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Conserved domains on  [gi|2217287185|ref|XP_047284153|]
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keratin, type II cytoskeletal 71 isoform X3 [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;
129-400 2.53e-115

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 341.90  E-value: 2.53e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 129 QEREQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQQLDLNNcKNNLEPILEGYISNLRKQLETLSGDRVRLDSELRN 208
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 209 VRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMDQEIKFFRCLFEAEITQIQSHISDMSVILS 288
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 289 MDNNRNLDLDSIIDEVRTQYEEIALKSKAEAEALYQTK------------------------------------------ 326
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKleelqqaaarngdalrsakeeitelrrtiqsleielqslkkq 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217287185 327 ASNLETAIADAEQRGDNALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEECR 400
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
16-126 6.71e-28

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 108.59  E-value: 6.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  16 GFSGCSAVLSGGSSSSFRAGS------------KGLSGGFGSRSLYSLGGVR--SLNVASGSGKSGGYGFG--------- 72
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSssrrggggggggGGGGGGFGSRSLYNLGGSKsiSISVAGGGSRPGSGFGFgggggggfg 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217287185  73 --------------RGRASGFAGSMFGSVALGP--------VCPTVCPPGGIHQVTVNESLLAPLNVELDPEIQKV 126
Cdd:pfam16208  81 ggfgggggggfgggGGFGGGFGGGGYGGGGFGGggfggrggFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
129-400 2.53e-115

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 341.90  E-value: 2.53e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 129 QEREQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQQLDLNNcKNNLEPILEGYISNLRKQLETLSGDRVRLDSELRN 208
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 209 VRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMDQEIKFFRCLFEAEITQIQSHISDMSVILS 288
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 289 MDNNRNLDLDSIIDEVRTQYEEIALKSKAEAEALYQTK------------------------------------------ 326
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKleelqqaaarngdalrsakeeitelrrtiqsleielqslkkq 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217287185 327 ASNLETAIADAEQRGDNALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEECR 400
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
16-126 6.71e-28

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 108.59  E-value: 6.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  16 GFSGCSAVLSGGSSSSFRAGS------------KGLSGGFGSRSLYSLGGVR--SLNVASGSGKSGGYGFG--------- 72
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSssrrggggggggGGGGGGFGSRSLYNLGGSKsiSISVAGGGSRPGSGFGFgggggggfg 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217287185  73 --------------RGRASGFAGSMFGSVALGP--------VCPTVCPPGGIHQVTVNESLLAPLNVELDPEIQKV 126
Cdd:pfam16208  81 ggfgggggggfgggGGFGGGFGGGGYGGGGFGGggfggrggFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
46 PHA02562
endonuclease subunit; Provisional
 146-390 1.02e-09

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 60.80  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 146 DKVRFLEQQNQVLETKWELL-QQLDLNNcknnlepileGYISNLRKQletlSGDRVrldSELRNVRDVVEDYKKRYEEEI 224
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIqQQIKTYN----------KNIEEQRKK----NGENI---ARKQNKYDELVEEAKTIKAEI 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 225 NKRTAAENEFVLLKKDVDAAYAN----KVELQAKVESMDQEIKFFR-------CL-----FEAEITQIQSHISDMSVILS 288
Cdd:PHA02562  237 EELTDELLNLVMDIEDPSAALNKlntaAAKIKSKIEQFQKVIKMYEkggvcptCTqqiseGPDRITKIKDKLKELQHSLE 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 289 MDNNRNLDLDSIIDEVRTQyeeialkSKAEAEalYQTKASNLETAIadaeQRGDNALKDARAKLDELEGALHQAKEELAR 368
Cdd:PHA02562  317 KLDTAIDELEEIMDEFNEQ-------SKKLLE--LKNKISTNKQSL----ITLVDKAKKVKAAIEELQAEFVDNAEELAK 383

                         250       260
                  ....*....|....*....|..
gi 2217287185 369 MLREYQELMSLKLALDMEIATY 390
Cdd:PHA02562  384 LQDELDKIVKTKSELVKEKYHR 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 128-376 3.27e-07

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: 53.14  E-value: 3.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  128 AQEREQ-IKALNNKFASFIDKVRFLEQQNQVLETKWELLQQL--DLNNCKNNLEPILEGY---ISNLRKQLETLSGDRVR 201
Cdd:TIGR02168  672 ILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEEleQLRKELEELSRQISALrkdLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  202 LDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMDQEIKffrcLFEAEITQIQSHIS 281
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT----LLNEEAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  282 DMSVILSMDNNRNLDLDSIIDEVRTQYEEIAL----------KSKAEAEALYQTKASnLETAIADAEQRGDNA---LKDA 348
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAeieeleelieELESELEALLNERAS-LEEALALLRSELEELseeLREL 906

                          250       260
                   ....*....|....*....|....*...
gi 2217287185  349 RAKLDELEGALHQAKEELARMLREYQEL 376
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGL 934
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 181-409 2.24e-06

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: 49.76  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 181 LEGYISNLRKQLETLSGDRVRLDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMDQ 260
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 261 EIKffRCLFEAeitQIQSHISDMSVILSMDN----NRNLD-LDSIIDEVRTQYEEIALKSK--AEAEALYQTKASNLETA 333
Cdd:COG4942   105 ELA--ELLRAL---YRLGRQPPLALLLSPEDfldaVRRLQyLKYLAPARREQAEELRADLAelAALRAELEAERAELEAL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 334 IAD--AEQRGDNALKDARAK-LDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEEC-RMSGEFPSPV 409
Cdd:COG4942   180 LAEleEERAALEALKAERQKlLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFaALKGKLPWPV 259
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 180-322 8.51e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.54  E-value: 8.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  180 ILEGYISNLRKQLETLSGDRVRLDSELRNVRDVVEDYKKRY---EEEINKRTAAENEFVLLKKDVDAAyankveLQAKVE 256
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKdalEEELRQLKQLEDELEDCDPTELDR------AKEKLK 214

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217287185  257 SMDQEIKFFRclfeAEITQIQSHISDMSVILSMDNNRNLDLDSIIDEVRTQYEEIALKSKAEAEAL 322
Cdd:smart00787 215 KLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKL 276
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
129-400 2.53e-115

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 341.90  E-value: 2.53e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 129 QEREQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQQLDLNNcKNNLEPILEGYISNLRKQLETLSGDRVRLDSELRN 208
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 209 VRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMDQEIKFFRCLFEAEITQIQSHISDMSVILS 288
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 289 MDNNRNLDLDSIIDEVRTQYEEIALKSKAEAEALYQTK------------------------------------------ 326
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKleelqqaaarngdalrsakeeitelrrtiqsleielqslkkq 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217287185 327 ASNLETAIADAEQRGDNALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEECR 400
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
16-126 6.71e-28

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 108.59  E-value: 6.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  16 GFSGCSAVLSGGSSSSFRAGS------------KGLSGGFGSRSLYSLGGVR--SLNVASGSGKSGGYGFG--------- 72
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSssrrggggggggGGGGGGFGSRSLYNLGGSKsiSISVAGGGSRPGSGFGFgggggggfg 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217287185  73 --------------RGRASGFAGSMFGSVALGP--------VCPTVCPPGGIHQVTVNESLLAPLNVELDPEIQKV 126
Cdd:pfam16208  81 ggfgggggggfgggGGFGGGFGGGGYGGGGFGGggfggrggFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
46 PHA02562
endonuclease subunit; Provisional
 146-390 1.02e-09

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 60.80  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 146 DKVRFLEQQNQVLETKWELL-QQLDLNNcknnlepileGYISNLRKQletlSGDRVrldSELRNVRDVVEDYKKRYEEEI 224
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIqQQIKTYN----------KNIEEQRKK----NGENI---ARKQNKYDELVEEAKTIKAEI 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 225 NKRTAAENEFVLLKKDVDAAYAN----KVELQAKVESMDQEIKFFR-------CL-----FEAEITQIQSHISDMSVILS 288
Cdd:PHA02562  237 EELTDELLNLVMDIEDPSAALNKlntaAAKIKSKIEQFQKVIKMYEkggvcptCTqqiseGPDRITKIKDKLKELQHSLE 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 289 MDNNRNLDLDSIIDEVRTQyeeialkSKAEAEalYQTKASNLETAIadaeQRGDNALKDARAKLDELEGALHQAKEELAR 368
Cdd:PHA02562  317 KLDTAIDELEEIMDEFNEQ-------SKKLLE--LKNKISTNKQSL----ITLVDKAKKVKAAIEELQAEFVDNAEELAK 383

                         250       260
                  ....*....|....*....|..
gi 2217287185 369 MLREYQELMSLKLALDMEIATY 390
Cdd:PHA02562  384 LQDELDKIVKTKSELVKEKYHR 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 128-376 3.27e-07

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: 53.14  E-value: 3.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  128 AQEREQ-IKALNNKFASFIDKVRFLEQQNQVLETKWELLQQL--DLNNCKNNLEPILEGY---ISNLRKQLETLSGDRVR 201
Cdd:TIGR02168  672 ILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEEleQLRKELEELSRQISALrkdLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  202 LDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMDQEIKffrcLFEAEITQIQSHIS 281
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT----LLNEEAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  282 DMSVILSMDNNRNLDLDSIIDEVRTQYEEIAL----------KSKAEAEALYQTKASnLETAIADAEQRGDNA---LKDA 348
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAeieeleelieELESELEALLNERAS-LEEALALLRSELEELseeLREL 906

                          250       260
                   ....*....|....*....|....*...
gi 2217287185  349 RAKLDELEGALHQAKEELARMLREYQEL 376
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGL 934
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 109-368 3.29e-07

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: 53.15  E-value: 3.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  109 ESLLAPLNVELDPEIQKVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLEtkwELLQQLDLNNCKnnlepiLEGYISNL 188
Cdd:TIGR02169  271 EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE---ERLAKLEAEIDK------LLAEIEEL 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  189 RKQLETLSGDRVRLDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMDQEIKffrcl 268
Cdd:TIGR02169  342 EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ----- 416

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  269 feaeitQIQSHISDMsvilsmdNNRNLDLDSIIDEVRTQYEEIALKSKAEAEALYQTKASnletaIADAEQRgdnaLKDA 348
Cdd:TIGR02169  417 ------RLSEELADL-------NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD-----LSKYEQE----LYDL 474

                          250       260
                   ....*....|....*....|
gi 2217287185  349 RAKLDELEGALHQAKEELAR 368
Cdd:TIGR02169  475 KEEYDRVEKELSKLQRELAE 494
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 102-396 5.16e-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: 52.42  E-value: 5.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 102 IHQVTVNESLLAPLNVELDPEIQKVRAQ-EREQIKalNNKFASFIDKVrFLEQQNQVLETKWELL----QQLDLNNCKNN 176
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTElEKEKLK--NIELTAHCDKL-LLENKELTQEASDMTLelkkHQEDIINCKKQ 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 177 LEPILegyisnlrKQLETLSGDRVRLDSELRNVRdvvEDYKKRYEE-----EINKRTAAENEFVLLKKDVDAAYAN---- 247
Cdd:pfam05483 529 EERML--------KQIENLEEKEMNLRDELESVR---EEFIQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILEnkcn 597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 248 ----KVELQAK-VESMDQEIKFFRCLFEAEITQIQSHisDMSVilsmdNNRNLDLDSiideVRTQYEEIALKSKAEAEaL 322
Cdd:pfam05483 598 nlkkQIENKNKnIEELHQENKALKKKGSAENKQLNAY--EIKV-----NKLELELAS----AKQKFEEIIDNYQKEIE-D 665

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 323 YQTKASNLETAIADAEQRGDNALK-----DARA--KLDELEGALHQAKEELARMLREY-----------QELMSLKLALD 384
Cdd:pfam05483 666 KKISEEKLLEEVEKAKAIADEAVKlqkeiDKRCqhKIAEMVALMEKHKHQYDKIIEERdselglyknkeQEQSSAKAALE 745

                         330
                  ....*....|..
gi 2217287185 385 MEIATYRKLLES 396
Cdd:pfam05483 746 IELSNIKAELLS 757
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 118-398 6.84e-07

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: 51.99  E-value: 6.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  118 ELDPEIQKVRAqEREQIKALNNKFASFIDKVRfleQQNQVLET-KWELLQQLDLNNCKNNLE-PILEGYISNLRKQLETL 195
Cdd:TIGR02169  167 EFDRKKEKALE-ELEEVEENIERLDLIIDEKR---QQLERLRReREKAERYQALLKEKREYEgYELLKEKEALERQKEAI 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  196 SGDRVRLDSELRNVRDVVEDYKKRYE------EEINKRTAA--ENEFVLLKKDVDAAYANKVELQAKVESMDQEIKffrc 267
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEeieqllEELNKKIKDlgEEEQLRVKEKIGELEAEIASLERSIAEKERELE---- 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  268 LFEAEITQIQSHISdmsvilsmdnnrnlDLDSIIDEVRTQYEEIALKsKAEAEALYQTKASNLETAIADAEQRgDNALKD 347
Cdd:TIGR02169  319 DAEERLAKLEAEID--------------KLLAEIEELEREIEEERKR-RDKLTEEYAELKEELEDLRAELEEV-DKEFAE 382

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217287185  348 ARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEE 398
Cdd:TIGR02169  383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 181-409 2.24e-06

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: 49.76  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 181 LEGYISNLRKQLETLSGDRVRLDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMDQ 260
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 261 EIKffRCLFEAeitQIQSHISDMSVILSMDN----NRNLD-LDSIIDEVRTQYEEIALKSK--AEAEALYQTKASNLETA 333
Cdd:COG4942   105 ELA--ELLRAL---YRLGRQPPLALLLSPEDfldaVRRLQyLKYLAPARREQAEELRADLAelAALRAELEAERAELEAL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 334 IAD--AEQRGDNALKDARAK-LDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEEC-RMSGEFPSPV 409
Cdd:COG4942   180 LAEleEERAALEALKAERQKlLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFaALKGKLPWPV 259
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 201-376 2.33e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.77  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 201 RLDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMDQEIKffRclFEAEITQIQshi 280
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK--K--YEEQLGNVR--- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 281 sdmsvilsmdNNRnlDLDSIIDEVRTQYEEIALKSKAEAEALYQtkASNLETAIADAEQRGDNALKDARAKLDELEGALH 360
Cdd:COG1579    87 ----------NNK--EYEALQKEIESLKRRISDLEDEILELMER--IEELEEELAELEAELAELEAELEEKKAELDEELA 152

                         170
                  ....*....|....*.
gi 2217287185 361 QAKEELARMLREYQEL 376
Cdd:COG1579   153 ELEAELEELEAEREEL 168
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-398 3.05e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 181 LEGYISNLRKQLETLSGDRVRLDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMDQ 260
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 261 EIKffrcLFEAEITQIQSHISDMSVILSMDNNRNLDLDSIIDEVRTQYEEiALKSKAEAEALYQTKASNLEtAIADAEQR 340
Cdd:COG1196   317 RLE----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-AEEALLEAEAELAEAEEELE-ELAEELLE 390

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217287185 341 GDNALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEE 398
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
180-408 9.84e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 9.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 180 ILEGYI-SNLRKQLETLSGDRVRLDSELRNVRDVVEDYKKRYEEeinkrTAAENEFVLLKKDVDAAYANKVELQAKVESM 258
Cdd:COG3206   157 LAEAYLeQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEA 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 259 DQEIKffrcLFEAEITQIQSHISDMSVILSMDNNrnldlDSIIDEVRTQYEEIALKsKAEAEALY----------QTKAS 328
Cdd:COG3206   232 RAELA----EAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAE-LAELSARYtpnhpdvialRAQIA 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 329 NLETAIADAEQRG----DNALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLE-SEECRMSG 403
Cdd:COG3206   302 ALRAQLQQEAQRIlaslEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQrLEEARLAE 381


                  ....*
gi 2217287185 404 EFPSP 408
Cdd:COG3206   382 ALTVG 386
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 129-380 1.26e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.71  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 129 QEREQIKALNNKFASfidKVRFLEQQNQVLETKWELLQQL---------DLNNCKNNLEPI---LEGYISNLRKQLETLS 196
Cdd:TIGR04523 398 SKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETiiknnseikDLTNQDSVKELIiknLDNTRESLETQLKVLS 474

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 197 GDRVRLDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDaayankvELQAKVESMdqeikffrclfEAEITQI 276
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS-------SLKEKIEKL-----------ESEKKEK 536

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 277 QSHISDM-SVILSMDNnrNLDLDSIIDEVRTQYEEIAlKSKAEAEALyqtKASN--LETAIADAEQRgdnaLKDARAKLD 353
Cdd:TIGR04523 537 ESKISDLeDELNKDDF--ELKKENLEKEIDEKNKEIE-ELKQTQKSL---KKKQeeKQELIDQKEKE----KKDLIKEIE 606

                         250       260
                  ....*....|....*....|....*..
gi 2217287185 354 ELEGALHQAKEELARMLREYQELMSLK 380
Cdd:TIGR04523 607 EKEKKISSLEKELEKAKKENEKLSSII 633
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 122-387 1.62e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 122 EIQKVRAQEREQ------IKALNNKFASFIDKVRFLEQQNQVLETKWELLQQ------LDLNNCKNNLEPILEGYISNLR 189
Cdd:TIGR04523 188 NIDKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQeinektTEISNTQTQLNQLKDEQNKIKK 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 190 ------KQLETLSGDRVRLDSELRNVRDVVEDYKKRYEEEINKRtaaenefvlLKKDVDAAYANKVELQAKVesmDQEIK 263
Cdd:TIGR04523 268 qlsekqKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKE---------LKSELKNQEKKLEEIQNQI---SQNNK 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 264 ffrclfeaEITQIQSHISDMSVILSMDNNRNLDLDSIIDEVRTQYEEIalksKAEAEAlYQTKASNLETAIADAEQRGDN 343
Cdd:TIGR04523 336 --------IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL----KKENQS-YKQEIKNLESQINDLESKIQN 402

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2217287185 344 ALKDARakldELEGALHQAKEELARMLREYQELMSLKLALDMEI 387
Cdd:TIGR04523 403 QEKLNQ----QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI 442
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
132-395 2.43e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 132 EQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQQLdlnncKNNLEPILEgYISNLRKQLETLSGDRVRLDSELRNVRD 211
Cdd:PRK03918  193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKE-EIEELEKELESLEGSKRKLEEKIRELEE 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 212 VVEDYKKRyEEEINKRTAAENEfvlLKKDVDaAYANKVELQAKVESMDQEIKFFRCLFEAEITQIQSHISDmsviLSMDN 291
Cdd:PRK03918  267 RIEELKKE-IEELEEKVKELKE---LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKE 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 292 NRNLDLDSIIDEVRTQYEEiaLKSKAEaeaLYQTKASNLETAIADAEQRGDNALKDARAKLDELEgalhQAKEELArmlR 371
Cdd:PRK03918  338 ERLEELKKKLKELEKRLEE--LEERHE---LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE----KAKEEIE---E 405

                         250       260
                  ....*....|....*....|....
gi 2217287185 372 EYQELMSLKLALDMEIATYRKLLE 395
Cdd:PRK03918  406 EISKITARIGELKKEIKELKKAIE 429
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 185-398 4.20e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 185 ISNLRKQLETLSGDRVRLDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESM------ 258
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyr 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 259 -DQEIKFFRCLFEAE-ITQIQSHISDMSVILSMDNNrnldldsIIDEVRTQYEEIalkskAEAEALYQTKASNLETAIAD 336
Cdd:COG3883    98 sGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADAD-------LLEELKADKAEL-----EAKKAELEAKLAELEALKAE 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217287185 337 AEQrgdnALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEE 398
Cdd:COG3883   166 LEA----AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
180-376 1.29e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 180 ILEGYISNLRKQLETLSGDRVRLDS----ELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDaayankvELQAKV 255
Cdd:COG4717    46 MLLERLEKEADELFKPQGRKPELNLkelkELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE-------ELREEL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 256 ESMDQEIKFFRCLfeAEITQIQSHISDmsvilsmdnnrnldLDSIIDEVRTQYEEI--ALKSKAEAEALYQTKASNLETA 333
Cdd:COG4717   119 EKLEKLLQLLPLY--QELEALEAELAE--------------LPERLEELEERLEELreLEEELEELEAELAELQEELEEL 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217287185 334 IADAEQRGDNALKDARAKLDELEGALHQAKEELARMLREYQEL 376
Cdd:COG4717   183 LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
185-397 2.33e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  185 ISNLRKQLETLSGDRVRLDSELRNVR---DVVEDYKKRYEEEINKRT-----------AAENEFVLLKKDVDAAYANKVE 250
Cdd:COG4913    227 ADALVEHFDDLERAHEALEDAREQIEllePIRELAERYAAARERLAEleylraalrlwFAQRRLELLEAELEELRAELAR 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  251 LQAKVESMDQEIKffrcLFEAEITQIQSHISDmsvilsmDNNRNLD-LDSIIDEVRTQYEEIALKSKAEAEALYQTKASN 329
Cdd:COG4913    307 LEAELERLEARLD----ALREELDELEAQIRG-------NGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPL 375

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217287185  330 LETA---------IADAEQRGDNALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESE 397
Cdd:COG4913    376 PASAeefaalraeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
189-375 2.44e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  189 RKQLETLSGDRVRLDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANK--VELQAKVESMDQEIKFFR 266
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiAELEAELERLDASSDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  267 CL------FEAEITQIQSHISDMSVILSMDNNRNLDLDSIIDEVRTQYEEIALKSKAEAEALYQTKASNletaiADAEQR 340
Cdd:COG4913    689 ALeeqleeLEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA-----ALGDAV 763

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2217287185  341 GDNALKDARAKLDELEGALHQAKEELARMLREYQE 375
Cdd:COG4913    764 ERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-392 3.10e-04

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: 43.51  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  167 QLDLNNCKNNLEPiLEGYISNLRKQLETLSGDRVR------LDSELRNVRdvVEDYKKRYEEEINKRTAAENEFVLLKKD 240
Cdd:TIGR02168  178 ERKLERTRENLDR-LEDILNELERQLKSLERQAEKaerykeLKAELRELE--LALLVLRLEELREELEELQEELKEAEEE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  241 VDAAYANKVELQAKVEsmdqEIKFFRCLFEAEITQIQShisdmsvilsmdnnRNLDLDSIIDEVRTQYEEIalksKAEAE 320
Cdd:TIGR02168  255 LEELTAELQELEEKLE----ELRLEVSELEEEIEELQK--------------ELYALANEISRLEQQKQIL----RERLA 312

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217287185  321 ALyQTKASNLETAIADAEQRGDNA---LKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRK 392
Cdd:TIGR02168  313 NL-ERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
151-395 4.31e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 151 LEQQNQVLETKWELLQQL--DLNNCKNNLEPiLEGYISNLRKQLETLSGDRVRLDSELRnvrdVVEDYKKRYEEEINKrt 228
Cdd:COG4372    47 LEQLREELEQAREELEQLeeELEQARSELEQ-LEEELEELNEQLQAAQAELAQAQEELE----SLQEEAEELQEELEE-- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 229 aAENEFVLLKKDVDAAYANKVELQAKVESMDQEIKffrcLFEAEITQIQSHISDMSVILSMDNNRNldLDSIIDEVRTQY 308
Cdd:COG4372   120 -LQKERQDLEQQRKQLEAQIAELQSEIAEREEELK----ELEEQLESLQEELAALEQELQALSEAE--AEQALDELLKEA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 309 EEIALKSKAEAEALYQTKASNLETAIADAEQRGDNALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIA 388
Cdd:COG4372   193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272


                  ....*..
gi 2217287185 389 TYRKLLE 395
Cdd:COG4372   273 TEEEELE 279
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 180-322 8.51e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.54  E-value: 8.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  180 ILEGYISNLRKQLETLSGDRVRLDSELRNVRDVVEDYKKRY---EEEINKRTAAENEFVLLKKDVDAAyankveLQAKVE 256
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKdalEEELRQLKQLEDELEDCDPTELDR------AKEKLK 214

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217287185  257 SMDQEIKFFRclfeAEITQIQSHISDMSVILSMDNNRNLDLDSIIDEVRTQYEEIALKSKAEAEAL 322
Cdd:smart00787 215 KLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKL 276
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 122-263 1.12e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 122 EIQKVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQQL------DLNNCKNNLEpilegyISNLRKQLETL 195
Cdd:COG1579    28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeQLGNVRNNKE------YEALQKEIESL 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217287185 196 SGDRVRLDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYAnkvELQAKVESMDQEIK 263
Cdd:COG1579   102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAERE 166
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 188-374 1.23e-03

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: 41.59  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  188 LRKQLETLSGDRVRLDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMDQEIKFFRc 267
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK- 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  268 lfeAEITQIQSHISDMSVILS-----MDNNRNLDLDSIIDEVRTQYEEI----------------ALKSKAEAEALYQTK 326
Cdd:TIGR02169  758 ---SELKELEARIEELEEDLHkleeaLNDLEARLSHSRIPEIQAELSKLeeevsriearlreieqKLNRLTLEKEYLEKE 834

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2217287185  327 ASNLETAIADAEQRgdnaLKDARAKLDELEGalhqAKEELARMLREYQ 374
Cdd:TIGR02169  835 IQELQEQRIDLKEQ----IKSIEKEIENLNG----KKEELEEELEELE 874
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 106-369 1.93e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 40.10  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 106 TVNESLLAPLNVELDPEIQKVRAQEreqikalnnkfASFIDKVRFLEqqNQVLEtKWELLQQLDlnncknnlepilegyI 185
Cdd:pfam00529   3 PLTKGVEAPGRVVVSGNAKAVQPQV-----------SGIVTRVLVKE--GDRVK-AGDVLFQLD---------------P 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 186 SNLRKQLETLSGDRVRLDSELRnvrdvvedykkRYEEEINKRTAAENEFVLLKKDVDAAYANKVELQAKVESMdqeikff 265
Cdd:pfam00529  54 TDYQAALDSAEAQLAKAQAQVA-----------RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAA------- 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 266 rclfEAEITQIQSHISDMSVILSMDNNRNLDLDSIIDEVRTQyEEIALKSKAEAEALYQTKASNLETAIADAEQRgdnaL 345
Cdd:pfam00529 116 ----QAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQA-QANLLATVAQLDQIYVQITQSAAENQAEVRSE----L 186

                         250       260
                  ....*....|....*....|....
gi 2217287185 346 KDARAKLDELEGALHQAKEELARM 369
Cdd:pfam00529 187 SGAQLQIAEAEAELKLAKLDLERT 210
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 122-368 1.93e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.61  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 122 EIQKVRAQE---REQIKALNNKFASFIDKVrfLEQQNQVLETKWELLQQLDlnncknNLEPILEGYiSNL---------R 189
Cdd:pfam06160 108 ELDELLESEeknREEVEELKDKYRELRKTL--LANRFSYGPAIDELEKQLA------EIEEEFSQF-EELtesgdyleaR 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 190 KQLETLSGDRVRLDSELRNVRDVVEDYKKRYEEEINK-----RTAAENEFVL-----------LKKDVDAAYANKVEL-- 251
Cdd:pfam06160 179 EVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEElkegyREMEEEGYALehlnvdkeiqqLEEQLEENLALLENLel 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 252 ---QAKVESMDQEIKFFRCLFEAEIT---QIQSHISDMSVILS--MDNNRNL----------------------DLDSII 301
Cdd:pfam06160 259 deaEEALEEIEERIDQLYDLLEKEVDakkYVEKNLPEIEDYLEhaEEQNKELkeelervqqsytlnenelervrGLEKQL 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 302 DEVRTQYEEIALKSkAEAEALYQTKASNLE------TAIADAEQRGDNAL-------KDARAKLDELEGALHQAKEELAR 368
Cdd:pfam06160 339 EELEKRYDEIVERL-EEKEVAYSELQEELEeileqlEEIEEEQEEFKESLqslrkdeLEAREKLDEFKLELREIKRLVEK 417
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
120-372 2.38e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 120 DPEIQKVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLETKWEllqqldlnncknnlepILEGYISNLRKQLETLSGDR 199
Cdd:PRK02224  323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA----------------ELESELEEAREAVEDRREEI 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 200 VRLDSELRNVRDVVEDYKKRYEEeinkrtaAENEFVLLKKDVDAAYANKVELQAKVESMDQEIKFFRCLFEA----EITQ 275
Cdd:PRK02224  387 EELEEEIEELRERFGDAPVDLGN-------AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpECGQ 459

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 276 IQSHISDMSVIlSMDNNRNLDLDSIIDEVRTQYEEIA-----LKSKAEAEALYQT---KASNLETAIADAEQRGDN---A 344
Cdd:PRK02224  460 PVEGSPHVETI-EEDRERVEELEAELEDLEEEVEEVEerlerAEDLVEAEDRIERleeRREDLEELIAERRETIEEkreR 538

                         250       260
                  ....*....|....*....|....*...
gi 2217287185 345 LKDARAKLDELEgALHQAKEELARMLRE 372
Cdd:PRK02224  539 AEELRERAAELE-AEAEEKREAAAEAEE 565
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 310-375 3.22e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 38.23  E-value: 3.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217287185 310 EIALKSKAEAEALYQTKASNLETAIADAEQRGDNALKDARAKLDElegALHQAKEELARMLREYQE 375
Cdd:COG0711    41 AEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEE---AKAEAEAEAERIIAQAEA 103
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
122-398 4.15e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 122 EIQKVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLETkWELLQQLD--LNNCKNNLEPILEGY--ISNLRKQLETLSG 197
Cdd:COG4717    92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEaeLAELPERLEELEERLeeLRELEEELEELEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 198 DRVRLDSELRNVRDV--------VEDYKKRYEEEINKRTAAENEFVLLKKDVDAA------YANKVELQAKVESMDQ--- 260
Cdd:COG4717   171 ELAELQEELEELLEQlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELeeeleqLENELEAAALEERLKEarl 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 261 -------------------------------------------------------EIKFFRCLFEAEITQIQSHISDMSV 285
Cdd:COG4717   251 llliaaallallglggsllsliltiagvlflvlgllallflllarekaslgkeaeELQALPALEELEEEELEELLAALGL 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 286 ILSMDNNRNLDLDSIIDEVRTQYEEIA-LKSKAEAEALYQTKASNLETAIADAEQRGDNALKDARaKLDELEGALHQAKE 364
Cdd:COG4717   331 PPDLSPEELLELLDRIEELQELLREAEeLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEELEE 409

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2217287185 365 ELARMLREYQELMSL--KLALDMEIATYRKLLESEE 398
Cdd:COG4717   410 QLEELLGELEELLEAldEEELEEELEELEEELEELE 445
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 181-380 4.75e-03

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: 39.77  E-value: 4.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  181 LEGYISNLRKQLETLSGDRVRLDSELRNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAyanKVELQAKVESMDQ 260
Cdd:pfam01576  494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAL---TQQLEEKAAAYDK 570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  261 eikffrclFEAEITQIQSHISDMSVILsmDNNRNldLDSIIDEVRTQYEEIAlkskAEAEALYQTKASNLETAIADAEQR 340
Cdd:pfam01576  571 --------LEKTKNRLQQELDDLLVDL--DHQRQ--LVSNLEKKQKKFDQML----AEEKAISARYAEERDRAEAEAREK 634

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2217287185  341 GDNALKDARAkLDELEGalhqAKEELAR---MLR-EYQELMSLK 380
Cdd:pfam01576  635 ETRALSLARA-LEEALE----AKEELERtnkQLRaEMEDLVSSK 673
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-398 6.22e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 188 LRKQLETLSGDRvrldselrnvrDVVEDYKKrYEEEINKRtaaENEFVLLKKDvdaayankvELQAKVESMDQEIKffrc 267
Cdd:COG1196   198 LERQLEPLERQA-----------EKAERYRE-LKEELKEL---EAELLLLKLR---------ELEAELEELEAELE---- 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 268 LFEAEITQIQSHISDmsvilsmdnnrnldLDSIIDEVRTQYEEIALKSKAEAEALYQTKAS--NLETAIADAEQRgdnaL 345
Cdd:COG1196   250 ELEAELEELEAELAE--------------LEAELEELRLELEELELELEEAQAEEYELLAElaRLEQDIARLEER----R 311

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217287185 346 KDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEE 398
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
PRK09039 PRK09039
peptidoglycan -binding protein;
270-400 7.15e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.41  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 270 EAEITQIQSHISDMSVILSMDNNRNLDLDSIIDEVRtqyeeiALKSKAEAEalyqtkASNLETAIADAEQRGDNALKDAr 349
Cdd:PRK09039   52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR------ASLSAAEAE------RSRLQALLAELAGAGAAAEGRA- 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217287185 350 aklDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEECR 400
Cdd:PRK09039  119 ---GELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKR 166
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 296-367 7.74e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 38.55  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 296 DLDSIIDEVRTQYEEI------ALKSKAEAEALYQTKASNLETAI-------ADAEQRGDNALKDARAKLDELEGALHQA 362
Cdd:TIGR04320 258 ALQAKLATAQADLAAAqtalntAQAALTSAQTAYAAAQAALATAQkelanaqAQALQTAQNNLATAQAALANAEARLAKA 337


                  ....*
gi 2217287185 363 KEELA 367
Cdd:TIGR04320 338 KEALA 342
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
131-389 8.37e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 8.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  131 REQIKALNNKFASFIDKVRFLEQQNQVLETKWELLQQL-DLNNCKNNLEPILEGyISNLRKQLETL---SGDRVRLDSEL 206
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLaEYSWDEIDVASAERE-IAELEAELERLdasSDDLAALEEQL 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  207 RNVRDVVEDYKKRYEEEINKRTAAENEFVLLKKDVDAAYANKVELqakvESMDQEIKFFRC--LFEAEItqIQSHISDMS 284
Cdd:COG4913    695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA----EDLARLELRALLeeRFAAAL--GDAVERELR 768

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185  285 VILSmdnNRNLDLDSIIDEVRTQYEEIALKSKAEaealYQTKASNLETAIADAEqrgdnalkDARAKLDELEG-ALHQAK 363
Cdd:COG4913    769 ENLE---ERIDALRARLNRAEEELERAMRAFNRE----WPAETADLDADLESLP--------EYLALLDRLEEdGLPEYE 833

                          250       260
                   ....*....|....*....|....*...
gi 2217287185  364 EELARMLRE--YQELMSLKLALDMEIAT 389
Cdd:COG4913    834 ERFKELLNEnsIEFVADLLSKLRRAIRE 861
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
301-395 1.00e-02

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 1.00e-02
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287185 301 IDEVRTQYEEIALKSKAEAEALY----QTKASNLETAIADAEQRgdnaLKDARAKLDELEGALHQAKE--ELARMLREYQ 374
Cdd:COG4717   404 LEELEEQLEELLGELEELLEALDeeelEEELEELEEELEELEEE----LEELREELAELEAELEQLEEdgELAELLQELE 479

                          90       100
                  ....*....|....*....|.
gi 2217287185 375 ELMSLKLALDMEIATYRKLLE 395
Cdd:COG4717   480 ELKAELRELAEEWAALKLALE 500
 
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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