NCBI Conserved Domain Search

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: 111.92 E-value: 3.82e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 343 GDKGEKGLDGPKGDKGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKGLDGPKGDKGADGTPGAKGDKGE 422
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 423 KGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGD--KGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGS 500
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392901970 501 KGDKGDKGLDGPKGDKGADGTPGSKGDKGEKGDIGQPGQKGDKGEKGQDGQPGQKGQDGQPGQKGDK 567
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343

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: 108.07 E-value: 6.94e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 298 GDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPGSKGDKGEKGLDGPKGDKGADGAKGANGTPGAKGDKGE 377
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 378 KGTDGAKGADGTPGAKGDKGEKGLDGPKGDKG--ADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQ 455
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392901970 456 KGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKG 517
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338

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: 107.30 E-value: 1.24e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 421 GEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGS 500
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 501 KGDKGDKGLDGPKGDKGADGTPGSKGDKGEKGDIGQpGQKGDKGEKGQDGQPGQKGQDGQPGqkgdkgdkgqgEKGQDGQ 580
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAG-----------KDGPRGD 264

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 581 PGQKGQDGQPGQKGDKGEKGDIGQPGQKGDKGDKGQDGQPGQKGQDGQPGQKGQDGQPGQ 640
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324

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: 106.53 E-value: 2.16e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 184 GEKGADGNPGPKGDKGADGAKGADGTPGSKGDKGSDGAKGADGNPGSKGDTGDKGEKGSDGAKGDKGANGTPGSKGDKGE 263
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 264 KGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDkgekGLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPGSKG 343
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970 344 DKGEKGLDGPKGDKGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKGLDGPKGDKG 409
Cdd:NF038329 273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338

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: 98.44 E-value: 1.12e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 450 DGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGADGTPGSKGDKG 529
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 530 EKGDIGQPGQKGDKGEKGQDGQPGQKGQDGQPGQKGDKGDKGQGEKGQDGQPGQKGQDGQPGQKGDKGEKGDIGQPGQKG 609
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 392901970 610 DKGDKGQDGQPGQKGQDGQP------GQKGQDGQPG 639
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDglpgkdGKDGQNGKDG 311

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: 87.65 E-value: 3.75e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970  75 KDGVPGTNGKDGTPGDKGDTGDKGDKGDTGAPGVgvKGDPGAQGPPGEKGKDGDKGAPGakgskgddgkkgdkgssgEKG 154
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP--AGPQGEAGPQGPAGKDGEAGAKG------------------PAG 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 155 EKGSPGQKGDKGEKGEKGSNGSPGSKGDKGEKGADGNPGPKGDkGADGAKGADGTPGSKGDKGSDGAKGADGNPGSKGDT 234
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392901970 235 GDKGEKGSDGAKGDKGANGTPGSKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPK 309
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343

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: 84.96 E-value: 2.75e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 464 LDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGADGTPGSKGDKGEKGDIGQPGQKGDK 543
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 544 GEKGQDGQPGQKGQDGQPGQKGdkgdkgqgEKGQDGQPGQKGQDGQpGQKGDKGEKGDIGQPGQKGDKGDKGQDGQPGQK 623
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDG--------EAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                        170
                 ....*....|....*.
gi 392901970 624 GQDGQPGQKGQDGQPG 639
Cdd:NF038329 266 GEAGPDGPDGKDGERG 281

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 66.94 E-value: 2.91e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   341 SKGDKGEKGldgPKGDKGADGAKGANGTPGAKGDkgEKGTDGAKgadgtPGAKGDKGEKGLDGPKGDKGADGTPGAKGDK 420
Cdd:TIGR00927  631 SKGDVAEAE---HTGERTGEEGERPTEAEGENGE--ESGGEAEQ-----EGETETKGENESEGEIPAERKGEQEGEGEIE 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   421 GEKGADGAKGADGTPGSKGDKGADGAKgaDGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGS 500
Cdd:TIGR00927  701 AKEADHKGETEAEEVEHEGETEAEGTE--DEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDE 778

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   501 KGDKGDKGLDGP-KGDKGADGTPGSKGDKGEKGDIGQPGQKGDKgekgQDGQPGQKGQDGQPGQKGDKGDKGQGEKGQDG 579
Cdd:TIGR00927  779 DEGEIQAGEDGEmKGDEGAEGKVEHEGETEAGEKDEHEGQSETQ----ADDTEVKDETGEQELNAENQGEAKQDEKGVDG 854

                          250       260
                   ....*....|....*....|
gi 392901970   580 QPGQKGQDGQPGQKGDKGEK 599
Cdd:TIGR00927  855 GGGSDGGDSEEEEEEEEEEE 874

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 63.48 E-value: 3.79e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   192 PGPKGDKGADGAKGADGTPGSKGDKGSDGAKGADGNPGSKGDTGDkGEKGSDGAKGDKGANGtpgSKGDKGEKGADGAKG 271
Cdd:TIGR00927  620 PVAKVMALGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESG-GEAEQEGETETKGENE---SEGEIPAERKGEQEG 695

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   272 ADGTPGSKGDKGADGAKGADGTPGQKGDKGEKglDGPKGDKGADGTpgAKGDKGDKGADGAKGADgtpgSKGDKGEKGLD 351
Cdd:TIGR00927  696 EGEIEAKEADHKGETEAEEVEHEGETEAEGTE--DEGEIETGEEGE--EVEDEGEGEAEGKHEVE----TEGDRKETEHE 767

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   352 GPKGDKGADGAKgaNGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKGLDGPKGDKGADgtpgaKGDKGEKGADGAKGA 431
Cdd:TIGR00927  768 GETEAEGKEDED--EGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADD-----TEVKDETGEQELNAE 840

                          250       260
                   ....*....|....*....|
gi 392901970   432 DGTPGSKGDKGADGAKGADG 451
Cdd:TIGR00927  841 NQGEAKQDEKGVDGGGGSDG 860

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: 61.07 E-value: 1.05e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970  66 PgppgtgtgkdgvpgtnGKDGTPGDKGDTGDKGDKGDTGAPgvGVKGDPGAQGPPGEKGKDGDKGAPGAkgskgddgkkG 145
Cdd:NF038329 176 A----------------GKDGEAGAKGPAGEKGPQGPRGET--GPAGEQGPAGPAGPDGEAGPAGEDGP----------A 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 146 DKGSSGEKGEKGSPGQKGDKGEKGEKGSNGSPGSKGDKGEKGADGNPGPKGDKGADGAKGADGTPGSKGDKGSDGAKGAD 225
Cdd:NF038329 228 GPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                        170       180       190
                 ....*....|....*....|....*....|.
gi 392901970 226 GNPGSKGDTGDKGEKGSDGAKGDKGANGTPG 256
Cdd:NF038329 308 GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 61.94 E-value: 1.08e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   127 GDKGAPGAKGSKGDDGKKGDKGSSGEKGEKGSpGQKGDKGEKGEKGSNGSPGSKGDKGeKGADGNPGPKGDKGADGAKGA 206
Cdd:TIGR00927  633 GDVAEAEHTGERTGEEGERPTEAEGENGEESG-GEAEQEGETETKGENESEGEIPAER-KGEQEGEGEIEAKEADHKGET 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   207 DGTPGSKGDKGSDGAKGADGnpgsKGDTGDKGEKGSDGAKGDKGANGTPGSKGDKGEKGADGAKGADGtpgsKGDKGaDG 286
Cdd:TIGR00927  711 EAEEVEHEGETEAEGTEDEG----EIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEG----KEDED-EG 781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   287 AKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADgakgadgtPGSKGDKGEKGLDGPKGDKGADGAKGAN 366
Cdd:TIGR00927  782 EIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADD--------TEVKDETGEQELNAENQGEAKQDEKGVD 853

                          250
                   ....*....|.
gi 392901970   367 GTPGAKGDKGE 377
Cdd:TIGR00927  854 GGGGSDGGDSE 864

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 61.16 E-value: 1.63e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   297 KGDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKgadgTPGSKGDKGEKGLDG-----PKGDKGADG-AKGANGTPG 370
Cdd:TIGR00927  632 KGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAE----QEGETETKGENESEGeipaeRKGEQEGEGeIEAKEADHK 707

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   371 AKGDKGEKGTDGAKGADGTP----GAKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGtpgsKGDKGaDGA 446
Cdd:TIGR00927  708 GETEAEEVEHEGETEAEGTEdegeIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEG----KEDED-EGE 782

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   447 KGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKgADGAKGADGTPGSKGDKGDKGlDGPKGDKGADGTPGSKG 526
Cdd:TIGR00927  783 IQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQ-ADDTEVKDETGEQELNAENQG-EAKQDEKGVDGGGGSDG 860


                   ....
gi 392901970   527 DKGE 530
Cdd:TIGR00927  861 GDSE 864

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 59.24 E-value: 7.13e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   162 KGDKGEKGEKGSngspgSKGDKGEKGADGnPGPKGDKGADGAKGADGTPGsKGDKGSDGAKGADGnpgsKGDTGDKGEKG 241
Cdd:TIGR00927  632 KGDVAEAEHTGE-----RTGEEGERPTEA-EGENGEESGGEAEQEGETET-KGENESEGEIPAER----KGEQEGEGEIE 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   242 SDGA--KGDKGANGTPGSKGDKGEKGADGAKGADGTPGS-KGDKGADGAKGA-----DGTPGQKGDKGEKGLDGPKGDKG 313
Cdd:TIGR00927  701 AKEAdhKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEeVEDEGEGEAEGKhevetEGDRKETEHEGETEAEGKEDEDE 780

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   314 ADGTPGAKGD-KGDKGADGAKGADGTPGSKGDKGEKGLDGPKGD----KGADGAKGANGTPGAKGDKGEKGTDGAKGADG 388
Cdd:TIGR00927  781 GEIQAGEDGEmKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADdtevKDETGEQELNAENQGEAKQDEKGVDGGGGSDG 860

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 58.85 E-value: 9.62e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   392 AKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKgadgTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDK 471
Cdd:TIGR00927  631 SKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAE----QEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADH 706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   472 GADGTPGAKGDKGEKGADGAKgaDGTPGSKGDKGDKGLDGPKGDKGADGTPGSKGDKGEKGDIGQPGQKGDKGEKGQDGQ 551
Cdd:TIGR00927  707 KGETEAEEVEHEGETEAEGTE--DEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQ 784

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   552 PGQ----KGQDGQPGQKGDKGDKGQGEKGQDGQPGQKGQDGQPGqKGDKGEKGDIGQPGQKGDKGDKGQDGQpgqKGQDG 627
Cdd:TIGR00927  785 AGEdgemKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEV-KDETGEQELNAENQGEAKQDEKGVDGG---GGSDG 860

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 56.54 E-value: 4.56e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   381 DGAKGADGTPGAKGD------KGEKGLDGPKGDKGADGT--PGAKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGT 452
Cdd:TIGR00927  629 DLSKGDVAEAEHTGErtgeegERPTEAEGENGEESGGEAeqEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKG 708

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   453 PGQKGDKGEKGLDGPKGDKG-ADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGADGTPGSKGDKGEK 531
Cdd:TIGR00927  709 ETEAEEVEHEGETEAEGTEDeGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGED 788

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   532 GDIgqpgqKGDKGEKGQDGQPGQKGQDGQPGQKGDKGDKGQGEKGQDGQPGQKGQDGQPGQKGDkGEKGDIGQPGqkGDK 611
Cdd:TIGR00927  789 GEM-----KGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQ-DEKGVDGGGG--SDG 860


                   ..
gi 392901970   612 GD 613
Cdd:TIGR00927  861 GD 862

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 55.77 E-value: 7.11e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970    91 KGDTGDKGDKGDTgaPGVGVKGDPGAQGPPGEKGkdGDKGAPGAKGSKGDDGKKGDKGSSGEKGEKGSPGQ--------K 162
Cdd:TIGR00927  632 KGDVAEAEHTGER--TGEEGERPTEAEGENGEES--GGEAEQEGETETKGENESEGEIPAERKGEQEGEGEieakeadhK 707

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   163 GD-KGEKGEKGSNGSPGSKGDKGEKGADGNPGPKGDKGADGAKGADGTPgSKGDKGSDGAKGADGNPGSKGDTGDKGEKG 241
Cdd:TIGR00927  708 GEtEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVE-TEGDRKETEHEGETEAEGKEDEDEGEIQAG 786

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392901970   242 SDGA-KGDKGANGTPGSKGDKGEKGADGAKGADGTPgSKGDKGADGAKGADGTPGQKGD--KGEKGLDGPKGDKGAD 315
Cdd:TIGR00927  787 EDGEmKGDEGAEGKVEHEGETEAGEKDEHEGQSETQ-ADDTEVKDETGEQELNAENQGEakQDEKGVDGGGGSDGGD 862

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 55.77 E-value: 8.15e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   426 DGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEkgldgpkGDKGADGTPGAKGDKGEKGADGAKGADGTPGsKGDKG 505
Cdd:TIGR00927  629 DLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESG-------GEAEQEGETETKGENESEGEIPAERKGEQEG-EGEIE 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   506 DKGLDgPKGDKGADGTPGSKGDKGEKGDIGQPGQKGDKGEKGQDGQPGQKGQDGQPGQKGDK-------GDKGQGEKGQD 578
Cdd:TIGR00927  701 AKEAD-HKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRketehegETEAEGKEDED 779

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 392901970   579 GQPGQKGQDGQpgQKGDKGEKGDIGQPGQKGDKGDKGQDGQPGQKgQDGQPGQKGQDGQ 637
Cdd:TIGR00927  780 EGEIQAGEDGE--MKGDEGAEGKVEHEGETEAGEKDEHEGQSETQ-ADDTEVKDETGEQ 835

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.

Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 54.95 E-value: 1.37e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970  106 PGVGVKGDPGAQGPPGEKGKDGDKGAPGAKGSKGDDGKKGDKGSSGEKGEKGSPGQKGDKGEKGEKGSNGSPGSKGDKGE 185
Cdd:pfam03157 173 SGQRQQPGQGQQLRQGQQGQQSGQGQPGYYPTSSQQPGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQGQQGQQPGQPQ 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970  186 KGADGNPGPKGDKGADGAKGADGTPGSKGDKGSDGAKGADGNPGSKGDTGDKGEKGSDGAKGDKGANGTPGSKGDKGEKG 265
Cdd:pfam03157 253 QLGQGQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSGYYPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQP 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970  266 ADGAKGADGtpgSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPGSKGDK 345
Cdd:pfam03157 333 GQGQQGQQP---AQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQ 409

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970  346 GEKGLDGPKGDKGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEkGLDGPKGDKGADGTPGAKGDKGEKGA 425
Cdd:pfam03157 410 GQPGYYPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQEQPGQGQQPGQ-GQQGQQPGQPEQGQQPGQGQPGYYPT 488

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970  426 DGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKG 505
Cdd:pfam03157 489 SPQQSGQGQQLGQWQQQGQGQPGYYPTSPLQPGQGQPGYYPTSPQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQG 568

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970  506 DKGLDGPKGDKGADGTPGSKGDKGEKGDI-GQPGQKGDKGEKGQDGQPGQKGQDGQPGQKGDKGDKGQG-------EKGQ 577
Cdd:pfam03157 569 QQGQQPGQGQQGQQPGQGQQPGQGQPGYYpTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLGQGQQGyyptspqQPGQ 648

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392901970  578 DGQPGQKGQDGQPGQKGDKGEKGDIGQPGQKGDKGDKGQDGQPGQKGQDGQPGQKGQDGQPGQ 640
Cdd:pfam03157 649 GQQPGQWQQSGQGQQGYYPTSPQQSGQAQQPGQGQQPGQWLQPGQGQQGYYPTSPQQPGQGQQ 711

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 52.31 E-value: 8.68e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970    79 PGTNG--KDGTPGDKGDTGDKGDKGDTGAPGVGVKGDPGAQGPPGEKGKD--GDKGAPGAKGSKGDDGKKGDKGSSGEKG 154
Cdd:TIGR00927  656 EGENGeeSGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADhkGETEAEEVEHEGETEAEGTEDEGEIETG 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   155 EKGSpgQKGDKGEkGEKGSNGSPGSKGDKGEKGADGNPGPKGDKGAD-GAKGADGTPGSKGDKGSDGAKGADGNPGSKGD 233
Cdd:TIGR00927  736 EEGE--EVEDEGE-GEAEGKHEVETEGDRKETEHEGETEAEGKEDEDeGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEK 812

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392901970   234 TGDKGEKGSDGA-KGDKGANGTPGSKGDKGEKGADGAKGADGTPGSKGDKGAD 285
Cdd:TIGR00927  813 DEHEGQSETQADdTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEE 865

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.

Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 51.83 E-value: 1.27e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 159 PGQKGDKGEKGEKGSNGSPGSKGDKGEKGADGNPGPKGDKGADGAKGADGTPGSKGDKGSDGAKGADGNPGSKGDTGDKG 238
Cdd:NF033609 551 PGEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDS 630

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 239 EKGSDGAKGDKGANGTPGSKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTP 318
Cdd:NF033609 631 ASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 710

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 319 GAKGDK-GDKGADGAKGADGTPGSKGDKGEKGLDGPKGDKGADGAKGANGTPGAKGDKgEKGTDGAKGADGTPGAKGDKG 397
Cdd:NF033609 711 DSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSD 789

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392901970 398 EKGLDGPKGDKGADGTPGAKGDKgEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGD 458
Cdd:NF033609 790 SDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 849

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: 40.94 E-value: 5.87e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  157 GSPGQKGDKGEKGEKGSNGSPGSKGDKGEKGADGNPGPKGDKGADGAKGADGTPG 211
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

hypothetical protein; Provisional

Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 45.73 E-value: 7.76e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 376 GEKGTDGAKGADGTPGAKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGaDGAKGADGTPGQ 455
Cdd:PHA03169  28 GTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSG-SGSESVGSPTPS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 456 KGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGADGTPGSKGDKGEKGDIG 535
Cdd:PHA03169 107 PSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPE 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392901970 536 QPGQKGDKGEKGQDGQPGQKGQDGQPGQKGDKGDKGQGEKGQDG 579
Cdd:PHA03169 187 PDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQA 230

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: 40.55 E-value: 1.01e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392901970  582 GQKGQDGQPGQKGDKGEKGDIGQPGQKGDKGDKGQDGQPGQKGQDGQPGQKGQDGQP 638
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57

hypothetical protein; Provisional

Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 44.96 E-value: 1.05e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 124 GKDGDKGAPGAKGSKGDDGKKGDKGSSGEKGEKGSPGQKGDKGEKGEKGSNGSPGSKGDKGEkGADGNPGPKGDKGADGA 203
Cdd:PHA03169  34 GRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGS-GSESVGSPTPSPSGSAE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 204 KGADGTPGSKGDKGSDGAKGADGNPGSKGDTGDKGEKGSDGAKGDKGANGTPGSKGDKGEKGADGAKGADGTPGSKGDKG 283
Cdd:PHA03169 113 ELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGP 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 392901970 284 ADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPGSK 342
Cdd:PHA03169 193 PQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHR 251

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: 40.17 E-value: 1.23e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  169 GEKGSNGSPGSKGDKGEKGADGNPGPKGDKGADGAKGADGTPGSKGDKGSDGAKGA 224
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

hypothetical protein; Provisional

Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 44.96 E-value: 1.29e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 154 GEKGSPGQKGDKGEKGEKGSNGSPGSKGDKGEKGADGNPGPKGDKGADGAKGADGTPGSKGDkGSDGAKGADGNPGSKGD 233
Cdd:PHA03169  28 GTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQ-GGPSGSGSESVGSPTPS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 234 TGDKGEKGSDGAKGDKGANGTPGSKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKG 313
Cdd:PHA03169 107 PSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPE 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392901970 314 ADGTPGAKGDKGDKGADGAKGADgtpgskgDKGEKGLDGPKGDKGADGAKGANGTPGAKGDKGE 377
Cdd:PHA03169 187 PDSPGPPQSETPTSSPPPQSPPD-------EPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPERE 243

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: 40.17 E-value: 1.33e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  400 GLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQ 455
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 40.17 E-value: 1.35e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392901970  154 GEKGSPGQKGDKGEKGEKGSNGSPGSKGDKGEKGADGNPGPKGDKGADGAKGADGTP 210
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57

hypothetical protein; Provisional

Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 44.58 E-value: 1.41e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 397 GEKGLDGPKGDKGaDGTPGAKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGT 476
Cdd:PHA03169  82 GEKEERGQGGPSG-SGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPN 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 477 PGAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGADGTPGSKGDKGEKGDIGQPGQKGDKGEKGQDGQPGQKG 556
Cdd:PHA03169 161 QQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEP 240


                 ....*....
gi 392901970 557 QDGQPGQKG 565
Cdd:PHA03169 241 EREGPPFPG 249

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: 39.78 E-value: 1.46e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  376 GEKGTDGAKGADGTPGAKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGA 431
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 39.78 E-value: 1.66e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  208 GTPGSKGDKGSDGAKGADGNPGSKGDTGDKGEKGSDGAKGDKGANGTPGSKGDKGE 263
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

hypothetical protein; Provisional

Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 44.58 E-value: 1.71e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 191 NPGPKGDKGADGAKGADGTPGSKGDKGSDGAKGADGNPGSKGDTGDKGEKGSDGAKGDKG--ANGTPGSKGDKGEKGADG 268
Cdd:PHA03169  32 QAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGpsGSGSESVGSPTPSPSGSA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 269 AKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPGSKGDKGEK 348
Cdd:PHA03169 112 EELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPG 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392901970 349 GLDGPKGDKGADGAKGANgTPGAKGDKGEKGTDGAKGADG 388
Cdd:PHA03169 192 PPQSETPTSSPPPQSPPD-EPGEPQSPTPQQAPSPNTQQA 230

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: 39.78 E-value: 1.82e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  367 GTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKGLDGPKGDKGADGTPGAKGDKGE 422
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 44.60 E-value: 1.97e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   471 KGADGTPGAKGDKGEKGADGAKGADGTPGSKGDkGDKGLDGPKGDKGADGTPGS-----KGDKGEKGDIgqpgqKGDKGE 545
Cdd:TIGR00927  632 KGDVAEAEHTGERTGEEGERPTEAEGENGEESG-GEAEQEGETETKGENESEGEipaerKGEQEGEGEI-----EAKEAD 705

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970   546 KGQDGQPGQKGQDGQPGQKGDKgDKGQGEKGQDGQP-GQKGQ-DGQPGQKGD-KGEKGDIGQPGQKGDKGDKGQDGQPGQ 622
Cdd:TIGR00927  706 HKGETEAEEVEHEGETEAEGTE-DEGEIETGEEGEEvEDEGEgEAEGKHEVEtEGDRKETEHEGETEAEGKEDEDEGEIQ 784

                          170
                   ....*....|....*...
gi 392901970   623 KGQDGQpgQKGQDGQPGQ 640
Cdd:TIGR00927  785 AGEDGE--MKGDEGAEGK 800

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: 39.01 E-value: 2.83e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  514 GDKGADGTPGSKGDKGEKGDIGQPGQKGDKGEKGQDGQPGQKGQDGQPGQKGDKG 568
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 39.01 E-value: 3.15e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  439 GDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGA 494
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 39.01 E-value: 3.31e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  475 GTPGAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGADGTPGSKGDKGE 530
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 39.01 E-value: 3.48e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  152 EKGEKGSPGQKGDKGEKGEKGSNGSPGSKGDKGEKGADGNPGPKGDKGADGAKGA 206
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 39.01 E-value: 3.66e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  166 GEKGEKGSNGSPGSKGDKGEKGADGNPGPKGDKGADGAKGADGTPGSKGDKGSDGA 221
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 38.63 E-value: 3.84e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  316 GTPGAKGDKGDKGADGAKGADGTPGSKGDKGEKGLDGPKGDKGADGAKGANGTPGA 371
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

hypothetical protein; Provisional

Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 3.87e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 277 GSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPGSKGDKGEKGLDGPKGD 356
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 357 KGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPG 436
Cdd:PHA03169 170 SHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPG 249


                 ..
gi 392901970 437 SK 438
Cdd:PHA03169 250 HR 251

hypothetical protein; Provisional

Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 3.98e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 402 DGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDkGADGTPGAKG 481
Cdd:PHA03169  27 GGTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGS-GSESVGSPTP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 482 DKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGADGTPGSKGDKGEKGDIGQPGQKGDKGEKGQDGQPGQKGQDGQP 561
Cdd:PHA03169 106 SPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEP 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970 562 gqKGDKGDKGQGEKGQDGQPGQKGQDGQPGQKGDKGEKGDIGQPGQKGDKGDKGQDGQPGQKGQDG 627
Cdd:PHA03169 186 --EPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPG 249

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: 38.63 E-value: 4.24e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  430 GADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGE 485
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 38.63 E-value: 4.63e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  394 GDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGADGAKGA 449
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 38.63 E-value: 4.96e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  175 GSPGSKGDKGEKGADGNPGPKGDKGADGAKGADGTPGSKGDKGSDGAKGADGNPG 229
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

Domain of unknown function (DUF4175);

Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 43.44 E-value: 5.01e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 392901970  548 QDGQPGQKGQDGQPGQKGDKGDKGQGEKGQDGQPGQKGQDGQPGQKGD 595
Cdd:pfam13779 628 RQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGD 675

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: 38.24 E-value: 5.37e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  325 GDKGADGAKGADGTPGSKGDKGEKGLDGPKGDKGADGAKGANGTPGAKGDKGEKG 379
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 38.24 E-value: 5.37e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  463 GLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGA 518
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 38.24 E-value: 5.37e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  331 GAKGADGTPGSKGDKGEKGLDGPKGDKGADGAKGANGTPGAKGDKGEKGTDGAKGA 386
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

Domain of unknown function (DUF4175);

Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 43.05 E-value: 5.85e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970  548 QDGQPGQKGQDGQ-PGQK-----GDKGDKGQG---EKGQDGQPGQKGQDGQPGQKGDKGEKGDIGQPGQKGDKGDKGQDG 618
Cdd:pfam13779 590 QAGQPQQQQQQGQsEMQQamdelGDLLREQQQlldETFRQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGG 669

                          90
                  ....*....|.
gi 392901970  619 QPGQKG-QDGQ 628
Cdd:pfam13779 670 AEALGDlAERQ 680

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: 38.24 E-value: 6.22e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  241 GSDGAKGDKGANGTPGSKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQ 296
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 38.24 E-value: 6.28e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  508 GLDGPKGDKGADGTPGSKGDKGEKGDIGQPGQKGDKGEKGQDGQPGQKGQDGQPGQ 563
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

hypothetical protein; Provisional

Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 42.65 E-value: 6.41e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 340 GSKGDKGEKGLDGPKGDKGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKGLDGPKGDKGADGTPGAKGD 419
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 420 KGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPG 499
Cdd:PHA03169 170 SHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPG 249


                 ..
gi 392901970 500 SK 501
Cdd:PHA03169 250 HR 251

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: 38.24 E-value: 6.47e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  391 GAKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGADGA 446
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 38.24 E-value: 7.00e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  361 GAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKGLDGPKGDKGADGTPGA 416
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 37.86 E-value: 7.07e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392901970  172 GSNGSPGSKGDKGEKGADGNPGPKGDKGADGAKGADGTPGSKGDKGSDGAKGADGNP 228
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57

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: 37.86 E-value: 7.50e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  271 GADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKG 325
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 37.86 E-value: 7.57e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  499 GSKGDKGDKGLDGPKGDKGADGTPGSKGDKGEKGDIGQPGQKGDKGEKGQDGQPGQ 554
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 37.86 E-value: 8.03e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  484 GEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGADGTPGSKGDKGEKGDIGQPGQ 539
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 37.86 E-value: 8.19e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  454 GQKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGDKG 508
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 37.86 E-value: 8.61e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  433 GTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGA 488
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 37.86 E-value: 8.78e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  349 GLDGPKGDKGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKGLDGP 404
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 37.86 E-value: 9.41e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  274 GTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGDKGA 329
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 37.86 E-value: 9.50e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  412 GTPGAKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGP 467
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 37.47 E-value: 9.69e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  253 GTPGSKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGP 308
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 37.47 E-value: 9.78e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  280 GDKGADGAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKGA 335
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 37.47 E-value: 9.78e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  256 GSKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKG 310
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 37.47 E-value: 1.09e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  415 GAKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKG 469
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 37.47 E-value: 1.23e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  193 GPKGDKGADGAKGADGTPGSKGDKGSDGAKGADGNPGSKGDTGDKGEKGSDGAKG 247
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 37.47 E-value: 1.29e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  295 GQKGDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPGSKGDKGEKG 349
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 37.47 E-value: 1.30e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  576 GQDGQPGQKGQDGQPGQKGDKGEKGDIGQPGQKGDKGDKGQDGQPGQKGQDGQPGQ 631
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 1.33e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  346 GEKGLDGPKGDKGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKG 400
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 1.34e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  232 GDTGDKGEKGSDGAKGDKGANGTPGSKGDKGEKGADGAKGADGTPGSKGDKGADGA 287
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 1.42e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  298 GDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPGSKGDKGEKGLDGP 353
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 1.48e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  409 GADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKG 463
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 1.63e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  304 GLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPGSKGDKGEKGLDGPKGDKGA 359
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

Domain of unknown function (DUF4175);

Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 41.51 E-value: 1.67e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970  524 SKGDKGEKGDIGQPGQKGDKGEKGQDGQPGQKGQDGQPGQKGDKGDKGQGEKGQD-GQPGQKGQDGQPGQKGdKGEKGDI 602
Cdd:pfam13779 628 RQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAERQQAlRRRLEELQDELKELGG-KEPGQAL 706

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392901970  603 GQPGQK-GDKGDKGQDGQPG-------------QKG---------QDGQPGQKGQDGQPGQ 640
Cdd:pfam13779 707 GDAGRAmRDAEEALGQGDLAgavdaqgralealRKGaqqlaeamqQQQGQGQQPGQGGQGG 767

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: 1.82e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  319 GAKGDKGDKGADGAKGADGTPGSKGDKGEKGLDGPKGDKGADGAKGANGTPGAKG 373
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 1.89e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  445 GAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPG 499
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 1.89e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392901970  588 GQPGQKGDKGEKGDIGQPGQKGDKGDKGQDGQPGQKGQDGQPGQKGQDGQPG 639
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52

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: 1.97e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392901970  572 QGEKGQDGQPGQKGQDGQPGQKGDKGEKGDIGQPGQKGDKGDKGQDGQPGQKGQ 625
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 2.09e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  406 GDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGE 461
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 2.11e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  178 GSKGDKGEKGADGNPGPKGDKGADGAKGADGTPGSKGDKGSDGAKGADGNPGSKG 232
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 2.19e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  247 GDKGANGTPGSKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGE 302
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 36.32 E-value: 2.49e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  478 GAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGADGTPGSKGDKGEKG 532
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 36.32 E-value: 2.59e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  250 GANGTPGSKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKG 304
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 36.32 E-value: 2.75e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  286 GAKGADGTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPG 340
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 36.32 E-value: 2.78e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  163 GDKGEKGEKGSNGSPGSKGDKGEKGADGNPGPKGDKGADGAKGADGTPGSKGDKG 217
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 36.32 E-value: 2.81e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  457 GDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGP 512
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 36.32 E-value: 3.19e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  352 GPKGDKGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKGLDGPKG 406
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

hypothetical protein; Provisional

Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 40.34 E-value: 3.45e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 243 DGAKGDKGANGTPGSKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGTPGQKGDKGEKGLDGPKGDkGADGTPGAKG 322
Cdd:PHA03169  27 GGTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGS-GSESVGSPTP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 323 DKGDKGADGAKGADGTPGSKGDKGEKGLDGPKGDKGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKGLD 402
Cdd:PHA03169 106 SPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEP 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392901970 403 GPKGDKGADGTPGAKGDKGEKGADgakgADGTPGSKGDKGADGAKGADG 451
Cdd:PHA03169 186 EPDSPGPPQSETPTSSPPPQSPPD----EPGEPQSPTPQQAPSPNTQQA 230

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: 35.93 E-value: 3.66e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  187 GADGNPGPKGDKGADGAKGADGTPGSKGDKGSDGAKGADGNPGSKGDTGDKGEKG 241
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 35.93 E-value: 3.70e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  469 GDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGADGTPG 523
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 35.93 E-value: 3.70e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  301 GEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPGSKGDKGEKGLDGPKG 355
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

hypothetical protein; Provisional

Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 39.95 E-value: 4.03e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 373 GDKGEKGTDGAKGADGTPGAKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGADGAKGADGT 452
Cdd:PHA03169  75 TAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPES 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 453 PGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGEKGADGAKGADGTPGSKGDKGDKGLDGPKGDKGADGTPGSKGDKGEKG 532
Cdd:PHA03169 155 HNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHE 234


                 .
gi 392901970 533 D 533
Cdd:PHA03169 235 D 235

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: 4.92e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  223 GADGNPGSKGDTGDKGEKGSDGAKGDKGANGTPGSKGDKGEKGADGAKGADGTPG 277
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

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: 5.33e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  292 GTPGQKGDKGEKGLDGPKGDKGADGTPGAKGDKGDKGADGAKGADGTPGSKGDKGE 347
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 6.55e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392901970  340 GSKGDKGEKGLDGPKGDKGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKG 394
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

hypothetical protein; Provisional

Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 39.18 E-value: 6.84e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392901970 499 GSKGDKGDKGLDGPKGDKGADGTPGSKGDKGEKGDIGQPGQKGDKGEKGQDGQPGQKGQDGQPGQKGDKGDKGQGEKGQD 578
Cdd:PHA03169  82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQ 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392901970 579 GQPGQKGQDGQPGQKGDKGEKGDIGQPGQKGDKGDKGQDGQPGQKG--QDGQPGQKGQDGQPG 639
Cdd:PHA03169 162 QPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPpdEPGEPQSPTPQQAPS 224

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: 7.45e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  355 GDKGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGEKGLDGPKGDKGA 410
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 8.30e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392901970  343 GDKGEKGLDGPKGDKGADGAKGANGTPGAKGDKGEKGTDGAKGADGTPGAKGDKGE 398
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 8.63e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392901970  573 GEKGQDGQPGQKGQDGQPGQKGDKGEKGDIGQPGQKGDKGDKGQDGQPGQKGQDGQP 629
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57