAEILRELLLe 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 220927203 268 -----FDAEILDVVRHHHEMLDGSGYPDGLRGGAIGDLVRLVTICDICSALT-ERRPYRAPIGPAEA 328
Cdd:cd00077   75 eviklIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrDSREKRRRIAEEDL 141
 
Name Accession Description Interval E-value
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
189-328 1.88e-22

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032  Cd Length: 145  Bit Score: 91.25  E-value: 1.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 189 GVYQHSLGVAGYAGAFAGLLGFRRHDQERLVRAALLHDVGKARIPLAILNkpsslsaEEMAVMRRHPVIGAALLARQPG- 267
Cdd:cd00077    2 HRFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITE-------EESELEKDHAIVGAEILRELLLe 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 220927203 268 -----FDAEILDVVRHHHEMLDGSGYPDGLRGGAIGDLVRLVTICDICSALT-ERRPYRAPIGPAEA 328
Cdd:cd00077   75 eviklIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrDSREKRRRIAEEDL 141
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic ...
190-320 2.05e-15

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679  Cd Length: 124  Bit Score: 71.56  E-value: 2.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203   190 VYQHSLGVAGYAGAFAGLLGFrrHDQERLVRAALLHDVGKARIPLAILNKPSslsaeemaVMRRHPVIGAALLARQPGFD 269
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGL--LDIELLLLAALLHDIGKPGTPDSFLVKTS--------VLEDHHFIGAEILLEEEEPR 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 220927203   270 AEILDV---VRHHHEMLdgsgypDGLRGGAIGDLVRLVTICDICSALTERRPYR 320
Cdd:smart00471  75 ILEEILrtaILSHHERP------DGLRGEPITLEARIVKVADRLDALRADRRYR 122
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
190-313 2.83e-14

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 251000  Cd Length: 110  Bit Score: 68.03  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203  190 VYQHSLGVAGYAGAFAGLLGFRrhDQERLVRAALLHDVGKARIPLAILnkpsslsaEEMAVMRRHPVIGAALLARQPGFD 269
Cdd:pfam01966   1 VLEHSLRVALLARELAEELGEL--DRELLLLAALLHDIGKPPFGDEKP--------LLFEIFLGHAVVGAEILRELEKPL 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 220927203  270 AE--ILDVVRHHHEMldgsgyPDGLRGGAIGDLVRLVTICDICSAL 313
Cdd:pfam01966  71 GLedVLKLILEHHES------WEGLYGEPISLEARIVKLADRLDAL 110
HDIG TIGR00277
uncharacterized domain HDIG; This domain is found in a few known nucleotidyltransferes and in ...
189-282 1.50e-10

uncharacterized domain HDIG; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. For proteins scoring above the trusted cutoff, confidence is high both that the domain is present and that the model produces an essentially correct alignment. Protein regions scoring between the trusted and noise cutoffs include correctly aligned domains, homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits indications of homology.


Pssm-ID: 232902  Cd Length: 80  Bit Score: 56.95  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203  189 GVYQHSLGVAGYAGAFAGLLGFrrhDQERLVRAALLHDVGKARIPlailnkpsslsaeEMAVMRRHPVIGAAlLARQPGF 268
Cdd:TIGR00277   4 NVLQHSLEVAKLAEALARELGL---DVELARRGALLHDIGKPITR-------------EGVIFESHAVVGAE-IARKYGE 66
                          90
                  ....*....|....
gi 220927203  269 DAEILDVVRHHHEM 282
Cdd:TIGR00277  67 PLEVIDIIAEHHGK 80
COG1713 COG1713
Predicted HD superfamily hydrolase involved in NAD metabolism [Coenzyme metabolism]
191-304 4.56e-06

Predicted HD superfamily hydrolase involved in NAD metabolism [Coenzyme metabolism]


Pssm-ID: 224627  Cd Length: 187  Bit Score: 45.37  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 191 YQHSLGVAGYAGAFAGLLGFrrhDQERLVRAALLHDVGKARIP---LAILNKPSSLSAEEmavmRRHPVI-----GAALL 262
Cdd:COG1713   19 FEHCLGVAETAIELAEAYGL---DPEKAYLAGILHDIAKELPEqklLKIAKKYGLELDLE----RESPLLlhgkvGAYLL 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 220927203 263 ARQPGF-DAEILDVVRHH----HEM--LD-----------GSGYP--DGLRGGAIGDLVRLV 304
Cdd:COG1713   92 KEEFGIkDEEVLSAIEYHttgrKQMtlLDkilyvadkiepGRGFPgvDKIRQIALKDLNKAI 153
COG2206 COG2206
c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms]
191-355 5.42e-49

c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms]


Pssm-ID: 225116 [Multi-domain]  Cd Length: 344  Bit Score: 169.59  E-value: 5.42e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 191 YQHSLGVAGYAGAFAGLLGFRRHDQERLVRAALLHDVGKARIPLAILNKPSSLSAEEMAVMRRHPVIGAALLARQPGFDA 270
Cdd:COG2206  150 YGHSVRVAELAEAIAKKLGLSEEKIEELALAGLLHDIGKIGIPDSILNKPGKLTEEEFEIIKKHPIYGYDILKDLPEFLE 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 271 EILDVVRHHHEMLDGSGYPDGLRGGAIGDLVRLVTICDICSALTERRPYRAPIGPAEAWAAM-DRMGQKLDRQLLAAFRP 349
Cdd:COG2206  230 SVRAVALRHHERWDGTGYPRGLKGEEIPLEARIIAVADVYDALTSDRPYKKAKSPEEALEELrKNSGGKFDPKVVDAFLK 309

                 ....*.
gi 220927203 350 VAMGLA 355
Cdd:COG2206  310 ALSKYP 315
PRK12705 PRK12705
hypothetical protein; Provisional
190-281 7.61e-09

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 55.49  E-value: 7.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 190 VYQHSLGVAGYAGAFAGLLGFrrhDQERLVRAALLHDVGKAriplailnkpsslsaEEMAVMRRHPVIGAaLLARQPGFD 269
Cdd:PRK12705 324 VLSHSLEVAHLAGIIAAEIGL---DPALAKRAGLLHDIGKS---------------IDRESDGNHVEIGA-ELARKFNEP 384
                         90
                 ....*....|..
gi 220927203 270 AEILDVVRHHHE 281
Cdd:PRK12705 385 DEVINAIASHHN 396
RNase_Y TIGR03319
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from ...
190-281 2.91e-05

ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from Bacillus subtilis, YmdA, has been shown to be involved in turnover of yitJ riboswitch [Transcription, Degradation of RNA].


Pssm-ID: 188306 [Multi-domain]  Cd Length: 514  Bit Score: 44.53  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203  190 VYQHSLGVAGYAGAFAGLLGFrrhDQERLVRAALLHDVGKAriplailnkpssLSAEemaVMRRHPVIGAAlLARQPGFD 269
Cdd:TIGR03319 330 VLQHSIEVAHLAGIMAAELGE---DVKLAKRAGLLHDIGKA------------VDHE---VEGSHVEIGAE-LAKKYKES 390
                          90
                  ....*....|..
gi 220927203  270 AEILDVVRHHHE 281
Cdd:TIGR03319 391 PEVVNAIAAHHG 402
 
Name Accession Description Interval E-value
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
189-328 1.88e-22

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032  Cd Length: 145  Bit Score: 91.25  E-value: 1.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 189 GVYQHSLGVAGYAGAFAGLLGFRRHDQERLVRAALLHDVGKARIPLAILNkpsslsaEEMAVMRRHPVIGAALLARQPG- 267
Cdd:cd00077    2 HRFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITE-------EESELEKDHAIVGAEILRELLLe 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 220927203 268 -----FDAEILDVVRHHHEMLDGSGYPDGLRGGAIGDLVRLVTICDICSALT-ERRPYRAPIGPAEA 328
Cdd:cd00077   75 eviklIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrDSREKRRRIAEEDL 141
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic ...
190-320 2.05e-15

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679  Cd Length: 124  Bit Score: 71.56  E-value: 2.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203   190 VYQHSLGVAGYAGAFAGLLGFrrHDQERLVRAALLHDVGKARIPLAILNKPSslsaeemaVMRRHPVIGAALLARQPGFD 269
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGL--LDIELLLLAALLHDIGKPGTPDSFLVKTS--------VLEDHHFIGAEILLEEEEPR 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 220927203   270 AEILDV---VRHHHEMLdgsgypDGLRGGAIGDLVRLVTICDICSALTERRPYR 320
Cdd:smart00471  75 ILEEILrtaILSHHERP------DGLRGEPITLEARIVKVADRLDALRADRRYR 122
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
190-313 2.83e-14

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 251000  Cd Length: 110  Bit Score: 68.03  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203  190 VYQHSLGVAGYAGAFAGLLGFRrhDQERLVRAALLHDVGKARIPLAILnkpsslsaEEMAVMRRHPVIGAALLARQPGFD 269
Cdd:pfam01966   1 VLEHSLRVALLARELAEELGEL--DRELLLLAALLHDIGKPPFGDEKP--------LLFEIFLGHAVVGAEILRELEKPL 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 220927203  270 AE--ILDVVRHHHEMldgsgyPDGLRGGAIGDLVRLVTICDICSAL 313
Cdd:pfam01966  71 GLedVLKLILEHHES------WEGLYGEPISLEARIVKLADRLDAL 110
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
241-303 4.64e-14

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 257811  Cd Length: 63  Bit Score: 66.43  E-value: 4.64e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 220927203  241 SSLSAEEMAVMRRHPVIGAALLARQPGFdAEILDVVRHHHEMLDGSGYPDGLRGGAIGDLVRL 303
Cdd:pfam13487   1 GTLTPEERAIINEHPEQTARLLEKIPRL-PPVAEIIGHHHERLDGSGYPRGLKGDEIPLGARI 62
HDIG TIGR00277
uncharacterized domain HDIG; This domain is found in a few known nucleotidyltransferes and in ...
189-282 1.50e-10

uncharacterized domain HDIG; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. For proteins scoring above the trusted cutoff, confidence is high both that the domain is present and that the model produces an essentially correct alignment. Protein regions scoring between the trusted and noise cutoffs include correctly aligned domains, homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits indications of homology.


Pssm-ID: 232902  Cd Length: 80  Bit Score: 56.95  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203  189 GVYQHSLGVAGYAGAFAGLLGFrrhDQERLVRAALLHDVGKARIPlailnkpsslsaeEMAVMRRHPVIGAAlLARQPGF 268
Cdd:TIGR00277   4 NVLQHSLEVAKLAEALARELGL---DVELARRGALLHDIGKPITR-------------EGVIFESHAVVGAE-IARKYGE 66
                          90
                  ....*....|....
gi 220927203  269 DAEILDVVRHHHEM 282
Cdd:TIGR00277  67 PLEVIDIIAEHHGK 80
HDOD pfam08668
HDOD domain;
192-281 5.21e-09

HDOD domain;


Pssm-ID: 254961  Cd Length: 196  Bit Score: 54.16  E-value: 5.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203  192 QHSLGVAGYAGAFAGLLGFrrHDQERLVRAALLHDVGK-------ARIPLAILNK-----PSSLSAEEMAVMRRHPVIGA 259
Cdd:pfam08668  97 RHSLACALAARLLARRLGL--DDPEEAFTAGLLHDIGKlillsllPDEYEEILERvaaegISLLEAERELLGTDHAEVGA 174
                          90       100
                  ....*....|....*....|..
gi 220927203  260 ALLARQpGFDAEILDVVRHHHE 281
Cdd:pfam08668 175 ALLERW-NLPEELVEAIAYHHD 195
COG1713 COG1713
Predicted HD superfamily hydrolase involved in NAD metabolism [Coenzyme metabolism]
191-304 4.56e-06

Predicted HD superfamily hydrolase involved in NAD metabolism [Coenzyme metabolism]


Pssm-ID: 224627  Cd Length: 187  Bit Score: 45.37  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 191 YQHSLGVAGYAGAFAGLLGFrrhDQERLVRAALLHDVGKARIP---LAILNKPSSLSAEEmavmRRHPVI-----GAALL 262
Cdd:COG1713   19 FEHCLGVAETAIELAEAYGL---DPEKAYLAGILHDIAKELPEqklLKIAKKYGLELDLE----RESPLLlhgkvGAYLL 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 220927203 263 ARQPGF-DAEILDVVRHH----HEM--LD-----------GSGYP--DGLRGGAIGDLVRLV 304
Cdd:COG1713   92 KEEFGIkDEEVLSAIEYHttgrKQMtlLDkilyvadkiepGRGFPgvDKIRQIALKDLNKAI 153
cas3_HD TIGR01596
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for ...
192-284 1.14e-04

CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for host defense against invasive elements such as phage. In these systems, Cas3 designates one of the core proteins shared widely by multiple types of CRISPR/Cas system. This model represents an HD-like endonuclease that occurs either separately or as the N-terminal region of Cas3, the helicase-containing CRISPR-associated protein [Mobile and extrachromosomal element functions, Other].


Pssm-ID: 233487  Cd Length: 177  Bit Score: 40.99  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203  192 QHSLGVAGYAGAFAGLLG-----FRRHDQERLVRAALLHDVGKA------RIPLAILNKPSSLSaeemavmrRHPVIGAA 260
Cdd:TIGR01596   3 EHLLDVAAVAEKLKNLRIkiadlIGKDLRELLALLALLHDIGKAspgfqaKLRKAYKRGRRKAV--------RHSVLSAA 74
                          90       100       110
                  ....*....|....*....|....*....|.
gi 220927203  261 LLAR------QPGFDAEIL-DVVRHHHEMLD 284
Cdd:TIGR01596  75 LLDAllikkgYEEEVAKLLaLAVAGHHGGLS 105
Cas3''_I cd09641
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced ...
191-284 3.00e-04

CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; HD-like nuclease, specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs; signature gene for Type I


Pssm-ID: 193608  Cd Length: 200  Bit Score: 40.34  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 191 YQHSLGVAGY----AGAFAGLLGFRRHDQERLVR-AALLHDVGKA------RIPLAILNKPSSLSAEEmavmrRHPVIGA 259
Cdd:cd09641   10 LEHLLDVAAWdaelAEEFARKLGLELGLSRELLAlAGLLHDLGKAtpafqkYLRGGKEALREGKRKEV-----RHSLLGA 84
                         90       100       110
                 ....*....|....*....|....*....|..
gi 220927203 260 ALL---ARQPGFDAE----ILDVVRHHHEMLD 284
Cdd:cd09641   85 LLLyelLKELGLDEElallLAYAIAGHHGGLP 116
Cas10_III cd09680
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short ...
218-281 4.20e-03

CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Multidomain protein with permuted HD nuclease domain, palm domain and Zn-ribbon; signature gene for type III; also known as Csm1 family


Pssm-ID: 187811 [Multi-domain]  Cd Length: 650  Bit Score: 37.69  E-value: 4.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 220927203 218 LVRAALLHDVGKArIPLAILNKPSslsaeemavmRRHPVIGAALLARQPGFDAEILDVVRHHHE 281
Cdd:cd09680    1 LALGALLHDIGKV-VQRAGLGFYS----------KTHSKFGAEFLKEFSKNKDDLGDCISYHHT 53
COG2206 COG2206
c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms]
191-355 5.42e-49

c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms]


Pssm-ID: 225116 [Multi-domain]  Cd Length: 344  Bit Score: 169.59  E-value: 5.42e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 191 YQHSLGVAGYAGAFAGLLGFRRHDQERLVRAALLHDVGKARIPLAILNKPSSLSAEEMAVMRRHPVIGAALLARQPGFDA 270
Cdd:COG2206  150 YGHSVRVAELAEAIAKKLGLSEEKIEELALAGLLHDIGKIGIPDSILNKPGKLTEEEFEIIKKHPIYGYDILKDLPEFLE 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 271 EILDVVRHHHEMLDGSGYPDGLRGGAIGDLVRLVTICDICSALTERRPYRAPIGPAEAWAAM-DRMGQKLDRQLLAAFRP 349
Cdd:COG2206  230 SVRAVALRHHERWDGTGYPRGLKGEEIPLEARIIAVADVYDALTSDRPYKKAKSPEEALEELrKNSGGKFDPKVVDAFLK 309

                 ....*.
gi 220927203 350 VAMGLA 355
Cdd:COG2206  310 ALSKYP 315
COG3437 COG3437
Response regulator containing a CheY-like receiver domain and an HD-GYP domain [Transcription ...
184-328 8.66e-36

Response regulator containing a CheY-like receiver domain and an HD-GYP domain [Transcription / Signal transduction mechanisms]


Pssm-ID: 225971 [Multi-domain]  Cd Length: 360  Bit Score: 134.02  E-value: 8.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 184 RTHEIGvyQHSLGVAGYAGAFAGLLGFRRHDQERLVRAALLHDVGKARIPLAILNKPSSLSAEEMAVMRRHPVIGAALLA 263
Cdd:COG3437  182 RDYETG--DHLERVAQYSELLAELLGLSEEEVDLIKKAAPLHDIGKVAIPDSILLKPGKLTSEEFEIMKGHPILGAEILK 259
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 220927203 264 RQPGFDAEILDVVRHHHEMLDGSGYPDGLRGGAIGDLVRLVTICDICSALTERRPYRAPIGPAEA 328
Cdd:COG3437  260 SSERLMQVAAEIARHHHERWDGSGYPDGLKGDEIPLSARIVAIADVFDALVSGRPYKEAMSTEEA 324
PRK12705 PRK12705
hypothetical protein; Provisional
190-281 7.61e-09

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 55.49  E-value: 7.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 190 VYQHSLGVAGYAGAFAGLLGFrrhDQERLVRAALLHDVGKAriplailnkpsslsaEEMAVMRRHPVIGAaLLARQPGFD 269
Cdd:PRK12705 324 VLSHSLEVAHLAGIIAAEIGL---DPALAKRAGLLHDIGKS---------------IDRESDGNHVEIGA-ELARKFNEP 384
                         90
                 ....*....|..
gi 220927203 270 AEILDVVRHHHE 281
Cdd:PRK12705 385 DEVINAIASHHN 396
RNase_Y TIGR03319
ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from ...
190-281 2.91e-05

ribonuclease Y; Members of this family are RNase Y, an endoribonuclease. The member from Bacillus subtilis, YmdA, has been shown to be involved in turnover of yitJ riboswitch [Transcription, Degradation of RNA].


Pssm-ID: 188306 [Multi-domain]  Cd Length: 514  Bit Score: 44.53  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203  190 VYQHSLGVAGYAGAFAGLLGFrrhDQERLVRAALLHDVGKAriplailnkpssLSAEemaVMRRHPVIGAAlLARQPGFD 269
Cdd:TIGR03319 330 VLQHSIEVAHLAGIMAAELGE---DVKLAKRAGLLHDIGKA------------VDHE---VEGSHVEIGAE-LAKKYKES 390
                          90
                  ....*....|..
gi 220927203  270 AEILDVVRHHHE 281
Cdd:TIGR03319 391 PEVVNAIAAHHG 402
COG1480 COG1480
Predicted membrane-associated HD superfamily hydrolase [General function prediction only]
189-280 4.71e-05

Predicted membrane-associated HD superfamily hydrolase [General function prediction only]


Pssm-ID: 224397 [Multi-domain]  Cd Length: 700  Bit Score: 43.91  E-value: 4.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 189 GVYQHSLGVAGYAGAFAGLLGfrrhDQERLVR-AALLHDVGKARIPL-------AILNKPSSLSAEEMA-VMRRHPVIGA 259
Cdd:COG1480  489 GTYQHSVMVANLAEAAAEEIG----ANSLLARvGAYYHDIGKMKRPLffienqmGGKNPHDDLSPQLSAlIIISHVKEGV 564
                         90       100
                 ....*....|....*....|.
gi 220927203 260 ALlARQPGFDAEILDVVRHHH 280
Cdd:COG1480  565 EM-AREYKLPQEIIDIIPEHH 584
PRK12704 PRK12704
phosphodiesterase; Provisional
190-281 6.71e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 190 VYQHSLGVAGYAGAFAGLLGFrrhDQERLVRAALLHDVGKAriplailnkpssLSAEemaVMRRHPVIGAAlLARQPGFD 269
Cdd:PRK12704 336 VLQHSIEVAHLAGLMAAELGL---DVKLAKRAGLLHDIGKA------------LDHE---VEGSHVEIGAE-LAKKYKES 396
                         90
                 ....*....|..
gi 220927203 270 AEILDVVRHHHE 281
Cdd:PRK12704 397 PVVINAIAAHHG 408
COG1639 COG1639
Predicted signal transduction protein [Signal transduction mechanisms]
190-281 4.68e-04

Predicted signal transduction protein [Signal transduction mechanisms]


Pssm-ID: 224554 [Multi-domain]  Cd Length: 289  Bit Score: 40.09  E-value: 4.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 190 VYQHSLGVAGYAGAFAGLLGfrRHDQERLVRAALLHDVGK----ARIP--------LAILNKPSSLSAEEMAVMRRHPVI 257
Cdd:COG1639  117 FWDTAIETAMIAEGLARALG--RADSDEAYTAGLLHNLGIlvllTDFPdhcelldyLLALNNDELLALDEELGIFGHASI 194
                         90       100
                 ....*....|....*....|....
gi 220927203 258 GAALLARQpGFDAEILDVVRHHHE 281
Cdd:COG1639  195 GAYLLRRW-NFPDDLIEAIRFHHN 217
COG1418 COG1418
Predicted HD superfamily hydrolase [General function prediction only]
190-281 9.87e-04

Predicted HD superfamily hydrolase [General function prediction only]


Pssm-ID: 224336 [Multi-domain]  Cd Length: 222  Bit Score: 38.96  E-value: 9.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203 190 VYQHSLGVAGYAGAFAGLLGFrrhDQERLVRAALLHDVGKariplAILNKPSslsaeemavmRRHPVIGAAlLARQPGFD 269
Cdd:COG1418   37 VLEHSLRVAYLAYRIAEEEGV---DPDLALRAALLHDIGK-----AIDHEPG----------GSHAEIGAE-IARKFLED 97
                         90
                 ....*....|..
gi 220927203 270 AEILDVVRHHHE 281
Cdd:COG1418   98 PVVINAIEAHHG 109
cas3_GSU0051 TIGR02621
CRISPR-associated helicase Cas3, subtype Dpsyc; This model describes a CRISPR-associated ...
159-280 3.94e-03

CRISPR-associated helicase Cas3, subtype Dpsyc; This model describes a CRISPR-associated putative DEAH-box helicase, or Cas3, of a subtype found in Actinomyces naeslundii MG1, Geobacter sulfurreducens PCA, Gemmata obscuriglobus UQM 2246, and Desulfotalea psychrophila. This protein includes both DEAH and HD motifs [Mobile and extrachromosomal element functions, Other].


Pssm-ID: 233953 [Multi-domain]  Cd Length: 862  Bit Score: 37.99  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220927203  159 DIDAGTEIVLEAIAEAGIRAWL----------DVIRTHEIGVYQ----HSLGVAGYAGAFAGLLGFRRHDQERLVRAALL 224
Cdd:TIGR02621 645 DVPPDWQEIEEELGADTGHPWWrwylveaateDPDGSKDDADEVtlcgHLDRVGERAKQWVRALGLGELLVEAVVTAARH 724
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 220927203  225 HDVGKARI-----------PLAILNKPSSLSAEEMAVMRRHP------VIGAALLARQPGFDAEILDVVRH----HH 280
Cdd:TIGR02621 725 HDLGKDDPrfqtalgarvyPPLSLAKSGRRYWNIAMSMYGHPsgwrheAASADRLPEFLELSEELADLVLHlvatHH 801
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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