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Conserved domains on  [gi|446364604|ref|WP_000442459|]
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MULTISPECIES: LamG-like jellyroll fold domain-containing protein [Bacillus cereus group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
52-306 4.66e-36

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 136.36  E-value: 4.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  52 VVSDVHI-KNSGTDDTFRWKRAIEQLNTLAPkqDAFVIVGDFTDSGSLQQYDRFMQVYNENankDAVRMNSLGNHDYWNG 130
Cdd:COG1409    5 HISDLHLgAPDGSDTAEVLAAALADINAPRP--DFVVVTGDLTDDGEPEEYAAAREILARL---GVPVYVVPGNHDIRAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 131 LSveGAQKRFLEKTGMESIYYHKVVKGYHFLVM-SPEDGTTHGYYSDKQINWLKEEMAKAqkddPEKPIFVFLHQHIKDT 209
Cdd:COG1409   80 MA--EAYREYFGDLPPGGLYYSFDYGGVRFIGLdSNVPGRSSGELGPEQLAWLEEELAAA----PAKPVIVFLHHPPYST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 210 VYGSQEWGTKDSAKFNEVLKEYPQVITFSGHSHYplddPRSIHQKDFTSVGTSSVSYmeveggkvQGTIPPGAstlsqgL 289
Cdd:COG1409  154 GSGSDRIGLRNAEELLALLARYGVDLVLSGHVHR----YERTRRDGVPYIVAGSTGG--------QVRLPPGY------R 215

                        250
                 ....*....|....*..
gi 446364604 290 LVEVDDKEVTINRRDFH 306
Cdd:COG1409  216 VIEVDGDGLTVEVRRVD 232
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 517-649 2.38e-16

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


:

Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 76.65  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  517 ANTFTLETVFSMNEI-RGQGILQNTEGGG---IGFESTGSGYVELWA-HIGGSYKRVGVQLEANKTYHLTGTYNGSEVAI 591
Cdd:pfam13385  16 TSDFTVSAWVKPDSLpGWARAIISSSGGGgysLGLDGDGRLRFAVNGgNGGWDTVTSGASVPLGQWTHVAVTYDGGTLRL 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446364604  592 YVDGKKVNSQPATGKVYHPN-VPFALGADPDSNGnggiPLNGQIALAKLYSKALSSSEV 649
Cdd:pfam13385  96 YVNGVLVGSSTLTGGPPPGTgGPLYIGRSPGGDD----YFNGLIDEVRIYDRALSAAEI 150
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 344-439 5.75e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 45.57  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 344 KLAVSNVTENAATVTFQQ-ALDNLLVHSYRVQARDKQTGEIKNkllafsefYRDPVPKDLTFTLAGLDGGKTYTLEVVAI 422
Cdd:cd00063    6 NLRVTDVTSTSVTLSWTPpEDDGGPITGYVVEYREKGSGDWKE--------VEVTPGSETSYTLTGLKPGTEYEFRVRAV 77

                         90
                 ....*....|....*..
gi 446364604 423 DSFGnESAQPLTAEITT 439
Cdd:cd00063   78 NGGG-ESPPSESVTVTT 93
PTZ00248 super family cl36533
eukaryotic translation initiation factor 2 subunit 1; Provisional
 659-818 9.08e-03

eukaryotic translation initiation factor 2 subunit 1; Provisional


The actual alignment was detected with superfamily member PTZ00248:

Pssm-ID: 240329 [Multi-domain]  Cd Length: 319  Bit Score: 39.26  E-value: 9.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 659 RTKLEQVNALFEELGKVKEVLAGTYEFGDKSGQYSKEAFQE----LEKSYNHAKQVFENVASTGEQIVQAYN---ELKTA 731
Cdd:PTZ00248  90 RVSPEDIEACEEKFSKSKKVHSIMRHIAQKHGMSVEELYTKiiwpLYKKYGHALDALKEALTNPDNVFEGLDipeEVKES 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 732 NQTFIQSKVVEQPKTLKEKLQI------NIESAKAVLKKAQ--AANVTDGSVKSLSQKITVAEAVLKDakvKDAQVETMN 803
Cdd:PTZ00248 170 LLQDIQRRLKPQPLKLRADIEVscfdyeGIDAVKEALIAGQevATDECKITIKLIAPPQYVIVTTCSD---KDKGMEIIG 246

                        170
                 ....*....|....*
gi 446364604 804 RTMEyAISLVEKSIN 818
Cdd:PTZ00248 247 AALE-AIKEVIKKKG 260
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
52-306 4.66e-36

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 136.36  E-value: 4.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  52 VVSDVHI-KNSGTDDTFRWKRAIEQLNTLAPkqDAFVIVGDFTDSGSLQQYDRFMQVYNENankDAVRMNSLGNHDYWNG 130
Cdd:COG1409    5 HISDLHLgAPDGSDTAEVLAAALADINAPRP--DFVVVTGDLTDDGEPEEYAAAREILARL---GVPVYVVPGNHDIRAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 131 LSveGAQKRFLEKTGMESIYYHKVVKGYHFLVM-SPEDGTTHGYYSDKQINWLKEEMAKAqkddPEKPIFVFLHQHIKDT 209
Cdd:COG1409   80 MA--EAYREYFGDLPPGGLYYSFDYGGVRFIGLdSNVPGRSSGELGPEQLAWLEEELAAA----PAKPVIVFLHHPPYST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 210 VYGSQEWGTKDSAKFNEVLKEYPQVITFSGHSHYplddPRSIHQKDFTSVGTSSVSYmeveggkvQGTIPPGAstlsqgL 289
Cdd:COG1409  154 GSGSDRIGLRNAEELLALLARYGVDLVLSGHVHR----YERTRRDGVPYIVAGSTGG--------QVRLPPGY------R 215

                        250
                 ....*....|....*..
gi 446364604 290 LVEVDDKEVTINRRDFH 306
Cdd:COG1409  216 VIEVDGDGLTVEVRRVD 232
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 53-246 5.49e-25

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 104.28  E-value: 5.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  53 VSDVHIKNSG--------TDDTFRwkRAIEQLNTLAPKQDAFVIVGDFTDSGSLQQYDRFMQVynenankdavrMNSL-- 122
Cdd:cd07402    4 ISDTHLFAPGegallgvdTAARLA--AAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLREL-----------LAPLpa 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 123 ------GNHDywnglSVEGAQKRFLEKT--GMESIYYHKVVKGYHFLVM-SPEDGTTHGYYSDKQINWLKEEMAKAqkdd 193
Cdd:cd07402   71 pvywipGNHD-----DRAAMREALPEPPydDNGPVQYVVDFGGWRLILLdTSVPGVHHGELSDEQLDWLEAALAEA---- 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446364604 194 PEKPIFVFLHQHIKDTVYGSQEW-GTKDSAKFNEVLKEYPQVI-TFSGHSHYPLD 246
Cdd:cd07402  142 PDRPTLIFLHHPPFPLGIPWMDAiRLRNSQALFAVLARHPQVKaILCGHIHRPIS 196
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 517-649 2.38e-16

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 76.65  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  517 ANTFTLETVFSMNEI-RGQGILQNTEGGG---IGFESTGSGYVELWA-HIGGSYKRVGVQLEANKTYHLTGTYNGSEVAI 591
Cdd:pfam13385  16 TSDFTVSAWVKPDSLpGWARAIISSSGGGgysLGLDGDGRLRFAVNGgNGGWDTVTSGASVPLGQWTHVAVTYDGGTLRL 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446364604  592 YVDGKKVNSQPATGKVYHPN-VPFALGADPDSNGnggiPLNGQIALAKLYSKALSSSEV 649
Cdd:pfam13385  96 YVNGVLVGSSTLTGGPPPGTgGPLYIGRSPGGDD----YFNGLIDEVRIYDRALSAAEI 150
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 344-439 5.75e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 45.57  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 344 KLAVSNVTENAATVTFQQ-ALDNLLVHSYRVQARDKQTGEIKNkllafsefYRDPVPKDLTFTLAGLDGGKTYTLEVVAI 422
Cdd:cd00063    6 NLRVTDVTSTSVTLSWTPpEDDGGPITGYVVEYREKGSGDWKE--------VEVTPGSETSYTLTGLKPGTEYEFRVRAV 77

                         90
                 ....*....|....*..
gi 446364604 423 DSFGnESAQPLTAEITT 439
Cdd:cd00063   78 NGGG-ESPPSESVTVTT 93
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 52-130 1.52e-05

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 44.90  E-value: 1.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446364604   52 VVSDVHIKNsGTDDTFRWKRAIEQlntlAPKQDAFVIVGDFTDSGSLqqYDRFMQVYNENANKDAVRMNsLGNHDYWNG 130
Cdd:pfam00149   5 VIGDLHLPG-QLDDLLELLKKLLE----EGKPDLVLHAGDLVDRGPP--SEEVLELLERLIKYVPVYLV-RGNHDFDYG 75
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 168-247 2.30e-05

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 46.85  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 168 GTTHGYYSDKQINWLKEEMAKAqkddPEKPIFVFLHQHIKDTvyGSQeW----GTKDSAKFNEVLKEYPQVIT-FSGHSH 242
Cdd:PRK11148 133 GVPHGELSEYQLEWLERKLADA----PERHTLVLLHHHPLPA--GCA-WldqhSLRNAHELAEVLAKFPNVKAiLCGHIH 205


                 ....*
gi 446364604 243 YPLDD 247
Cdd:PRK11148 206 QELDL 210
MJ1470 COG5306
Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type ...
 455-604 2.80e-05

Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type IV pili-like system [General function prediction only];


Pssm-ID: 444105 [Multi-domain]  Cd Length: 529  Bit Score: 47.59  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 455 VFDVNFADGTFKDNSPFGTKGDVKGNVtieYDKALKKNVMKLNGKANTfgYLPFSAAQKEKVANTFTLETVFSMNEIRGQ 534
Cdd:COG5306  139 VWHFAEAGGPPQDSTAYGNHAVGAGAS---VDGGLIGSGAQFDGTSPL--VVPASPSLALDAGGGFTFSAWIKPAQLDGN 213

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 535 GILQNTEGGGIGFEsTGSGYVElWAHIGGSYKRVGVQLEANKTYHLTGTYNGSEVAIYVDGKKVNSQPAT 604
Cdd:COG5306  214 AVLYSRRDGANGLD-NGAPFVE-VGGAGGTRSAAGAPLAAGTWHHLAVVADAGKVTLYVNGVAAGSLDAS 281
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
345-455 1.70e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 41.91  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 345 LAVSNVTENAATVTFQQALDNLlVHSYRVQaRDKQTGEIKNKLlafsefyrDPVPKDLTFTLAGLDGGKTYTLEVVAIDS 424
Cdd:COG3401  333 LTATAVGSSSITLSWTASSDAD-VTGYNVY-RSTSGGGTYTKI--------AETVTTTSYTDTGLTPGTTYYYKVTAVDA 402

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446364604 425 FGNESAQPLTAEITTKKDDIDPNVKVPKADV 455
Cdd:COG3401  403 AGNESAPSEEVSATTASAASGESLTASVDAV 433
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 345-426 3.12e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.21  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604   345 LAVSNVTENAATVTFQQALDNLLVH---SYRVQARDKQTGEIKNKllafsefyrdPVPKDLTFTLAGLDGGKTYTLEVVA 421
Cdd:smart00060   7 LRVTDVTSTSVTLSWEPPPDDGITGyivGYRVEYREEGSEWKEVN----------VTPSSTSYTLTGLKPGTEYEFRVRA 76


                   ....*
gi 446364604   422 IDSFG 426
Cdd:smart00060  77 VNGAG 81
PTZ00248 PTZ00248
eukaryotic translation initiation factor 2 subunit 1; Provisional
 659-818 9.08e-03

eukaryotic translation initiation factor 2 subunit 1; Provisional


Pssm-ID: 240329 [Multi-domain]  Cd Length: 319  Bit Score: 39.26  E-value: 9.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 659 RTKLEQVNALFEELGKVKEVLAGTYEFGDKSGQYSKEAFQE----LEKSYNHAKQVFENVASTGEQIVQAYN---ELKTA 731
Cdd:PTZ00248  90 RVSPEDIEACEEKFSKSKKVHSIMRHIAQKHGMSVEELYTKiiwpLYKKYGHALDALKEALTNPDNVFEGLDipeEVKES 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 732 NQTFIQSKVVEQPKTLKEKLQI------NIESAKAVLKKAQ--AANVTDGSVKSLSQKITVAEAVLKDakvKDAQVETMN 803
Cdd:PTZ00248 170 LLQDIQRRLKPQPLKLRADIEVscfdyeGIDAVKEALIAGQevATDECKITIKLIAPPQYVIVTTCSD---KDKGMEIIG 246

                        170
                 ....*....|....*
gi 446364604 804 RTMEyAISLVEKSIN 818
Cdd:PTZ00248 247 AALE-AIKEVIKKKG 260
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
52-306 4.66e-36

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 136.36  E-value: 4.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  52 VVSDVHI-KNSGTDDTFRWKRAIEQLNTLAPkqDAFVIVGDFTDSGSLQQYDRFMQVYNENankDAVRMNSLGNHDYWNG 130
Cdd:COG1409    5 HISDLHLgAPDGSDTAEVLAAALADINAPRP--DFVVVTGDLTDDGEPEEYAAAREILARL---GVPVYVVPGNHDIRAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 131 LSveGAQKRFLEKTGMESIYYHKVVKGYHFLVM-SPEDGTTHGYYSDKQINWLKEEMAKAqkddPEKPIFVFLHQHIKDT 209
Cdd:COG1409   80 MA--EAYREYFGDLPPGGLYYSFDYGGVRFIGLdSNVPGRSSGELGPEQLAWLEEELAAA----PAKPVIVFLHHPPYST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 210 VYGSQEWGTKDSAKFNEVLKEYPQVITFSGHSHYplddPRSIHQKDFTSVGTSSVSYmeveggkvQGTIPPGAstlsqgL 289
Cdd:COG1409  154 GSGSDRIGLRNAEELLALLARYGVDLVLSGHVHR----YERTRRDGVPYIVAGSTGG--------QVRLPPGY------R 215

                        250
                 ....*....|....*..
gi 446364604 290 LVEVDDKEVTINRRDFH 306
Cdd:COG1409  216 VIEVDGDGLTVEVRRVD 232
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 53-246 5.49e-25

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 104.28  E-value: 5.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  53 VSDVHIKNSG--------TDDTFRwkRAIEQLNTLAPKQDAFVIVGDFTDSGSLQQYDRFMQVynenankdavrMNSL-- 122
Cdd:cd07402    4 ISDTHLFAPGegallgvdTAARLA--AAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLREL-----------LAPLpa 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 123 ------GNHDywnglSVEGAQKRFLEKT--GMESIYYHKVVKGYHFLVM-SPEDGTTHGYYSDKQINWLKEEMAKAqkdd 193
Cdd:cd07402   71 pvywipGNHD-----DRAAMREALPEPPydDNGPVQYVVDFGGWRLILLdTSVPGVHHGELSDEQLDWLEAALAEA---- 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446364604 194 PEKPIFVFLHQHIKDTVYGSQEW-GTKDSAKFNEVLKEYPQVI-TFSGHSHYPLD 246
Cdd:cd07402  142 PDRPTLIFLHHPPFPLGIPWMDAiRLRNSQALFAVLARHPQVKaILCGHIHRPIS 196
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 517-649 2.38e-16

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 76.65  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  517 ANTFTLETVFSMNEI-RGQGILQNTEGGG---IGFESTGSGYVELWA-HIGGSYKRVGVQLEANKTYHLTGTYNGSEVAI 591
Cdd:pfam13385  16 TSDFTVSAWVKPDSLpGWARAIISSSGGGgysLGLDGDGRLRFAVNGgNGGWDTVTSGASVPLGQWTHVAVTYDGGTLRL 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446364604  592 YVDGKKVNSQPATGKVYHPN-VPFALGADPDSNGnggiPLNGQIALAKLYSKALSSSEV 649
Cdd:pfam13385  96 YVNGVLVGSSTLTGGPPPGTgGPLYIGRSPGGDD----YFNGLIDEVRIYDRALSAAEI 150
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 50-242 1.54e-07

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 53.84  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  50 FPVVSDVHIKNSGTDDTFRWKraIEQLNtlapKQDAFVIVGDF---TDSGSLQQYDRFMQvyneNANKDAVR---MNSLG 123
Cdd:cd00839    7 FAVFGDMGQNTNNSTNTLDHL--EKELG----NYDAIIHVGDIayaDGYNNGSRWDTFMR----QIEPLASYvpyMVAPG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 124 NH--DYWNGLSVEGAQKRFLEKTGMES-----IYYHKVVKGYHFLVMSPEDGTTHGYYSDKQINWLKEEMAKAqkDDPEK 196
Cdd:cd00839   77 NHeaDYNGSTSKIKFFMPGRGMPPSPSgstenLWYSFDVGPVHFISLSTETDFLKGDNISPQYDWLEADLAKV--DRSRT 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446364604 197 P-IFVFLHQHIkdtvYGSQEW------GTKDSAKFNEVLKEYpQV-ITFSGHSH 242
Cdd:cd00839  155 PwIIVMGHRPM----YCSNDDdadcieGEKMREALEDLFYKY-GVdLVLSGHVH 203
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 47-242 2.37e-07

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 52.28  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  47 KIVFpvVSDVHIKNSGTDDtfRWKRAIEQLNTLAPkqDAFVIVGDFTDsGSLQQYDRFMQVYNENANKD---AVrmnsLG 123
Cdd:cd07385    3 RIVQ--LSDIHLGPFVGRT--RLQKVVRKVNELNP--DLIVITGDLVD-GDVSVLRLLASPLSKLKAPLgvyFV----LG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 124 NHDYWNGLSVEgaQKRFLEKTGM-----ESIYYhKVVKGYHFLVMSPEDGTThgyysdkqinWLKEEMAKAQKD-DPEKP 197
Cdd:cd07385   72 NHDYYSGDVEV--WIAALEKAGItvlrnESVEL-SRDGATIGLAGSGVDDIG----------GHGEDLEKALKGlDENDP 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446364604 198 IFVFLHQ--HIKDTvygsqewgtkDSAKFNEVLkeypqvitfSGHSH 242
Cdd:cd07385  139 VILLAHNpdAAEEA----------QRPGVDLVL---------SGHTH 166
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
47-146 4.26e-07

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 52.10  E-value: 4.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  47 KIVFpvVSDVHIKNsgTDDTFRWKRAIEQLNTLAPkqDAFVIVGDFTDsGSLQQYDRFMQVYNENANKD---AVrmnsLG 123
Cdd:COG1408   44 RIVQ--LSDLHLGP--FIGGERLERLVEKINALKP--DLVVLTGDLVD-GSVAELEALLELLKKLKAPLgvyAV----LG 112

                         90       100
                 ....*....|....*....|...
gi 446364604 124 NHDYWNGLsveGAQKRFLEKTGM 146
Cdd:COG1408  113 NHDYYAGL---EELRAALEEAGV 132
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 50-242 9.94e-07

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 50.79  E-value: 9.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  50 FPVVSDVHIKN-------SGTDDTFR-----WKRAIEQLNTLAPKQdaFVI-VGDFtdsgslqqYDRFMQVYNENANKDA 116
Cdd:cd07396    3 FGIIADIQYADiddgknlGTRRRYYRnslgvLERAVEEWNRESNLA--FVVqLGDI--------IDGYNAKDRSKEALDA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 117 V-----RMNS-----LGNHDYWNGLSVEGAQKRflEKTGMESIYYH-KVVKGYHFLVMSPEDgtTHGYYSDKQINWLKEE 185
Cdd:cd07396   73 VlsildRLKGpvhhvLGNHEFYNFPREYLNHLK--TLNGEDAYYYSfSPGPGFRFLVLDFVK--FNGGIGEEQLAWLRNE 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 186 MAKAQKDdpEKPIFVFLHQ--HIKDTVYGSQEWgtkDSAKFNEVLKEYPQVIT-FSGHSH 242
Cdd:cd07396  149 LTSADAN--GEKVIVLSHLpiYPEAADPQCLLW---NYEEVLAILESYPCVKAcFSGHNH 203
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 344-439 5.75e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 45.57  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 344 KLAVSNVTENAATVTFQQ-ALDNLLVHSYRVQARDKQTGEIKNkllafsefYRDPVPKDLTFTLAGLDGGKTYTLEVVAI 422
Cdd:cd00063    6 NLRVTDVTSTSVTLSWTPpEDDGGPITGYVVEYREKGSGDWKE--------VEVTPGSETSYTLTGLKPGTEYEFRVRAV 77

                         90
                 ....*....|....*..
gi 446364604 423 DSFGnESAQPLTAEITT 439
Cdd:cd00063   78 NGGG-ESPPSESVTVTT 93
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 52-130 1.52e-05

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 44.90  E-value: 1.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446364604   52 VVSDVHIKNsGTDDTFRWKRAIEQlntlAPKQDAFVIVGDFTDSGSLqqYDRFMQVYNENANKDAVRMNsLGNHDYWNG 130
Cdd:pfam00149   5 VIGDLHLPG-QLDDLLELLKKLLE----EGKPDLVLHAGDLVDRGPP--SEEVLELLERLIKYVPVYLV-RGNHDFDYG 75
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 168-247 2.30e-05

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 46.85  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 168 GTTHGYYSDKQINWLKEEMAKAqkddPEKPIFVFLHQHIKDTvyGSQeW----GTKDSAKFNEVLKEYPQVIT-FSGHSH 242
Cdd:PRK11148 133 GVPHGELSEYQLEWLERKLADA----PERHTLVLLHHHPLPA--GCA-WldqhSLRNAHELAEVLAKFPNVKAiLCGHIH 205


                 ....*
gi 446364604 243 YPLDD 247
Cdd:PRK11148 206 QELDL 210
MJ1470 COG5306
Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type ...
 455-604 2.80e-05

Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type IV pili-like system [General function prediction only];


Pssm-ID: 444105 [Multi-domain]  Cd Length: 529  Bit Score: 47.59  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 455 VFDVNFADGTFKDNSPFGTKGDVKGNVtieYDKALKKNVMKLNGKANTfgYLPFSAAQKEKVANTFTLETVFSMNEIRGQ 534
Cdd:COG5306  139 VWHFAEAGGPPQDSTAYGNHAVGAGAS---VDGGLIGSGAQFDGTSPL--VVPASPSLALDAGGGFTFSAWIKPAQLDGN 213

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 535 GILQNTEGGGIGFEsTGSGYVElWAHIGGSYKRVGVQLEANKTYHLTGTYNGSEVAIYVDGKKVNSQPAT 604
Cdd:COG5306  214 AVLYSRRDGANGLD-NGAPFVE-VGGAGGTRSAAGAPLAAGTWHHLAVVADAGKVTLYVNGVAAGSLDAS 281
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
345-632 1.66e-04

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 44.76  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 345 LAVSNVTENAATVTFQQALDNLLVHSYRVqardkqtgeiknkllafsefYRD----PVPKDLT-FTLAGLDGGKTYTLEV 419
Cdd:COG3979    9 LTASNVTSSSVSLSWDASTDNVGVTGYDV--------------------YRGgdqvATVTGLTaWTVTGLTPGTEYTFTV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 420 VAIDSFGNESAQPLTAEITTKKDDIDPNVKVPKADVfDVNFADGTFKDNSPFGTKGDVKGNVTIEYDKALKKNVMKLNGK 499
Cdd:COG3979   69 GACDAAGNVSAASGTSTAMFGGSSTTLGSAEGVADT-SGNLAASGAFFGVTTPPTPSSTLVVDGTTTVNAAATANGGTGG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 500 ANTFGYLPFSAAQKEKVANTFTLETVFSMNEIRGQGILQNTEGGGIGFESTGSGYVELWAHIGGSYKRVGVQLEANKTYH 579
Cdd:COG3979  148 SGGTTTIITTGVEGGGGSKTAQSLNAITAAGTAALNGGVVGGADEVLTCSAVKDDGSGGAGAGNTYWALNTLGVSDTPSG 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446364604 580 LTGTYNGSEVAIYVDGKKVNSQPATGKVYHPNVPFALGADPDSNGNGGIPLNG 632
Cdd:COG3979  228 TTATGGTVGITSAYGAGVSGNAAVNVNAGFVVGNVGGAAGNTGTTSGTATSDA 280
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 70-242 1.16e-03

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 41.54  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  70 KRAIEQLNTLAPKQDAFVIVGDFTD-----SGSLQQYDRFMQVYNENANKDAVRMNSlGNHDYWNGLSVEGAQkRFLEKT 144
Cdd:cd07395   38 EQAVQAINKLNPKPKFVVVCGDLVHampgeEFREQQVSDLKDVLSKLDPDIPLVCVC-GNHDVGNTPTPETIQ-RYRDDF 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 145 GMEsiYYHKVVKGYHFLVMSP---EDGTTHGYYSDKQINWLKEEMAKAQKDDPeKPIFVFlhQHIKDTVYGSQEwgtkDS 221
Cdd:cd07395  116 GDD--YFSFWVGGVFFIVLNSqlfKDPSKVPELASAQDQWLEEQLQIARESDA-KHVVVF--QHIPLFLEDPDE----ED 186

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446364604 222 AKFN----------EVLKEYPQVITFSGHSH 242
Cdd:cd07395  187 DYFNipksvrrellDKFKKAGVKAVFSGHYH 217
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
345-455 1.70e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 41.91  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 345 LAVSNVTENAATVTFQQALDNLlVHSYRVQaRDKQTGEIKNKLlafsefyrDPVPKDLTFTLAGLDGGKTYTLEVVAIDS 424
Cdd:COG3401  333 LTATAVGSSSITLSWTASSDAD-VTGYNVY-RSTSGGGTYTKI--------AETVTTTSYTDTGLTPGTTYYYKVTAVDA 402

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446364604 425 FGNESAQPLTAEITTKKDDIDPNVKVPKADV 455
Cdd:COG3401  403 AGNESAPSEEVSATTASAASGESLTASVDAV 433
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 72-243 1.88e-03

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 41.13  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604  72 AIEQLNTLAPKQDaFVIV-GDFTD-------SGSLQQYDRFMQVYNENANKDAVRMNSLGNHDYW--NGLSVEG------ 135
Cdd:cd00842   59 ALEAIKKNHPKPD-FILWtGDLVRhdvdeqtPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYpvNQFPPHSnspswl 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 136 --------------AQKRFLEKTGmesiYYHKVVKG------------Y---HFLVMSPEDGtthgyysDKQINWLKEEM 186
Cdd:cd00842  138 ydalaelwkpwlptEAKETFKKGG----YYSVDVKDglrvislntnlyYkknFWLYSNNTDP-------CGQLQWLEDEL 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446364604 187 AKAQKddpeKPIFVFLHQHIKdtvYGSQEWGTKDSAKFNEVLKEYPQVIT--FSGHSHY 243
Cdd:cd00842  207 EDAEQ----KGEKVWIIGHIP---PGLNSYDADWSERFYQIINRYSDTIAgqFFGHTHR 258
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 345-426 3.12e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.21  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604   345 LAVSNVTENAATVTFQQALDNLLVH---SYRVQARDKQTGEIKNKllafsefyrdPVPKDLTFTLAGLDGGKTYTLEVVA 421
Cdd:smart00060   7 LRVTDVTSTSVTLSWEPPPDDGITGyivGYRVEYREEGSEWKEVN----------VTPSSTSYTLTGLKPGTEYEFRVRA 76


                   ....*
gi 446364604   422 IDSFG 426
Cdd:smart00060  77 VNGAG 81
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
345-441 4.78e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 40.37  E-value: 4.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 345 LAVSNVTENAATVTFQqALDNLLVHSYRVQARDKQTGEIKnkLLAFSefyrdpvpKDLTFTLAGLDGGKTYTLEVVAIDS 424
Cdd:COG3401  239 LTATADTPGSVTLSWD-PVTESDATGYRVYRSNSGDGPFT--KVATV--------TTTSYTDTGLTNGTTYYYRVTAVDA 307

                         90
                 ....*....|....*..
gi 446364604 425 FGNESAQPLTAEITTKK 441
Cdd:COG3401  308 AGNESAPSNVVSVTTDL 324
PTZ00248 PTZ00248
eukaryotic translation initiation factor 2 subunit 1; Provisional
 659-818 9.08e-03

eukaryotic translation initiation factor 2 subunit 1; Provisional


Pssm-ID: 240329 [Multi-domain]  Cd Length: 319  Bit Score: 39.26  E-value: 9.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 659 RTKLEQVNALFEELGKVKEVLAGTYEFGDKSGQYSKEAFQE----LEKSYNHAKQVFENVASTGEQIVQAYN---ELKTA 731
Cdd:PTZ00248  90 RVSPEDIEACEEKFSKSKKVHSIMRHIAQKHGMSVEELYTKiiwpLYKKYGHALDALKEALTNPDNVFEGLDipeEVKES 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446364604 732 NQTFIQSKVVEQPKTLKEKLQI------NIESAKAVLKKAQ--AANVTDGSVKSLSQKITVAEAVLKDakvKDAQVETMN 803
Cdd:PTZ00248 170 LLQDIQRRLKPQPLKLRADIEVscfdyeGIDAVKEALIAGQevATDECKITIKLIAPPQYVIVTTCSD---KDKGMEIIG 246

                        170
                 ....*....|....*
gi 446364604 804 RTMEyAISLVEKSIN 818
Cdd:PTZ00248 247 AALE-AIKEVIKKKG 260
 
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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