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Conserved domains on  [gi|489697658|ref|WP_003601810|]
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MULTISPECIES: YVTN family beta-propeller repeat protein [Methylorubrum]

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 ...
 19-327 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: 569.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   19 LGSAGSAQAFTAYVTNEKANTVSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRS 98
Cdd:TIGR03866   2 LLAAGSAAAETAYVSNEKDNTISVIDTATLKVTRTFPVGQRPRGITFSKDGKLLYVCASDSDTIQVIDPATGEVLHTLPS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   99 GPDPEQFILDQSGNPLYVANEDDSQVTILDIEKNKVLAEVPVGVEPEGMGLSPDGKILVNTSETTNMAHFIDTKTFEVID 178
Cdd:TIGR03866  82 GPDPEQFALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSETTNMAHWIDTATYEIVD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  179 NVLVDARPRFAEFSADGKFLWVSAEVGGTVSVIDVATRKVIKKITFKIPSVTDEQIQPVGVRLTKDGTRAFVALGPANRV 258
Cdd:TIGR03866 162 NTLVDARPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIPGVHPEKVQPVGIKLTKDGKTAFVALGPANRV 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489697658  259 AVVDAKTYEVQKYLPVGQRVWQLAFTPDEKQLYTTNGTSNDVSVIDVEGLKVVKSIPVGLLPWGVAISK 327
Cdd:TIGR03866 242 AVVDAKTYEVLDYLLVGQRVWQLAFTPDESRLLTTNGVSNDVSVIDVAALKVIKSIKVGRLPWGVVVRP 310
 
Name Accession Description Interval E-value
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 19-327 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: 569.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   19 LGSAGSAQAFTAYVTNEKANTVSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRS 98
Cdd:TIGR03866   2 LLAAGSAAAETAYVSNEKDNTISVIDTATLKVTRTFPVGQRPRGITFSKDGKLLYVCASDSDTIQVIDPATGEVLHTLPS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   99 GPDPEQFILDQSGNPLYVANEDDSQVTILDIEKNKVLAEVPVGVEPEGMGLSPDGKILVNTSETTNMAHFIDTKTFEVID 178
Cdd:TIGR03866  82 GPDPEQFALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSETTNMAHWIDTATYEIVD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  179 NVLVDARPRFAEFSADGKFLWVSAEVGGTVSVIDVATRKVIKKITFKIPSVTDEQIQPVGVRLTKDGTRAFVALGPANRV 258
Cdd:TIGR03866 162 NTLVDARPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIPGVHPEKVQPVGIKLTKDGKTAFVALGPANRV 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489697658  259 AVVDAKTYEVQKYLPVGQRVWQLAFTPDEKQLYTTNGTSNDVSVIDVEGLKVVKSIPVGLLPWGVAISK 327
Cdd:TIGR03866 242 AVVDAKTYEVLDYLLVGQRVWQLAFTPDESRLLTTNGVSNDVSVIDVAALKVIKSIKVGRLPWGVVVRP 310
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
1-216 2.27e-36

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 130.97  E-value: 2.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   1 MVARLRAGLGCALLAGVSLGSAGSAQAFTAYVTNEKANTVSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDD 80
Cdd:COG3391   11 VLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGSG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  81 RIDVLDTATGKVVRSLRSGPDPEQFILDQSGNPLYVANEDDSQVTILDIEKNKVLAEVPVGVEPEGMGLSPDGKILVNTS 160
Cdd:COG3391   91 RVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVAN 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489697658 161 ETTNMAHFI----DTKTFEVIDNVLVDARPRFAEFSADGKFLWV-------SAEVGGTVSVIDVATR 216
Cdd:COG3391  171 SGSNTVSVIvsviDTATGKVVATIPVGGGPVGVAVSPDGRRLYVanrgsntSNGGSNTVSVIDLATL 237
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 40-315 1.82e-17

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: 82.00  E-value: 1.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  40 VSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLR-SGPDPEQFIL--------DQS 110
Cdd:cd20718   82 LTKIDLYTLRPVASIRIGVNSRGIALSDDGKYVIAGNYEPGHVVILDADTLEPLKVIPtTGVNDDGIIEsrvgaileTPP 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 111 GNPLYVANEDDSQVTILD---IEKNKVLAEVPVGVEPEGMGLSPDGKILVNTSETTNMAHFIDTKTFEVIDNVLVDARPR 187
Cdd:cd20718  162 GPYFLVALKDAGSVWVIDysdPDGNKVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGKTPH 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 188 FAEFSADG-KFLWVSAEVG-GTVSVIDVATRKVIKKItfKIPSvtdeqiQPVGVRLTKDGTRAFV--ALGP--ANRVAVV 261
Cdd:cd20718  242 PGPGATWGrKGVTATPHLGeGIVTVWDLDTWKPVKYI--PTPG------PGRFVRTHPSSPYVWAdtVFGPenADEIYVI 313

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489697658 262 DAKTYEVQKYLPV--GQRVWQLAFTPDEKQLYTTNGTSNDVSVIDVEGLKVVKSIP 315
Cdd:cd20718  314 DKETLKVVKTLIPkpGKRALHPEFTRDGKYVYVSVWDGGEVVVYDAETLELVKRIP 369
Lactonase pfam10282
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ...
 43-317 5.19e-08

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: 53.77  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   43 IDTET--LAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDV----LDTATGKVV---RSLRSGPDPEQFILDQSGNP 113
Cdd:pfam10282  20 LDTETgaLTLLGLVAEVGNPSYLALSPDGRTLYAVNEEGDQGGVaafrIDPDSGALTllnQVPTGGASPCHLSVDPDGRF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  114 LYVANEDDSQVTILDIEKNKVLAEV----------PVGVEPEGM-----GLSPDGKILVntsettnmahFIDTKT----- 173
Cdd:pfam10282 100 LFVANYHGGSVSVFPLDADGSLGELsqvvqhegsgPPPERQESPhphsvDLTPDGKFLV----------VPDLGTdrvrv 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  174 FEVIDNVL-------VDAR----PRFAEFSADGKFLWVSAEVGGTVSV--IDVATRKVIKKITFK-IPSVTDEQIQPVGV 239
Cdd:pfam10282 170 YKLDAGGGkltppasVQTPpgsgPRHLAFHPNGKYAYVVNELSSTVTVfeYDPATGTFEELQTVStLPEGFTGTNGAAAI 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  240 RLTKDGTRAFValgpANR----VAV--VDAKTYEVQKylpvGQRVW-------QLAFTPDEKQLYTTNGTSNDVSV--ID 304
Cdd:pfam10282 250 RVSPDGKFLYV----SNRghdsIAVfaVDEAGGTLTL----VERVStegdfprDFNIDPDGKFLVVANQDSDNVTVfrRD 321

                         330
                  ....*....|....*.
gi 489697658  305 VE-GL--KVVKSIPVG 317
Cdd:pfam10282 322 PEtGKltLLGKDIEVP 337
 
Name Accession Description Interval E-value
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 19-327 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: 569.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   19 LGSAGSAQAFTAYVTNEKANTVSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRS 98
Cdd:TIGR03866   2 LLAAGSAAAETAYVSNEKDNTISVIDTATLKVTRTFPVGQRPRGITFSKDGKLLYVCASDSDTIQVIDPATGEVLHTLPS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   99 GPDPEQFILDQSGNPLYVANEDDSQVTILDIEKNKVLAEVPVGVEPEGMGLSPDGKILVNTSETTNMAHFIDTKTFEVID 178
Cdd:TIGR03866  82 GPDPEQFALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSETTNMAHWIDTATYEIVD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  179 NVLVDARPRFAEFSADGKFLWVSAEVGGTVSVIDVATRKVIKKITFKIPSVTDEQIQPVGVRLTKDGTRAFVALGPANRV 258
Cdd:TIGR03866 162 NTLVDARPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIPGVHPEKVQPVGIKLTKDGKTAFVALGPANRV 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489697658  259 AVVDAKTYEVQKYLPVGQRVWQLAFTPDEKQLYTTNGTSNDVSVIDVEGLKVVKSIPVGLLPWGVAISK 327
Cdd:TIGR03866 242 AVVDAKTYEVLDYLLVGQRVWQLAFTPDESRLLTTNGVSNDVSVIDVAALKVIKSIKVGRLPWGVVVRP 310
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
1-216 2.27e-36

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 130.97  E-value: 2.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   1 MVARLRAGLGCALLAGVSLGSAGSAQAFTAYVTNEKANTVSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDD 80
Cdd:COG3391   11 VLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGSG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  81 RIDVLDTATGKVVRSLRSGPDPEQFILDQSGNPLYVANEDDSQVTILDIEKNKVLAEVPVGVEPEGMGLSPDGKILVNTS 160
Cdd:COG3391   91 RVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVAN 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489697658 161 ETTNMAHFI----DTKTFEVIDNVLVDARPRFAEFSADGKFLWV-------SAEVGGTVSVIDVATR 216
Cdd:COG3391  171 SGSNTVSVIvsviDTATGKVVATIPVGGGPVGVAVSPDGRRLYVanrgsntSNGGSNTVSVIDLATL 237
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
178-327 1.45e-26

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 105.16  E-value: 1.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 178 DNVLVDARPRFAEFSADGKFLWVSAEVGGTVSVIDVATRKVIKKITFkipsvtdeQIQPVGVRLTKDGTRAFVALGPANR 257
Cdd:COG3391   62 LGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPV--------GGGPRGLAVDPDGGRLYVADSGNGR 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489697658 258 VAVVDAKTYEVQKYLPVGQRVWQLAFTPDEKQLYTTNGTSND----VSVIDVEGLKVVKSIPVGLLPWGVAISK 327
Cdd:COG3391  134 VSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSNTvsviVSVIDTATGKVVATIPVGGGPVGVAVSP 207
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
134-308 5.84e-26

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 103.24  E-value: 5.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 134 VLAEVPVGVEPEGMGLSPDGKILVNTSETTNMAHFIDTKTFEVIDNVLVDARPRFAEFSADGKFLWVSAEVGGTVSVIDV 213
Cdd:COG3391   60 LGLGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDT 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 214 ATRKVIKKITFKipsvtdeqIQPVGVRLTKDGTRAFVALGPANRVAVV----DAKTYEVQKYLPVGQRVWQLAFTPDEKQ 289
Cdd:COG3391  140 ATGKVVATIPVG--------AGPHGIAVDPDGKRLYVANSGSNTVSVIvsviDTATGKVVATIPVGGGPVGVAVSPDGRR 211

                        170       180
                 ....*....|....*....|....*.
gi 489697658 290 LY-------TTNGTSNDVSVIDVEGL 308
Cdd:COG3391  212 LYvanrgsnTSNGGSNTVSVIDLATL 237
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
189-326 1.74e-17

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 80.12  E-value: 1.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 189 AEFSADGKFLWVSAEVGGTVSVIDVATRKVIKKITFKIPSVTDEQIQPVGVRLTKDGTRAFVALGPANRVAVVDAKTYEV 268
Cdd:COG3391   23 VAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLATGKV 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489697658 269 QKYLPVGQRVWQLAFTPDEKQLYTTNGTSNDVSVIDVEGLKVVKSIPVGLLPWGVAIS 326
Cdd:COG3391  103 VATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVD 160
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 40-315 1.82e-17

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: 82.00  E-value: 1.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  40 VSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLR-SGPDPEQFIL--------DQS 110
Cdd:cd20718   82 LTKIDLYTLRPVASIRIGVNSRGIALSDDGKYVIAGNYEPGHVVILDADTLEPLKVIPtTGVNDDGIIEsrvgaileTPP 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 111 GNPLYVANEDDSQVTILD---IEKNKVLAEVPVGVEPEGMGLSPDGKILVNTSETTNMAHFIDTKTFEVIDNVLVDARPR 187
Cdd:cd20718  162 GPYFLVALKDAGSVWVIDysdPDGNKVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGKTPH 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 188 FAEFSADG-KFLWVSAEVG-GTVSVIDVATRKVIKKItfKIPSvtdeqiQPVGVRLTKDGTRAFV--ALGP--ANRVAVV 261
Cdd:cd20718  242 PGPGATWGrKGVTATPHLGeGIVTVWDLDTWKPVKYI--PTPG------PGRFVRTHPSSPYVWAdtVFGPenADEIYVI 313

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489697658 262 DAKTYEVQKYLPV--GQRVWQLAFTPDEKQLYTTNGTSNDVSVIDVEGLKVVKSIP 315
Cdd:cd20718  314 DKETLKVVKTLIPkpGKRALHPEFTRDGKYVYVSVWDGGEVVVYDAETLELVKRIP 369
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 37-228 2.75e-17

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: 81.61  E-value: 2.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  37 ANTVSVIDT---ETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRSG--PDPEQFILDQSG 111
Cdd:cd20718  172 AGSVWVIDYsdpDGNKVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGktPHPGPGATWGRK 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 112 NPLYVANEDDSQVTILDIEKNKVLAEVPVGVEPEGMGLSPDGK-ILVNTSETTNMAHF---IDTKTFEVIDNVLVDARPR 187
Cdd:cd20718  252 GVTATPHLGEGIVTVWDLDTWKPVKYIPTPGPGRFVRTHPSSPyVWADTVFGPENADEiyvIDKETLKVVKTLIPKPGKR 331

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489697658 188 --FAEFSADGKFLWVSAEVGGTVSVIDVATRKVIKKITFKIPS 228
Cdd:cd20718  332 alHPEFTRDGKYVYVSVWDGGEVVVYDAETLELVKRIPAETPT 374
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
27-317 5.36e-17

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


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 80.72  E-value: 5.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  27 AFTAYV---TNEKANTVSV--IDTET--LAVTGTWKVGRRPRGVTLSKDDKELF-VCASDDDRIDVL--DTATGKVV--- 93
Cdd:COG2706    7 STFVYVgtyTSGESEGIYVfrLDTATgeLTLLGLVAALGNPSFLALSPDGRFLYaVNEVDDGGVSAFriDPADGTLTlln 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  94 RSLRSGPDPEQFILDQSGNPLYVANEDDSQVTILDIEKNKVLAEVPVGVEPEGMG---------------LSPDGKILVN 158
Cdd:COG2706   87 TVSSGGASPCHLSVDPDGRFLFVANYGGGSVSVFPIDADGSLGEPVQVIQHEGSGpnperqegphahsvvFDPDGRFLYV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 159 TSETTNMAHF----IDTKTFEVIDNVLVDA--RPRFAEFSADGKFLWVSAEVGGTVSVIDVA----TRKVIKKITFkIPS 228
Cdd:COG2706  167 PDLGTDRIYVyrldPATGKLPEPPEVSLPPgsGPRHLAFHPNGRFAYVINELDSTVSVYAYDaatgTLTLIQTVST-LPE 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 229 VTDEQIQPVGVRLTKDGTRAFVALGPANRVAV--VDAKTYEVQK--YLPV-GQRVWQLAFTPDEKQLYTTNGTSNDVSV- 302
Cdd:COG2706  246 DFTGENWAADIHISPDGRFLYVSNRGHNSIAVfaIDADGGKLTLvgHVPTgGKWPRDFAIDPDGRFLLVANQKSDNITVf 325

                        330
                 ....*....|....*....
gi 489697658 303 -IDVE-GL--KVVKSIPVG 317
Cdd:COG2706  326 rIDADtGKltPTGRSVPVP 344
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 40-274 1.27e-16

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: 79.63  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  40 VSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRSGPDPEQF------ILDQSGNP 113
Cdd:cd20778   74 LSKVDLLTLKVVARVKQSGNSIGGAISQDGRYVAVANYDPGGVKILDADTLKVLADIPAGSKGGGQrsrvvgLVDAPGNR 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 114 LYVANEDDSQVTILDIEKN---KVLAEVPVGVEP-EGMgLSPDG--------------------------KILVNTSETT 163
Cdd:cd20778  154 FIFSLMDADEIWVLDASDPdfpVVKKFKDIGRMPyDAL-ITPDGryyiaglfnsdgvglldlwkpergvrRILLDYGKGE 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 164 N------MAHF----------------------IDTKTFEVIDNVLVDARPRFAEFSADGKFLWV--SAEVGGTVSVIDV 213
Cdd:cd20778  233 EklpvykMPHLegwavagdkafvpavgehrvlvYDTNDWKFIKSIPLAGQPVFAVARPDGRYVWVnfSGPDNDTVQVIDT 312

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489697658 214 ATRKVIKKITFKiPSVTDeqiqpvgVRLTKDGTRAFVALGPANRVAVVDAKTYEVQKYLPV 274
Cdd:cd20778  313 KTLKVVKTLEPG-KRVLH-------MEFTPRGEAVYISVNDDNKVVVYDTRTFREIKEVPA 365
WD40 COG2319
WD40 repeat [General function prediction only];
38-326 1.79e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.57  E-value: 1.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  38 NTVSVIDTET-LAVTGTWKVGRRPRGVTLSKDDKELfVCASDDDRIDVLDTATGKVVRSLRSGPDP-EQFILDQSGNPLY 115
Cdd:COG2319  100 GTVRLWDLATgLLLRTLTGHTGAVRSVAFSPDGKTL-ASGSADGTVRLWDLATGKLLRTLTGHSGAvTSVAFSPDGKLLA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 116 VANeDDSQVTILDIEKNKVLAEVPVGVEP-EGMGLSPDGKILVnTSETTNMAHFIDTKTFEVIDnVLV--DARPRFAEFS 192
Cdd:COG2319  179 SGS-DDGTVRLWDLATGKLLRTLTGHTGAvRSVAFSPDGKLLA-SGSADGTVRLWDLATGKLLR-TLTghSGSVRSVAFS 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 193 ADGKFLwVSAEVGGTVSVIDVATRKVIKKITFKIPSVTdeqiqpvGVRLTKDGTRAFVAlGPANRVAVVDAKTYEVQKYL 272
Cdd:COG2319  256 PDGRLL-ASGSADGTVRLWDLATGELLRTLTGHSGGVN-------SVAFSPDGKLLASG-SDDGTVRLWDLATGKLLRTL 326

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489697658 273 PV-GQRVWQLAFTPDEKQLYTTnGTSNDVSVIDVEGLKVVKSIPVGLLP-WGVAIS 326
Cdd:COG2319  327 TGhTGAVRSVAFSPDGKTLASG-SDDGTVRLWDLATGELLRTLTGHTGAvTSVAFS 381
WD40 COG2319
WD40 repeat [General function prediction only];
3-326 4.67e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.41  E-value: 4.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   3 ARLRAGLGCALLAGVSLGSAGSAQAFTAYVTNEKANTVSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRI 82
Cdd:COG2319   23 AALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  83 DVLDTATGKVVRSLRSGPDPEQFI-LDQSGNPLYVANEDDSqVTILDIEKNKVLAEVPVGVEP-EGMGLSPDGKILVnTS 160
Cdd:COG2319  103 RLWDLATGLLLRTLTGHTGAVRSVaFSPDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAvTSVAFSPDGKLLA-SG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 161 ETTNMAHFIDTKTFEVIDNVLV-DARPRFAEFSADGKFLwVSAEVGGTVSVIDVATRKVIKKITFKIPSVTDeqiqpvgV 239
Cdd:COG2319  181 SDDGTVRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKLL-ASGSADGTVRLWDLATGKLLRTLTGHSGSVRS-------V 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 240 RLTKDGTRAFVAlGPANRVAVVDAKTYEVQKYLPV-GQRVWQLAFTPDEKQLYTTnGTSNDVSVIDVEGLKVVKSIPV-G 317
Cdd:COG2319  253 AFSPDGRLLASG-SADGTVRLWDLATGELLRTLTGhSGGVNSVAFSPDGKLLASG-SDDGTVRLWDLATGKLLRTLTGhT 330


                 ....*....
gi 489697658 318 LLPWGVAIS 326
Cdd:COG2319  331 GAVRSVAFS 339
WD40 COG2319
WD40 repeat [General function prediction only];
38-292 1.64e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.49  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  38 NTVSVIDTETLAVTGTWKVGRRP-RGVTLSKDDKeLFVCASDDDRIDVLDTATGKVVRSLRSGPDP-EQFILDQSGNPLY 115
Cdd:COG2319  142 GTVRLWDLATGKLLRTLTGHSGAvTSVAFSPDGK-LLASGSDDGTVRLWDLATGKLLRTLTGHTGAvRSVAFSPDGKLLA 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 116 VANEDDSqVTILDIEKNKVLAEVPV-GVEPEGMGLSPDGKILVnTSETTNMAHFIDTKTFEVIDNVLVDARP-RFAEFSA 193
Cdd:COG2319  221 SGSADGT-VRLWDLATGKLLRTLTGhSGSVRSVAFSPDGRLLA-SGSADGTVRLWDLATGELLRTLTGHSGGvNSVAFSP 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 194 DGKFLwVSAEVGGTVSVIDVATRKVIKKITFKIPSVTdeqiqpvGVRLTKDGTRAFVAlGPANRVAVVDAKTYEVQKYLP 273
Cdd:COG2319  299 DGKLL-ASGSDDGTVRLWDLATGKLLRTLTGHTGAVR-------SVAFSPDGKTLASG-SDDGTVRLWDLATGELLRTLT 369

                        250       260
                 ....*....|....*....|
gi 489697658 274 VGQ-RVWQLAFTPDEKQLYT 292
Cdd:COG2319  370 GHTgAVTSVAFSPDGRTLAS 389
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 87-320 2.35e-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: 75.84  E-value: 2.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  87 TATGKVVRSLRSGPDPEQFILDqSGNPLYVANEDDSQVTILDIEKNKVLAEVP-VGVEPEGMGLSPDGKILVNTSETTNM 165
Cdd:cd20718    4 KKSLEVLVPERELPPVAYGIWD-LENLMVVVERDAGSVLVIDGSTHEVLGRIDdGGAQVHVVVFSPDGRFAYVISRDGWL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 166 AHfIDTKTFEVIDNVLVDARPRFAEFSADGKFLWVSAEVGGTVSVIDVATRKVIKKITFKIPSVTDEQIQPVGVRLTKD- 244
Cdd:cd20718   83 TK-IDLYTLRPVASIRIGVNSRGIALSDDGKYVIAGNYEPGHVVILDADTLEPLKVIPTTGVNDDGIIESRVGAILETPp 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489697658 245 GTRAFVALGPANRVAVVDAKTYEVQKYLPVGQ--RVWQLAF-TPDEKQLYTTNGTSNDVSVIDVEGLKVVKSIPVGLLP 320
Cdd:cd20718  162 GPYFLVALKDAGSVWVIDYSDPDGNKVTDIGNigRPLHDAFlDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGKTP 240
8prop_hemeD1_cyt_cd1-like cd20785
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and ...
 32-228 2.78e-15

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: 75.80  E-value: 2.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  32 VTNEKANTVSVIDT--ETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRSGPDPE---QFI 106
Cdd:cd20785  186 IALEQAGQVWIVDLdkPGMPVTKIKNVGRHLHDAFLSPDGRYLMVASYDDNKNAVIDLKEKKVVKKIPAGCQPHlgsGAV 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 107 LDQSGNPLYV-----ANEDDSQVTILDIEKNKVLAEVPVGVEPEGMGLSPDGKI----LVNTSETTNMAHFIDTKTFEVI 177
Cdd:cd20785  266 VKVGGRLLGFgtnigSCDDKTVVTVWDMDTFEVVKQIPVSGPTESPAAHPNAPYvavdIVGKDPRARKIQLIDKNTLEVV 345

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489697658 178 DNVLVDARPRFAEFSADGKFLWVSAEV-GGTVSVIDVATRKVIKKITFKIPS 228
Cdd:cd20785  346 KTLDVGGHSHFPEYTADGDYLYVSAGYnGDRLVIYDSKTLKKVKEIPMESPA 397
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
53-315 5.57e-15

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 73.52  E-value: 5.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  53 TWKV---GRRPRGVTLSKDDkELFVCASDDDRIDVLDTATGKVVR-SLRSGPDPEQFILDQSGNpLYVANEDDSQVTILD 128
Cdd:COG4257    9 EYPVpapGSGPRDVAVDPDG-AVWFTDQGGGRIGRLDPATGEFTEyPLGGGSGPHGIAVDPDGN-LWFTDNGNNRIGRID 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 129 IeKNKVLAEVPVGVE---PEGMGLSPDGKILVnTSETTNMAHFIDTKT--FEVIDNVLVDARPRFAEFSADGKfLWVSAE 203
Cdd:COG4257   87 P-KTGEITTFALPGGgsnPHGIAFDPDGNLWF-TDQGGNRIGRLDPATgeVTEFPLPTGGAGPYGIAVDPDGN-LWVTDF 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 204 VGGTVSVIDVATRKVikkITFKIPSvtdEQIQPVGVRLTKDGtRAFVALGPANRVAVVDAKTYEVQKY-LPVGQ-RVWQL 281
Cdd:COG4257  164 GANAIGRIDPDTGTL---TEYALPT---PGAGPRGLAVDPDG-NLWVADTGSGRIGRFDPKTGTVTEYpLPGGGaRPYGV 236

                        250       260       270
                 ....*....|....*....|....*....|....
gi 489697658 282 AFTPDEKqLYTTNGTSNDVSVIDVEGLKVVKSIP 315
Cdd:COG4257  237 AVDGDGR-VWFAESGANRIVRFDPDTELTEYVLP 269
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 285-326 4.19e-12

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: 60.00  E-value: 4.19e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 489697658  285 PDEKQLYTTNGTSNDVSVIDVEGLKVVKSIPVGLLPWGVAIS 326
Cdd:TIGR02276   1 PDGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
16-216 6.20e-12

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 65.04  E-value: 6.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  16 GVSLGSAGSAqaftaYVTNEKANTVSVIDTETLAVTgTWKV---GRRPRGVTLSKDDKeLFVCASDDDRIDVLDTATGKV 92
Cdd:COG4257   63 GIAVDPDGNL-----WFTDNGNNRIGRIDPKTGEIT-TFALpggGSNPHGIAFDPDGN-LWFTDQGGNRIGRLDPATGEV 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  93 --VRSLRSGPDPEQFILDQSGNpLYVANEDDSQVTILDIEKNKVlAEVPV---GVEPEGMGLSPDGKILVNTSETTNMAH 167
Cdd:COG4257  136 teFPLPTGGAGPYGIAVDPDGN-LWVTDFGANAIGRIDPDTGTL-TEYALptpGAGPRGLAVDPDGNLWVADTGSGRIGR 213

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489697658 168 FI-DTKTFEVIDNVLVDARPRFAEFSADGKfLWVSAEVGGTVSVIDVATR 216
Cdd:COG4257  214 FDpKTGTVTEYPLPGGGARPYGVAVDGDGR-VWFAESGANRIVRFDPDTE 262
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 66-316 1.39e-11

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: 64.67  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  66 SKDDKELF-VCASDDDRIDVLDTATGKVVRSLRSGPD-PEQFILDQSGNPLYVANeDDSQVTILDIEKNKVLAEVPVGVE 143
Cdd:cd20718   23 IWDLENLMvVVERDAGSVLVIDGSTHEVLGRIDDGGAqVHVVVFSPDGRFAYVIS-RDGWLTKIDLYTLRPVASIRIGVN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 144 PEGMGLSPDGKILVNTSETTNMAHFIDTKTFEVIDNV-LVDARPRFAEFSADG---------KFLwVSAEVGGTVSVIDV 213
Cdd:cd20718  102 SRGIALSDDGKYVIAGNYEPGHVVILDADTLEPLKVIpTTGVNDDGIIESRVGailetppgpYFL-VALKDAGSVWVIDY 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 214 ATRKvikkiTFKIPSVTDEQIQPVGVRLTKDGTRAFVALGPANRVAVVDAKTYEVQKYLPVGQrvwqlafTP-------D 286
Cdd:cd20718  181 SDPD-----GNKVTDIGNIGRPLHDAFLDPDGRYFIVASQGSNTMWVLDLKTGKVVARIPTGK-------TPhpgpgatW 248

                        250       260       270
                 ....*....|....*....|....*....|..
gi 489697658 287 EKQLYTTNGTSND--VSVIDVEGLKVVKSIPV 316
Cdd:cd20718  249 GRKGVTATPHLGEgiVTVWDLDTWKPVKYIPT 280
8prop_hemeD1_cyt_cd1-like cd20783
eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt ...
 49-223 2.78e-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: 2.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  49 AVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRSG--PDPEQFILDQSGNPLYVA--NEDDSQV 124
Cdd:cd20783  190 PITKVENVGHILHDGFLSPDNKTFYLASQTDNWMAAIDVATMKIVAKIPTGdkPHPGSGAVWEADGKEYAAtvHAGEGKV 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 125 TILDIEKNKVLAEVPVgvepEGMGL----SPDGKILVNTSETTNMAHFI----DTKTFEVIDNVLVDARPRFAEFSADGK 196
Cdd:cd20783  270 TIWDLDTNEIVGEVPT----SGPGLfirtTENMPYVWADSMFAPEPNEItvheKAPPFKVVKRITDGTRTLHPEPTADGK 345

                        170       180
                 ....*....|....*....|....*..
gi 489697658 197 FLWVSAEVGGTVSVIDVATRKVIKKIT 223
Cdd:cd20783  346 YVYVSDWDGNVVRVYDAETLELVKEIT 372
8prop_hemeD1_cyt_cd1-like cd20783
eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt ...
 111-320 4.53e-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: 53.93  E-value: 4.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 111 GNPLYVANEDDSQVTILDIEKNKVLAEVPVGVEPEGMGLSP-DGKILVNTSETtNMAHFIDTKTFEVIDNVLVDARPRFA 189
Cdd:cd20783   27 DNLLLVTEREARSIAVIDGDTHTLLGHIEAGYRAHGYTFSPtDGRWAYNLGRD-GWLYKIDLYSLQPVAKVRVGLDARGI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 190 EFSADGKFLWVSAEVGGTVSVIDVATRKVIKKITfkiPSVTDEQIQPVGVRL--------TKDGTRAFVALGPANRVAVV 261
Cdd:cd20783  106 AISDDGKYLIAGNYIPATAVILDAKTLEPLKVID---TSGVDPDGKMVDSRVasvndvapDLVGPYFLLALKEAGQVWRI 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489697658 262 D--AKTYEVQKYLPVGQRVWQLAFTPDEKQLYTTNGTSNDVSVIDVEGLKVVKSIPVGLLP 320
Cdd:cd20783  183 DysKPDFPITKVENVGHILHDGFLSPDNKTFYLASQTDNWMAAIDVATMKIVAKIPTGDKP 243
8prop_hemeD1_cyt_cd1-like cd20785
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and ...
 77-317 4.85e-08

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: 53.84  E-value: 4.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  77 SDDDRIDVLDTATGKVVRSLRSGPDPEQFILDQSGNPL----YVANeddsQVTILDIEKNKVLAEVPV-GVEPEGMGLSP 151
Cdd:cd20785   95 TDTGEVYKIDLYSMQAVRSVKAGLNGPSLAVSRDGKYLaagsFVPH----TAVILDADTLEPLKYFELeGVDPDGKMVES 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 152 DGKILVNTS---------ETTNMAHFIDTKT--FEV--IDNV---LVDArprFaeFSADGKFLWVSAEVGGTVSVIDVAT 215
Cdd:cd20785  171 DSGMITGTPyanyfaialEQAGQVWIVDLDKpgMPVtkIKNVgrhLHDA---F--LSPDGRYLMVASYDDNKNAVIDLKE 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 216 RKVIKKITFK-IPSVTDEQIQPVGVRLTKDGTRaFVALGPANRVAVVDAKTYEVQKYLPVGQRVWQLAFTPDEK----QL 290
Cdd:cd20785  246 KKVVKKIPAGcQPHLGSGAVVKVGGRLLGFGTN-IGSCDDKTVVTVWDMDTFEVVKQIPVSGPTESPAAHPNAPyvavDI 324

                        250       260
                 ....*....|....*....|....*..
gi 489697658 291 YTTNGTSNDVSVIDVEGLKVVKSIPVG 317
Cdd:cd20785  325 VGKDPRARKIQLIDKNTLEVVKTLDVG 351
Lactonase pfam10282
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ...
 43-317 5.19e-08

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: 53.77  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   43 IDTET--LAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDV----LDTATGKVV---RSLRSGPDPEQFILDQSGNP 113
Cdd:pfam10282  20 LDTETgaLTLLGLVAEVGNPSYLALSPDGRTLYAVNEEGDQGGVaafrIDPDSGALTllnQVPTGGASPCHLSVDPDGRF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  114 LYVANEDDSQVTILDIEKNKVLAEV----------PVGVEPEGM-----GLSPDGKILVntsettnmahFIDTKT----- 173
Cdd:pfam10282 100 LFVANYHGGSVSVFPLDADGSLGELsqvvqhegsgPPPERQESPhphsvDLTPDGKFLV----------VPDLGTdrvrv 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  174 FEVIDNVL-------VDAR----PRFAEFSADGKFLWVSAEVGGTVSV--IDVATRKVIKKITFK-IPSVTDEQIQPVGV 239
Cdd:pfam10282 170 YKLDAGGGkltppasVQTPpgsgPRHLAFHPNGKYAYVVNELSSTVTVfeYDPATGTFEELQTVStLPEGFTGTNGAAAI 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  240 RLTKDGTRAFValgpANR----VAV--VDAKTYEVQKylpvGQRVW-------QLAFTPDEKQLYTTNGTSNDVSV--ID 304
Cdd:pfam10282 250 RVSPDGKFLYV----SNRghdsIAVfaVDEAGGTLTL----VERVStegdfprDFNIDPDGKFLVVANQDSDNVTVfrRD 321

                         330
                  ....*....|....*.
gi 489697658  305 VE-GL--KVVKSIPVG 317
Cdd:pfam10282 322 PEtGKltLLGKDIEVP 337
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 31-66 8.28e-08

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: 8.28e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 489697658   31 YVTNEKANTVSVIDTETLAVTGTWKVGRRPRGVTLS 66
Cdd:TIGR02276   7 YVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 54-228 1.78e-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: 52.29  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  54 WKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDT---ATGKVVRSLRSGPDPEQFILDQ---------SGNPLYVANEDD 121
Cdd:cd20778  181 KDIGRMPYDALITPDGRYYIAGLFNSDGVGLLDLwkpERGVRRILLDYGKGEEKLPVYKmphlegwavAGDKAFVPAVGE 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 122 SQVTILDIEKNKVLAEVPVGVEPEGMGLSPDGK-ILVNTSETTN-MAHFIDTKTFEVIDNVLVDARPRFAEFSADGKFLW 199
Cdd:cd20778  261 HRVLVYDTNDWKFIKSIPLAGQPVFAVARPDGRyVWVNFSGPDNdTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVY 340

                        170       180
                 ....*....|....*....|....*....
gi 489697658 200 VSAEVGGTVSVIDVATRKVIKKITFKIPS 228
Cdd:cd20778  341 ISVNDDNKVVVYDTRTFREIKEVPAKKPS 369
8prop_hemeD1_NiR_delta_epsilon cd20780
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NiR ...
 31-175 7.07e-07

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: 50.61  E-value: 7.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  31 YVTNEKANTVSVIDTEtlAVTGTWK--------VGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRSGPDP 102
Cdd:cd20780    5 WLMHWKNTVELKLDLD--EVKKTWKkladreelAKKYPHAVDVKSVTDITFATERDASLVDFIDGTTGKVLSRHKAGFAV 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489697658 103 EQFILDQSgNPLYVANEDDS-QVTILDIEK--NKVLAEVPVGVEPEGMGLSPDGKILVNTSETTNMAHFIDTKTFE 175
Cdd:cd20780   83 HVTVTNKR-NPRYAYSISRSgRLTMFDLAApgQPALASVQVGQESRGLAVSPDGKYVMAGNYNPGGAVLCDAMTLE 157
8prop_hemeD1_cyt_cd1-like cd20785
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase and ...
 117-320 1.09e-06

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: 49.99  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 117 ANEDDSQVTILDIEKNKVLAEVPVGVEPEGMGLSPDGKILVNTSETTNMAHFIDTKTFEVIDNVLVDAR-PRFAeFSADG 195
Cdd:cd20785   51 GRGKGSKVVFFDGKTNRKVGEIPTGFAPHIMDFHPVNPRWAYVKTDTGEVYKIDLYSMQAVRSVKAGLNgPSLA-VSRDG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 196 KFLWVSAEVGGTVSVIDVATRKVIKKITFkipsvtdEQIQPVGVRLTKD-----GTR---AFV-ALGPANRVAVVDAKT- 265
Cdd:cd20785  130 KYLAAGSFVPHTAVILDADTLEPLKYFEL-------EGVDPDGKMVESDsgmitGTPyanYFAiALEQAGQVWIVDLDKp 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489697658 266 -YEVQKYLPVGQRVWQLAFTPDEKQLYTTNGTSNDVSVIDVEGLKVVKSIPVGLLP 320
Cdd:cd20785  203 gMPVTKIKNVGRHLHDAFLSPDGRYLMVASYDDNKNAVIDLKEKKVVKKIPAGCQP 258
8prop_hemeD1_cyt_cd1-like cd20783
eight-bladed heme d1-binding beta-propeller domain and similar proteins; Cytochrome cd1 (cyt ...
 32-315 1.42e-06

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: 49.31  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  32 VTNEKANTVSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRSGPDPEQFILDQSG 111
Cdd:cd20783   32 VTEREARSIAVIDGDTHTLLGHIEAGYRAHGYTFSPTDGRWAYNLGRDGWLYKIDLYSLQPVAKVRVGLDARGIAISDDG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 112 NPLYVANEDDSQVTILD---IEKNKVL---AEVPVG------------VEPEGMG------------------------- 148
Cdd:cd20783  112 KYLIAGNYIPATAVILDaktLEPLKVIdtsGVDPDGkmvdsrvasvndVAPDLVGpyfllalkeagqvwridyskpdfpi 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 149 --------------LSPDGKILVNTSETTNMAHFIDTKTFEVIDNVLVDARPR---FAEFSADGKFLWVSAEVG-GTVSV 210
Cdd:cd20783  192 tkvenvghilhdgfLSPDNKTFYLASQTDNWMAAIDVATMKIVAKIPTGDKPHpgsGAVWEADGKEYAATVHAGeGKVTI 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 211 IDVATRKVIKKITFKIPSVTdeqiqpvgVRLTKDGTRAF---VALGPANRVAVVD-AKTYEVQKYLPVGQRVWQLAFTPD 286
Cdd:cd20783  272 WDLDTNEIVGEVPTSGPGLF--------IRTTENMPYVWadsMFAPEPNEITVHEkAPPFKVVKRITDGTRTLHPEPTAD 343

                        330       340
                 ....*....|....*....|....*....
gi 489697658 287 EKQLYTTNGTSNDVSVIDVEGLKVVKSIP 315
Cdd:cd20783  344 GKYVYVSDWDGNVVRVYDAETLELVKEIT 372
8prop_hemeD1_cyt_cd1-like cd20782
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ...
 37-248 2.45e-06

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: 48.63  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  37 ANTVSVID--TETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRSG--PDPEQFILDQSGN 112
Cdd:cd20782  199 AGQVWLIDytQDDFPVVDEIDCGRTLHDGFFTPDGRYFMLASQTDNCMSVLDVEEREVVDRIPTAgvPHPGPGALDPDRG 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 113 PLYVANEDDSQVTILDIEKNKVLAEVPVgvepEGMGL----SPDGK------ILVNTSETTNMAHFIDTKTFEVIDNV-- 180
Cdd:cd20782  279 LAFTTHVGTDAVTAWDTETWEPEADIEV----PGGGLflrsHPDSDyvwgdvILDDTDRLDQLIYAIDPDTLEVATVIdt 354

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 181 --LVDARPRFAEFSADGKFLWVSAEVGGTVSVIDVATRKVIKKItfkipsvtDEQIQPVGVRLtkdGTRA 248
Cdd:cd20782  355 seWGEGRAIHPEFSRDGEKVYVSHWDAGEILVFDSHTGELIEEI--------DGLETPTGKFL---GNRA 413
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 58-328 2.93e-06

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: 48.08  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  58 RRPRGVTLSkDDKELFVCASDDDRIDVLDTATGKVVRSLRSGPDPEQFI------LDQSGNpLYVANEDDSQVTILDIEK 131
Cdd:cd05819    8 NNPQGIAVD-SSGNIYVADTGNNRIQVFDPDGNFITSFGSFGSGDGQFNepagvaVDSDGN-LYVADTGNHRIQKFDPDG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 132 NKVLAEVPVG------VEPEGMGLSPDGKILVntSETTNmahfidtktfeviDNVLVdarprfaeFSADGKFLWvsaevg 205
Cdd:cd05819   86 NFLASFGGSGdgdgefNGPRGIAVDSSGNIYV--ADTGN-------------HRIQK--------FDPDGEFLT------ 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 206 gtvsvidvatrkvikkiTFKIPSVTDEQIQ-PVGvrltkdgtrafVALGPANRVAVVDAKTYEVQKYLPVGQRV------ 278
Cdd:cd05819  137 -----------------TFGSGGSGPGQFNgPTG-----------VAVDSDGNIYVADTGNHRIQVFDPDGNFLttfgst 188

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489697658 279 ----------WQLAFTPDEKqLYTTNGTSNDVSVIDVEGL------KVVKSIPVGLLPWGVAISKK 328
Cdd:cd05819  189 gtgpgqfnypTGIAVDSDGN-IYVADSGNNRVQVFDPDGAgfggngNFLGSDGQFNRPSGLAVDSD 253
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 110-150 5.82e-06

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: 42.67  E-value: 5.82e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 489697658  110 SGNPLYVANEDDSQVTILDIEKNKVLAEVPVGVEPEGMGLS 150
Cdd:TIGR02276   2 DGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 39-98 6.20e-06

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: 47.28  E-value: 6.20e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  39 TVSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRS 98
Cdd:cd20778  306 TVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNKVVVYDTRTFREIKEVPA 365
Cytochrom_D1 pfam02239
Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of ...
 40-315 8.32e-06

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: 47.08  E-value: 8.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   40 VSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRS----GPDPEQ---FILDQSGN 112
Cdd:pfam02239  59 LTKIDLWNQEIVAEVRQGGNARSVATSYDGRYVIVGNYWPGQYVIMDGRTLELVKVIPArgmtGDSPESrvaAIVASPGR 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  113 PLYVANEDDS-QVTILDI--EKNKVLAEVPVGVEPEGMGLSPDGKILVNTSETTNMAHFIDTKTFEVIDNVLVDARP--- 186
Cdd:pfam02239 139 PEFVVNLKDTgEIWLVDYsdGKNLKTTFIEAAKFLHDGGFDPDGRYFMAAANASDKIAVWDTKRGKLVALLDYGKTPhpg 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  187 RFAEF---------SADGKFLWVSAEVG-GTVSVIDVATRKVIKKItfkipsvtDEQIQPVGVRLTKDGTRAFV--ALGP 254
Cdd:pfam02239 219 PGANMphleggpvwTTSHLGDFVTPLIGtDPVLVHDLQAWKQVKEI--------DVAGGGLFVKTHPDSRYLWVdtFLNP 290

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489697658  255 AN-RVAVVDAKTYEvqKYLPV----GQRVWQLAFTPDEKQLY-TTNGTSNDVSVIDVEGLKVVKSIP 315
Cdd:pfam02239 291 DNdSVAVIDSETLE--KVLTLapwpGLVVVHMEFNKRGDEVWlSVWDGKGALVVYDDKTLKLKKVIP 355
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 38-302 2.55e-05

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: 45.02  E-value: 2.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  38 NTVSVIDTETLAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVVRSLRsGPDPEQFILDQSGNPLYV- 116
Cdd:cd00200   31 GTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT-GHTSYVSSVAFSPDGRILs 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 117 ANEDDSQVTILDIEKNKVLAEVPvGVEPEGMGL--SPDGKILVnTSETTNMAHFIDTKTFEVI-------DNVlvdarpR 187
Cdd:cd00200  110 SSSRDKTIKVWDVETGKCLTTLR-GHTDWVNSVafSPDGTFVA-SSSQDGTIKLWDLRTGKCVatltghtGEV------N 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 188 FAEFSADGKFLWVSAEVgGTVSVIDVATRKVIKKITFKIPSVTDeqiqpvgvrLTKDGTRAFVALGPANRVAVV-DAKTY 266
Cdd:cd00200  182 SVAFSPDGEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNS---------VAFSPDGYLLASGSEDGTIRVwDLRTG 251

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489697658 267 EVQKYLPVGQ-RVWQLAFTPDEKQLYTtngTSNDVSV 302
Cdd:cd00200  252 ECVQTLSGHTnSVTSLAWSPDGKRLAS---GSADGTI 285
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
251-328 2.64e-05

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 44.69  E-value: 2.64e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489697658 251 ALGPANRVAVVDAKTYEVQKYLPVGQRVWQLAFTPDEKQLYTTNGTSNDVSVIDVEGLKVVKSIPVGLLPWGVAISKK 328
Cdd:COG3391   43 GVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPD 120
8prop_hemeD1_cyt_cd1-like cd20782
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ...
 100-320 4.13e-05

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: 44.78  E-value: 4.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 100 PDPEQFILDQSgNPLYVANEDDSQVTILDIEKNKVLAEVP-VGVEPEGMGLSPDgkILVNTSETTNM--------AHFID 170
Cdd:cd20782   36 PQEPQHDDDLR-DLLVVAERRNASVSLVDTVNHERLGRIEdVGRAIHVIEFHRD--LPENEREGAYAytqsrqgwVSKLD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 171 TKTFEVIDNVLVDARPRFAEFSADGKFLWVSAEVGGTVSVIDVATRKVIKKITFKipsVTDEQIQPVGVRLTK----DGT 246
Cdd:cd20782  113 LFGGERVARVRAGTDARDIAVSRDSNYLIAGYYNPNHLVVVDAETMEPLKRIPTH---GVDPDGQSVESRVCTlydvPGE 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489697658 247 RAFVA-LGPANRVAVVDAKT--YEVQKYLPVGQRVWQLAFTPDEKQLYTTNGTSNDVSVIDVEGLKVVKSIPVGLLP 320
Cdd:cd20782  190 GCFLAaLKEAGQVWLIDYTQddFPVVDEIDCGRTLHDGFFTPDGRYFMLASQTDNCMSVLDVEEREVVDRIPTAGVP 266
WD40 COG2319
WD40 repeat [General function prediction only];
38-161 5.52e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 44.52  E-value: 5.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  38 NTVSVIDTETLAVTGTWKV-GRRPRGVTLSKDDKeLFVCASDDDRIDVLDTATGKVVRSLRSGPDPEQFI-LDQSGNPLY 115
Cdd:COG2319  268 GTVRLWDLATGELLRTLTGhSGGVNSVAFSPDGK-LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVaFSPDGKTLA 346

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489697658 116 VANeDDSQVTILDIEKNKVLAEVPVGVEP-EGMGLSPDGKILVNTSE 161
Cdd:COG2319  347 SGS-DDGTVRLWDLATGELLRTLTGHTGAvTSVAFSPDGRTLASGSA 392
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 57-199 8.79e-05

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 44.26  E-value: 8.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   57 GRRPRGVTLSKDDKELFVcASDDDRIDVLdtatgkVVRSLRSGPDPEQFILDQSGNPL---------YVA-NEDDSQVTI 126
Cdd:COG4946   342 GVRERLPAWSPDGKSIAY-FSDASGEYEL------YIAPADGSGEPKQLTLGDLGRVFnpvwspdgkKIAfTDNRGRLWV 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  127 LDIE--KNKVLAEVPVGVEPEGMGLSPDGKILVNTSETTN------MAHFIDTKTFEVIDNVLVDARPRFaefSADGKFL 198
Cdd:COG4946   415 VDLAsgKVRKVDTDGYGDGISDLAWSPDSKWLAYSKPGPNqlsqifLYDVETGKTVQLTDGRYDDGSPAF---SPDGKYL 491


                  .
gi 489697658  199 W 199
Cdd:COG4946   492 Y 492
8prop_heme-binding_NirN cd20777
eight-bladed heme d1-binding beta-propeller domain in dihydro-heme d1 dehydrogenase NirN; The ...
 118-228 9.93e-05

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: 43.89  E-value: 9.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 118 NEDDSQVTILDIEKNKVLAEVPVgvepEGMGL-------SPDGKILVNTSETTNMAHFIDTKTFEVIDNVLVDARPRFA- 189
Cdd:cd20777  282 NLSRGVISVIDLQTWAIVKEIPT----PGPGFfmrshenSPYAWADVFMGPKRDKLHLIDKQTLEIVKTLRPEPGKTAAh 357

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489697658 190 -EFSADGKFLWVSA-EVGGTVSVIDVATRKVIKKITFKIPS 228
Cdd:cd20777  358 vEFTRDGRYALASVwEDDGALIVYDAHTLKEVKRLPMNKPS 398
Cytochrom_D1 pfam02239
Cytochrome D1 heme domain; Cytochrome cd1 (nitrite reductase) catalyzes the conversion of ...
 56-228 1.29e-04

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: 43.22  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   56 VGRRPRGVTLSKDDKELFVCASDDDRIDVLDTATGKVV------RSLRSGPDPeQFILDQSGNPLYVA-NEDDS------ 122
Cdd:pfam02239 169 AAKFLHDGGFDPDGRYFMAAANASDKIAVWDTKRGKLValldygKTPHPGPGA-NMPHLEGGPVWTTShLGDFVtpligt 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  123 -QVTILDIEKNKVLAEVPVGVEPEGMGLSPDGK-ILVNT--SETTNMAHFIDTKTFEVIDNVLVDARPRFA--EFSADGK 196
Cdd:pfam02239 248 dPVLVHDLQAWKQVKEIDVAGGGLFVKTHPDSRyLWVDTflNPDNDSVAVIDSETLEKVLTLAPWPGLVVVhmEFNKRGD 327

                         170       180       190
                  ....*....|....*....|....*....|...
gi 489697658  197 FLWVSAEVG-GTVSVIDVATRKVIKKITFKIPS 228
Cdd:pfam02239 328 EVWLSVWDGkGALVVYDDKTLKLKKVIPLNTPS 360
8prop_hemeD1_cyt_cd1-like cd20782
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ...
 85-274 2.25e-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: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  85 LDTATGKVVRSLRSGPDPEQFILDQSGNPLYVANEDDSQVTILDIEKNKVLAEVPV-GVEPEGMGLS---------PDGK 154
Cdd:cd20782  111 LDLFGGERVARVRAGTDARDIAVSRDSNYLIAGYYNPNHLVVVDAETMEPLKRIPThGVDPDGQSVEsrvctlydvPGEG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 155 ILVNTSETTNMAHFID--TKTFEVIDNVLVDARPRFAEFSADGKFLWVSAEVGGTVSVIDVATRKVIKKITfkipsvTDE 232
Cdd:cd20782  191 CFLAALKEAGQVWLIDytQDDFPVVDEIDCGRTLHDGFFTPDGRYFMLASQTDNCMSVLDVEEREVVDRIP------TAG 264

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489697658 233 QIQPVGVRLTKDGTRAFVALGPANRVAVVDAKTYEVQKYLPV 274
Cdd:cd20782  265 VPHPGPGALDPDRGLAFTTHVGTDAVTAWDTETWEPEADIEV 306
8prop_hemeD1_cyt_cd1-like cd20782
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ...
 73-267 3.04e-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: 42.08  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  73 FVCASDDDRIDVLDTATGKVVRSLRSGPDPEQFildqsgnplYVANEDDSQVTILDIEKNKVLAEVPVGVEPE-GMG-LS 150
Cdd:cd20782  204 LIDYTQDDFPVVDEIDCGRTLHDGFFTPDGRYF---------MLASQTDNCMSVLDVEEREVVDRIPTAGVPHpGPGaLD 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 151 PDGKILVNTSETTNMAHFIDTKTFEVIDNVLVDARPRFAEFSADGKFLWV------SAEVGGTVSVIDVATRKVIKKITF 224
Cdd:cd20782  275 PDRGLAFTTHVGTDAVTAWDTETWEPEADIEVPGGGLFLRSHPDSDYVWGdvilddTDRLDQLIYAIDPDTLEVATVIDT 354

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489697658 225 KIPSVtDEQIQPVgvrLTKDGTRAFVALGPANRVAVVDAKTYE 267
Cdd:cd20782  355 SEWGE-GRAIHPE---FSRDGEKVYVSHWDAGEILVFDSHTGE 393
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 31-260 3.60e-04

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: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 41.51  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  31 YVTNEKANTVSVIDTETLAVTgtwKVGRR---------PRGVTLSKDDkELFVCASDDDRIDVLDtATGKVVRSLRSGPD 101
Cdd:cd14963   23 YVADTNNHRVQVFDYEGKFKK---SFGGPgtgpgefkyPYGIAVDSDG-NIYVADLYNGRIQVFD-PDGKFLKYFPEKKD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 102 PEQFI----LDQSGNPLYVANEDDSQVTILDIEKNKVLAEVPVGVE------PEGMGLSPDGKILVntSETTN------- 164
Cdd:cd14963   98 RVKLIspagLAIDDGKLYVSDVKKHKVIVFDLEGKLLLEFGKPGSEpgelsyPNGIAVDEDGNIYV--ADSGNgriqvfd 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 165 -MAHFIDTKTFEVIDNVLVdARPRFAEFSADGKFLWVSAeVGGTVSVIDvatRKVIKKITFKIPSVTDEQIQ-PVGVRLT 242
Cdd:cd14963  176 kNGKFIKELNGSPDGKSGF-VNPRGIAVDPDGNLYVVDN-LSHRVYVFD---EQGKELFTFGGRGKDDGQFNlPNGLFID 250

                        250
                 ....*....|....*...
gi 489697658 243 KDGtRAFVALGPANRVAV 260
Cdd:cd14963  251 DDG-RLYVTDRENNRVAV 267
Lactonase pfam10282
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ...
 29-141 4.65e-04

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: 41.44  E-value: 4.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   29 TAYVTNEKANTVSV--IDTETLAVT---------GTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVL--DTATGKVV-- 93
Cdd:pfam10282 204 YAYVVNELSSTVTVfeYDPATGTFEelqtvstlpEGFTGTNGAAAIRVSPDGKFLYVSNRGHDSIAVFavDEAGGTLTlv 283

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489697658   94 -RSLRSGPDPEQFILDQSGNPLYVANEDDSQVTILDIEKN-----KVLAEVPVG 141
Cdd:pfam10282 284 eRVSTEGDFPRDFNIDPDGKFLVVANQDSDNVTVFRRDPEtgkltLLGKDIEVP 337
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 255-327 1.29e-03

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: 40.01  E-value: 1.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489697658 255 ANRVAVVDAKTYEVQKYLP-VGQRVWQLAFTPDEKQLYttnGTSND--VSVIDVEGLKVVKSIPVGLLPWGVAISK 327
Cdd:cd20718   37 AGSVLVIDGSTHEVLGRIDdGGAQVHVVVFSPDGRFAY---VISRDgwLTKIDLYTLRPVASIRIGVNSRGIALSD 109
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 16-130 1.42e-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: 39.88  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  16 GVSLGSAGsaqafTAYVTNEKANTVSVIDTET--LAVTGTWKVGRRPRGVTLSKDDKELFVCASDDDRIDVLDTAtGKVV 93
Cdd:cd14962   61 GVAIDANG-----NLYVSDAELGKVFVFDRDGkfLRAIGAGALFKRPTGIAVDPAGKRLYVVDTLAHKVKVFDLD-GRLL 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489697658  94 RSL-RSGPDPEQF------ILDQSGNpLYVANEDDSQVTILDIE 130
Cdd:cd14962  135 FDIgKRGSGPGEFnlptdlAVDRDGN-LYVTDTMNFRVQIFDAD 177
8prop_hemeD1_cyt_cd1-like cd20784
cytochrome cd1 nitrate reductase eight-bladed heme d1-binding beta-propeller domain and ...
 123-227 1.68e-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: 467728 [Multi-domain]  Cd Length: 367  Bit Score: 39.91  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 123 QVTILDIEKNKVLAEVPVGvepeGMGLspdgkiLVNTSETT---------NMAHFIDTKTFEV-IDNVLVDARPRFAEFS 192
Cdd:cd20784  251 YVSIWKMYDWKFVKEIDLG----GDGF------FVRTHPKTpylwvdngtDKLVLIDKKDLSVkKITPPKGKKAIHTEFS 320

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489697658 193 ADGKFLWVSA-EVGGTVSVIDVATRKVIKKITFKIP 227
Cdd:cd20784  321 GDGKYAYVSIyEKDGALVVYDTFTLKELKRYPANIP 356
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
 60-157 3.96e-03

NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. 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: 271324 [Multi-domain]  Cd Length: 285  Bit Score: 38.30  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  60 PRGVTLSKDDKeLFVCASDDDRIDVLDtATGKVVRSLRS-GPDPEQFI------LDQSGNpLYVANEDDSQVTILDIEKN 132
Cdd:cd14954  167 PRGVAVNPDGN-IVVSDFNNHRLQVFD-PDGQFLRFFGSeGSGNGQFKrprgvaVDDEGN-IIVADSGNHRVQVFSPDGE 243

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489697658 133 KVLAEVPVGVE------PEGMGLSPDGKILV 157
Cdd:cd14954  244 FLCSFGTEGNGegqfdrPSGVAVTPDGRIVV 274
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 194-223 4.11e-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: 34.58  E-value: 4.11e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 489697658  194 DGKFLWVSAEVGGTVSVIDVATRKVIKKIT 223
Cdd:TIGR02276   2 DGTKLYVTNSGSNTVSVIDTATNKVIATIP 31
8prop_heme-binding_NirN cd20777
eight-bladed heme d1-binding beta-propeller domain in dihydro-heme d1 dehydrogenase NirN; The ...
 100-273 5.16e-03

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: 38.50  E-value: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 100 PDP-EQFILDQSGNPLYVANEDDSQVTILDIEKNKVLAEVPVGVEPE-GMGLS--PDGKILVntsETTN----MAHFIDT 171
Cdd:cd20777  217 PAPlDDFFFDPDYRNLLGASRQGGGGQVIDLDVGRVIASLPLSGMPHlGSGIYwkRDGRRVM---ATPNlsrgVISVIDL 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 172 KTFEVIDNVLVDARPRFAEFSADGKFLWVSAEVG---GTVSVIDVATRKVIKKITfKIPSVTDEQiqpvgVRLTKDGTRA 248
Cdd:cd20777  294 QTWAIVKEIPTPGPGFFMRSHENSPYAWADVFMGpkrDKLHLIDKQTLEIVKTLR-PEPGKTAAH-----VEFTRDGRYA 367

                        170       180
                 ....*....|....*....|....*.
gi 489697658 249 FVAL-GPANRVAVVDAKTYEVQKYLP 273
Cdd:cd20777  368 LASVwEDDGALIVYDAHTLKEVKRLP 393
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 191-309 6.03e-03

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 36.96  E-value: 6.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 191 FSADGKFLWVSAEVGGT--VSVIDVATRKViKKITFKIPSVTDEQIQPvgvrltkDGTR-AFVALGPAN-RVAVVDAKTY 266
Cdd:COG0823   38 WSPDGRRIAFTSDRGGGpqIYVVDADGGEP-RRLTFGGGYNASPSWSP-------DGKRlAFVSRSDGRfDIYVLDLDGG 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489697658 267 EVQkylPVGQRVWQLAFTPDEKQLY--TTNGTSNDVSVIDVEGLK 309
Cdd:COG0823  110 APR---RLTDGPGSPSWSPDGRRIVfsSDRGGRPDLYVVDLDGRK 151
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
 7-297 7.75e-03

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 37.56  E-value: 7.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658   7 AGLGCALLAGVSLGSAGsaqafTAYVTNEKANTVSVIDTETLAVTgTWK-VGRRPRGVTLSKDDKelFVCASDDDRIDVL 85
Cdd:COG3386    3 ADAGFRLGEGPVWDPDG-----RLYWVDIPGGRIHRYDPDGGAVE-VFAePSGRPNGLAFDPDGR--LLVADHGRGLVRF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658  86 DTATGKVVRslrsgpdpeqfILDQSGNPLYVANEddsqvtildieknkvlaevpvgvepegMGLSPDGKILVntsetTNM 165
Cdd:COG3386   75 DPADGEVTV-----------LADEYGKPLNRPND---------------------------GVVDPDGRLYF-----TDM 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489697658 166 AHFIDTKTFEVIDN----VLVDARPRFA---EFSADGKFLWVSAEVGGTVSVIDV-ATRKVIKKITFKipSVTDEQIQPV 237
Cdd:COG3386  112 GEYLPTGALYRVDPdgslRVLADGLTFPngiAFSPDGRTLYVADTGAGRIYRFDLdADGTLGNRRVFA--DLPDGPGGPD 189

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489697658 238 GVRLTKDGtRAFVALGPANRVAVVDAKTYEVQKY-LPVgQRVWQLAF-TPDEKQLYTTNGTS 297
Cdd:COG3386  190 GLAVDADG-NLWVALWGGGGVVRFDPDGELLGRIeLPE-RRPTNVAFgGPDLRTLYVTTARS 249
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
 244-284 8.53e-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: 33.81  E-value: 8.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 489697658  244 DGTRAFVALGPANRVAVVDAKTYEVQKYLPVGQRVWQLAFT 284
Cdd:TIGR02276   2 DGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
 
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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