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Conserved domains on  [gi|148672943|gb|EDL04890|]
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procollagen, type X, alpha 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 545-680 5.93e-67

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


:

Pssm-ID: 128420  Cd Length: 135  Bit Score: 216.01  E-value: 5.93e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943   545 GVTGMPVSAFTVILSKAYPAVGAPIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVHVKGTHVWVGLYKNGTPTMYT 624
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148672943   625 YDEYSKGYLDQASGSAIMELTENDQVWLQLPNaESNGLYSSEYVHSSFSGFLVAPM 680
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPD-EKNGLYAGEYVDSTFSGFLLFPD 135
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 279-478 4.89e-28

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: 117.70  E-value: 4.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 279 GEKGHPGAPGIAGPPGAPGfgKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHGIP 358
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQG--PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 359 GAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGL--NGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHN 436
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148672943 437 GEAGPRGEPGIPGtrgptgppgvpgfpgSKGDPGNPGAPGPA 478
Cdd:NF038329 275 GKDGERGPVGPAG---------------KDGQNGKDGLPGKD 301
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 545-680 5.93e-67

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


Pssm-ID: 128420  Cd Length: 135  Bit Score: 216.01  E-value: 5.93e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943   545 GVTGMPVSAFTVILSKAYPAVGAPIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVHVKGTHVWVGLYKNGTPTMYT 624
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148672943   625 YDEYSKGYLDQASGSAIMELTENDQVWLQLPNaESNGLYSSEYVHSSFSGFLVAPM 680
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPD-EKNGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 553-677 9.78e-50

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


Pssm-ID: 395310 [Multi-domain]  Cd Length: 126  Bit Score: 169.39  E-value: 9.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943  553 AFTVILSKAYPAVGA-PIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVH-VKGTHVWVGLYKNGTPTMYTYDEYSK 630
Cdd:pfam00386   1 AFSAGRTTGLTAPNEqPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 148672943  631 GYLDQASGSAIMELTENDQVWLQLPNAesNGLYSSEY-VHSSFSGFLV 677
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTGY--NGLYYDGSdTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 279-478 4.89e-28

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: 117.70  E-value: 4.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 279 GEKGHPGAPGIAGPPGAPGfgKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHGIP 358
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQG--PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 359 GAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGL--NGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHN 436
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148672943 437 GEAGPRGEPGIPGtrgptgppgvpgfpgSKGDPGNPGAPGPA 478
Cdd:NF038329 275 GKDGERGPVGPAG---------------KDGQNGKDGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 155-426 3.96e-27

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: 115.00  E-value: 3.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 155 PGKPGQQGLTGAPGPRGFPGEKGAQGAPGVNGRKGETGY-GSPGRPGERGLpgpqgpigppgpsgvgrRGENGFPGQPGI 233
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEkGPAGPQGEAGP-----------------QGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 234 KGDRGFPGEMGPSgppgpqgppgkqgregiGKPGAIGSPGQPGIPGEKGHPGAPGIAGPPGAPGfgkqglpglRGQRGPA 313
Cdd:NF038329 185 KGPAGEKGPQGPR-----------------GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG---------DGQQGPD 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 314 GLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGipgnhgipgAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGE 393
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG---------KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309

                        250       260       270
                 ....*....|....*....|....*....|...
gi 148672943 394 PGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGP 426
Cdd:NF038329 310 DGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 161-434 4.55e-27

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: 114.62  E-value: 4.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 161 QGLTGAPGPRGFPGEKGAQGAPGVNGRKGEtgygspgrpgerglpgpqgpigppgpsgvgrRGENGFPGQPGIKGDRgfp 240
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGE-------------------------------RGEKGPAGPQGEAGPQ--- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 241 gemgpsgppgpqgppgkqgregiGKPGAIGSPGQPGIPGEKGHPGAPGIAGPPGAPgfGKQGLPGLRGQRGPAGLPGAPG 320
Cdd:NF038329 174 -----------------------GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ--GPAGPAGPDGEAGPAGEDGPAG 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 321 AKGErgpaGHPGEPGLPGSPGNMGPQGPKGIPGNHGIPGAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPK 400
Cdd:NF038329 229 PAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304

                        250       260       270
                 ....*....|....*....|....*....|....
gi 148672943 401 GNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPG 434
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 124-408 5.60e-22

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: 99.21  E-value: 5.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 124 GHKGDIGPAGLPgprgppgppgipgpagisvpGKPGQQGLTGAPGPRGFPGEKGAQGAPGVNGRKGETG-YGSPGRPGEr 202
Cdd:NF038329 123 GPAGPAGPAGEQ--------------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpQGPAGKDGE- 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 203 glpgpqgpigppgpsgvgrRGENGFPGQPGIKGDRgfpgemgpsgppgpqgppgkqgregiGKPGAIGSPGQPGIPGEKG 282
Cdd:NF038329 182 -------------------AGAKGPAGEKGPQGPR--------------------------GETGPAGEQGPAGPAGPDG 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 283 HPGAPGIAGPPGAPGFGKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHgipGAKG 362
Cdd:NF038329 217 EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKD---GQNG 293

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148672943 363 EIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQ 408
Cdd:NF038329 294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 308-481 2.94e-19

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: 91.12  E-value: 2.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 308 GQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNhgiPGAKGEIGLVGPAGPPGARGARGPPGLDGK 387
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP---AGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 388 TGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGpvgakgvpghNGEAGPRGEPGipgtrgptgppgvpgfpgskg 467
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------DGQQGPDGDPG--------------------- 242

                        170
                 ....*....|....
gi 148672943 468 DPGNPGAPGPAGIA 481
Cdd:NF038329 243 PTGEDGPQGPDGPA 256
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
316-482 1.57e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 54.27  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 316 PGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHGIPGAKGEIGLVGPAGPpgaRGARGPPGLDGKTGYPGEPG 395
Cdd:COG5164    3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGN---TGGTRPAGNQGATGPAQNQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 396 LNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTRGPTGPPGVPGFPGSKGDPGNPGAP 475
Cdd:COG5164   80 GTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPP 159


                 ....*..
gi 148672943 476 GPAGIAT 482
Cdd:COG5164  160 GDGGSTT 166
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 302-353 1.89e-07

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: 48.26  E-value: 1.89e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 148672943  302 GLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPG 353
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 289-479 4.05e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 4.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 289 IAGPPGAPGFGKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGlPGSPGNMGPQGPKGIPGNHGIPGAKGEIGLVG 368
Cdd:PRK07764 588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAA-APAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 369 PAGPPGARGARGppgldgkTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGH-NGEAGPRGEPGI 447
Cdd:PRK07764 667 DGWPAKAGGAAP-------AAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQgASAPSPAADDPV 739

                        170       180       190
                 ....*....|....*....|....*....|..
gi 148672943 448 PGTRGPTGPPGVPGFPGSKGDPGNPGAPGPAG 479
Cdd:PRK07764 740 PLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPA 771
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 545-680 5.93e-67

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


Pssm-ID: 128420  Cd Length: 135  Bit Score: 216.01  E-value: 5.93e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943   545 GVTGMPVSAFTVILSKAYPAVGAPIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVHVKGTHVWVGLYKNGTPTMYT 624
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148672943   625 YDEYSKGYLDQASGSAIMELTENDQVWLQLPNaESNGLYSSEYVHSSFSGFLVAPM 680
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPD-EKNGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 553-677 9.78e-50

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


Pssm-ID: 395310 [Multi-domain]  Cd Length: 126  Bit Score: 169.39  E-value: 9.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943  553 AFTVILSKAYPAVGA-PIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVH-VKGTHVWVGLYKNGTPTMYTYDEYSK 630
Cdd:pfam00386   1 AFSAGRTTGLTAPNEqPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 148672943  631 GYLDQASGSAIMELTENDQVWLQLPNAesNGLYSSEY-VHSSFSGFLV 677
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTGY--NGLYYDGSdTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 279-478 4.89e-28

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: 117.70  E-value: 4.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 279 GEKGHPGAPGIAGPPGAPGfgKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHGIP 358
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQG--PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 359 GAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGL--NGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHN 436
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148672943 437 GEAGPRGEPGIPGtrgptgppgvpgfpgSKGDPGNPGAPGPA 478
Cdd:NF038329 275 GKDGERGPVGPAG---------------KDGQNGKDGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 155-426 3.96e-27

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: 115.00  E-value: 3.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 155 PGKPGQQGLTGAPGPRGFPGEKGAQGAPGVNGRKGETGY-GSPGRPGERGLpgpqgpigppgpsgvgrRGENGFPGQPGI 233
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEkGPAGPQGEAGP-----------------QGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 234 KGDRGFPGEMGPSgppgpqgppgkqgregiGKPGAIGSPGQPGIPGEKGHPGAPGIAGPPGAPGfgkqglpglRGQRGPA 313
Cdd:NF038329 185 KGPAGEKGPQGPR-----------------GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG---------DGQQGPD 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 314 GLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGipgnhgipgAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGE 393
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG---------KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309

                        250       260       270
                 ....*....|....*....|....*....|...
gi 148672943 394 PGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGP 426
Cdd:NF038329 310 DGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 161-434 4.55e-27

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: 114.62  E-value: 4.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 161 QGLTGAPGPRGFPGEKGAQGAPGVNGRKGEtgygspgrpgerglpgpqgpigppgpsgvgrRGENGFPGQPGIKGDRgfp 240
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGE-------------------------------RGEKGPAGPQGEAGPQ--- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 241 gemgpsgppgpqgppgkqgregiGKPGAIGSPGQPGIPGEKGHPGAPGIAGPPGAPgfGKQGLPGLRGQRGPAGLPGAPG 320
Cdd:NF038329 174 -----------------------GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ--GPAGPAGPDGEAGPAGEDGPAG 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 321 AKGErgpaGHPGEPGLPGSPGNMGPQGPKGIPGNHGIPGAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPK 400
Cdd:NF038329 229 PAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304

                        250       260       270
                 ....*....|....*....|....*....|....
gi 148672943 401 GNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPG 434
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 124-408 5.60e-22

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: 99.21  E-value: 5.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 124 GHKGDIGPAGLPgprgppgppgipgpagisvpGKPGQQGLTGAPGPRGFPGEKGAQGAPGVNGRKGETG-YGSPGRPGEr 202
Cdd:NF038329 123 GPAGPAGPAGEQ--------------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpQGPAGKDGE- 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 203 glpgpqgpigppgpsgvgrRGENGFPGQPGIKGDRgfpgemgpsgppgpqgppgkqgregiGKPGAIGSPGQPGIPGEKG 282
Cdd:NF038329 182 -------------------AGAKGPAGEKGPQGPR--------------------------GETGPAGEQGPAGPAGPDG 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 283 HPGAPGIAGPPGAPGFGKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHgipGAKG 362
Cdd:NF038329 217 EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKD---GQNG 293

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148672943 363 EIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQ 408
Cdd:NF038329 294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 308-481 2.94e-19

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: 91.12  E-value: 2.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 308 GQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNhgiPGAKGEIGLVGPAGPPGARGARGPPGLDGK 387
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP---AGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 388 TGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGpvgakgvpghNGEAGPRGEPGipgtrgptgppgvpgfpgskg 467
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------DGQQGPDGDPG--------------------- 242

                        170
                 ....*....|....
gi 148672943 468 DPGNPGAPGPAGIA 481
Cdd:NF038329 243 PTGEDGPQGPDGPA 256
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
316-482 1.57e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 54.27  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 316 PGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHGIPGAKGEIGLVGPAGPpgaRGARGPPGLDGKTGYPGEPG 395
Cdd:COG5164    3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGN---TGGTRPAGNQGATGPAQNQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 396 LNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTRGPTGPPGVPGFPGSKGDPGNPGAP 475
Cdd:COG5164   80 GTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPP 159


                 ....*..
gi 148672943 476 GPAGIAT 482
Cdd:COG5164  160 GDGGSTT 166
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 302-353 1.89e-07

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: 48.26  E-value: 1.89e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 148672943  302 GLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPG 353
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 299-353 6.42e-07

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: 46.72  E-value: 6.42e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148672943  299 GKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPG 353
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 264-325 1.75e-06

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: 45.56  E-value: 1.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148672943  264 GKPGAIGSPGQPGIPGEKGHPGAPGIAGPPGAPGFgkqglPGLRGQRGPAGLPGAPGAKGER 325
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP-----PGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 308-363 3.41e-06

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: 44.79  E-value: 3.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148672943  308 GQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHGIPGAKGE 363
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 289-479 4.05e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 4.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 289 IAGPPGAPGFGKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGlPGSPGNMGPQGPKGIPGNHGIPGAKGEIGLVG 368
Cdd:PRK07764 588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAA-APAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 369 PAGPPGARGARGppgldgkTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGH-NGEAGPRGEPGI 447
Cdd:PRK07764 667 DGWPAKAGGAAP-------AAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQgASAPSPAADDPV 739

                        170       180       190
                 ....*....|....*....|....*....|..
gi 148672943 448 PGTRGPTGPPGVPGFPGSKGDPGNPGAPGPAG 479
Cdd:PRK07764 740 PLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPA 771
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 314-370 7.77e-06

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: 43.64  E-value: 7.77e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148672943  314 GLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKGIPGNHGIPGAKGEIGLVGPA 370
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 282-340 9.73e-06

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: 43.25  E-value: 9.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148672943  282 GHPGAPGIAGPPGAPGFgkQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSP 340
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGP--PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 291-348 9.93e-06

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: 43.25  E-value: 9.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 148672943  291 GPPGAPGfgKQGLPGLRGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGP 348
Cdd:pfam01391   1 GPPGPPG--PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 371-427 1.21e-05

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: 43.25  E-value: 1.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148672943  371 GPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPV 427
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 365-419 1.23e-05

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: 42.87  E-value: 1.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148672943  365 GLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPG 419
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 347-403 1.28e-05

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: 42.87  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148672943  347 GPKGIPGNHGIPGAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNP 403
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 368-424 1.84e-05

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: 42.48  E-value: 1.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148672943  368 GPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPV 424
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 389-445 2.16e-05

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: 42.48  E-value: 2.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148672943  389 GYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEP 445
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 362-418 2.90e-05

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: 42.10  E-value: 2.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148672943  362 GEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTP 418
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 329-383 3.26e-05

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: 41.71  E-value: 3.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148672943  329 GHPGEPGLPGSPGNMGPQGPKGIPGNHGIPGAKGEIGLVGPAGPPGARGARGPPG 383
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 338-394 3.36e-05

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: 41.71  E-value: 3.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148672943  338 GSPGNMGPQGPKGIPGNHGIPGAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEP 394
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 392-446 4.46e-05

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: 41.33  E-value: 4.46e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148672943  392 GEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPG 446
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 265-423 8.95e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 8.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 265 KPGAIGSPGQPGIPGEKGHPGAPGIAGPPGAPGFGKQGLPGLRGQRGPA--GLPGAPGAKGERGPAGHPGEPGLPGSPGN 342
Cdd:PRK07764 614 RPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAsdGGDGWPAKAGGAAPAAPPPAPAPAAPAAP 693

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 343 MGPQGPKGIPGNHGIPGAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRG 422
Cdd:PRK07764 694 AGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773


                 .
gi 148672943 423 P 423
Cdd:PRK07764 774 P 774
PHA03169 PHA03169
hypothetical protein; Provisional
 279-451 2.97e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.81  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 279 GEKGHPGAPGIAGPPGAPGFGKQGLPGLRGQRGPAGL-PGAPGAKGERGPAGHPGEPGLPGSPGnmgpQGPKGIPGNHGI 357
Cdd:PHA03169  82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLsPENTSGSSPESPASHSPPPSPPSHPG----PHEPAPPESHNP 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 358 PGAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPglPGQKGD-PGVGGTPGLRGPVGPVGAKGVPGHN 436
Cdd:PHA03169 158 SPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPP--PQSPPDePGEPQSPTPQQAPSPNTQQAVEHED 235

                        170
                 ....*....|....*.
gi 148672943 437 GEAGP-RGEPGIPGTR 451
Cdd:PHA03169 236 EPTEPeREGPPFPGHR 251
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 264-446 4.50e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 264 GKPGAIGSPGQPGIPGEKGHPGAPGIAGPPGAPGFGKQGlpglrGQRGPAGLPGAPGAKGERGPAGHPGEPGLPGSPGNM 343
Cdd:PRK07764 592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPA-----GAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 344 GPQGPK-GIPGNHGIPGAKGEIGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQK-GDPGVGGTPGLR 421
Cdd:PRK07764 667 DGWPAKaGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPaADDPVPLPPEPD 746

                        170       180
                 ....*....|....*....|....*
gi 148672943 422 GPVGPVGAKGVPGHNGEAGPRGEPG 446
Cdd:PRK07764 747 DPPDPAGAPAQPPPPPAPAPAAAPA 771
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 268-404 9.71e-04

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 42.36  E-value: 9.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 268 AIGSPGQPGIPGEKGHPGaPGIAGPPGAPGFGKQGLPGLRGQRGPAglPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQG 347
Cdd:COG5180  356 PPAEEAVPGKPLEQGAPR-PGSSGGDGAPFQPPNGAPQPGLGRRGA--PGPPMGAGDLVQAALDGGGRETASLGGAAGGA 432

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148672943 348 PKGIPGNHGIPGAKGEIGLVGPAGPPGARG-----ARGPPGLDGKTGYPGEPGLNGPKGNPG 404
Cdd:COG5180  433 GQGPKADFVPGDAESVSGPAGLADQAGAAAstamaDFVAPVTDATPVDVADVLGVRPDAILG 494
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 266-478 2.92e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 40.76  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943  266 PGAIGSPGQPGIPGEKGHPGAPGIAGPPGAPGFGKQGLPGLRGQRGPAGLPGAPG--------AKGERGPAGHPGEPGLP 337
Cdd:pfam09606 174 MGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGmnpqqmggAPNQVAMQQQQPQQQGQ 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943  338 GSPGNMGPQGPKGIPGnhGIPGAKGEIGLVGPAGPPGARGARGPPGLdgktgypgepglnGPKGNPGLPGQKGDPGVGGT 417
Cdd:pfam09606 254 QSQLGMGINQMQQMPQ--GVGGGAGQGGPGQPMGPPGQQPGAMPNVM-------------SIGDQNNYQQQQTRQQQQQQ 318

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148672943  418 PGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTRGPTGPPGVPGFPGSKGDPGNPGAPGPA 478
Cdd:pfam09606 319 GGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPV 379
PPE COG5651
PPE-repeat protein [Function unknown];
273-443 9.61e-03

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 38.72  E-value: 9.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 273 GQPGIPGEKGHPGAPGIAGPPGAPGFGKQGLPGLRGQRG--PAGLPGAPGAKGERGPAGHPGEPGLPGSPGNMGPQGPKG 350
Cdd:COG5651  206 NQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAAGAAAAAaaAAAAAGAGASAALASLAATLLNASSLGLAATAASSAATN 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148672943 351 IPGNHGIPGAKGE--IGLVGPAGPPGARGARGPPGLDGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVG 428
Cdd:COG5651  286 LGLAGSPLGLAGGgaGAAAATGLGLGAGGAAGAAGATGAGAALGAGAAAAAAGAAAGAGAAAAAAAGGAGGGGGGALGAG 365

                        170
                 ....*....|....*
gi 148672943 429 AKGVPGHNGEAGPRG 443
Cdd:COG5651  366 GGGGSAGAAAGAASG 380
 
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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