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Conserved domains on  [gi|15608235|ref|NP_215611|]
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phosphate starvation-inducible protein PsiH [Mycobacterium tuberculosis H37Rv]

Protein Classification

PhoH family protein( domain architecture ID 11449002)

PhoH family protein similar to Bacillus subtilis protein YlaK; contains an N-terminal PIN (PilT N terminus) domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YlaK COG1875
Predicted ribonuclease YlaK, contains NYN-type RNase and PhoH-family ATPase domains [General ...
1-426 0e+00

Predicted ribonuclease YlaK, contains NYN-type RNase and PhoH-family ATPase domains [General function prediction only];


:

Pssm-ID: 441479 [Multi-domain]  Cd Length: 441  Bit Score: 619.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   1 MTDTRTYVLDTSVLLSDPWACSRFAEHDVVVPLVVISELEA-KRHHHELGWFARQALRLFDDLRlEHGRLDQPIPVGTqG 79
Cdd:COG1875   1 MSMKKTYVLDTNVLLHDPNAIFRFEEHDVVIPMVVLEELDKfKKGMSELGRNARQASRLLDELR-AKGNLDEGVPLPN-G 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235  80 GTLHVELNHTDpAVLPAGFRTDSNDSRILSCAANLAAE--GKRVTLVSKDIPLRVKAAAVGLAADEYHAQDVVV--SGWS 155
Cdd:COG1875  79 GTLRVELNHKD-SELPAGLPLDKNDNRILAVALNLQEEypGRPVILVSKDINLRIKADALGLEAEDYRNDKVLDidLLYT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235 156 GMHELETASADIDALFADGEIDLVEARDLPCHTGIRLLG--GGSHALGRVNA-HKRVQLVR--GDREAFGLRGRSAEQRV 230
Cdd:COG1875 158 GVKELPVSDEEIDSLYEGGRIDLPELPELYPNQFVILESenPFKSALGRVDGdTAKLVLLKdlGDRSVWGIKPRNREQRF 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235 231 ALDLLLDESVGIVSLGGKAGTGKSALALCAGLEAVLERRTHRKVVVFRPLYAVGgQELGYLPGSESEKMGPWAQAVFDTL 310
Cdd:COG1875 238 ALDLLLDPDIDLVTLLGKAGTGKTLLALAAGLEQVLEEKRYRKIIVTRPTVPVG-EDIGFLPGTEEEKMAPWMQAIYDNL 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235 311 EGLASP--------AVLEEVLSRGMLEVLPLTHIRGRSLHDSFVIVDEAQSLERNVLLTVLSRLGTGSRVVLTHDIAQRD 382
Cdd:COG1875 317 EFLVSSdekkgewgRSIDELLDRGRIEIESLTFIRGRSLPNQFVIIDEAQNLTPHQVKTIITRAGEGTKIVLTGDPAQID 396
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 15608235 383 NLRVGRH-DGVAAVIEKLKGHPLFAHITLLRSERSPIAALVTEML 426
Cdd:COG1875 397 NPYLDEHsNGLTYVVERFKGWPLSGHITLTRGERSRLAELAAELL 441
 
Name Accession Description Interval E-value
YlaK COG1875
Predicted ribonuclease YlaK, contains NYN-type RNase and PhoH-family ATPase domains [General ...
1-426 0e+00

Predicted ribonuclease YlaK, contains NYN-type RNase and PhoH-family ATPase domains [General function prediction only];


Pssm-ID: 441479 [Multi-domain]  Cd Length: 441  Bit Score: 619.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   1 MTDTRTYVLDTSVLLSDPWACSRFAEHDVVVPLVVISELEA-KRHHHELGWFARQALRLFDDLRlEHGRLDQPIPVGTqG 79
Cdd:COG1875   1 MSMKKTYVLDTNVLLHDPNAIFRFEEHDVVIPMVVLEELDKfKKGMSELGRNARQASRLLDELR-AKGNLDEGVPLPN-G 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235  80 GTLHVELNHTDpAVLPAGFRTDSNDSRILSCAANLAAE--GKRVTLVSKDIPLRVKAAAVGLAADEYHAQDVVV--SGWS 155
Cdd:COG1875  79 GTLRVELNHKD-SELPAGLPLDKNDNRILAVALNLQEEypGRPVILVSKDINLRIKADALGLEAEDYRNDKVLDidLLYT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235 156 GMHELETASADIDALFADGEIDLVEARDLPCHTGIRLLG--GGSHALGRVNA-HKRVQLVR--GDREAFGLRGRSAEQRV 230
Cdd:COG1875 158 GVKELPVSDEEIDSLYEGGRIDLPELPELYPNQFVILESenPFKSALGRVDGdTAKLVLLKdlGDRSVWGIKPRNREQRF 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235 231 ALDLLLDESVGIVSLGGKAGTGKSALALCAGLEAVLERRTHRKVVVFRPLYAVGgQELGYLPGSESEKMGPWAQAVFDTL 310
Cdd:COG1875 238 ALDLLLDPDIDLVTLLGKAGTGKTLLALAAGLEQVLEEKRYRKIIVTRPTVPVG-EDIGFLPGTEEEKMAPWMQAIYDNL 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235 311 EGLASP--------AVLEEVLSRGMLEVLPLTHIRGRSLHDSFVIVDEAQSLERNVLLTVLSRLGTGSRVVLTHDIAQRD 382
Cdd:COG1875 317 EFLVSSdekkgewgRSIDELLDRGRIEIESLTFIRGRSLPNQFVIIDEAQNLTPHQVKTIITRAGEGTKIVLTGDPAQID 396
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 15608235 383 NLRVGRH-DGVAAVIEKLKGHPLFAHITLLRSERSPIAALVTEML 426
Cdd:COG1875 397 NPYLDEHsNGLTYVVERFKGWPLSGHITLTRGERSRLAELAAELL 441
PhoH pfam02562
PhoH-like protein; PhoH is a cytoplasmic protein and predicted ATPase that is induced by ...
221-427 2.58e-58

PhoH-like protein; PhoH is a cytoplasmic protein and predicted ATPase that is induced by phosphate starvation.


Pssm-ID: 460592 [Multi-domain]  Cd Length: 204  Bit Score: 190.00  E-value: 2.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   221 LRGRSAEQRVALDLLLDESvgIVSLGGKAGTGKSALALCAGLEAVLERRThRKVVVFRPlyAV-GGQELGYLPGSESEKM 299
Cdd:pfam02562   1 IKPKTLGQKRYVEAIKKND--IVFGIGPAGTGKTYLAVAMAVDALKNGKV-KRIILTRP--AVeAGEKLGFLPGDLEEKV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   300 GPWAQAVFDTLEGLASPAVLEEVLSRGMLEVLPLTHIRGRSLHDSFVIVDEAQSLERNVLLTVLSRLGTGSRVVLTHDIA 379
Cdd:pfam02562  76 DPYLRPLYDALYDMLGAEKVEKLLERGVIEVAPLAYMRGRTLNDAFIILDEAQNTTPEQMKMFLTRLGFNSKMVVTGDPT 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 15608235   380 QRDnLRVGRHDGVAAVIEKLKGHPL--FAHITLLRSERSPIAALVTEMLE 427
Cdd:pfam02562 156 QID-LPKGQKSGLVEALEILKGVEGigFIDFTLKDVVRHPLVQRIVDAYE 204
PIN_VapC_PhoHL-ATPase cd09883
VapC-like PIN domain of bacterial Smg6-like proteins with C-terminal PhoH-like ATPase domains; ...
5-150 3.55e-52

VapC-like PIN domain of bacterial Smg6-like proteins with C-terminal PhoH-like ATPase domains; PIN (PilT N terminus) domain of Smg6-like bacterial proteins with C-terminal PhoH-like ATPase domains and other similar homologs are included in this family. Eukaryotic Smg5 and Smg6 nucleases are essential factors in nonsense-mediated mRNA decay (NMD), a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. PIN domains within this subgroup contain four highly conserved acidic residues (putative metal-binding, active site residues). Many of the bacterial homologs in this group have an N-terminal PIN domain and a C-terminal PhoH-like ATPase domain and are predicted to be ATPases which are induced by phosphate starvation.


Pssm-ID: 350231  Cd Length: 146  Bit Score: 171.96  E-value: 3.55e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   5 RTYVLDTSVLLSDPWACSRFAEHDVVVPLVVISELEA-KRHHHELGWFARQALRLFDDLRlEHGRLDQPIPvGTQGGTLH 83
Cdd:cd09883   2 KTYVLDTNVLLHDPNAIFKFEDNDVVIPITVLEELDKlKKRNDELGRNAREAIRNLDELR-EKGSLAEGVP-LENGGTLR 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15608235  84 VELNHTDPAVLPaGFRTDSNDSRILSCAANLAAEGKR-VTLVSKDIPLRVKAAAVGLAADEYHAQDVV 150
Cdd:cd09883  80 VELNHKDLLPLP-ELDLDKNDNRILAVALKLKEEGDRpVILVTKDINLRIKADALGIKAEDYETDKVS 146
PRK10536 PRK10536
phosphate starvation-inducible protein PhoH;
247-400 3.19e-17

phosphate starvation-inducible protein PhoH;


Pssm-ID: 182529  Cd Length: 262  Bit Score: 80.98  E-value: 3.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235  247 GKAGTGKSALALCAGLEAVLERRTHRkVVVFRPLYAVGgQELGYLPGSESEKMGPWAQAVFDTLEGLASPAVLEEVLSR- 325
Cdd:PRK10536  81 GEAGCGKTWISAAKAAEALIHKDVDR-IIVTRPVLQAD-EDLGFLPGDIAEKFAPYFRPVYDVLVRRLGASFMQYCLRPe 158
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15608235  326 -GMLEVLPLTHIRGRSLHDSFVIVDEAQSLERNVLLTVLSRLGTGSRVVLTHDIAQRDnLRVGRHDGVAAVIEKLK 400
Cdd:PRK10536 159 iGKVEIAPFAYMRGRTFENAVVILDEAQNVTAAQMKMFLTRLGENVTVIVNGDITQCD-LPRGVKSGLSDALERFE 233
PINc smart00670
Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, ...
6-132 1.05e-08

Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, these domains are predicted to be RNases. PINc domains in nematode SMG-5 and yeast NMD4p are predicted to be involved in RNAi.


Pssm-ID: 214771 [Multi-domain]  Cd Length: 111  Bit Score: 52.81  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235      6 TYVLDTSVLLSDP--WACSRFAE--HDVVVPLVVISELEakrhhhelgWFARQALRLFDDL-RLEHGRLDQPIPVGTQgg 80
Cdd:smart00670   2 KVVLDTNVLIDGLirDALEKLLEkkGEVYIPQTVLEELE---------YLALRSLKKLEELaLEGKIILKVLKEERIE-- 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 15608235     81 tlHVELNHTDPAVLpagfrTDSNDSRILSCAANLaaegKRVTLVSKDIPLRV 132
Cdd:smart00670  71 --EEILERLSLKLE-----LLPNDALILATAKEL----GNVVLVTNDRDLRR 111
 
Name Accession Description Interval E-value
YlaK COG1875
Predicted ribonuclease YlaK, contains NYN-type RNase and PhoH-family ATPase domains [General ...
1-426 0e+00

Predicted ribonuclease YlaK, contains NYN-type RNase and PhoH-family ATPase domains [General function prediction only];


Pssm-ID: 441479 [Multi-domain]  Cd Length: 441  Bit Score: 619.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   1 MTDTRTYVLDTSVLLSDPWACSRFAEHDVVVPLVVISELEA-KRHHHELGWFARQALRLFDDLRlEHGRLDQPIPVGTqG 79
Cdd:COG1875   1 MSMKKTYVLDTNVLLHDPNAIFRFEEHDVVIPMVVLEELDKfKKGMSELGRNARQASRLLDELR-AKGNLDEGVPLPN-G 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235  80 GTLHVELNHTDpAVLPAGFRTDSNDSRILSCAANLAAE--GKRVTLVSKDIPLRVKAAAVGLAADEYHAQDVVV--SGWS 155
Cdd:COG1875  79 GTLRVELNHKD-SELPAGLPLDKNDNRILAVALNLQEEypGRPVILVSKDINLRIKADALGLEAEDYRNDKVLDidLLYT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235 156 GMHELETASADIDALFADGEIDLVEARDLPCHTGIRLLG--GGSHALGRVNA-HKRVQLVR--GDREAFGLRGRSAEQRV 230
Cdd:COG1875 158 GVKELPVSDEEIDSLYEGGRIDLPELPELYPNQFVILESenPFKSALGRVDGdTAKLVLLKdlGDRSVWGIKPRNREQRF 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235 231 ALDLLLDESVGIVSLGGKAGTGKSALALCAGLEAVLERRTHRKVVVFRPLYAVGgQELGYLPGSESEKMGPWAQAVFDTL 310
Cdd:COG1875 238 ALDLLLDPDIDLVTLLGKAGTGKTLLALAAGLEQVLEEKRYRKIIVTRPTVPVG-EDIGFLPGTEEEKMAPWMQAIYDNL 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235 311 EGLASP--------AVLEEVLSRGMLEVLPLTHIRGRSLHDSFVIVDEAQSLERNVLLTVLSRLGTGSRVVLTHDIAQRD 382
Cdd:COG1875 317 EFLVSSdekkgewgRSIDELLDRGRIEIESLTFIRGRSLPNQFVIIDEAQNLTPHQVKTIITRAGEGTKIVLTGDPAQID 396
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 15608235 383 NLRVGRH-DGVAAVIEKLKGHPLFAHITLLRSERSPIAALVTEML 426
Cdd:COG1875 397 NPYLDEHsNGLTYVVERFKGWPLSGHITLTRGERSRLAELAAELL 441
PhoH pfam02562
PhoH-like protein; PhoH is a cytoplasmic protein and predicted ATPase that is induced by ...
221-427 2.58e-58

PhoH-like protein; PhoH is a cytoplasmic protein and predicted ATPase that is induced by phosphate starvation.


Pssm-ID: 460592 [Multi-domain]  Cd Length: 204  Bit Score: 190.00  E-value: 2.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   221 LRGRSAEQRVALDLLLDESvgIVSLGGKAGTGKSALALCAGLEAVLERRThRKVVVFRPlyAV-GGQELGYLPGSESEKM 299
Cdd:pfam02562   1 IKPKTLGQKRYVEAIKKND--IVFGIGPAGTGKTYLAVAMAVDALKNGKV-KRIILTRP--AVeAGEKLGFLPGDLEEKV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   300 GPWAQAVFDTLEGLASPAVLEEVLSRGMLEVLPLTHIRGRSLHDSFVIVDEAQSLERNVLLTVLSRLGTGSRVVLTHDIA 379
Cdd:pfam02562  76 DPYLRPLYDALYDMLGAEKVEKLLERGVIEVAPLAYMRGRTLNDAFIILDEAQNTTPEQMKMFLTRLGFNSKMVVTGDPT 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 15608235   380 QRDnLRVGRHDGVAAVIEKLKGHPL--FAHITLLRSERSPIAALVTEMLE 427
Cdd:pfam02562 156 QID-LPKGQKSGLVEALEILKGVEGigFIDFTLKDVVRHPLVQRIVDAYE 204
PIN_VapC_PhoHL-ATPase cd09883
VapC-like PIN domain of bacterial Smg6-like proteins with C-terminal PhoH-like ATPase domains; ...
5-150 3.55e-52

VapC-like PIN domain of bacterial Smg6-like proteins with C-terminal PhoH-like ATPase domains; PIN (PilT N terminus) domain of Smg6-like bacterial proteins with C-terminal PhoH-like ATPase domains and other similar homologs are included in this family. Eukaryotic Smg5 and Smg6 nucleases are essential factors in nonsense-mediated mRNA decay (NMD), a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. PIN domains within this subgroup contain four highly conserved acidic residues (putative metal-binding, active site residues). Many of the bacterial homologs in this group have an N-terminal PIN domain and a C-terminal PhoH-like ATPase domain and are predicted to be ATPases which are induced by phosphate starvation.


Pssm-ID: 350231  Cd Length: 146  Bit Score: 171.96  E-value: 3.55e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   5 RTYVLDTSVLLSDPWACSRFAEHDVVVPLVVISELEA-KRHHHELGWFARQALRLFDDLRlEHGRLDQPIPvGTQGGTLH 83
Cdd:cd09883   2 KTYVLDTNVLLHDPNAIFKFEDNDVVIPITVLEELDKlKKRNDELGRNAREAIRNLDELR-EKGSLAEGVP-LENGGTLR 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15608235  84 VELNHTDPAVLPaGFRTDSNDSRILSCAANLAAEGKR-VTLVSKDIPLRVKAAAVGLAADEYHAQDVV 150
Cdd:cd09883  80 VELNHKDLLPLP-ELDLDKNDNRILAVALKLKEEGDRpVILVTKDINLRIKADALGIKAEDYETDKVS 146
PIN_4 pfam13638
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from ...
7-145 7.97e-32

PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).


Pssm-ID: 433369  Cd Length: 131  Bit Score: 117.72  E-value: 7.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235     7 YVLDTSVLLSDPWACSRFA-EHDVVVPLVVISELEAKRHHH-----ELGWFARQALRLFDD-LRLEHGRLdqpipvgtQG 79
Cdd:pfam13638   1 YVLDTNVLLHDPDALFNFGeENDVVIPITVLEELDGLKKGSdesgrELARLARQANRWLDElLENNGGRL--------RG 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15608235    80 GTLHVELNHTDpavlpagfrTDSNDSRILSCAANLAAE--GKRVTLVSKDIPLRVKAAAVGLAADEYH 145
Cdd:pfam13638  73 QTLDERLPPDP---------FDKNDNRILAVALYLKEElpDRPVILVSKDINLRIKADALGIPAEDYE 131
PhoH COG1702
Phosphate starvation-inducible protein PhoH, predicted ATPase [Signal transduction mechanisms]; ...
221-408 9.52e-20

Phosphate starvation-inducible protein PhoH, predicted ATPase [Signal transduction mechanisms];


Pssm-ID: 441308 [Multi-domain]  Cd Length: 325  Bit Score: 89.35  E-value: 9.52e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235 221 LRGRSAEQRVALDLLLDESV--GIvslgGKAGTGKSALALCAGLEAvLERRTHRKVVVFRPlyAV-GGQELGYLPGSESE 297
Cdd:COG1702 111 IRPKTPGQKRYVDAIRKNDIvfGI----GPAGTGKTYLAVAMAVAA-LKRGEVKRIILTRP--AVeAGEKLGFLPGDLKE 183
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235 298 KMGPWAQAVFDTLEGLASPAVLEEVLSRGMLEVLPLTHIRGRSLHDSFVIVDEAQslerNVllTV------LSRLGTGSR 371
Cdd:COG1702 184 KVDPYLRPLYDALYDMLGPEKVERLIERGVIEIAPLAYMRGRTLNDAFVILDEAQ----NT--TPeqmkmfLTRLGFGSK 257
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15608235 372 VVLTHDIAQRDnLRVGRHDGVAAVIEKLKG----------------HPLFAHI 408
Cdd:COG1702 258 MVITGDITQID-LPRGQKSGLVEALEILKGvegiafvyftskdvvrHPLVQRI 309
PRK10536 PRK10536
phosphate starvation-inducible protein PhoH;
247-400 3.19e-17

phosphate starvation-inducible protein PhoH;


Pssm-ID: 182529  Cd Length: 262  Bit Score: 80.98  E-value: 3.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235  247 GKAGTGKSALALCAGLEAVLERRTHRkVVVFRPLYAVGgQELGYLPGSESEKMGPWAQAVFDTLEGLASPAVLEEVLSR- 325
Cdd:PRK10536  81 GEAGCGKTWISAAKAAEALIHKDVDR-IIVTRPVLQAD-EDLGFLPGDIAEKFAPYFRPVYDVLVRRLGASFMQYCLRPe 158
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15608235  326 -GMLEVLPLTHIRGRSLHDSFVIVDEAQSLERNVLLTVLSRLGTGSRVVLTHDIAQRDnLRVGRHDGVAAVIEKLK 400
Cdd:PRK10536 159 iGKVEIAPFAYMRGRTFENAVVILDEAQNVTAAQMKMFLTRLGENVTVIVNGDITQCD-LPRGVKSGLSDALERFE 233
PIN_Smg5-6-like cd09880
VapC-like PIN domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and related ...
8-146 4.04e-16

VapC-like PIN domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and related proteins; PIN (PilT N terminus) domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and homologs are included in this family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo. Many of the bacterial homologs in this group have an N-terminal PIN domain and a C-terminal PhoH-like ATPase domain.


Pssm-ID: 350228  Cd Length: 152  Bit Score: 75.02  E-value: 4.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   8 VLDTSVLLSDPWACSRFAEH---DVVVPLVVISELEA-KRHHHELGWFARQALRLFDDLRLEHGRLdqpIPVGT-QGGTL 82
Cdd:cd09880   1 VFDTNILLSHLDVLKLLVESgkwTVVIPLIVITELDGlKKNPDPLGPKARSALRYIEACLKKHSRW---LRVQTsKGNYL 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608235  83 HVELNHTDPAVLPAGFRTDSNDSRILSCA-------ANLAAEGKRVTLVSKDIPLRVKAAAVGLAADEYHA 146
Cdd:cd09880  78 ADLTIRSEQLSDASELRRRNNDDRILECAlwqqkhfVDREDGDGKVVLVTNDRNLRLKARARGVEAVTVKE 148
PIN_Swt1-like cd18727
VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; ...
8-134 8.34e-13

VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; Saccharomyces cerevisiae mRNA-processing endoribonuclease Swt1p plays an important role in quality control of nuclear mRNPs in eukaryotes. Human transcriptional protein SWT1 (RNA endoribonuclease homolog, also known as HsSwt1, C1orf26, and chromosome 1 open reading frame 26) is an RNA endonuclease that participates in quality control of nuclear mRNPs and can associate with the nuclear pore complex (NPC). This subfamily belongs to the Smg5 and Smg6-like PIN domain family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo.


Pssm-ID: 350294  Cd Length: 141  Bit Score: 65.27  E-value: 8.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   8 VLDTSVLLSDPWACSRFAEHD--------VVVPLVVISELEAKRHHH---ELGWFARQALR-LFDDLRLEHGRLdqpipv 75
Cdd:cd18727   1 VLDTNVLISHLDLLKQLVEDVeklslpvvIVIPWVVLQELDGLKKSKrksSLGWLARRASTwLLEKLRSKHPRV------ 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235  76 gtqggtlHVElnHTDPAVLPAGFRTDSNDSRILSCAANLAAE-GKRVTLVSKDIPLRVKA 134
Cdd:cd18727  75 -------RGQ--ALSETLRASGDPGESNDDAILDCCLYFQEKyGAPVVLLSNDKNLCNKA 125
PINc smart00670
Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, ...
6-132 1.05e-08

Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, these domains are predicted to be RNases. PINc domains in nematode SMG-5 and yeast NMD4p are predicted to be involved in RNAi.


Pssm-ID: 214771 [Multi-domain]  Cd Length: 111  Bit Score: 52.81  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235      6 TYVLDTSVLLSDP--WACSRFAE--HDVVVPLVVISELEakrhhhelgWFARQALRLFDDL-RLEHGRLDQPIPVGTQgg 80
Cdd:smart00670   2 KVVLDTNVLIDGLirDALEKLLEkkGEVYIPQTVLEELE---------YLALRSLKKLEELaLEGKIILKVLKEERIE-- 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 15608235     81 tlHVELNHTDPAVLpagfrTDSNDSRILSCAANLaaegKRVTLVSKDIPLRV 132
Cdd:smart00670  71 --EEILERLSLKLE-----LLPNDALILATAKEL----GNVVLVTNDRDLRR 111
PIN_Smg6-like cd09885
VapC-like PIN domain of human telomerase-binding protein EST1, Smg6, and other similar ...
8-134 2.56e-05

VapC-like PIN domain of human telomerase-binding protein EST1, Smg6, and other similar eukaryotic homologs; Nonsense-mediated decay (NMD) factors, Smg5 and Smg6 are essential to the post-transcriptional regulatory pathway, NMD, which recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN (PilT N terminus) domain elicits degradation of bound mRNAs, as well as, metal ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. PIN domains within this subgroup contain four highly conserved acidic residues (putative metal-binding, active site residues) which cluster at the C-terminal end of the beta-sheet and form a negatively charged pocket near the center of the molecule. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo. Eukaryotic Smg6 PIN domains are present at the C-terminal end of the telomerase activating proteins, EST1.


Pssm-ID: 350233  Cd Length: 178  Bit Score: 44.56  E-value: 2.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235   8 VLDTSVLLSD-PW-----ACSRFAehdVVVPLVVISELE--AKR----------HHHELGWFARQALRLFDDlRLEHgRL 69
Cdd:cd09885   9 VPDTNCFIDHlELieklvESRKFT---VLVPLIVVNELDglAKGsesdsyadeaHAEEVQAKARKAVKFLEE-QFEA-RN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608235  70 DQPIPVGTQGGTL------HVELNHTDPAvlpagfrtdSNDSRILSCAANLAAEG----------------KRVTLVSKD 127
Cdd:cd09885  84 PYVRALTSKGTLLdtiafrSEDINDGDGG---------NNDDLILSCCLNLCKDKavdfmpaskdqpirlyREVVLLTDD 154

                ....*..
gi 15608235 128 IPLRVKA 134
Cdd:cd09885 155 RNLRVKA 161
 
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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