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Conserved domains on  [gi|27477127|ref|NP_149022|]
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keratin, type II cuticular Hb2 [Homo sapiens]

Protein Classification

type II keratin( domain architecture ID 12177255)

type II keratin is an intermediate filament-forming protein that provides mechanical support and fulfills a variety of additional functions in epithelial cells

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
120-430 4.68e-132

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.81  E-value: 4.68e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   120 EKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCCQ-TNIEPIFEGYISALRRQLDCVSGDRVRLESELCSLQ 198
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   199 AALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEEICLLQSQISETSVIVKMD 278
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   279 NSRELDVDGIIAEIKAQYDDIASRSKAEAEAWYQCRYEELRVTAGNHCDNLRNRKNEILEMNKLIQRLQQETENVKAQRC 358
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477127   359 KLEGAIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 430
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
61-116 1.21e-11

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 62.75  E-value: 1.21e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 27477127    61 GFGRPRVASRCGGTlPGFGYRLG---ATCGPSAcITPVTINESLLVPLALEIDPTVQRV 116
Cdd:pfam16208 100 GFGGGGYGGGGFGG-GGFGGRGGfggPPCPPGG-IQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
120-430 4.68e-132

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.81  E-value: 4.68e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   120 EKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCCQ-TNIEPIFEGYISALRRQLDCVSGDRVRLESELCSLQ 198
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   199 AALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEEICLLQSQISETSVIVKMD 278
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   279 NSRELDVDGIIAEIKAQYDDIASRSKAEAEAWYQCRYEELRVTAGNHCDNLRNRKNEILEMNKLIQRLQQETENVKAQRC 358
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477127   359 KLEGAIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 430
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
61-116 1.21e-11

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 62.75  E-value: 1.21e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 27477127    61 GFGRPRVASRCGGTlPGFGYRLG---ATCGPSAcITPVTINESLLVPLALEIDPTVQRV 116
Cdd:pfam16208 100 GFGGGGYGGGGFGG-GGFGGRGGfggPPCPPGG-IQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 175-425 1.13e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    175 ALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLK 254
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    255 S---LYEEEICLLQSQISETSVIVKmdnsrelDVDGIIAEIKAQYDDIASRSKAEAEAWYQcrYEELRVTAGNHCDNLRN 331
Cdd:TIGR02168  316 RqleELEAQLEELESKLDELAEELA-------ELEEKLEELKEELESLEAELEELEAELEE--LESRLEELEEQLETLRS 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    332 R-----------KNEILEMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQG--------EAALNDAKCKLAGLEEALQKA 392
Cdd:TIGR02168  387 KvaqlelqiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleelEEELEELQEELERLEEALEEL 466

                          250       260       270
                   ....*....|....*....|....*....|...
gi 27477127    393 KQDMACLLKEYQEVMNSKLGLDIEIATYRRLLE 425
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQLQARLDSLERLQE 499
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
145-406 4.52e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.24  E-value: 4.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 145 NKLLEtkwNFMQQQRccQTNIEPIfEGYISALRRQLDcvsgdrvRLESELCSLQAALEGYKKKyeeelslrpcveNEFVA 224
Cdd:COG3206 155 NALAE---AYLEQNL--ELRREEA-RKALEFLEEQLP-------ELRKELEEAEAALEEFRQK------------NGLVD 209

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 225 LKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEeiclLQSQISETSvivkmDNSRELDVDGIIAEIKAQYddiasrsk 304
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGSGP-----DALPELLQSPVIQQLRAQL-------- 272

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 305 AEAEAwyqcRYEELRVTAG-NHCD--NLRNRKNEIL-----EMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQGeAALN 376
Cdd:COG3206 273 AELEA----ELAELSARYTpNHPDviALRAQIAALRaqlqqEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELP 347

                       250       260       270
                ....*....|....*....|....*....|
gi 27477127 377 DAKCKLAGLEEALQKAKQDMACLLKEYQEV 406
Cdd:COG3206 348 ELEAELRRLEREVEVARELYESLLQRLEEA 377
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
121-428 3.36e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 3.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  121 KEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRccqTNIEPIFEgYISALRRQLDCVSGDRVRLESELCSLQAA 200
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKE-EIEELEKELESLEGSKRKLEEKIRELEER 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  201 LEGYKKKYEEelsLRPCVEnEFVALKKDVDTAFLMKADLETNAEALvQEIDFLKSLYEEEICLLQSQISETSvivkMDNS 280
Cdd:PRK03918 268 IEELKKEIEE---LEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGIEERIKELE----EKEE 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  281 RELDVDGIIAEIKAQYDDIASRSKAeaeawyqcrYEELRVTAGNhCDNLRNRK--NEILEMNKLIQRLQQETENVKAQRC 358
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE-LERLKKRLtgLTPEKLEKELEELEKAKEEIEEEIS 408

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  359 KLEGAIAEAEQQGE---AALND-----AKCKLAGLE-------EALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRL 423
Cdd:PRK03918 409 KITARIGELKKEIKelkKAIEElkkakGKCPVCGRElteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488


                 ....*
gi 27477127  424 LEGEE 428
Cdd:PRK03918 489 LKKES 493
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
120-430 4.68e-132

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.81  E-value: 4.68e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   120 EKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCCQ-TNIEPIFEGYISALRRQLDCVSGDRVRLESELCSLQ 198
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   199 AALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEEICLLQSQISETSVIVKMD 278
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   279 NSRELDVDGIIAEIKAQYDDIASRSKAEAEAWYQCRYEELRVTAGNHCDNLRNRKNEILEMNKLIQRLQQETENVKAQRC 358
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477127   359 KLEGAIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 430
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
61-116 1.21e-11

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 62.75  E-value: 1.21e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 27477127    61 GFGRPRVASRCGGTlPGFGYRLG---ATCGPSAcITPVTINESLLVPLALEIDPTVQRV 116
Cdd:pfam16208 100 GFGGGGYGGGGFGG-GGFGGRGGfggPPCPPGG-IQEVTVNQSLLQPLNLEIDPEIQRV 156
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 98-410 1.42e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 54.34  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    98 NESLLVPLALEIdptvQRVKRDEKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCCQTNiEPIFEGYISALR 177
Cdd:pfam05483 375 NEDQLKIITMEL----QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGK-EQELIFLLQARE 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   178 RQLDcvsgdrvRLESELCSLQAALEGYKKKYEEelsLRPCVENEfvALKKDVDTAFLMKADLETnaEALVQEI-DFLKSL 256
Cdd:pfam05483 450 KEIH-------DLEIQLTAIKTSEEHYLKEVED---LKTELEKE--KLKNIELTAHCDKLLLEN--KELTQEAsDMTLEL 515

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   257 YEEEICLLQSQISETSVIVKMDNSRELD------VDGIIAEIKAQYDDIASRSKAEAEAWYQCRYEELRVTAG-----NH 325
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEmnlrdeLESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQmkileNK 595

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   326 CDNLRNrknEILEMNKLIQRLQQETENVKAQrcklegAIAEAEQqgeaaLNDAKCKLAGLEEALQKAKQDMACLLKEYQE 405
Cdd:pfam05483 596 CNNLKK---QIENKNKNIEELHQENKALKKK------GSAENKQ-----LNAYEIKVNKLELELASAKQKFEEIIDNYQK 661


                  ....*
gi 27477127   406 VMNSK 410
Cdd:pfam05483 662 EIEDK 666
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 175-425 1.13e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    175 ALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLK 254
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    255 S---LYEEEICLLQSQISETSVIVKmdnsrelDVDGIIAEIKAQYDDIASRSKAEAEAWYQcrYEELRVTAGNHCDNLRN 331
Cdd:TIGR02168  316 RqleELEAQLEELESKLDELAEELA-------ELEEKLEELKEELESLEAELEELEAELEE--LESRLEELEEQLETLRS 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    332 R-----------KNEILEMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQG--------EAALNDAKCKLAGLEEALQKA 392
Cdd:TIGR02168  387 KvaqlelqiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleelEEELEELQEELERLEEALEEL 466

                          250       260       270
                   ....*....|....*....|....*....|...
gi 27477127    393 KQDMACLLKEYQEVMNSKLGLDIEIATYRRLLE 425
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQLQARLDSLERLQE 499
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 112-357 2.52e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 2.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    112 TVQRVKRDEKEQIKCLNNRFASfinKVRFLEQKNKLLETKWNfmQQQRCCQTNIEPI------FEGYISALRRQLDCVSG 185
Cdd:TIGR02169  248 SLEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGE--EEQLRVKEKIGELeaeiasLERSIAEKERELEDAEE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    186 DRVRLESELCSLQAALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEidfLKSlYEEEICLLQ 265
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE---LKD-YREKLEKLK 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    266 SQISE--TSVIVKMDNSRELDVDGI-----IAEIKAQYDDIASRSKAEAEAWYQCRY--EELRVTAGNHCDNLRNRKNEI 336
Cdd:TIGR02169  399 REINElkRELDRLQEELQRLSEELAdlnaaIAGIEAKINELEEEKEDKALEIKKQEWklEQLAADLSKYEQELYDLKEEY 478

                          250       260
                   ....*....|....*....|.
gi 27477127    337 LEMNKLIQRLQQETENVKAQR 357
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAEAQA 499
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
145-406 4.52e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.24  E-value: 4.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 145 NKLLEtkwNFMQQQRccQTNIEPIfEGYISALRRQLDcvsgdrvRLESELCSLQAALEGYKKKyeeelslrpcveNEFVA 224
Cdd:COG3206 155 NALAE---AYLEQNL--ELRREEA-RKALEFLEEQLP-------ELRKELEEAEAALEEFRQK------------NGLVD 209

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 225 LKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEeiclLQSQISETSvivkmDNSRELDVDGIIAEIKAQYddiasrsk 304
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGSGP-----DALPELLQSPVIQQLRAQL-------- 272

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 305 AEAEAwyqcRYEELRVTAG-NHCD--NLRNRKNEIL-----EMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQGeAALN 376
Cdd:COG3206 273 AELEA----ELAELSARYTpNHPDviALRAQIAALRaqlqqEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELP 347

                       250       260       270
                ....*....|....*....|....*....|
gi 27477127 377 DAKCKLAGLEEALQKAKQDMACLLKEYQEV 406
Cdd:COG3206 348 ELEAELRRLEREVEVARELYESLLQRLEEA 377
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 175-430 2.25e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.48  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    175 ALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEELSLRPCVENEFVALKKDVDTAflmKADLETNAEAlVQEIDFLK 254
Cdd:pfam01576  500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAL---TQQLEEKAAA-YDKLEKTK 575

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    255 SLYEEEIcllqsqiseTSVIVKMDNSREL---------DVDGIIAE---IKAQYDDiaSRSKAEAEAwyqcRYEELRVTA 322
Cdd:pfam01576  576 NRLQQEL---------DDLLVDLDHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERDRAEAEA----REKETRALS 640

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    323 GNH-CDNLRNRKNEILEMNKLiqrlqqetenvkaQRCKLEGAIAEAEQQGEAALNDAKCKLAgLEEALQKAKQDMACLLK 401
Cdd:pfam01576  641 LARaLEEALEAKEELERTNKQ-------------LRAEMEDLVSSKDDVGKNVHELERSKRA-LEQQVEEMKTQLEELED 706

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 27477127    402 EYQEVMNSKLGLDIEI----ATYRRLLE-----GEEHR 430
Cdd:pfam01576  707 ELQATEDAKLRLEVNMqalkAQFERDLQardeqGEEKR 744
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
121-428 3.36e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 3.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  121 KEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRccqTNIEPIFEgYISALRRQLDCVSGDRVRLESELCSLQAA 200
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKE-EIEELEKELESLEGSKRKLEEKIRELEER 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  201 LEGYKKKYEEelsLRPCVEnEFVALKKDVDTAFLMKADLETNAEALvQEIDFLKSLYEEEICLLQSQISETSvivkMDNS 280
Cdd:PRK03918 268 IEELKKEIEE---LEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGIEERIKELE----EKEE 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  281 RELDVDGIIAEIKAQYDDIASRSKAeaeawyqcrYEELRVTAGNhCDNLRNRK--NEILEMNKLIQRLQQETENVKAQRC 358
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE-LERLKKRLtgLTPEKLEKELEELEKAKEEIEEEIS 408

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  359 KLEGAIAEAEQQGE---AALND-----AKCKLAGLE-------EALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRL 423
Cdd:PRK03918 409 KITARIGELKKEIKelkKAIEElkkakGKCPVCGRElteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488


                 ....*
gi 27477127  424 LEGEE 428
Cdd:PRK03918 489 LKKES 493
PRK01156 PRK01156
chromosome segregation protein; Provisional
 108-428 3.52e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.43  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  108 EIDPTVQRVKRDE-KEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCC--------QTNIEPIFEGY---ISA 175
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCpvcgttlgEEKSNHIINHYnekKSR 480

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  176 LRRQLDCVSGDRVRLESE---LCSLQAALEGYK-KKYEEELSLRPCVENEFVALKKDVDTAflmkADLETNAEALVQE-- 249
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKivdLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINEL----KDKHDKYEEIKNRyk 556

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  250 ---IDFLKSLYEEEICLLqSQISetsvIVKMDNSRELDvdgiiAEIKAQYDDIASRSK------AEAEAWYQCRYEELRv 320
Cdd:PRK01156 557 slkLEDLDSKRTSWLNAL-AVIS----LIDIETNRSRS-----NEIKKQLNDLESRLQeieigfPDDKSYIDKSIREIE- 625

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  321 tagNHCDNLRNRKNEILEMNKLIQRLQQETENVKAQRCKLEGaIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMAcLL 400
Cdd:PRK01156 626 ---NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS-IIPDLKEITSRINDIEDNLKKSRKALDDAKANRA-RL 700

                        330       340
                 ....*....|....*....|....*....
gi 27477127  401 KEYQEVMNSKLG-LDIEIATYRRLLEGEE 428
Cdd:PRK01156 701 ESTIEILRTRINeLSDRINDINETLESMK 729
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
222-416 9.51e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 9.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  222 FVALK--KDVDTAF----LMKADLETNAEALVQEIDFLKSLYEEeicllqsqisetsvIVKMDNSRELdvdgiIAEIKAQ 295
Cdd:COG4913  200 TQSFKpiGDLDDFVreymLEEPDTFEAADALVEHFDDLERAHEA--------------LEDAREQIEL-----LEPIREL 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  296 YDDIAsRSKAEAEAWYQCRyEELRVTAGNHCDNLRnrKNEILEMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQ----G 371
Cdd:COG4913  261 AERYA-AARERLAELEYLR-AALRLWFAQRRLELL--EAELEELRAELARLEAELERLEARLDALREELDELEAQirgnG 336

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 27477127  372 EAALNDAKCKLAGLEEALQKAKQDmaclLKEYQEVMNSkLGLDIE 416
Cdd:COG4913  337 GDRLEQLEREIERLERELEERERR----RARLEALLAA-LGLPLP 376
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 327-396 2.55e-04

Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.


Pssm-ID: 426757 [Multi-domain]  Cd Length: 108  Bit Score: 40.65  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   327 DNLRNRKNEILEMNKLIQ------RLQQETENVKAQRCKLEGAIAEAEQQGE------AALNDAKCKLAGLEEALQKAKQ 394
Cdd:pfam02403  16 ESLKKRGVDVLDVDELLEldekrrELQVELEELQAERNELSKEIGQAKKKKEdadaliAEVKELKDELKALEAELKELEA 95


                  ..
gi 27477127   395 DM 396
Cdd:pfam02403  96 EL 97
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 173-511 3.14e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 3.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 173 ISALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEelslrpcVENEFVALKKDVDTAflmKADLETNAEALV--QEI 250
Cdd:COG3883  18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEIDKL---QAEIAEAEAEIEerREE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 251 --DFLKSLYEE-------EIcLLQSQ-----ISETSVIVK-MDNSREldvdgIIAEIKAQYDDIASRsKAEAEAwyqcRY 315
Cdd:COG3883  88 lgERARALYRSggsvsylDV-LLGSEsfsdfLDRLSALSKiADADAD-----LLEELKADKAELEAK-KAELEA----KL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 316 EELRVTAgnhcDNLRNRKNEIL----EMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQGEAALNDAKCKLAGLEEALQK 391
Cdd:COG3883 157 AELEALK----AELEAAKAELEaqqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 392 AKQDMAcllKEYQEVMNSKLGLDIEIATYRRLLEGEEHRLCEGIGPVniSVSSSKGAFLYEPCGVSTPVLSTGVLRSNGG 471
Cdd:COG3883 233 AAAAAA---AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGA--AAASAAGGGAGGAGGGGGGGGAASGGSGGGS 307

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 27477127 472 CSIVGTGELYVPCEPQGLLSCGSGRKSSMTLGAGGSSPSH 511
Cdd:COG3883 308 GGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGG 347
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 196-422 3.18e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 3.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 196 SLQAALEGYKKKYEEelslrpcVENEFVALKKDVDTAFLMKADLETNAEALVQEIDflksLYEEEICLLQSQISETsviv 275
Cdd:COG4942  24 EAEAELEQLQQEIAE-------LEKELAALKKEEKALLKQLAALERRIAALARRIR----ALEQELAALEAELAEL---- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 276 kmdnsrELDVDGIIAEIKAQYDDIASRSKAeAEAWYQCRYEELRVTAGNHCDNLRN----------RKNEILEMNKLIQR 345
Cdd:COG4942  89 ------EKEIAELRAELEAQKEELAELLRA-LYRLGRQPPLALLLSPEDFLDAVRRlqylkylapaRREQAEELRADLAE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 346 LQQETENVKAQRCKLEGAIAEAEQQG---EAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRR 422
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERaalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
fliH PRK06669
flagellar assembly protein H; Validated
 252-408 7.08e-04

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 41.54  E-value: 7.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  252 FLKSLYEEEICLLQSQISETSVIVKMDNSREldVDGIIAEIKAQYDDIASRSKAEAEAwyqcryEELRVTAgnhcdnlrn 331
Cdd:PRK06669  26 RFKVLSIKEKERLREEEEEQVEQLREEANDE--AKEIIEEAEEDAFEIVEAAEEEAKE------ELLKKTD--------- 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477127  332 rkneilEMNKLIQRLQQETENvkaqrcklegAIAEAEQQGEAALNDAKCKlaGLEEALQKAKQDMaclLKEYQEVMN 408
Cdd:PRK06669  89 ------EASSIIEKLQMQIER----------EQEEWEEELERLIEEAKAE--GYEEGYEKGREEG---LEEVRELIE 144
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 331-430 1.85e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127    331 NRKNEILEMNKLIQRLQQETENVKAQRCKLEGAIAEAEQQGEAA----------LNDAKCKLAGLEEALQKAKQDMACLL 400
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeleelsrqISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110
                   ....*....|....*....|....*....|.
gi 27477127    401 KEYQEVMNSKLGLDIEIATYR-RLLEGEEHR 430
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEeELAEAEAEI 784
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 219-508 5.29e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 5.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 219 ENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEeiclLQSQISETSVivKMDNSRElDVDGIIAEIKAQYDD 298
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQA--EIDKLQA-EIAEAEAEIEERREE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 299 IASRSKAEAEAWYQCRYEELRVTAGNHCDNLRN---------RKNEILEmnkLIQRLQQETENVKAQrckLEGAIAEAEQ 369
Cdd:COG3883  88 LGERARALYRSGGSVSYLDVLLGSESFSDFLDRlsalskiadADADLLE---ELKADKAELEAKKAE---LEAKLAELEA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 370 QgeaaLNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEI-ATYRRLLEGEEHRLCEGIGPVNISVSSSKGA 448
Cdd:COG3883 162 L----KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELaAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127 449 FLYEPCGVSTPVLSTGVLRSNGGCSIVGTGELYVPCEPQGLLSCGSGRKSSMTLGAGGSS 508
Cdd:COG3883 238 AAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGG 297
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
117-405 7.65e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 7.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  117 KRDEKEQIKCLNNRFASFINKVRFLEQKNKLL-ETKW---------NFMQQQRCCQTNIEPIFEGY---ISALRRQLDCV 183
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELkELKEkaeeyiklsEFYEEYLDELREIEKRLSRLeeeINGIEERIKEL 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  184 SGDRVRLE------SELCSLQAALEGYKKKYEEELSLrpcvENEFVALKKDvdtaflmKADLET-NAEALVQEIDFLKSL 256
Cdd:PRK03918 334 EEKEERLEelkkklKELEKRLEELEERHELYEEAKAK----KEELERLKKR-------LTGLTPeKLEKELEELEKAKEE 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  257 YEEEICLLQSQISETSVIVKMDNS----------------RELDVD---GIIAEIKAQYDDIASRSKAEAEAWYQCRYEE 317
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgRELTEEhrkELLEEYTAELKRIEKELKEIEEKERKLRKEL 482

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  318 LRVtagnhcDNLRNRKNEILEMNKLIQRLQ------------------QETENVKAQRCKLEGAIAEAEQQGEAaLNDAK 379
Cdd:PRK03918 483 REL------EKVLKKESELIKLKELAEQLKeleeklkkynleelekkaEEYEKLKEKLIKLKGEIKSLKKELEK-LEELK 555

                        330       340
                 ....*....|....*....|....*.
gi 27477127  380 CKLAGLEEALQKAKQDMACLLKEYQE 405
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEE 581
TMCO5 pfam14992
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ...
 302-427 8.40e-03

TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.


Pssm-ID: 464427 [Multi-domain]  Cd Length: 278  Bit Score: 38.16  E-value: 8.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127   302 RSKAEAEAWyqcryEELRVTAGNHCDNLRN---------RKNEILemNKLIQRLQQETE-----NVKAQRCKLEGAIAEA 367
Cdd:pfam14992  44 RSLAEDEER-----EELNFTIMEKEDALQEleletakleKKNEIL--VKSVMELQRKLSrksdkNTGLEQETLKQMLEEL 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477127   368 E---QQGEAALNDAKCKLAGLEEALQKAKQ---DMACLLKEYQEVMNSklgldIEIATYRRLLEGE 427
Cdd:pfam14992 117 KvklQQSEESCADQEKELAKVESDYQSVHQlceDQALCIKKYQEILRK-----MEEEKETRLLEKE 177
PRK12704 PRK12704
phosphodiesterase; Provisional
 331-405 8.55e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 8.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477127  331 NRKNEILE-----MNKLIQRLQQETENVKAQRCKLEGAIAEAEQQGE--AALN--DAKCKLagLEEALQKAKQDMACLLK 401
Cdd:PRK12704  99 DRKLELLEkreeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELEriSGLTaeEAKEIL--LEKVEEEARHEAAVLIK 176


                 ....
gi 27477127  402 EYQE 405
Cdd:PRK12704 177 EIEE 180
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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