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Conserved domains on  [gi|464098413|dbj|BAN01295|]
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hypothetical protein YM304_09810 [Ilumatobacter coccineus YM16-304]

Protein Classification

YncE and beta_rpt_yvtn domain-containing protein( domain architecture ID 11465369)

YncE and beta_rpt_yvtn domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
258-473 1.85e-20

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


:

Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 90.52  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 258 TVIDPGTNSVVARVPVDGYTNDLHVHDGLVYVAVGHPDGVSPGTVRTIDPATRAFTGTSVTVGVIPAGMTVVD-DVLFVA 336
Cdd:COG3391    6 SLLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADgRRLYVA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 337 NAASNSVSVVDLASGTVVATISVGASPRGVARSATD--VYVANALGNTVSVIDPNDlGSGATSITVGLGPNDVAYGAGQI 414
Cdd:COG3391   86 NSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGgrLYVADSGNGRVSVIDTAT-GKVVATIPVGAGPHGIAVDPDGK 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 464098413 415 WVANTNFANTSGESSVSVIDPSTNTVTNTILLGEPTSPTAVAFDGTSVYLANYYSNTVD 473
Cdd:COG3391  165 RLYVANSGSNTVSVIVSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLYVANRGSNTSN 223
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
458-498 3.51e-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: 43.82  E-value: 3.51e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 464098413  458 DGTSVYLANYYSNTVDVIDPLFQTVVGTIPVGAGPWGAMFD 498
Cdd:TIGR02276   2 DGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
175-242 1.57e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 47.21  E-value: 1.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 464098413 175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPATIGPTGDVPHAMVTDGD 242
Cdd:NF038329 165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD 232
 
Name Accession Description Interval E-value
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
258-473 1.85e-20

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 90.52  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 258 TVIDPGTNSVVARVPVDGYTNDLHVHDGLVYVAVGHPDGVSPGTVRTIDPATRAFTGTSVTVGVIPAGMTVVD-DVLFVA 336
Cdd:COG3391    6 SLLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADgRRLYVA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 337 NAASNSVSVVDLASGTVVATISVGASPRGVARSATD--VYVANALGNTVSVIDPNDlGSGATSITVGLGPNDVAYGAGQI 414
Cdd:COG3391   86 NSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGgrLYVADSGNGRVSVIDTAT-GKVVATIPVGAGPHGIAVDPDGK 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 464098413 415 WVANTNFANTSGESSVSVIDPSTNTVTNTILLGEPTSPTAVAFDGTSVYLANYYSNTVD 473
Cdd:COG3391  165 RLYVANSGSNTVSVIVSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLYVANRGSNTSN 223
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
229-495 6.22e-16

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: 78.54  E-value: 6.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  229 PTGDVPHAMV--TDGDVVYVANfsnTGSSEVTVIDPGTNSVVARVPV--DGYTNDLHVHDGLVYVAvghpdGVSPGTVRT 304
Cdd:TIGR03866  38 PVGQRPRGITfsKDGKLLYVCA---SDSDTIQVIDPATGEVLHTLPSgpDPEQFALHPNGKILYIA-----NEDDALVTV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  305 IDPATRAFTGtSVTVGVIPAGMTVVDDVLFVANAA--SNSVSVVDLASGTVVATISVGASPRGVARSA--TDVYVANALG 380
Cdd:TIGR03866 110 IDIETRKVLA-QIDVGVEPEGMAVSPDGKIVVNTSetTNMAHWIDTATYEIVDNTLVDARPRFAEFTAdgKELWVSSEIG 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  381 NTVSVIDPND---LGSGATSITvGLGPNDV-AYGAGQIWVANTNFANTSGESSVSVIDPSTNTVTNTILLGEPTSPTAVA 456
Cdd:TIGR03866 189 GTVTVIDVATrkvIKKITFAIP-GVHPEKVqPVGIKLTKDGKTAFVALGPANRVAVVDAKTYEVLDYLLVGQRVWQLAFT 267
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 464098413  457 FDGTSVYLANYYSNTVDVIDPLFQTVVGTIPVGAGPWGA 495
Cdd:TIGR03866 268 PDESRLLTTNGVSNDVSVIDVAALKVIKSIKVGRLPWGV 306
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
231-513 8.29e-07

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: 51.18  E-value: 8.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 231 GDVPHAMVTDGDVVYVANFSNTGssEVTVIDPGTNSVVARVPVDGYTNDLHVHDGLVYVAVGHPDgvsPGTVRTIDPATR 310
Cdd:cd20718   58 GAQVHVVVFSPDGRFAYVISRDG--WLTKIDLYTLRPVASIRIGVNSRGIALSDDGKYVIAGNYE---PGHVVILDADTL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 311 AFTGTSVTVGVIPAGM------TVVD----DVLFVANAASNSVSVVDLASGT---VVATISVGASPRGVARSATDVYVAN 377
Cdd:cd20718  133 EPLKVIPTTGVNDDGIiesrvgAILEtppgPYFLVALKDAGSVWVIDYSDPDgnkVTDIGNIGRPLHDAFLDPDGRYFIV 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 378 AL--GNTVSVIDpNDLGSGATSITVGLGPNDvayGAGQIWVANTNFANTS-GESSVSVIDPSTNTVTNTI-LLGEPTSPT 453
Cdd:cd20718  213 ASqgSNTMWVLD-LKTGKVVARIPTGKTPHP---GPGATWGRKGVTATPHlGEGIVTVWDLDTWKPVKYIpTPGPGRFVR 288
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 464098413 454 A------VAFDGTsvyLANYYSNTVDVIDPLFQTVVGTIPVGAGPWgAMF-----DGTSVWVSNSLDNTVQ 513
Cdd:cd20718  289 ThpsspyVWADTV---FGPENADEIYVIDKETLKVVKTLIPKPGKR-ALHpeftrDGKYVYVSVWDGGEVV 355
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
458-498 3.51e-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: 43.82  E-value: 3.51e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 464098413  458 DGTSVYLANYYSNTVDVIDPLFQTVVGTIPVGAGPWGAMFD 498
Cdd:TIGR02276   2 DGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
175-242 1.57e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 47.21  E-value: 1.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 464098413 175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPATIGPTGDVPHAMVTDGD 242
Cdd:NF038329 165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
166-231 1.62e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 47.21  E-value: 1.62e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 464098413 166 GFFQPSDDVGAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPAtiGPTG 231
Cdd:NF038329 150 GPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA--GPAG 213
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
173-232 8.00e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 45.28  E-value: 8.00e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 173 DVGAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPAtiGPTGD 232
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ--GPAGK 178
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
170-232 2.33e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 43.74  E-value: 2.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 464098413 170 PSDDVGAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPAtiGPTGD 232
Cdd:NF038329 136 PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK--GPQGP 196
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
175-204 1.26e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 1.26e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 464098413  175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDP 204
Cdd:pfam01391  16 GPPGPPGPPGPPGPPGEPGPPGPPGPPGPP 45
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
178-231 7.11e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 38.73  E-value: 7.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 464098413 178 GPQGDQGPTGPDGTDGAVGPAG---ASGDPYRFDPADMRDERWELDPAKPAtiGPTG 231
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGdrgETGPAGPAGPPGPQGERGEKGPAGPQ--GEAG 171
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
174-202 8.17e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 38.73  E-value: 8.17e-03
                         10        20
                 ....*....|....*....|....*....
gi 464098413 174 VGAKGPQGDQGPTGPDGTDGAVGPAGASG 202
Cdd:NF038329 244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
175-231 8.46e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 38.73  E-value: 8.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 464098413 175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPAtiGPTG 231
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA--GPQG 174
 
Name Accession Description Interval E-value
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
258-473 1.85e-20

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 90.52  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 258 TVIDPGTNSVVARVPVDGYTNDLHVHDGLVYVAVGHPDGVSPGTVRTIDPATRAFTGTSVTVGVIPAGMTVVD-DVLFVA 336
Cdd:COG3391    6 SLLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADgRRLYVA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 337 NAASNSVSVVDLASGTVVATISVGASPRGVARSATD--VYVANALGNTVSVIDPNDlGSGATSITVGLGPNDVAYGAGQI 414
Cdd:COG3391   86 NSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGgrLYVADSGNGRVSVIDTAT-GKVVATIPVGAGPHGIAVDPDGK 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 464098413 415 WVANTNFANTSGESSVSVIDPSTNTVTNTILLGEPTSPTAVAFDGTSVYLANYYSNTVD 473
Cdd:COG3391  165 RLYVANSGSNTVSVIVSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLYVANRGSNTSN 223
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
163-391 5.98e-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: 5.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 163 DVNGFFQPSDDVGAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPATIGPTGDVPHAMVTDGD 242
Cdd:COG3391    1 ALVASSLLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 243 VVYVANfsnTGSSEVTVIDPGTNSVVARVPVDGYTNDLHVH--DGLVYVAVGhpdgvSPGTVRTIDPATRAFTGTsVTVG 320
Cdd:COG3391   81 RLYVAN---SGSGRVSVIDLATGKVVATIPVGGGPRGLAVDpdGGRLYVADS-----GNGRVSVIDTATGKVVAT-IPVG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 321 VIPAGMTVVDD--VLFVANAASNSVSVV----DLASGTVVATISVGASPRGVARSA--TDVYVAN-------ALGNTVSV 385
Cdd:COG3391  152 AGPHGIAVDPDgkRLYVANSGSNTVSVIvsviDTATGKVVATIPVGGGPVGVAVSPdgRRLYVANrgsntsnGGSNTVSV 231

                 ....*.
gi 464098413 386 IDPNDL 391
Cdd:COG3391  232 IDLATL 237
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
299-512 5.46e-16

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 77.43  E-value: 5.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 299 PGTVRTIDPATRAFTGTSVTVGVIPAGMTVVDDVLFVANAASNSVSVVDLASGTVVATISVGASPRGVARSATDVYVANA 378
Cdd:COG3391    8 LVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 379 LGNTVSVIDPNDlGSGATSITVGLGPNDVAYGA--GQIWVANTnfantsGESSVSVIDPSTNTVTNTILLGEptSPTAVA 456
Cdd:COG3391   88 GSGRVSVIDLAT-GKVVATIPVGGGPRGLAVDPdgGRLYVADS------GNGRVSVIDTATGKVVATIPVGA--GPHGIA 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 464098413 457 F--DGTSVYLANYYSNT----VDVIDPLFQTVVGTIPVGAGPWGAMF--DGTSVWVSNSLDNTV 512
Cdd:COG3391  159 VdpDGKRLYVANSGSNTvsviVSVIDTATGKVVATIPVGGGPVGVAVspDGRRLYVANRGSNTS 222
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
229-495 6.22e-16

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: 78.54  E-value: 6.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  229 PTGDVPHAMV--TDGDVVYVANfsnTGSSEVTVIDPGTNSVVARVPV--DGYTNDLHVHDGLVYVAvghpdGVSPGTVRT 304
Cdd:TIGR03866  38 PVGQRPRGITfsKDGKLLYVCA---SDSDTIQVIDPATGEVLHTLPSgpDPEQFALHPNGKILYIA-----NEDDALVTV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  305 IDPATRAFTGtSVTVGVIPAGMTVVDDVLFVANAA--SNSVSVVDLASGTVVATISVGASPRGVARSA--TDVYVANALG 380
Cdd:TIGR03866 110 IDIETRKVLA-QIDVGVEPEGMAVSPDGKIVVNTSetTNMAHWIDTATYEIVDNTLVDARPRFAEFTAdgKELWVSSEIG 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  381 NTVSVIDPND---LGSGATSITvGLGPNDV-AYGAGQIWVANTNFANTSGESSVSVIDPSTNTVTNTILLGEPTSPTAVA 456
Cdd:TIGR03866 189 GTVTVIDVATrkvIKKITFAIP-GVHPEKVqPVGIKLTKDGKTAFVALGPANRVAVVDAKTYEVLDYLLVGQRVWQLAFT 267
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 464098413  457 FDGTSVYLANYYSNTVDVIDPLFQTVVGTIPVGAGPWGA 495
Cdd:TIGR03866 268 PDESRLLTTNGVSNDVSVIDVAALKVIKSIKVGRLPWGV 306
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
334-512 1.06e-15

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: 77.77  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  334 FVANAASNSVSVVDLASGTVVATISVGASPRGV--ARSATDVYVANALGNTVSVIDP------NDLGSGATSITVGLGPN 405
Cdd:TIGR03866  14 YVSNEKDNTISVIDTATLKVTRTFPVGQRPRGItfSKDGKLLYVCASDSDTIQVIDPatgevlHTLPSGPDPEQFALHPN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  406 DvaygaGQIWVANTNfantsgESSVSVIDPSTNTVTNTILLGEPTSPTAVAFDGTSVYLANYYSNTVDVIDPLFQTVVGT 485
Cdd:TIGR03866  94 G-----KILYIANED------DALVTVIDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSETTNMAHWIDTATYEIVDN 162
                         170       180
                  ....*....|....*....|....*....
gi 464098413  486 IPVGAGPWGAMF--DGTSVWVSNSLDNTV 512
Cdd:TIGR03866 163 TLVDARPRFAEFtaDGKELWVSSEIGGTV 191
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
339-516 1.31e-14

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 73.57  E-value: 1.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 339 ASNSVSVVDLASGTVVATISVGASPRGVARSATDVYVANALGNTVSVIDPNDLGSGATSITVGLGPNDVAYGAGQIWVAN 418
Cdd:COG3391    1 ALVASSLLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 419 TNFANTSGESSVSVIDPSTNTVTNTILLGEPTSPTAVAFDGTSVYLANYYSNTVDVIDPLFQTVVGTIPVGAGPWGAMF- 497
Cdd:COG3391   81 RLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVd 160
                        170       180
                 ....*....|....*....|
gi 464098413 498 -DGTSVWVSNSLDNTVQRIL 516
Cdd:COG3391  161 pDGKRLYVANSGSNTVSVIV 180
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
225-487 1.61e-14

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 73.90  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 225 ATIGPTGDVPHAMVTDGD-VVYvanFSNTGSSEVTVIDPGTNSVVARVPVDG-YTNDLHV-HDGLVYVAvghpdGVSPGT 301
Cdd:COG4257   10 YPVPAPGSGPRDVAVDPDgAVW---FTDQGGGRIGRLDPATGEFTEYPLGGGsGPHGIAVdPDGNLWFT-----DNGNNR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 302 VRTIDPATRAFTGTSVTVGVI-PAGMTV-VDDVLFVANAASNSVSVVDLASGTV--VATISVGASPRGVARSATD-VYVA 376
Cdd:COG4257   82 IGRIDPKTGEITTFALPGGGSnPHGIAFdPDGNLWFTDQGGNRIGRLDPATGEVteFPLPTGGAGPYGIAVDPDGnLWVT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 377 NALGNTVSVIDPndlGSGATSI----TVGLGPNDVAYGA-GQIWVANTnfantsGESSVSVIDPSTNTVTNTILLGEPTS 451
Cdd:COG4257  162 DFGANAIGRIDP---DTGTLTEyalpTPGAGPRGLAVDPdGNLWVADT------GSGRIGRFDPKTGTVTEYPLPGGGAR 232
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 464098413 452 PTAVAFDGT-SVYLANYYSNTVDVIDPLFQTVVGTIP 487
Cdd:COG4257  233 PYGVAVDGDgRVWFAESGANRIVRFDPDTELTEYVLP 269
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
409-512 2.72e-08

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: 55.43  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  409 YGAGQIWVANTNfantsgESSVSVIDPSTNTVTNTILLGEPTSPTAVAFDGTSVYLANYYSNTVDVIDPLFQTVVGTIPV 488
Cdd:TIGR03866   8 AAAETAYVSNEK------DNTISVIDTATLKVTRTFPVGQRPRGITFSKDGKLLYVCASDSDTIQVIDPATGEVLHTLPS 81
                          90       100
                  ....*....|....*....|....*...
gi 464098413  489 GAGPwgAMF----DGTSVWVSNSLDNTV 512
Cdd:TIGR03866  82 GPDP--EQFalhpNGKILYIANEDDALV 107
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
360-515 6.77e-08

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 53.87  E-value: 6.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 360 GASPRGVARSATD-VYVANALGNTVSVIDPNDLGSGATSITVGLGPNDVAYGA-GQIWVANtnfantSGESSVSVIDPST 437
Cdd:COG4257   16 GSGPRDVAVDPDGaVWFTDQGGGRIGRLDPATGEFTEYPLGGGSGPHGIAVDPdGNLWFTD------NGNNRIGRIDPKT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 438 NTVTNTILLGEPTSPTAVAFDGT-SVYLANYYSNTVDVIDPLFQTV-VGTIPV-GAGPWGAMFDGT-SVWVSNSLDNTVQ 513
Cdd:COG4257   90 GEITTFALPGGGSNPHGIAFDPDgNLWFTDQGGNRIGRLDPATGEVtEFPLPTgGAGPYGIAVDPDgNLWVTDFGANAIG 169

                 ..
gi 464098413 514 RI 515
Cdd:COG4257  170 RI 171
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
370-494 4.14e-07

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: 51.96  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  370 ATDVYVANALGNTVSVIDpNDLGSGATSITVGLGPNDVAYGAGQiwvaNTNFANTSGESSVSVIDPSTNTVTNTILLGEP 449
Cdd:TIGR03866  10 AETAYVSNEKDNTISVID-TATLKVTRTFPVGQRPRGITFSKDG----KLLYVCASDSDTIQVIDPATGEVLHTLPSGPD 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 464098413  450 TSPTAVAFDGTSVYLANYYSNTVDVIDPLFQTVVGTIPVGAGPWG 494
Cdd:TIGR03866  85 PEQFALHPNGKILYIANEDDALVTVIDIETRKVLAQIDVGVEPEG 129
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
231-513 8.29e-07

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: 51.18  E-value: 8.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 231 GDVPHAMVTDGDVVYVANFSNTGssEVTVIDPGTNSVVARVPVDGYTNDLHVHDGLVYVAVGHPDgvsPGTVRTIDPATR 310
Cdd:cd20718   58 GAQVHVVVFSPDGRFAYVISRDG--WLTKIDLYTLRPVASIRIGVNSRGIALSDDGKYVIAGNYE---PGHVVILDADTL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 311 AFTGTSVTVGVIPAGM------TVVD----DVLFVANAASNSVSVVDLASGT---VVATISVGASPRGVARSATDVYVAN 377
Cdd:cd20718  133 EPLKVIPTTGVNDDGIiesrvgAILEtppgPYFLVALKDAGSVWVIDYSDPDgnkVTDIGNIGRPLHDAFLDPDGRYFIV 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 378 AL--GNTVSVIDpNDLGSGATSITVGLGPNDvayGAGQIWVANTNFANTS-GESSVSVIDPSTNTVTNTI-LLGEPTSPT 453
Cdd:cd20718  213 ASqgSNTMWVLD-LKTGKVVARIPTGKTPHP---GPGATWGRKGVTATPHlGEGIVTVWDLDTWKPVKYIpTPGPGRFVR 288
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 464098413 454 A------VAFDGTsvyLANYYSNTVDVIDPLFQTVVGTIPVGAGPWgAMF-----DGTSVWVSNSLDNTVQ 513
Cdd:cd20718  289 ThpsspyVWADTV---FGPENADEIYVIDKETLKVVKTLIPKPGKR-ALHpeftrDGKYVYVSVWDGGEVV 355
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
323-515 1.10e-06

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: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 50.36  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 323 PAGMTVV-DDVLFVANAASNSVSVVDLAsGTVVATISVGAS-------PRGVARSAT-DVYVANALGNTVSVIDPNdlGS 393
Cdd:cd14956   62 PRGLAVDkDGWLYVADYWGDRIQVFTLT-GELQTIGGSSGSgpgqfnaPRGVAVDADgNLYVADFGNQRIQKFDPD--GS 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 394 -----GATSITVG--LGPNDVAYGA-GQIWVANTNfantsgESSVSVIDPSTNTV----TNTILLGEPTSPTAVAFDGT- 460
Cdd:cd14956  139 flrqwGGTGIEPGsfNYPRGVAVDPdGTLYVADTY------NDRIQVFDNDGAFLrkwgGRGTGPGQFNYPYGIAIDPDg 212
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 464098413 461 SVYLANYYSNTVDVIDP--LFQTVVGTIPVGAG----PWGAMFDGT-SVWVSNSLDNTVQRI 515
Cdd:cd14956  213 NVFVADFGNNRIQKFTAdgTFLTSWGSPGTGPGqfknPWGVVVDADgTVYVADSNNNRVQRF 274
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
362-515 1.55e-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: 49.62  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 362 SPRGVA-RSATDVYVANALGNTVSVIDPN-----DLGSGATSITVGLGPNDVAYGA-GQIWVANTnfantsGESSVSVID 434
Cdd:cd05819    9 NPQGIAvDSSGNIYVADTGNNRIQVFDPDgnfitSFGSFGSGDGQFNEPAGVAVDSdGNLYVADT------GNHRIQKFD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 435 PSTNTVTNTILLGEPT----SPTAVAFDGT-SVYLANYYSNTVDVIDP--LFQTVVGTIPVGAG----PWGAMFDGT-SV 502
Cdd:cd05819   83 PDGNFLASFGGSGDGDgefnGPRGIAVDSSgNIYVADTGNHRIQKFDPdgEFLTTFGSGGSGPGqfngPTGVAVDSDgNI 162
                        170
                 ....*....|...
gi 464098413 503 WVSNSLDNTVQRI 515
Cdd:cd05819  163 YVADTGNHRIQVF 175
COG5276 COG5276
Uncharacterized secreted protein, contains LVIVD repeats, choice-of-anchor domain [Function ...
229-477 3.11e-06

Uncharacterized secreted protein, contains LVIVD repeats, choice-of-anchor domain [Function unknown];


Pssm-ID: 444087 [Multi-domain]  Cd Length: 320  Bit Score: 49.17  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 229 PTGDVPHAMVTDGDVVYVANFSNtGSSEVTVIDPGTNSVVARVPV-DGYTNDLHVHDGLVYVAVGHPDGVSPGTVRtiDP 307
Cdd:COG5276   17 DLGGRANDVWVSGEYAYVAGGSN-GLAIVDVSDPANPVLVGSLPTpGGTWRDVKVSGDYLYVASEGSEGLQIFDIS--DP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 308 ATRAFTGTSVTVGVIPAGMTVVDDVLFVANAASNSVSVVDL---ASGTVVATISVG--ASPRGVARSATDVYVANAlGNT 382
Cdd:COG5276   94 ANPKLVGRYDTGGSGAHNIAVDGNYAYVAGGSDNGLVIVDIsdpTNPVLVGRYSLPgqAYLHDVQVVGDYAYVADW-EDG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 383 VSVIDPND------LGSGATSiTVGLGPNDVAYGAGQIWVANTNFANTSGESSVSVIDPSTNTVTNTILLGEPTSPTAVA 456
Cdd:COG5276  173 LVIVDVSDpsnpklIGSYDYS-PPGYTHTAVPVEDGNYAYVGDELGGPNGLRILDVSDPANPVLIGTYPTPGADGAHNLY 251
                        250       260
                 ....*....|....*....|...
gi 464098413 457 FDGTSVYLANYYS--NTVDVIDP 477
Cdd:COG5276  252 VSGNYLYVADYNAglRVLDISDP 274
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
458-498 3.51e-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: 43.82  E-value: 3.51e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 464098413  458 DGTSVYLANYYSNTVDVIDPLFQTVVGTIPVGAGPWGAMFD 498
Cdd:TIGR02276   2 DGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
175-242 1.57e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 47.21  E-value: 1.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 464098413 175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPATIGPTGDVPHAMVTDGD 242
Cdd:NF038329 165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
166-231 1.62e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 47.21  E-value: 1.62e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 464098413 166 GFFQPSDDVGAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPAtiGPTG 231
Cdd:NF038329 150 GPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA--GPAG 213
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
333-367 4.84e-05

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: 40.74  E-value: 4.84e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 464098413  333 LFVANAASNSVSVVDLASGTVVATISVGASPRGVA 367
Cdd:TIGR02276   6 LYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVA 40
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
216-477 5.92e-05

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


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 45.28  E-value: 5.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 216 RWELDPA----KPATIGPTGDVPHAMVT--DGDVVYVANFSNTGSseVTV--IDPGTNS--VVARVPVDGytndlhvhDG 285
Cdd:COG2706   25 VFRLDTAtgelTLLGLVAALGNPSFLALspDGRFLYAVNEVDDGG--VSAfrIDPADGTltLLNTVSSGG--------AS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 286 LVYVAVgHPDG--------------VSP----GTVRTIdPATRAFTGTSVTVGVIP---AGMTVVD---DVLFVANAASN 341
Cdd:COG2706   95 PCHLSV-DPDGrflfvanygggsvsVFPidadGSLGEP-VQVIQHEGSGPNPERQEgphAHSVVFDpdgRFLYVPDLGTD 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 342 SVSV--VDLASGTVVATISV----GASPRGVARSATD--VYVANALGNTVSVIDPNDLGSGATSI-TVGLGPNDVaygAG 412
Cdd:COG2706  173 RIYVyrLDPATGKLPEPPEVslppGSGPRHLAFHPNGrfAYVINELDSTVSVYAYDAATGTLTLIqTVSTLPEDF---TG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 413 QIWVA------NTNFANTS--GESSVSV--IDPSTNTVTntiLLGE-PTS---PTAVAFD--GTSVYLANYYSNTVDV-- 474
Cdd:COG2706  250 ENWAAdihispDGRFLYVSnrGHNSIAVfaIDADGGKLT---LVGHvPTGgkwPRDFAIDpdGRFLLVANQKSDNITVfr 326

                 ...
gi 464098413 475 IDP 477
Cdd:COG2706  327 IDA 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
173-232 8.00e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 45.28  E-value: 8.00e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 173 DVGAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPAtiGPTGD 232
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ--GPAGK 178
COG5276 COG5276
Uncharacterized secreted protein, contains LVIVD repeats, choice-of-anchor domain [Function ...
268-489 8.86e-05

Uncharacterized secreted protein, contains LVIVD repeats, choice-of-anchor domain [Function unknown];


Pssm-ID: 444087 [Multi-domain]  Cd Length: 320  Bit Score: 44.55  E-value: 8.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 268 VARVPVDGYTNDLHVHDGLVYVAVGhPDGVSpgTVRTIDPATRAFTGTSVTVGVIPAGMTVVDDVLFVANAASNSVSVVD 347
Cdd:COG5276   13 LGNVDLGGRANDVWVSGEYAYVAGG-SNGLA--IVDVSDPANPVLVGSLPTPGGTWRDVKVSGDYLYVASEGSEGLQIFD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 348 L---ASGTVVATISVGASprGVARSATD---VYVANALGNTVSVID------PNDLGSGATSITVGLgpNDVAYGAGQIW 415
Cdd:COG5276   90 IsdpANPKLVGRYDTGGS--GAHNIAVDgnyAYVAGGSDNGLVIVDisdptnPVLVGRYSLPGQAYL--HDVQVVGDYAY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 416 VAntnfANTSGESSVSVIDPSTNTVTNTILLGEP--TSPTAVAFDGTSVYLANYYSNT-----VDVIDPLFQTVVGTIPV 488
Cdd:COG5276  166 VA----DWEDGLVIVDVSDPSNPKLIGSYDYSPPgyTHTAVPVEDGNYAYVGDELGGPnglriLDVSDPANPVLIGTYPT 241

                 .
gi 464098413 489 G 489
Cdd:COG5276  242 P 242
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
323-475 1.48e-04

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


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 43.46  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 323 PAGMTV-VDDVLFVANAASNSVSVVDlASGTVVATISVGAS-------PRGVA-RSATDVYVANALGNTVSVIDPND--- 390
Cdd:cd05819  104 PRGIAVdSSGNIYVADTGNHRIQKFD-PDGEFLTTFGSGGSgpgqfngPTGVAvDSDGNIYVADTGNHRIQVFDPDGnfl 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 391 --LGSGATSITVGLGPNDVAY-GAGQIWVANTNFantsgeSSVSVIDPSTNTVTNT----ILLGEPTSPTAVAFDGT-SV 462
Cdd:cd05819  183 ttFGSTGTGPGQFNYPTGIAVdSDGNIYVADSGN------NRVQVFDPDGAGFGGNgnflGSDGQFNRPSGLAVDSDgNL 256
                        170
                 ....*....|...
gi 464098413 463 YLANYYSNTVDVI 475
Cdd:cd05819  257 YVADTGNNRIQVF 269
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
219-367 2.12e-04

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: 43.49  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  219 LDPAKPATIG--PTGDVPH--AMVTDGDVVYVANFSNtgsSEVTVIDPGTNSVVARVPV-----------DG-------- 275
Cdd:TIGR03866  68 IDPATGEVLHtlPSGPDPEqfALHPNGKILYIANEDD---ALVTVIDIETRKVLAQIDVgvepegmavspDGkivvntse 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  276 YTNDLH---------VHDGLV--------YVAVGHPDGVSP---GTVRTIDPATRAFTGT------SVT------VGVI- 322
Cdd:TIGR03866 145 TTNMAHwidtatyeiVDNTLVdarprfaeFTADGKELWVSSeigGTVTVIDVATRKVIKKitfaipGVHpekvqpVGIKl 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  323 ------------PAGMTVVDDV--------------------------LFVANAASNSVSVVDLASGTVVATISVGASPR 364
Cdd:TIGR03866 225 tkdgktafvalgPANRVAVVDAktyevldyllvgqrvwqlaftpdesrLLTTNGVSNDVSVIDVAALKVIKSIKVGRLPW 304

                  ...
gi 464098413  365 GVA 367
Cdd:TIGR03866 305 GVV 307
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
170-232 2.33e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 43.74  E-value: 2.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 464098413 170 PSDDVGAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPAtiGPTGD 232
Cdd:NF038329 136 PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK--GPQGP 196
COG5276 COG5276
Uncharacterized secreted protein, contains LVIVD repeats, choice-of-anchor domain [Function ...
220-420 6.72e-04

Uncharacterized secreted protein, contains LVIVD repeats, choice-of-anchor domain [Function unknown];


Pssm-ID: 444087 [Multi-domain]  Cd Length: 320  Bit Score: 41.85  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 220 DPAKP---ATIGPTGDVPHAMVTDGDVVYVANFSNTGSSEVTVIDPGTNSVVARVPVDG--YTNDLHVHDGLVYVAVGHp 294
Cdd:COG5276   92 DPANPklvGRYDTGGSGAHNIAVDGNYAYVAGGSDNGLVIVDISDPTNPVLVGRYSLPGqaYLHDVQVVGDYAYVADWE- 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 295 DGV---------SPGTVRTIDPATRAFTGTSVTVgvipagmtVVDDVLFVAN--AASNSVSVVD---LASGTVVATISVG 360
Cdd:COG5276  171 DGLvivdvsdpsNPKLIGSYDYSPPGYTHTAVPV--------EDGNYAYVGDelGGPNGLRILDvsdPANPVLIGTYPTP 242
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 464098413 361 --ASPRGVARSATDVYVANAlGNTVSVID------PNDLGSGATSITVGLGPNDVA-YGAGQIWVANTN 420
Cdd:COG5276  243 gaDGAHNLYVSGNYLYVADY-NAGLRVLDisdpsnPVEIGYFDTYDAGFGGAWDVYvDPGGYIYVSDIN 310
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
175-204 1.26e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 1.26e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 464098413  175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDP 204
Cdd:pfam01391  16 GPPGPPGPPGPPGPPGEPGPPGPPGPPGPP 45
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
175-204 1.43e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 1.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 464098413  175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDP 204
Cdd:pfam01391  25 GPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
175-204 1.66e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 1.66e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 464098413  175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDP 204
Cdd:pfam01391  22 GPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
177-366 1.79e-03

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 40.69  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  177 KGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRdERWELDPAKPATIGPTgdvphamvTDGDVVYVAnfsnTGSSE 256
Cdd:TIGR03300  50 DGVGHYYLRLQPAVAGGKVYAADADGTVAALDAETGK-RLWRVDLDERLSGGVG--------ADGGLVFVG----TEKGE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413  257 VTVIDPGTNSVVARVPVDG--YTNDLhVHDGLVyvavghpdgvspgTVRTIDPATRAFTGTS-----VTVGVIP------ 323
Cdd:TIGR03300 117 VIALDAEDGKELWRAKLSSevLSPPL-VANGLV-------------VVRTNDGRLTALDAATgerlwTYSRVTPpltlrg 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 464098413  324 -AGMTVVDDVLFVANaASNSVSVVDLASGTVVATISVgASPRGV 366
Cdd:TIGR03300 183 sASPVIADGGVLVGF-AGGKLVALDLQTGQPLWEQRV-ALPKGR 224
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
175-204 4.91e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 4.91e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 464098413  175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDP 204
Cdd:pfam01391  19 GPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
175-204 5.70e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 5.70e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 464098413  175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDP 204
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPP 36
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
175-204 5.93e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 5.93e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 464098413  175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDP 204
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEP 33
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
330-476 6.60e-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: 38.33  E-value: 6.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464098413 330 DDVLFVANAASNSVSVVDLASGTVVATISVGASPRGVARSATDVYVANALGNTVSVIDPNDlgsgaTSITV--------G 401
Cdd:COG3386   18 DGRLYWVDIPGGRIHRYDPDGGAVEVFAEPSGRPNGLAFDPDGRLLVADHGRGLVRFDPAD-----GEVTVladeygkpL 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 464098413 402 LGPNDVAYGA-GQIWVanTNFANTSGESSVSVIDPSTNTvtnTILLGEPTSPTAVAF--DGTSVYLANYYSNTVDVID 476
Cdd:COG3386   93 NRPNDGVVDPdGRLYF--TDMGEYLPTGALYRVDPDGSL---RVLADGLTFPNGIAFspDGRTLYVADTGAGRIYRFD 165
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
178-231 7.11e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 38.73  E-value: 7.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 464098413 178 GPQGDQGPTGPDGTDGAVGPAG---ASGDPYRFDPADMRDERWELDPAKPAtiGPTG 231
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGdrgETGPAGPAGPPGPQGERGEKGPAGPQ--GEAG 171
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
175-204 7.29e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 34.78  E-value: 7.29e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 464098413  175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDP 204
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPP 30
beta_rpt_yvtn TIGR02276
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ...
240-276 7.77e-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: 7.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 464098413  240 DGDVVYVANfsnTGSSEVTVIDPGTNSVVARVPVDGY 276
Cdd:TIGR02276   2 DGTKLYVTN---SGSNTVSVIDTATNKVIATIPVGGY 35
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
174-202 8.17e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 38.73  E-value: 8.17e-03
                         10        20
                 ....*....|....*....|....*....
gi 464098413 174 VGAKGPQGDQGPTGPDGTDGAVGPAGASG 202
Cdd:NF038329 244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
175-231 8.46e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 38.73  E-value: 8.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 464098413 175 GAKGPQGDQGPTGPDGTDGAVGPAGASGDPYRFDPADMRDERWELDPAKPAtiGPTG 231
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA--GPQG 174
 
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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