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Conserved domains on  [gi|1402805036|ref|WP_110679312|]
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MULTISPECIES: YVTN family beta-propeller repeat protein [Pseudomonas]

Protein Classification

YVTN family beta-propeller repeat protein( domain architecture ID 11498960)

YVTN (Tyr-Val-Thr-Asn) family beta-propeller repeat protein such as PQQ-dependent catabolism-associated beta-propeller repeat-containing protein, which consists of seven repeats each of the YVTN family beta-propeller repeat

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 20-329 0e+00

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


:

Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 597.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  20 LALACGHAVAATAWVSNEKDNSLSLIDLQTLEVTETLAVGQRPRGLLLSHDNKLLYICASDSDRVQVMDVATRKIIKELP 99
Cdd:TIGR03866   1 LLLAAGSAAAETAYVSNEKDNTISVIDTATLKVTRTFPVGQRPRGITFSKDGKLLYVCASDSDTIQVIDPATGEVLHTLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 100 SGKDPEQFALHPNDRWLYVSNEDDALVTVIDTVTDQVLGQIDVGIEPEGMAVSPDGKWAVNTSETTNMLHWIDTSTQTLA 179
Cdd:TIGR03866  81 SGPDPEQFALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSETTNMAHWIDTATYEIV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 180 DSTLVDQRPRFVEFSQDGSRLWASAEIGGTVTVLDVATRQVLKTLNFQIKGVHPDKVQPVGIKLSADGKYAFVALGPANH 259
Cdd:TIGR03866 161 DNTLVDARPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIPGVHPEKVQPVGIKLTKDGKTAFVALGPANR 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 260 VAVIDAKTYEVLDYLLVGRRVWQLAFSPDQRRLLATNGVSGDVSVIDTQNLKVLKSVKVGRYPWGVVVTP 329
Cdd:TIGR03866 241 VAVVDAKTYEVLDYLLVGQRVWQLAFTPDESRLLTTNGVSNDVSVIDVAALKVIKSIKVGRLPWGVVVRP 310
 
Name Accession Description Interval E-value
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 20-329 0e+00

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 597.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  20 LALACGHAVAATAWVSNEKDNSLSLIDLQTLEVTETLAVGQRPRGLLLSHDNKLLYICASDSDRVQVMDVATRKIIKELP 99
Cdd:TIGR03866   1 LLLAAGSAAAETAYVSNEKDNTISVIDTATLKVTRTFPVGQRPRGITFSKDGKLLYVCASDSDTIQVIDPATGEVLHTLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 100 SGKDPEQFALHPNDRWLYVSNEDDALVTVIDTVTDQVLGQIDVGIEPEGMAVSPDGKWAVNTSETTNMLHWIDTSTQTLA 179
Cdd:TIGR03866  81 SGPDPEQFALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSETTNMAHWIDTATYEIV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 180 DSTLVDQRPRFVEFSQDGSRLWASAEIGGTVTVLDVATRQVLKTLNFQIKGVHPDKVQPVGIKLSADGKYAFVALGPANH 259
Cdd:TIGR03866 161 DNTLVDARPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIPGVHPEKVQPVGIKLTKDGKTAFVALGPANR 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 260 VAVIDAKTYEVLDYLLVGRRVWQLAFSPDQRRLLATNGVSGDVSVIDTQNLKVLKSVKVGRYPWGVVVTP 329
Cdd:TIGR03866 241 VAVVDAKTYEVLDYLLVGQRVWQLAFTPDESRLLTTNGVSNDVSVIDVAALKVIKSIKVGRLPWGVVVRP 310
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
1-218 3.54e-37

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 133.28  E-value: 3.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036   1 MRRPLLSRALLYPSLLTGALALACGHAVAATAWVSNEKDNSLSLIDLQTLEVTETLAVGQRPRGLLLSHDNKLLYICASD 80
Cdd:COG3391     9 VAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  81 SDRVQVMDVATRKIIKELPSGKDPEQFALHPNDRWLYVSNEDDALVTVIDTVTDQVLGQIDVGIEPEGMAVSPDGKWAVN 160
Cdd:COG3391    89 SGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYV 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1402805036 161 TSETTNMLHWI----DTSTQTLADSTLVDQRPRFVEFSQDGSRLW-------ASAEIGGTVTVLDVATR 218
Cdd:COG3391   169 ANSGSNTVSVIvsviDTATGKVVATIPVGGGPVGVAVSPDGRRLYvanrgsnTSNGGSNTVSVIDLATL 237
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 108-322 2.07e-15

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 76.22  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 108 ALHPND-RWLYVSNEDDA-LVTVIDTVTDQVLGQID-VGIEPEGMAVSPDGKWAVNTSETtNMLHWIDTSTQTLADSTLV 184
Cdd:cd20718    20 AYGIWDlENLMVVVERDAgSVLVIDGSTHEVLGRIDdGGAQVHVVVFSPDGRFAYVISRD-GWLTKIDLYTLRPVASIRI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 185 DQRPRFVEFSQDGSRLWASAEIGGTVTVLDVATRQVLKTLNFqiKGVHPDKVQP---VGIKLSADGKYAFVALGPANHVA 261
Cdd:cd20718    99 GVNSRGIALSDDGKYVIAGNYEPGHVVILDADTLEPLKVIPT--TGVNDDGIIEsrvGAILETPPGPYFLVALKDAGSVW 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1402805036 262 VID---AKTYEVLDYLLVGRRVWQLAFSPDQRRLLATNGVSGDVSVIDTQNLKVLKSVKVGRYP 322
Cdd:cd20718   177 VIDysdPDGNKVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGKTP 240
Lactonase pfam10282
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ...
 50-319 3.39e-09

Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyse 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.


Pssm-ID: 431196 [Multi-domain]  Cd Length: 340  Bit Score: 57.23  E-value: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  50 LEVTETLAVGQRPRGLLLSHDNKLLYICASDSD--RVQVMDVATRK-----IIKELPSGKDPEQFALHPNDRWLYVSNED 122
Cdd:pfam10282  27 LTLLGLVAEVGNPSYLALSPDGRTLYAVNEEGDqgGVAAFRIDPDSgaltlLNQVPTGGASPCHLSVDPDGRFLFVANYH 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 123 DALVTVIDTVTDQVLGQIDVGIEPEG--------------MAV-SPDGKWAVNTSETTNMLHW--IDTSTQTLADSTLVD 185
Cdd:pfam10282 107 GGSVSVFPLDADGSLGELSQVVQHEGsgppperqesphphSVDlTPDGKFLVVPDLGTDRVRVykLDAGGGKLTPPASVQ 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 186 QR----PRFVEFSQDGSRLWASAEIGGTVTVL--DVAT-----RQVLKTLNFQIKGvhpdKVQPVGIKLSADGKYAFVAL 254
Cdd:pfam10282 187 TPpgsgPRHLAFHPNGKYAYVVNELSSTVTVFeyDPATgtfeeLQTVSTLPEGFTG----TNGAAAIRVSPDGKFLYVSN 262

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1402805036 255 GPANHVAV--IDAKTYEVldyLLVGRR----VW--QLAFSPDQRRLLATNGVSGDVSVI----DTQNLK-VLKSVKVG 319
Cdd:pfam10282 263 RGHDSIAVfaVDEAGGTL---TLVERVstegDFprDFNIDPDGKFLVVANQDSDNVTVFrrdpETGKLTlLGKDIEVP 337
 
Name Accession Description Interval E-value
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 20-329 0e+00

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 597.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  20 LALACGHAVAATAWVSNEKDNSLSLIDLQTLEVTETLAVGQRPRGLLLSHDNKLLYICASDSDRVQVMDVATRKIIKELP 99
Cdd:TIGR03866   1 LLLAAGSAAAETAYVSNEKDNTISVIDTATLKVTRTFPVGQRPRGITFSKDGKLLYVCASDSDTIQVIDPATGEVLHTLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 100 SGKDPEQFALHPNDRWLYVSNEDDALVTVIDTVTDQVLGQIDVGIEPEGMAVSPDGKWAVNTSETTNMLHWIDTSTQTLA 179
Cdd:TIGR03866  81 SGPDPEQFALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSETTNMAHWIDTATYEIV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 180 DSTLVDQRPRFVEFSQDGSRLWASAEIGGTVTVLDVATRQVLKTLNFQIKGVHPDKVQPVGIKLSADGKYAFVALGPANH 259
Cdd:TIGR03866 161 DNTLVDARPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIPGVHPEKVQPVGIKLTKDGKTAFVALGPANR 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 260 VAVIDAKTYEVLDYLLVGRRVWQLAFSPDQRRLLATNGVSGDVSVIDTQNLKVLKSVKVGRYPWGVVVTP 329
Cdd:TIGR03866 241 VAVVDAKTYEVLDYLLVGQRVWQLAFTPDESRLLTTNGVSNDVSVIDVAALKVIKSIKVGRLPWGVVVRP 310
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
1-218 3.54e-37

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 133.28  E-value: 3.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036   1 MRRPLLSRALLYPSLLTGALALACGHAVAATAWVSNEKDNSLSLIDLQTLEVTETLAVGQRPRGLLLSHDNKLLYICASD 80
Cdd:COG3391     9 VAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  81 SDRVQVMDVATRKIIKELPSGKDPEQFALHPNDRWLYVSNEDDALVTVIDTVTDQVLGQIDVGIEPEGMAVSPDGKWAVN 160
Cdd:COG3391    89 SGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYV 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1402805036 161 TSETTNMLHWI----DTSTQTLADSTLVDQRPRFVEFSQDGSRLW-------ASAEIGGTVTVLDVATR 218
Cdd:COG3391   169 ANSGSNTVSVIvsviDTATGKVVATIPVGGGPVGVAVSPDGRRLYvanrgsnTSNGGSNTVSVIDLATL 237
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
99-310 1.72e-25

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 102.08  E-value: 1.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  99 PSGKDPEQFALHPNDRWLYVSNEDDALVTVIDTVTDQVLGQIDVGIEPEGMAVSPDGKwavntsettnmlhwidtstqtl 178
Cdd:COG3391    65 AAVADADGADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGG---------------------- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 179 adstlvdqrprfvefsqdgsRLWASAEIGGTVTVLDVATRQVLKTLnfqikgvhPDKVQPVGIKLSADGKYAFVALGPAN 258
Cdd:COG3391   123 --------------------RLYVADSGNGRVSVIDTATGKVVATI--------PVGAGPHGIAVDPDGKRLYVANSGSN 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1402805036 259 HVA----VIDAKTYEVLDYLLVGRRVWQLAFSPDQRRLLATNGVSG-------DVSVIDTQNL 310
Cdd:COG3391   175 TVSvivsVIDTATGKVVATIPVGGGPVGVAVSPDGRRLYVANRGSNtsnggsnTVSVIDLATL 237
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
196-329 3.32e-25

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 101.31  E-value: 3.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 196 DGSRLWASAEIGGTVTVLDVATRQVLKTLnfqikgvhPDKVQPVGIKLSADGKYAFVALGPANHVAVIDAKTYEVLDYLL 275
Cdd:COG3391    78 DGRRLYVANSGSGRVSVIDLATGKVVATI--------PVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIP 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1402805036 276 VGRRVWQLAFSPDQRRLLATNGVSGD----VSVIDTQNLKVLKSVKVGRYPWGVVVTP 329
Cdd:COG3391   150 VGAGPHGIAVDPDGKRLYVANSGSNTvsviVSVIDTATGKVVATIPVGGGPVGVAVSP 207
WD40 COG2319
WD40 repeat [General function prediction only];
25-304 9.31e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 89.20  E-value: 9.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  25 GHAVAATAWvsnekDNSLSLIDLQTLEVTETLAVGQRP-RGLLLSHDNKLLyICASDSDRVQVMDVATRKIIKELPSGKD 103
Cdd:COG2319   132 GKTLASGSA-----DGTVRLWDLATGKLLRTLTGHSGAvTSVAFSPDGKLL-ASGSDDGTVRLWDLATGKLLRTLTGHTG 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 104 P-EQFALHPNDRWLyVSNEDDALVTVIDTVTDQVLGQIDV-GIEPEGMAVSPDGKWAVnTSETTNMLHWIDTST-QTLAD 180
Cdd:COG2319   206 AvRSVAFSPDGKLL-ASGSADGTVRLWDLATGKLLRTLTGhSGSVRSVAFSPDGRLLA-SGSADGTVRLWDLATgELLRT 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 181 STLVDQRPRFVEFSQDGSRLwASAEIGGTVTVLDVATRQVLKTLNFqikgvHPDKVQPVGIklSADGKYAFVAlGPANHV 260
Cdd:COG2319   284 LTGHSGGVNSVAFSPDGKLL-ASGSDDGTVRLWDLATGKLLRTLTG-----HTGAVRSVAF--SPDGKTLASG-SDDGTV 354

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1402805036 261 AVIDAKTYEVLDYLLV-GRRVWQLAFSPDQRRLLATngvSGDVSV 304
Cdd:COG2319   355 RLWDLATGELLRTLTGhTGAVTSVAFSPDGRTLASG---SADGTV 396
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
49-309 2.04e-19

6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 87.65  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  49 TLEVTETLAVGQRPRGLLLSHDNKLLY-ICASDSDRVQVMDVATR----KIIKELPS-GKDPEQFALHPNDRWLYVSNED 122
Cdd:COG2706    34 ELTLLGLVAALGNPSFLALSPDGRFLYaVNEVDDGGVSAFRIDPAdgtlTLLNTVSSgGASPCHLSVDPDGRFLFVANYG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 123 DALVTVIDTVTDQVLGQIDVGIEPEG---------------MAVSPDGKWAVNTSETTNMLHW--IDTSTQTLADSTLVD 185
Cdd:COG2706   114 GGSVSVFPIDADGSLGEPVQVIQHEGsgpnperqegphahsVVFDPDGRFLYVPDLGTDRIYVyrLDPATGKLPEPPEVS 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 186 QR----PRFVEFSQDGSRLWASAEIGGTVTVLDVAT-------RQVLKTLNFQIKGvhpdKVQPVGIKLSADGKYAFVAL 254
Cdd:COG2706   194 LPpgsgPRHLAFHPNGRFAYVINELDSTVSVYAYDAatgtltlIQTVSTLPEDFTG----ENWAADIHISPDGRFLYVSN 269

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1402805036 255 GPANHVAV--IDAKT--YEVLDYLLV-GRRVWQLAFSPDQRRLLATNGVSGDVSV--IDTQN 309
Cdd:COG2706   270 RGHNSIAVfaIDADGgkLTLVGHVPTgGKWPRDFAIDPDGRFLLVANQKSDNITVfrIDADT 331
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
173-329 6.84e-19

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 83.98  E-value: 6.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 173 TSTQTLADSTLVDQRPRFVEFSQDGSRLWASAEIGGTVTVLDVATRQVLKTLNFQIKGVHPDKVQPVGIKLS-ADGKYAF 251
Cdd:COG3391     4 ASSLLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAgADGRRLY 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1402805036 252 VALGPANHVAVIDAKTYEVLDYLLVGRRVWQLAFSPDQRRLLATNGVSGDVSVIDTQNLKVLKSVKVGRYPWGVVVTP 329
Cdd:COG3391    84 VANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDP 161
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
18-267 1.10e-16

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 78.52  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  18 GALALACGHAVAA--TAWVSNEKDNSLSLIDLQTLEVTE-TLAVGQRPRGLLLSHDNKlLYICASDSDRVQVMDVATRKI 94
Cdd:COG4257    14 APGSGPRDVAVDPdgAVWFTDQGGGRIGRLDPATGEFTEyPLGGGSGPHGIAVDPDGN-LWFTDNGNNRIGRIDPKTGEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  95 IK-ELPSGK-DPEQFALHPNDRwLYVSNEDDALVTVIDTVTDQVLgQIDVGIE---PEGMAVSPDGK-WAVNTSetTNML 168
Cdd:COG4257    93 TTfALPGGGsNPHGIAFDPDGN-LWFTDQGGNRIGRLDPATGEVT-EFPLPTGgagPYGIAVDPDGNlWVTDFG--ANAI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 169 HWIDTSTQTLADSTLVD--QRPRFVEFSQDGsRLWASAEIGGTVTVLDVATRQVlKTLNfqikgVHPDKVQPVGIKLSAD 246
Cdd:COG4257   169 GRIDPDTGTLTEYALPTpgAGPRGLAVDPDG-NLWVADTGSGRIGRFDPKTGTV-TEYP-----LPGGGARPYGVAVDGD 241

                         250       260
                  ....*....|....*....|.
gi 1402805036 247 GKYAFVALGPaNHVAVIDAKT 267
Cdd:COG4257   242 GRVWFAESGA-NRIVRFDPDT 261
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 108-322 2.07e-15

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 76.22  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 108 ALHPND-RWLYVSNEDDA-LVTVIDTVTDQVLGQID-VGIEPEGMAVSPDGKWAVNTSETtNMLHWIDTSTQTLADSTLV 184
Cdd:cd20718    20 AYGIWDlENLMVVVERDAgSVLVIDGSTHEVLGRIDdGGAQVHVVVFSPDGRFAYVISRD-GWLTKIDLYTLRPVASIRI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 185 DQRPRFVEFSQDGSRLWASAEIGGTVTVLDVATRQVLKTLNFqiKGVHPDKVQP---VGIKLSADGKYAFVALGPANHVA 261
Cdd:cd20718    99 GVNSRGIALSDDGKYVIAGNYEPGHVVILDADTLEPLKVIPT--TGVNDDGIIEsrvGAILETPPGPYFLVALKDAGSVW 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1402805036 262 VID---AKTYEVLDYLLVGRRVWQLAFSPDQRRLLATNGVSGDVSVIDTQNLKVLKSVKVGRYP 322
Cdd:cd20718   177 VIDysdPDGNKVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGKTP 240
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 33-240 1.33e-14

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 73.91  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  33 WVSNEKD-NSLSLIDLQTLE---VTETLAVGQRPRGLLLSHDNKLLYICASDSDRVQVMDVATRKIIKELPSGKDP--EQ 106
Cdd:cd20718   165 FLVALKDaGSVWVIDYSDPDgnkVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGKTPhpGP 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 107 FALHPNDRWLYVSNEDDALVTVIDTVTDQVLGQIDVGIEPEGMAVSPDGKWA-VNTS---ETTNMLHWIDTSTQTLADS- 181
Cdd:cd20718   245 GATWGRKGVTATPHLGEGIVTVWDLDTWKPVKYIPTPGPGRFVRTHPSSPYVwADTVfgpENADEIYVIDKETLKVVKTl 324

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 182 -TLVDQRPRFVEFSQDGSRLWASAEIGGTVTVLDVATRQVLKTlnfqIKGVHPDKVQPVG 240
Cdd:cd20718   325 iPKPGKRALHPEFTRDGKYVYVSVWDGGEVVVYDAETLELVKR----IPAETPTGIFNVG 380
WD40 COG2319
WD40 repeat [General function prediction only];
66-329 6.94e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 68.78  E-value: 6.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  66 LLSHDNKLLYICASDSDRVQVMDVATRKIIKELPSGKDPEQFALHPNDRWLYVSNEDDALVTVIDTVTDQVLGQIDVGIE 145
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 146 PEGMAVSPDGKWAVNTSETTNMLHWIDTSTQTLADSTLVDQRPRFVEFSQDGSRLwASAEIGGTVTVLDVATRQVLKTLN 225
Cdd:COG2319    81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTL-ASGSADGTVRLWDLATGKLLRTLT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 226 fqikgVHPDKVQPVGIklSADGKYAFVAlGPANHVAVIDAKTYEVLDYLLV-GRRVWQLAFSPDQRRlLATNGVSGDVSV 304
Cdd:COG2319   160 -----GHSGAVTSVAF--SPDGKLLASG-SDDGTVRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKL-LASGSADGTVRL 230

                         250       260
                  ....*....|....*....|....*.
gi 1402805036 305 IDTQNLKVLKSVKV-GRYPWGVVVTP 329
Cdd:COG2319   231 WDLATGKLLRTLTGhSGSVRSVAFSP 256
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 38-317 1.06e-12

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 68.13  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  38 KDNSLSLIDLQTLEVTETLAVGQRPRGLLLSHDNKLLYICASDSDRVQVMDVATRKIIKELP-SGKDPEQ---------F 107
Cdd:cd20718    78 RDGWLTKIDLYTLRPVASIRIGVNSRGIALSDDGKYVIAGNYEPGHVVILDADTLEPLKVIPtTGVNDDGiiesrvgaiL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 108 ALHPNDRWLyVSNEDDALVTVIDTV---TDQVLGQIDVGIEPEGMAVSPDGKWAVNTSETTNMLHWIDTSTQTLADSTLV 184
Cdd:cd20718   158 ETPPGPYFL-VALKDAGSVWVIDYSdpdGNKVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPT 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 185 DQRPRFVEFSQDGSR-LWASAEIG-GTVTVLDVATRQVLKTLNFQIKGVHPDKvqpvgiklSADGKYAFV--ALGPANH- 259
Cdd:cd20718   237 GKTPHPGPGATWGRKgVTATPHLGeGIVTVWDLDTWKPVKYIPTPGPGRFVRT--------HPSSPYVWAdtVFGPENAd 308

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1402805036 260 -VAVIDAKTYEVLDYLLV--GRRVWQLAFSPDQRRLLATNGVSGDVSVIDTQNLKVLKSVK 317
Cdd:cd20718   309 eIYVIDKETLKVVKTLIPkpGKRALHPEFTRDGKYVYVSVWDGGEVVVYDAETLELVKRIP 369
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 38-325 3.87e-12

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 66.54  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  38 KDNSLSLIDLQTLEVTETLAVGQRPRGLLLSHDNKLLYICASDSDRVQVMDVATRKIIKELPSGKDPEQF-------ALH 110
Cdd:cd20778    70 RDGGLSKVDLLTLKVVARVKQSGNSIGGAISQDGRYVAVANYDPGGVKILDADTLKVLADIPAGSKGGGQrsrvvglVDA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 111 PNDRWLYVSNEDDAlVTVID---TVTDQVLGQIDVGIEP-EGMaVSPDGKW------------AVNTSETTNMLHWIDTS 174
Cdd:cd20778   150 PGNRFIFSLMDADE-IWVLDasdPDFPVVKKFKDIGRMPyDAL-ITPDGRYyiaglfnsdgvgLLDLWKPERGVRRILLD 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 175 TQTLADSTLVDQRPRFvefsqdgsRLWASAeiGGTVTVLDVATRQVL--KTLNFQIKGVHPDKVQPVGIKLSADGKYAFV 252
Cdd:cd20778   228 YGKGEEKLPVYKMPHL--------EGWAVA--GDKAFVPAVGEHRVLvyDTNDWKFIKSIPLAGQPVFAVARPDGRYVWV 297

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1402805036 253 ALGPAN--HVAVIDAKTYEVLDYLLVGRRVWQLAFSPDQRRLLATNGVSGDVSVIDTQNLKVLKSVKVgRYPWGV 325
Cdd:cd20778   298 NFSGPDndTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNKVVVYDTRTFREIKEVPA-KKPSGI 371
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 34-269 3.07e-11

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 63.84  E-value: 3.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  34 VSNEKDNSLSLIDLQTLEV-----TETLAVGQRPR--GLLLSHDNKLlyICAS-DSDRVQVMDVA---TRKIIKELPSGK 102
Cdd:cd20778   108 VANYDPGGVKILDADTLKVladipAGSKGGGQRSRvvGLVDAPGNRF--IFSLmDADEIWVLDASdpdFPVVKKFKDIGR 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 103 DPEQFALHPNDRWlYVS---NEDDalVTVIDTVTDQVLGQIDVGIEPEGMAVSPDGK------WAVNTSET------TNM 167
Cdd:cd20778   186 MPYDALITPDGRY-YIAglfNSDG--VGLLDLWKPERGVRRILLDYGKGEEKLPVYKmphlegWAVAGDKAfvpavgEHR 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 168 LHWIDTSTQTLADSTLVDQRPRFVEFSQDGSRLWA--SAEIGGTVTVLDVATRQVLKTLNFQIKGVHPDkvqpvgikLSA 245
Cdd:cd20778   263 VLVYDTNDWKFIKSIPLAGQPVFAVARPDGRYVWVnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHME--------FTP 334

                         250       260
                  ....*....|....*....|....
gi 1402805036 246 DGKYAFVALGPANHVAVIDAKTYE 269
Cdd:cd20778   335 RGEAVYISVNDDNKVVVYDTRTFR 358
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
26-218 5.47e-11

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 61.96  E-value: 5.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  26 HAVAATA----WVSNEKDNSLSLIDLQTLEVTETL--AVGQRPRGLLLSHDNKLlYICASDSDRVQVMDVATRKIIK-EL 98
Cdd:COG4257    62 HGIAVDPdgnlWFTDNGNNRIGRIDPKTGEITTFAlpGGGSNPHGIAFDPDGNL-WFTDQGGNRIGRLDPATGEVTEfPL 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  99 PS-GKDPEQFALHPNDRWLYVSNEDDALVTvIDTVTdqvlGQIDV------GIEPEGMAVSPDGK-WAVNTseTTNMLHW 170
Cdd:COG4257   141 PTgGAGPYGIAVDPDGNLWVTDFGANAIGR-IDPDT----GTLTEyalptpGAGPRGLAVDPDGNlWVADT--GSGRIGR 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1402805036 171 IDTSTQTLADSTLVD--QRPRFVEFSQDGsRLWASAEIGGTVTVLDVATR 218
Cdd:COG4257   214 FDPKTGTVTEYPLPGggARPYGVAVDGDG-RVWFAESGANRIVRFDPDTE 262
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 287-328 8.67e-11

40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in up to 14 copies per protein. Archaea Methanosarcina mazei and Methanosarcina acetivorans each have over 10 genes that encode tandem copies of this repeat, which is also found in other species. PSIPRED predicts with high confidence that each 40-residue repeats contains four beta strands. This model overlaps somewhat with the NHL repeat (pfam01436) and also shows sequence similarity to the WD domain, G-beta repeat (pfam00400).


Pssm-ID: 213697 [Multi-domain]  Cd Length: 42  Bit Score: 56.15  E-value: 8.67e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1402805036 287 PDQRRLLATNGVSGDVSVIDTQNLKVLKSVKVGRYPWGVVVT 328
Cdd:TIGR02276   1 PDGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
8prop_hemeD1_cyt_cd1-like cd20783
eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt ...
 110-322 3.64e-10

eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.


Pssm-ID: 467727 [Multi-domain]  Cd Length: 388  Bit Score: 60.48  E-value: 3.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 110 HPNDRWLYVSNEDDALVTVIDTVTDQVLGQIDVGIEPEGMAVSP-DGKWAVNTSETtNMLHWIDTSTQTLADSTLVDQRP 188
Cdd:cd20783    24 GNVDNLLLVTEREARSIAVIDGDTHTLLGHIEAGYRAHGYTFSPtDGRWAYNLGRD-GWLYKIDLYSLQPVAKVRVGLDA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 189 RFVEFSQDGSRLWASAEIGGTVTVLDVATRQVLKTLNFQ---------------IKGVHPDKVQPvgiklsadgkYAFVA 253
Cdd:cd20783   103 RGIAISDDGKYLIAGNYIPATAVILDAKTLEPLKVIDTSgvdpdgkmvdsrvasVNDVAPDLVGP----------YFLLA 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1402805036 254 LGPANHVAVIDaktYEVLDYLL-----VGRRVWQLAFSPDQRRLLATNGVSGDVSVIDTQNLKVLKSVKVGRYP 322
Cdd:cd20783   173 LKEAGQVWRID---YSKPDFPItkvenVGHILHDGFLSPDNKTFYLASQTDNWMAAIDVATMKIVAKIPTGDKP 243
8prop_hemeD1_cyt_cd1-like cd20785
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and ...
 78-322 4.86e-10

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.


Pssm-ID: 467729 [Multi-domain]  Cd Length: 412  Bit Score: 60.00  E-value: 4.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  78 ASDSDRVQVMDVATRKIIKELPSGKDPEQFALHP-NDRWLYVSNeDDALVTVIDTVTDQVLGQIDVGIEPEGMAVSPDGK 156
Cdd:cd20785    52 RGKGSKVVFFDGKTNRKVGEIPTGFAPHIMDFHPvNPRWAYVKT-DTGEVYKIDLYSMQAVRSVKAGLNGPSLAVSRDGK 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 157 WavntsettnmlhwidtstqtladstlvdqrprfvefsqdgsrLWASAEIGGTVTVLDVATRQVLKTlnFQIKGVHPDkv 236
Cdd:cd20785   131 Y------------------------------------------LAAGSFVPHTAVILDADTLEPLKY--FELEGVDPD-- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 237 qpvGIKLSADG---------KYAFVALGPANHVAVIDAKT--YEVLDYLLVGRRVWQLAFSPDQRRLLATNGVSGDVSVI 305
Cdd:cd20785   165 ---GKMVESDSgmitgtpyaNYFAIALEQAGQVWIVDLDKpgMPVTKIKNVGRHLHDAFLSPDGRYLMVASYDDNKNAVI 241

                         250
                  ....*....|....*..
gi 1402805036 306 DTQNLKVLKSVKVGRYP 322
Cdd:cd20785   242 DLKEKKVVKKIPAGCQP 258
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
31-215 1.36e-09

6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 58.38  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  31 TAWVSNEKDNSLSLIDL----------QTLEVTETLAVGQRPRG-----LLLSHDNKLLYICASDSDRVQV--MDVATRK 93
Cdd:COG2706   106 FLFVANYGGGSVSVFPIdadgslgepvQVIQHEGSGPNPERQEGphahsVVFDPDGRFLYVPDLGTDRIYVyrLDPATGK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  94 IIK----ELPSGKDPEQFALHPNDRWLYVSNEDDALVTVID-TVTDQVLGQID-VGIEPEG---------MAVSPDGKWA 158
Cdd:COG2706   186 LPEppevSLPPGSGPRHLAFHPNGRFAYVINELDSTVSVYAyDAATGTLTLIQtVSTLPEDftgenwaadIHISPDGRFL 265

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1402805036 159 VNTSETTNMLHW--IDTSTQTLadsTLVDQR------PRFVEFSQDGSRLWASAEIGGTVTVLDV 215
Cdd:COG2706   266 YVSNRGHNSIAVfaIDADGGKL---TLVGHVptggkwPRDFAIDPDGRFLLVANQKSDNITVFRI 327
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 73-325 1.71e-09

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 58.50  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  73 LLYICASDSDRVQVMDVATRKIIKELP-SGKDPEQFALHPNDRWLYVSNeDDALVTVIDTVTDQVLGQIDVGIEPEGMAV 151
Cdd:cd20718    29 LMVVVERDAGSVLVIDGSTHEVLGRIDdGGAQVHVVVFSPDGRFAYVIS-RDGWLTKIDLYTLRPVASIRIGVNSRGIAL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 152 SPDGKWAVNTSETTNMLHWIDTST-QTLADSTLVDQRPRFVEFSQDG--------SRLWASAEIGGTVTVLDVATRQVLK 222
Cdd:cd20718   108 SDDGKYVIAGNYEPGHVVILDADTlEPLKVIPTTGVNDDGIIESRVGailetppgPYFLVALKDAGSVWVIDYSDPDGNK 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 223 TLNF-QIKGVHPDKvqpvgiKLSADGKYAFVALGPANHVAVIDAKTYEVLDYL------------LVGRR---------- 279
Cdd:cd20718   188 VTDIgNIGRPLHDA------FLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIptgktphpgpgaTWGRKgvtatphlge 261

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1402805036 280 ----VWQLA--------------FSPDQR---RLLATNGV-----SGDVSVIDTQNLKVLKSVKVGRYPWGV 325
Cdd:cd20718   262 givtVWDLDtwkpvkyiptpgpgRFVRTHpssPYVWADTVfgpenADEIYVIDKETLKVVKTLIPKPGKRAL 333
Lactonase pfam10282
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ...
 50-319 3.39e-09

Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyse 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.


Pssm-ID: 431196 [Multi-domain]  Cd Length: 340  Bit Score: 57.23  E-value: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  50 LEVTETLAVGQRPRGLLLSHDNKLLYICASDSD--RVQVMDVATRK-----IIKELPSGKDPEQFALHPNDRWLYVSNED 122
Cdd:pfam10282  27 LTLLGLVAEVGNPSYLALSPDGRTLYAVNEEGDqgGVAAFRIDPDSgaltlLNQVPTGGASPCHLSVDPDGRFLFVANYH 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 123 DALVTVIDTVTDQVLGQIDVGIEPEG--------------MAV-SPDGKWAVNTSETTNMLHW--IDTSTQTLADSTLVD 185
Cdd:pfam10282 107 GGSVSVFPLDADGSLGELSQVVQHEGsgppperqesphphSVDlTPDGKFLVVPDLGTDRVRVykLDAGGGKLTPPASVQ 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 186 QR----PRFVEFSQDGSRLWASAEIGGTVTVL--DVAT-----RQVLKTLNFQIKGvhpdKVQPVGIKLSADGKYAFVAL 254
Cdd:pfam10282 187 TPpgsgPRHLAFHPNGKYAYVVNELSSTVTVFeyDPATgtfeeLQTVSTLPEGFTG----TNGAAAIRVSPDGKFLYVSN 262

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1402805036 255 GPANHVAV--IDAKTYEVldyLLVGRR----VW--QLAFSPDQRRLLATNGVSGDVSVI----DTQNLK-VLKSVKVG 319
Cdd:pfam10282 263 RGHDSIAVfaVDEAGGTL---TLVERVstegDFprDFNIDPDGKFLVVANQDSDNVTVFrrdpETGKLTlLGKDIEVP 337
8prop_hemeD1_cyt_cd1-like cd20785
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and ...
 44-223 5.78e-09

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.


Pssm-ID: 467729 [Multi-domain]  Cd Length: 412  Bit Score: 56.92  E-value: 5.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  44 LIDLQT--LEVTETLAVGQRPRGLLLSHDNKLLYICASDSDRVQVMDVATRKIIKELPSGKDPE--QFALHPND-RWLYV 118
Cdd:cd20785   196 IVDLDKpgMPVTKIKNVGRHLHDAFLSPDGRYLMVASYDDNKNAVIDLKEKKVVKKIPAGCQPHlgSGAVVKVGgRLLGF 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 119 -----SNEDDALVTVIDTVTDQVLGQIDVGIEPEGMAVSPDGKWA----VNTSETTNMLHWIDTSTQTLADSTLVDQRPR 189
Cdd:cd20785   276 gtnigSCDDKTVVTVWDMDTFEVVKQIPVSGPTESPAAHPNAPYVavdiVGKDPRARKIQLIDKNTLEVVKTLDVGGHSH 355

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1402805036 190 FVEFSQDGSRLWASAEI-GGTVTVLDVATRQVLKT 223
Cdd:cd20785   356 FPEYTADGDYLYVSAGYnGDRLVIYDSKTLKKVKE 390
8prop_hemeD1_cyt_cd1-like cd20783
eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt ...
 52-271 2.88e-08

eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.


Pssm-ID: 467727 [Multi-domain]  Cd Length: 388  Bit Score: 54.70  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  52 VTETLAVGQRPRGLLLSHDNKLLYICASDSDRVQVMDVATRKIIKELPSGKDPeqfalHPN-------DRWLYVS--NED 122
Cdd:cd20783   191 ITKVENVGHILHDGFLSPDNKTFYLASQTDNWMAAIDVATMKIVAKIPTGDKP-----HPGsgavweaDGKEYAAtvHAG 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 123 DALVTVIDTVTDQVLGQIDvgiepegmavspdgkwavntsettnmlhwidTSTQTLadstlvdqrprFVEFSQDGSRLWA 202
Cdd:cd20783   266 EGKVTIWDLDTNEIVGEVP-------------------------------TSGPGL-----------FIRTTENMPYVWA 303

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1402805036 203 SAEIGG---TVTVLDVATR-QVLKTLNFQIKGVHPDkvqpvgikLSADGKYAFVALGPANHVAVIDAKTYEVL 271
Cdd:cd20783   304 DSMFAPepnEITVHEKAPPfKVVKRITDGTRTLHPE--------PTADGKYVYVSDWDGNVVRVYDAETLELV 368
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
89-329 3.45e-08

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 53.87  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  89 VATRKIIKELP---SGKDPEQFALHPNDRwLYVSNEDDALVTVIDTVTDQVLG-QIDVGIEPEGMAVSPDGK-WAvnTSE 163
Cdd:COG4257     1 AASAVDITEYPvpaPGSGPRDVAVDPDGA-VWFTDQGGGRIGRLDPATGEFTEyPLGGGSGPHGIAVDPDGNlWF--TDN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 164 TTNMLHWIDTST---QTLADSTLVDQrPRFVEFSQDGsRLWASAEIGGTVTVLDVATRQVLKTlnfqikGVHPDKVQPVG 240
Cdd:COG4257    78 GNNRIGRIDPKTgeiTTFALPGGGSN-PHGIAFDPDG-NLWFTDQGGNRIGRLDPATGEVTEF------PLPTGGAGPYG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 241 IKLSADGKyAFVALGPANHVAVIDAKTYEVLDYLL--VGRRVWQLAFSPDQrRLLATNGVSGDVSVIDTQNLKVLKSVKV 318
Cdd:COG4257   150 IAVDPDGN-LWVTDFGANAIGRIDPDTGTLTEYALptPGAGPRGLAVDPDG-NLWVADTGSGRIGRFDPKTGTVTEYPLP 227

                         250
                  ....*....|...
gi 1402805036 319 GRY--PWGVVVTP 329
Cdd:COG4257   228 GGGarPYGVAVDG 240
Cytochrom_D1 pfam02239
Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of ...
 38-317 3.72e-08

Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of nitrite to nitric oxide in the nitrogen cycle. This family represents the d1 heme binding domain of cytochrome cd1, in which His/Tyr side chains ligate the d1 heme iron of the active site in the oxidized state.


Pssm-ID: 366994 [Multi-domain]  Cd Length: 368  Bit Score: 54.39  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  38 KDNSLSLIDLQTLEVTETLAVGQRPRGLLLSHDNKLLYICASDSDRVQVMDVATRKIIKELPS----GKDPEQ-----FA 108
Cdd:pfam02239  55 RDGGLTKIDLWNQEIVAEVRQGGNARSVATSYDGRYVIVGNYWPGQYVIMDGRTLELVKVIPArgmtGDSPESrvaaiVA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 109 LHPNDRWLYVSNEDDALVTVIDTVTDQVLGQ-IDVGIEPEGMAVSPDGKWAVNTSETTNMLHWIDTSTQTLADSTLVDQR 187
Cdd:pfam02239 135 SPGRPEFVVNLKDTGEIWLVDYSDGKNLKTTfIEAAKFLHDGGFDPDGRYFMAAANASDKIAVWDTKRGKLVALLDYGKT 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 188 PRFVEFSQ----DGSRLWASAEIG---------GTVTVLDVATRQVLKTLnfQIKGvhpdkvQPVGIKLSADGKYAFV-- 252
Cdd:pfam02239 215 PHPGPGANmphlEGGPVWTTSHLGdfvtpligtDPVLVHDLQAWKQVKEI--DVAG------GGLFVKTHPDSRYLWVdt 286

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1402805036 253 ALGPAN-HVAVIDAKTYEVLDYL--LVGRRVWQLAFSPDQRR-LLATNGVSGDVSVIDTQNLKVLKSVK 317
Cdd:pfam02239 287 FLNPDNdSVAVIDSETLEKVLTLapWPGLVVVHMEFNKRGDEvWLSVWDGKGALVVYDDKTLKLKKVIP 355
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 111-152 1.13e-07

40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in up to 14 copies per protein. Archaea Methanosarcina mazei and Methanosarcina acetivorans each have over 10 genes that encode tandem copies of this repeat, which is also found in other species. PSIPRED predicts with high confidence that each 40-residue repeats contains four beta strands. This model overlaps somewhat with the NHL repeat (pfam01436) and also shows sequence similarity to the WD domain, G-beta repeat (pfam00400).


Pssm-ID: 213697 [Multi-domain]  Cd Length: 42  Bit Score: 47.68  E-value: 1.13e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1402805036 111 PNDRWLYVSNEDDALVTVIDTVTDQVLGQIDVGIEPEGMAVS 152
Cdd:TIGR02276   1 PDGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 39-304 1.50e-07

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 51.95  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  39 DNSLSLIDLQTLEVTETLAVGQRP-RGLLLSHDNKLLYICASDSDrVQVMDVATRKIIKELPSGKDPEQ-FALHPNDRWL 116
Cdd:cd00200    30 DGTIKVWDLETGELLRTLKGHTGPvRDVAASADGTYLASGSSDKT-IRLWDLETGECVRTLTGHTSYVSsVAFSPDGRIL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 117 YVSNED----------DALVTVIDTVTDQVLgqiDVGIEPEGMAV---SPDGK---WAVNTSETTNMLH----WIdtstq 176
Cdd:cd00200   109 SSSSRDktikvwdvetGKCLTTLRGHTDWVN---SVAFSPDGTFVassSQDGTiklWDLRTGKCVATLTghtgEV----- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 177 tladstlvdqrpRFVEFSQDGSRLWASAEiGGTVTVLDVATRQVLKTLNfqikgVHPDKVqpVGIKLSADGKYaFVALGP 256
Cdd:cd00200   181 ------------NSVAFSPDGEKLLSSSS-DGTIKLWDLSTGKCLGTLR-----GHENGV--NSVAFSPDGYL-LASGSE 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1402805036 257 ANHVAVIDAKTYEVLdYLLVG--RRVWQLAFSPDQRRLLATngvSGDVSV 304
Cdd:cd00200   240 DGTIRVWDLRTGECV-QTLSGhtNSVTSLAWSPDGKRLASG---SADGTI 285
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 18-102 6.08e-07

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 50.36  E-value: 6.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  18 GALALAcGHAVAATA-------WVSN-EKDNS-LSLIDLQTLEVTETLAVGQR-------PRGlllshdnKLLYICASDS 81
Cdd:cd20778   275 KSIPLA-GQPVFAVArpdgryvWVNFsGPDNDtVQVIDTKTLKVVKTLEPGKRvlhmeftPRG-------EAVYISVNDD 346

                          90       100
                  ....*....|....*....|.
gi 1402805036  82 DRVQVMDVATRKIIKELPSGK 102
Cdd:cd20778   347 NKVVVYDTRTFREIKEVPAKK 367
8prop_heme-binding_NirN cd20777
eight-bladed heme d1-binding beta-propeller domain in dihydro-heme d1 dehydrogenase NirN; The ...
 104-317 6.54e-07

eight-bladed heme d1-binding beta-propeller domain in dihydro-heme d1 dehydrogenase NirN; The monomeric dihydro-heme d1 dehydrogenase NirN is part of the denitrification process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. NirN, similar to the homodimeric cytochrome cd1 (nitrite reductase; NirS), consists of an eight-bladed heme d1-binding beta-propeller and a cytochrome c domain, but their relative orientation differs with respect to NirS. His147, His323 and Tyr461, but not His417 are essential for activity. All 8 blades of the propeller are included in this alignment.


Pssm-ID: 467721 [Multi-domain]  Cd Length: 405  Bit Score: 50.44  E-value: 6.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 104 PEQFALH------PNDRWLYVSNEDdALVTVIDTVTDQVLGQIDVGIEPEGMAVSPDGKWAVNTSETTNMLHWIDTSTQT 177
Cdd:cd20777    60 PTRFALHggpkfsPDGRFVYFASRD-GWVTKYDLWNLKVVAEVRAGLNTRNLAVSSDGRYVAVANYLPHTLVLLDARDLS 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 178 LAD--------------STLVDQRPR--FVEFSQDGSRLW--ASAEIGGTVTVLDVATRQvLKTLNFQIKGVHPDKVqPV 239
Cdd:cd20777   139 LLKvipaadaqgrssrvSAVYDAPPRrsFVVALKDVPELWelSYDEGADPVPIGLVHDFL-YEEGAASPGFFAPRRI-AL 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 240 GIKLSA---DGKYAFVaLGpanhvAVIDAKTYEVLDyLLVGRRVWQL------------AFSPDQRRLLAT-NGVSGDVS 303
Cdd:cd20777   217 PAPLDDfffDPDYRNL-LG-----ASRQGGGGQVID-LDVGRVIASLplsgmphlgsgiYWKRDGRRVMATpNLSRGVIS 289

                         250
                  ....*....|....
gi 1402805036 304 VIDTQNLKVLKSVK 317
Cdd:cd20777   290 VIDLQTWAIVKEIP 303
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 60-155 6.00e-05

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 43.85  E-value: 6.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  60 QRPRGLLLSHDNKLlYICASDSDRVQVMDVATRKIIKELPSGKDPEQF------ALHPNDRwLYVSNEDDALVTVIDTVT 133
Cdd:cd05819     8 NNPQGIAVDSSGNI-YVADTGNNRIQVFDPDGNFITSFGSFGSGDGQFnepagvAVDSDGN-LYVADTGNHRIQKFDPDG 85

                          90       100
                  ....*....|....*....|....*...
gi 1402805036 134 DQVLGQIDVGIE------PEGMAVSPDG 155
Cdd:cd05819    86 NFLASFGGSGDGdgefngPRGIAVDSSG 113
8prop_hemeD1_NiR_delta_epsilon cd20780
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR ...
 80-157 1.10e-04

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR delta/epsilon subdivisions; Cytochrome cd1 (nitrite reductase) catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide. Purification and characterization of NiR from several bacterial sources have shown that there are two distinct classes of dissimilatory NiRs that yield NO as the main reaction product, containing either copper or heme as cofactor- the heme-containing enzyme occurring more frequently. It forms a homodimer with each subunit containing one C and one D1 heme group. The C heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The D1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis. The heme-binding nitrite reductase in delta and epsilon subdivisions are present here.


Pssm-ID: 467724 [Multi-domain]  Cd Length: 436  Bit Score: 43.67  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  80 DSDRVQVMDVATRKIIKELPSGkdpeqFALH------PNDRWLYvSNEDDALVTVIDTVT--DQVLGQIDVGIEPEGMAV 151
Cdd:cd20780    58 DASLVDFIDGTTGKVLSRHKAG-----FAVHvtvtnkRNPRYAY-SISRSGRLTMFDLAApgQPALASVQVGQESRGLAV 131


                  ....*.
gi 1402805036 152 SPDGKW 157
Cdd:cd20780   132 SPDGKY 137
8prop_hemeD1_cyt_cd1-like cd20782
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ...
 91-322 2.77e-04

cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.


Pssm-ID: 467726 [Multi-domain]  Cd Length: 415  Bit Score: 42.47  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  91 TRKIIKELPSGKDPEQFALHPNDrWLYVSNEDDALVTVIDTVTDQVLGQI-DVGIEPEGMAVSPDgkWAVNTSETTNM-- 167
Cdd:cd20782    25 SHEIHKEEEELPQEPQHDDDLRD-LLVVAERRNASVSLVDTVNHERLGRIeDVGRAIHVIEFHRD--LPENEREGAYAyt 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 168 ------LHWIDTSTQTLADSTLVDQRPRFVEFSQDGSRLWASAEIGGTVTVLDVATRQVLKTLnfQIKGVHPDKvQPVGI 241
Cdd:cd20782   102 qsrqgwVSKLDLFGGERVARVRAGTDARDIAVSRDSNYLIAGYYNPNHLVVVDAETMEPLKRI--PTHGVDPDG-QSVES 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 242 K----LSADGKYAFVA-LGPANHVAVIDAKT--YEVLDYLLVGRRVWQLAFSPDQRRLLATNGVSGDVSVIDTQNLKVLK 314
Cdd:cd20782   179 RvctlYDVPGEGCFLAaLKEAGQVWLIDYTQddFPVVDEIDCGRTLHDGFFTPDGRYFMLASQTDNCMSVLDVEEREVVD 258


                  ....*...
gi 1402805036 315 SVKVGRYP 322
Cdd:cd20782   259 RIPTAGVP 266
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 257-329 5.53e-04

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 41.17  E-value: 5.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1402805036 257 ANHVAVIDAKTYEVLDYL-LVGRRVWQLAFSPDqRRLLATNGVSGDVSVIDTQNLKVLKSVKVGRYPWGVVVTP 329
Cdd:cd20718    37 AGSVLVIDGSTHEVLGRIdDGGAQVHVVVFSPD-GRFAYVISRDGWLTKIDLYTLRPVASIRIGVNSRGIALSD 109
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 30-68 8.96e-04

40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in up to 14 copies per protein. Archaea Methanosarcina mazei and Methanosarcina acetivorans each have over 10 genes that encode tandem copies of this repeat, which is also found in other species. PSIPRED predicts with high confidence that each 40-residue repeats contains four beta strands. This model overlaps somewhat with the NHL repeat (pfam01436) and also shows sequence similarity to the WD domain, G-beta repeat (pfam00400).


Pssm-ID: 213697 [Multi-domain]  Cd Length: 42  Bit Score: 36.51  E-value: 8.96e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1402805036  30 ATAWVSNEKDNSLSLIDLQTLEVTETLAVGQRPRGLLLS 68
Cdd:TIGR02276   4 TKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
Lactonase pfam10282
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ...
 26-129 1.20e-03

Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyse 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.


Pssm-ID: 431196 [Multi-domain]  Cd Length: 340  Bit Score: 40.28  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  26 HAVAATAWVSNEKDNSLS----------LIDLQTLEVTETLAVGQR-PRGLLLSHDNKLLYICASDSDRVQVMDV--ATR 92
Cdd:pfam10282 199 HPNGKYAYVVNELSSTVTvfeydpatgtFEELQTVSTLPEGFTGTNgAAAIRVSPDGKFLYVSNRGHDSIAVFAVdeAGG 278

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1402805036  93 KI--IKELPS-GKDPEQFALHPNDRWLYVSNEDDALVTVI 129
Cdd:pfam10282 279 TLtlVERVSTeGDFPRDFNIDPDGKFLVVANQDSDNVTVF 318
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 246-286 1.65e-03

40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in up to 14 copies per protein. Archaea Methanosarcina mazei and Methanosarcina acetivorans each have over 10 genes that encode tandem copies of this repeat, which is also found in other species. PSIPRED predicts with high confidence that each 40-residue repeats contains four beta strands. This model overlaps somewhat with the NHL repeat (pfam01436) and also shows sequence similarity to the WD domain, G-beta repeat (pfam00400).


Pssm-ID: 213697 [Multi-domain]  Cd Length: 42  Bit Score: 35.73  E-value: 1.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1402805036 246 DGKYAFVALGPANHVAVIDAKTYEVLDYLLVGRRVWQLAFS 286
Cdd:TIGR02276   2 DGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 25-201 2.23e-03

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 40.02  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036   25 GHAVAATA-----WVSNEKdnslslidLQTLEVTETLAVgqRPRGLLLSHDNK-LLYIC-ASDSDRVQVMDVATRKIIKE 97
Cdd:COG4946    313 GKRVAFEArgevfTVPAEK--------GPTRNLTNTPGV--RERLPAWSPDGKsIAYFSdASGEYELYIAPADGSGEPKQ 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036   98 LPSGKDPEQFALH--PNDRWLYVSNEDDALVTV-IDTVTDQVLGQIDVGIEPEGMAVSPDGKWAVNTSETTNMLHWI--- 171
Cdd:COG4946    383 LTLGDLGRVFNPVwsPDGKKIAFTDNRGRLWVVdLASGKVRKVDTDGYGDGISDLAWSPDSKWLAYSKPGPNQLSQIfly 462

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1402805036  172 ---DTSTQTLADSTLVDQRPRfveFSQDGSRLW 201
Cdd:COG4946    463 dveTGKTVQLTDGRYDDGSPA---FSPDGKYLY 492
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 70-108 2.62e-03

40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in up to 14 copies per protein. Archaea Methanosarcina mazei and Methanosarcina acetivorans each have over 10 genes that encode tandem copies of this repeat, which is also found in other species. PSIPRED predicts with high confidence that each 40-residue repeats contains four beta strands. This model overlaps somewhat with the NHL repeat (pfam01436) and also shows sequence similarity to the WD domain, G-beta repeat (pfam00400).


Pssm-ID: 213697 [Multi-domain]  Cd Length: 42  Bit Score: 35.35  E-value: 2.62e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1402805036  70 DNKLLYICASDSDRVQVMDVATRKIIKELPSGKDPEQFA 108
Cdd:TIGR02276   2 DGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVA 40
8prop_hemeD1_cyt_cd1-like cd20782
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ...
 44-217 2.84e-03

cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.


Pssm-ID: 467726 [Multi-domain]  Cd Length: 415  Bit Score: 39.00  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  44 LIDLQTLE--VTETLAVGQRPRGLLLSHDNKLLYICASDSDRVQVMDVATRKIIKELPSGKDPEQF--ALHPNDRWLYVS 119
Cdd:cd20782   204 LIDYTQDDfpVVDEIDCGRTLHDGFFTPDGRYFMLASQTDNCMSVLDVEEREVVDRIPTAGVPHPGpgALDPDRGLAFTT 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036 120 NEDDALVTVIDTVTDQVLGQIDVgiEPEGMAVS--PDGK--WA----VNTSETTNMLHWIDTSTQTLAD----STLVDQR 187
Cdd:cd20782   284 HVGTDAVTAWDTETWEPEADIEV--PGGGLFLRshPDSDyvWGdvilDDTDRLDQLIYAIDPDTLEVATvidtSEWGEGR 361

                         170       180       190
                  ....*....|....*....|....*....|
gi 1402805036 188 PRFVEFSQDGSRLWASAEIGGTVTVLDVAT 217
Cdd:cd20782   362 AIHPEFSRDGEKVYVSHWDAGEILVFDSHT 391
8prop_hemeD1_cyt_cd1-like cd20785
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and ...
 34-143 5.72e-03

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and similar proteins; Cytochrome cd1 (cyt cd1) nitrite reductase catalyzes in vitro the reduction of molecular oxygen to water and the reduction of nitrite to nitric oxide). It is a dimer of two identical subunits of 60 kDa, each containing one c and one d1 heme group. The c heme is the electron accepting pole of the molecule and is reduced in vitro by either azurin or cytochrome c551. The d1 heme is the site where nitrite, and oxygen reduction occur. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.


Pssm-ID: 467729 [Multi-domain]  Cd Length: 412  Bit Score: 38.05  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  34 VSNEKDNSLSLIDLQTLEVTETLAVGQRPR---GLLLSHDNKLLYI-----CASDSDRVQVMDVATRKIIKELPSGKDPE 105
Cdd:cd20785   230 VASYDDNKNAVIDLKEKKVVKKIPAGCQPHlgsGAVVKVGGRLLGFgtnigSCDDKTVVTVWDMDTFEVVKQIPVSGPTE 309

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1402805036 106 QFALHPNDRWLYV---SNEDDA-LVTVIDTVTDQVLGQIDVG 143
Cdd:cd20785   310 SPAAHPNAPYVAVdivGKDPRArKIQLIDKNTLEVVKTLDVG 351
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 60-157 8.95e-03

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 37.18  E-value: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402805036  60 QRPRGLLlSHDNKLLYICASDSDRVQVMDVATRKIIKELPSGkdPEQF------ALHPNDRwLYVSNEDDALVTVIDTVt 133
Cdd:cd14962    12 TRPYGVA-ADGRGRIYVADTGRGAVFVFDLPNGKVFVIGNAG--PNRFvspigvAIDANGN-LYVSDAELGKVFVFDRD- 86

                          90       100
                  ....*....|....*....|....*..
gi 1402805036 134 DQVLGQIDVGIE---PEGMAVSPDGKW 157
Cdd:cd14962    87 GKFLRAIGAGALfkrPTGIAVDPAGKR 113
 
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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