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Conserved domains on  [gi|226246663|ref|NP_001139697|]
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keratin, type II cytoskeletal 72 isoform 1 [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;
124-437 2.77e-139

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 403.92  E-value: 2.77e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  124 QEREQIKALNNKFASFIDKVRFLEQQNQVLETKWNLLQQLDLNNcRKNLEPIYEGYISNLQKQLEMLSGDGVRLDSELRN 203
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  204 MQDLVEDYKKRYEVEINRRTAAENEFVVLKKDVDAAYMNKVELQAKVDSLTDEIKFFKCLYEGEITQIQSHISDTSIVLS 283
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  284 MDNNRDLDLDSIIAEVRAQYEEIALKSKAEAETLYQTKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQ 363
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226246663  364 CADLETAIADAEQRGDCALKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRKLLESEECR 437
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
15-121 1.45e-18

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 82.78  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   15 GFSGCSAVLSGGIGSSSASFR-ARVKG---------SASFGSKSLSCLGGSRSLALSAAARRGGGRLGG----------- 73
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSsSRRGGgggggggggGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFgfgggggggfg 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226246663   74 --------------------FVGTAFGSAGL---------GPKCPsVCPPGGIPQVTVNKSLLAPLNVEMDPEIQRV 121
Cdd:pfam16208  81 ggfgggggggfgggggfgggFGGGGYGGGGFggggfggrgGFGGP-PCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
124-437 2.77e-139

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 403.92  E-value: 2.77e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  124 QEREQIKALNNKFASFIDKVRFLEQQNQVLETKWNLLQQLDLNNcRKNLEPIYEGYISNLQKQLEMLSGDGVRLDSELRN 203
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  204 MQDLVEDYKKRYEVEINRRTAAENEFVVLKKDVDAAYMNKVELQAKVDSLTDEIKFFKCLYEGEITQIQSHISDTSIVLS 283
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  284 MDNNRDLDLDSIIAEVRAQYEEIALKSKAEAETLYQTKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQ 363
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226246663  364 CADLETAIADAEQRGDCALKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRKLLESEECR 437
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
15-121 1.45e-18

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 82.78  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   15 GFSGCSAVLSGGIGSSSASFR-ARVKG---------SASFGSKSLSCLGGSRSLALSAAARRGGGRLGG----------- 73
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSsSRRGGgggggggggGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFgfgggggggfg 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226246663   74 --------------------FVGTAFGSAGL---------GPKCPsVCPPGGIPQVTVNKSLLAPLNVEMDPEIQRV 121
Cdd:pfam16208  81 ggfgggggggfgggggfgggFGGGGYGGGGFggggfggrgGFGGP-PCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
46 PHA02562
endonuclease subunit; Provisional
 141-427 2.95e-09

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 59.26  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 141 DKVRFLEQQNQVLETKWNLL-QQLDlnncrknlepIYEGYISNLQKQlemlsgDGVRLDsELRNMQDLVEDYKKRYEVEI 219
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIqQQIK----------TYNKNIEEQRKK------NGENIA-RKQNKYDELVEEAKTIKAEI 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 220 NRRTAAENEFVVLKKDVDAAY----MNKVELQAKVDSLTDEIKFFKclYEGEITQIQSHISDTsivlsmdnnrdldlDSI 295
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE--KGGVCPTCTQQISEG--------------PDR 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 296 IAEVRAQYEEIALKSKAEaetlyQTKIQELQVTagqhgddlkltKAEISELNRLIQRIRSEIGNVKkqcADLETAIADAe 375
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKL-----DTAIDELEEI-----------MDEFNEQSKKLLELKNKISTNK---QSLITLVDKA- 360

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 226246663 376 qrgdcalKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATY 427
Cdd:PHA02562 361 -------KKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 123-435 7.42e-09

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: 58.53  E-value: 7.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   123 AQEREQ-IKALNNKFASFIDKVRFLEQQNQVLETKWNLLQQlDLNNCRKNLEPIyEGYISNLQKQLEMLSGDGVRLDSEL 201
Cdd:TIGR02168  672 ILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   202 RNMQDLVEDYKKRYEVEINRRTAAENEFVVLKKdvdaaymNKVELQAKVDSLTDEIKffkcLYEGEITQIQSHISDTSIV 281
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELK----ALREALDELRAELTLLNEE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   282 LSMDNNRDLDLDSIIAEVRAQYEEIALKSKAEAETL--YQTKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGN 359
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   360 VKKQCADLETAIadaeqrgdcalKDARAKLDELEGALHQAKEELARMLREYQEL-----VSLKLALDMEIATYRKLLESE 434
Cdd:TIGR02168  899 LSEELRELESKR-----------SELRRELEELREKLAQLELRLEGLEVRIDNLqerlsEEYSLTLEEAEALENKIEDDE 967


                   .
gi 226246663   435 E 435
Cdd:TIGR02168  968 E 968
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
292-434 1.95e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  292 LDSIIAEVRAQYEEI--ALKSKAEAETLYQTKIQELQVTAGQH-GDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLE 368
Cdd:COG4913   293 LEAELEELRAELARLeaELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALG 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  369 --------------TAIADAEQRGDCALKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRKLLESE 434
Cdd:COG4913   373 lplpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 177-351 9.03e-03

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: 38.07  E-value: 9.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   177 EGYISNLQKQLEMLSGDGVRLDSELRNMQDLVEDYKKRYEV---EINRRTAAENEFVVLKKDVDAAymnkveLQAKVDSL 253
Cdd:smart00787 143 EGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDAleeELRQLKQLEDELEDCDPTELDR------AKEKLKKL 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   254 TDEIKFFKclyeGEITQIQSHISDTSIVLSMDNNRDLDLDSIIAEVRAQYEEIALKSKAEAETLyQTKIQELQVTAGQHg 333
Cdd:smart00787 217 LQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKL-KEQLKLLQSLTGWK- 290

                          170
                   ....*....|....*....
gi 226246663   334 dDLKLTKAEIS-ELNRLIQ 351
Cdd:smart00787 291 -ITKLSGNTLSmTYDREIN 308
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
124-437 2.77e-139

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 403.92  E-value: 2.77e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  124 QEREQIKALNNKFASFIDKVRFLEQQNQVLETKWNLLQQLDLNNcRKNLEPIYEGYISNLQKQLEMLSGDGVRLDSELRN 203
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  204 MQDLVEDYKKRYEVEINRRTAAENEFVVLKKDVDAAYMNKVELQAKVDSLTDEIKFFKCLYEGEITQIQSHISDTSIVLS 283
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  284 MDNNRDLDLDSIIAEVRAQYEEIALKSKAEAETLYQTKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQ 363
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226246663  364 CADLETAIADAEQRGDCALKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRKLLESEECR 437
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
15-121 1.45e-18

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 82.78  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   15 GFSGCSAVLSGGIGSSSASFR-ARVKG---------SASFGSKSLSCLGGSRSLALSAAARRGGGRLGG----------- 73
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSsSRRGGgggggggggGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFgfgggggggfg 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226246663   74 --------------------FVGTAFGSAGL---------GPKCPsVCPPGGIPQVTVNKSLLAPLNVEMDPEIQRV 121
Cdd:pfam16208  81 ggfgggggggfgggggfgggFGGGGYGGGGFggggfggrgGFGGP-PCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
46 PHA02562
endonuclease subunit; Provisional
 141-427 2.95e-09

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 59.26  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 141 DKVRFLEQQNQVLETKWNLL-QQLDlnncrknlepIYEGYISNLQKQlemlsgDGVRLDsELRNMQDLVEDYKKRYEVEI 219
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIqQQIK----------TYNKNIEEQRKK------NGENIA-RKQNKYDELVEEAKTIKAEI 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 220 NRRTAAENEFVVLKKDVDAAY----MNKVELQAKVDSLTDEIKFFKclYEGEITQIQSHISDTsivlsmdnnrdldlDSI 295
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE--KGGVCPTCTQQISEG--------------PDR 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 296 IAEVRAQYEEIALKSKAEaetlyQTKIQELQVTagqhgddlkltKAEISELNRLIQRIRSEIGNVKkqcADLETAIADAe 375
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKL-----DTAIDELEEI-----------MDEFNEQSKKLLELKNKISTNK---QSLITLVDKA- 360

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 226246663 376 qrgdcalKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATY 427
Cdd:PHA02562 361 -------KKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 123-435 7.42e-09

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: 58.53  E-value: 7.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   123 AQEREQ-IKALNNKFASFIDKVRFLEQQNQVLETKWNLLQQlDLNNCRKNLEPIyEGYISNLQKQLEMLSGDGVRLDSEL 201
Cdd:TIGR02168  672 ILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   202 RNMQDLVEDYKKRYEVEINRRTAAENEFVVLKKdvdaaymNKVELQAKVDSLTDEIKffkcLYEGEITQIQSHISDTSIV 281
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELK----ALREALDELRAELTLLNEE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   282 LSMDNNRDLDLDSIIAEVRAQYEEIALKSKAEAETL--YQTKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGN 359
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   360 VKKQCADLETAIadaeqrgdcalKDARAKLDELEGALHQAKEELARMLREYQEL-----VSLKLALDMEIATYRKLLESE 434
Cdd:TIGR02168  899 LSEELRELESKR-----------SELRRELEELREKLAQLELRLEGLEVRIDNLqerlsEEYSLTLEEAEALENKIEDDE 967


                   .
gi 226246663   435 E 435
Cdd:TIGR02168  968 E 968
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 292-429 1.33e-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: 54.68  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   292 LDSIIAEVRAQYEEIALKSKAEAETLYQTK--IQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLET 369
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226246663   370 AIADAEQRGDCA---LKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRK 429
Cdd:TIGR02168  324 QLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
292-434 1.95e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  292 LDSIIAEVRAQYEEI--ALKSKAEAETLYQTKIQELQVTAGQH-GDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLE 368
Cdd:COG4913   293 LEAELEELRAELARLeaELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALG 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  369 --------------TAIADAEQRGDCALKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRKLLESE 434
Cdd:COG4913   373 lplpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 335-411 6.04e-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: 48.61  E-value: 6.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 335 DLKLTKAEISELNRLIQRIRSEIGNVKKQCADLETAIADAEQR----------GDCALKDARAKLDELEGALHQAKEELA 404
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraleqelaaLEAELAELEKEIAELRAELEAQKEELA 107


                 ....*..
gi 226246663 405 RMLREYQ 411
Cdd:COG4942  108 ELLRALY 114
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 124-437 1.90e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.42  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   124 QEREQ-IKALNNKFASFIDKVRFLEQQNQVLETKWNLLQqldlnNCRKNLEPIyegyisnlqkQLEMLSGDGVR--LDSE 200
Cdd:pfam15921  506 QEKERaIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-----NVQTECEAL----------KLQMAEKDKVIeiLRQQ 570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   201 LRNMQDLVEDY----------KKRYEVEINRRTAAENEFVVLKKDVDAAYMnkvELQAKVDSLtdEIKFFKCLYEG---- 266
Cdd:pfam15921  571 IENMTQLVGQHgrtagamqveKAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDL--ELEKVKLVNAGserl 645

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   267 ----EITQIQSH-ISDTSIVLSMDNNRDLDLDSIIAEVRAQYEE-------IALKSKAEAETLYQTKiQELQVTAGQHGD 334
Cdd:pfam15921  646 ravkDIKQERDQlLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEmetttnkLKMQLKSAQSELEQTR-NTLKSMEGSDGH 724

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   335 DLKLTKAeiseLNRLIQRIRSEIGNVKKQCADLETAIADAEQRGDcALKDARAKLDELEGALHQAKEELA---RMLREYQ 411
Cdd:pfam15921  725 AMKVAMG----MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKH-FLKEEKNKLSQELSTVATEKNKMAgelEVLRSQE 799

                          330       340
                   ....*....|....*....|....*.
gi 226246663   412 ELVSLKLAlDMEIATYRKLLESEECR 437
Cdd:pfam15921  800 RRLKEKVA-NMEVALDKASLQFAECQ 824
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 288-435 1.96e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 288 RDLDLDSIIAEVRAQYEEIALKSKAEAETL---------YQTKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIG 358
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELaeleaeleeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 359 NVKKQCADLETAIADAEQRGDCA---LKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRKLLESEE 435
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
127-435 2.03e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 127 EQIKALNNKFASFIDKVRFLEQQNQVLETKwnllqqldLNNCRKNLEPIYE--GYISNLQKQLEMLSGDGVRLDSELRNM 204
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREE--------LEKLEKEVKELEElkEEIEELEKELESLEGSKRKLEEKIREL 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 205 QDLVEDYKKRYEvEINRRTAAENEfvvLKKDVDaAYMNKVELQAKVDSLTDEIKFFKCLYEGEITQIQSHISDtsivLSM 284
Cdd:PRK03918 265 EERIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEE 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 285 DNNRDLDLDSIIAEVRAQYEEiaLKSKAEA-ETLYQTKIQELQVTAGQHGDDLKLTKAEISELNRL-------IQRIRSE 356
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEE--LEERHELyEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAkeeieeeISKITAR 413

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 357 IGNVKKQCADLETAIADAEQ-RGDCALKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRKLLESEE 435
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKKaKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
117-432 2.38e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 117 EIQRVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLETKwnllqQLDLNNCRKNLEPIYEGYISNLQKQLEMLSGDGVR 196
Cdd:COG4717  136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAEL-----QEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 197 LDSELRNMQDLVEDYKKRYEVEINRRTAAENE---------------FVVLKKDVDAAYMNKVEL--------------- 246
Cdd:COG4717  211 LEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaaLLALLGLGGSLLSLILTIagvlflvlgllallf 290

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 247 ------QAKVDSLTDEIKFFKCLYEGEITQIQSHISDTSIVLSMDNNRDLDLDSIIAEVRAQYEEIALKSKAEAETLYQT 320
Cdd:COG4717  291 lllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 321 KIQELQVTAGQHGDD-----------LKLTKAEISELNRLIQRIRSEIG---------NVKKQCADLETAIADAEQRgdc 380
Cdd:COG4717  371 EIAALLAEAGVEDEEelraaleqaeeYQELKEELEELEEQLEELLGELEellealdeeELEEELEELEEELEELEEE--- 447

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226246663 381 aLKDARAKLDELEGALHQAKE--ELARMLREYQELVSLKLALDMEIATYRKLLE 432
Cdd:COG4717  448 -LEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALKLALE 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 180-435 2.61e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 180 ISNLQKQLEMLSGDGVRLDSELRNMQDLVEDYKKRYEVEINRRTAAENEFVVLKKDVDAAYMNKVELQAKVDSLTDEIKf 259
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE- 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 260 fkcLYEGEITQIQSHISDTSIVLSMDNNRDLDLDSIIAEVRAQYEEiALKSKAEAETLYQTKIQELQVTAGQHgddLKLT 339
Cdd:COG1196  320 ---ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-AEEALLEAEAELAEAEEELEELAEEL---LEAL 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 340 KAEISELNRLIQRIRSEIGNVKKQcADLETAIADAEQrgdcALKDARAKLDELEGALHQAKEELARMLREYQELVSLKLA 419
Cdd:COG1196  393 RAAAELAAQLEELEEAEEALLERL-ERLEEELEELEE----ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467

                        250
                 ....*....|....*.
gi 226246663 420 LDMEIATYRKLLESEE 435
Cdd:COG1196  468 LLEEAALLEAALAELL 483
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 117-403 2.91e-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: 46.94  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  117 EIQRVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLETKW----NLLQQLDLNncRKNLEPIYEgyisNLQKQLEMLSG 192
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqnqeKLNQQKDEQ--IKKLQQEKE----LLEKEIERLKE 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  193 DGVRLDSELRNMQDLVEDYKKRYEvEINRRTAAEN----------------------EFVVLKKDVDAAYMNKVELQAKV 250
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIK-NLDNTRESLEtqlkvlsrsinkikqnleqkqkELKSKEKELKKLNEEKKELEEKV 512

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  251 DSLTDEIKFFKC---LYEGEITQIQSHISD-TSIVLSMDNNrdLDLDSIIAEVRAQYEEIA-LKSKAEAETLYQTKIQEL 325
Cdd:TIGR04523 513 KDLTKKISSLKEkieKLESEKKEKESKISDlEDELNKDDFE--LKKENLEKEIDEKNKEIEeLKQTQKSLKKKQEEKQEL 590

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226246663  326 qvtAGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLETAIadaeqrgdcalKDARAKLDELEGALHQAKEEL 403
Cdd:TIGR04523 591 ---IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII-----------KNIKSKKNKLKQEVKQIKETI 654
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
125-435 3.44e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 125 EREQIKALNNKFASFIDKVRFLEQQNQVLETKWNLLQ---QLDLNNCRKNLEPIYEGYISNLQKQLEMLSGDG-----VR 196
Cdd:COG3206   62 EPQSSDVLLSGLSSLSASDSPLETQIEILKSRPVLERvvdKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGsnvieIS 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 197 LDSELRNM-----QDLVEDYKKRYEVEINRRTAAENEFV-----VLKKDVDAA------YMNK---VELQAKVDSLTDEI 257
Cdd:COG3206  142 YTSPDPELaaavaNALAEAYLEQNLELRREEARKALEFLeeqlpELRKELEEAeaaleeFRQKnglVDLSEEAKLLLQQL 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 258 KffkcLYEGEITQIQSHISD---------TSIVLSMDNNRDLDLDSIIAEVRAQYEEIalkskaeaetlyQTKIQELQVT 328
Cdd:COG3206  222 S----ELESQLAEARAELAEaearlaalrAQLGSGPDALPELLQSPVIQQLRAQLAEL------------EAELAELSAR 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 329 AGQHGDDLKLTKAEISELNRLIQRIRSEIgnvkkqcadLETAIADAEQrgdcalkdARAKLDELEGALHQAKEELARMLR 408
Cdd:COG3206  286 YTPNHPDVIALRAQIAALRAQLQQEAQRI---------LASLEAELEA--------LQAREASLQAQLAQLEARLAELPE 348

                        330       340
                 ....*....|....*....|....*..
gi 226246663 409 EYQELVSLKLALDMEIATYRKLLESEE 435
Cdd:COG3206  349 LEAELRRLEREVEVARELYESLLQRLE 375
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 179-422 5.75e-05

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: 45.83  E-value: 5.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   179 YISNLQKQLEMLSGDGVRLD------SELRN-MQDLVEDYKKRYEVEINRRTAAENEFVVLKKDVDAAYMNKVELQAKVD 251
Cdd:TIGR02169  168 FDRKKEKALEELEEVEENIErldliiDEKRQqLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLA 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   252 SLtdeikffkclyEGEITQIQSHISDtsivlsmdnnrdldLDSIIAEVRAQYEEIALKSKAEAETLY---QTKIQELQVT 328
Cdd:TIGR02169  248 SL-----------EEELEKLTEEISE--------------LEKRLEEIEQLLEELNKKIKDLGEEEQlrvKEKIGELEAE 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   329 AGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLETAIADAEQRGDC---ALKDARAKLDELEGALhQAKEELAR 405
Cdd:TIGR02169  303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKEELEDLRAEL-EEVDKEFA 381

                          250
                   ....*....|....*..
gi 226246663   406 MLREyqELVSLKLALDM 422
Cdd:TIGR02169  382 ETRD--ELKDYREKLEK 396
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 183-435 1.06e-04

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: 45.06  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   183 LQKQLEMLSGDGVRLDSELRNMQDLVEDYKKRYEVEINRRTAAENEFVVLKKDVDAAYMNKVELQAKVDSLTDEIKFFKC 262
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   263 L---YEGEITQIQSHISdtSIVLSMDNNRDLDLDSIIAEVRAQYEEI----------------ALKSKAEAETLYQTKIQ 323
Cdd:TIGR02169  759 ElkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeeevsriearlreieqKLNRLTLEKEYLEKEIQ 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   324 ELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLETAIADAEQRgdcaLKDARAKLDELEGALHQAKEEL 403
Cdd:TIGR02169  837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE----RDELEAQLRELERKIEELEAQI 912

                          250       260       270
                   ....*....|....*....|....*....|..
gi 226246663   404 ARMLREYQELVSLKLALDMEIATYRKLLESEE 435
Cdd:TIGR02169  913 EKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
184-412 1.65e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  184 QKQLEMLSGDGVRLDSELRNMQDLVEDYKKRYEVEINRRTAAENEFVVLKKDVDAAymnkvELQAKVDSLTDEIkffkcl 263
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAEL------ 677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  264 yegeitqiqshisdtsivlsmdnnRDLDLDSiiAEVRAQYEEIAlKSKAEAETLYQtKIQELQVTAGQHGDDLKLTKAEI 343
Cdd:COG4913   678 ------------------------ERLDASS--DDLAALEEQLE-ELEAELEELEE-ELDELKGEIGRLEKELEQAEEEL 729

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226246663  344 SELNRLIQRIRSEIGNVKKQCADLETAIADAEQRGDCALKDARAKLDELEGALHQAKEELARMLREYQE 412
Cdd:COG4913   730 DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 291-429 1.65e-04

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: 43.37  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 291 DLDSIIAEVRAQYEEI--ALKSKAEAETLYQTKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGNV-------- 360
Cdd:COG1579   14 ELDSELDRLEHRLKELpaELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyea 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226246663 361 --------KKQCADLETAIADAEQRgdcaLKDARAKLDELEGALHQAKEELARMLREYQELVSlklALDMEIATYRK 429
Cdd:COG1579   94 lqkeieslKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEA 163
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
291-429 2.04e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 291 DLDSIIAEVRAQYEEIALKSK-AEAETLYQTKIQELQVTAGQHgdDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLET 369
Cdd:COG4717  383 DEEELRAALEQAEEYQELKEElEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEA 460

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 370 AIADAEQRGDcalkdarakLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRK 429
Cdd:COG4717  461 ELEQLEEDGE---------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 288-432 4.51e-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: 43.12  E-value: 4.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   288 RDLDLDSIIAEVRAQYEEIALKSKAEAEtlYQTKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADL 367
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226246663   368 ETAIADAEQRGDCA---LKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRKLLE 432
Cdd:TIGR02168  301 EQQKQILRERLANLerqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
117-434 6.72e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 117 EIQRVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLETkWNLLQQLD--LNNCRKNLEPIYEGY--ISNLQKQLEMLSG 192
Cdd:COG4717   92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEaeLAELPERLEELEERLeeLRELEEELEELEA 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 193 DGVRLDSELRN-MQDLVEDYKKRYEVEINRRTAAENEFVVLKKDVDAAYMNKVELQAKVDSLTDEIKFFKclYEGEITQI 271
Cdd:COG4717  171 ELAELQEELEElLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA--LEERLKEA 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 272 QSHISDTSIVLSMDNNRDLDLDS---------IIAEVRAQYEEIALKSKAEAET----------LYQTKIQELQVTAGQH 332
Cdd:COG4717  249 RLLLLIAAALLALLGLGGSLLSLiltiagvlfLVLGLLALLFLLLAREKASLGKeaeelqalpaLEELEEEELEELLAAL 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 333 GDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLETAIADAEQRGDCALKDArAKLDELEGALHQAkeelarmlREYQE 412
Cdd:COG4717  329 GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV-EDEEELRAALEQA--------EEYQE 399

                        330       340
                 ....*....|....*....|..
gi 226246663 413 LVSLKLALDMEIATYRKLLESE 434
Cdd:COG4717  400 LKEELEELEEQLEELLGELEEL 421
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 325-413 7.59e-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: 41.67  E-value: 7.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 325 LQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLETAIADAEQRgdcaLKDARAKLDELEGALHQAKEELA 404
Cdd:COG4942   11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELA 86


                 ....*....
gi 226246663 405 RMLREYQEL 413
Cdd:COG4942   87 ELEKEIAEL 95
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 307-401 1.39e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 39.20  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  307 ALKSKAEAETLyQTKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLETAIADAEQRGDCALKDAR 386
Cdd:pfam10473  47 AENSKAEVETL-KAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESK 125

                          90
                  ....*....|....*
gi 226246663  387 AKLDELEGALHQAKE 401
Cdd:pfam10473 126 TAVEMLQTQLKELNE 140
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 319-412 3.59e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 319 QTKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIgnvkkqcADLETAIADAEQRgdcaLKDARAKLDELEGALHQ 398
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEY-------NELQAELEALQAE----IDKLQAEIAEAEAEIEE 83

                         90
                 ....*....|....
gi 226246663 399 AKEELARMLREYQE 412
Cdd:COG3883   84 RREELGERARALYR 97
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
321-435 4.40e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663  321 KIQELQvtagqhgDDLKLTKAEISELNRLIQRIRSEIGNVKKQC----------------ADLETAIADAEQRGDcALKD 384
Cdd:COG4913   611 KLAALE-------AELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvASAEREIAELEAELE-RLDA 682

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 226246663  385 ARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRKLLESEE 435
Cdd:COG4913   683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
PRK12704 PRK12704
phosphodiesterase; Provisional
 297-412 5.61e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 5.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 297 AEVRAQYEEIALKSKAEAE-TLYQTKIQELQVTAGQHGDDLK-----LTKAEiSELNRLIQRIRSEIGNVKKQCADLETA 370
Cdd:PRK12704  58 ALLEAKEEIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDrklelLEKRE-EELEKKEKELEQKQQELEKKEEELEEL 136

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226246663 371 IADAEQRgdcaLK--------DARAKLdeLEGALHQAKEELARMLREYQE 412
Cdd:PRK12704 137 IEEQLQE----LErisgltaeEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 225-503 6.38e-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: 6.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 225 AENEFVVLKKDVDAAYMNKVELQAKVDSLTDEIKFfkclYEGEITQIQSHISDTSIvlSMDNNRDlDLDSIIAEVRAQYE 304
Cdd:COG3883   14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEE----LNEEYNELQAELEALQA--EIDKLQA-EIAEAEAEIEERRE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 305 EIALKSKAEAETLYQTKIQELQVTAGQHGDDLkltkAEISELNRLIQRIRSEIGNVKKQCADLETAIADAEQrgdcALKD 384
Cdd:COG3883   87 ELGERARALYRSGGSVSYLDVLLGSESFSDFL----DRLSALSKIADADADLLEELKADKAELEAKKAELEA----KLAE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 385 ARAKLDELEgalhQAKEELARMLREYQELVSlklALDMEIATYRKLLESEECRMSGEYPNSVSISVISSTNAGAGGAGFS 464
Cdd:COG3883  159 LEALKAELE----AAKAELEAQQAEQEALLA---QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 226246663 465 MGFGASSSYSYKTAAADVKTKGSCGSELKDPLAKTSGSS 503
Cdd:COG3883  232 AAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 320-435 6.49e-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: 38.37  E-value: 6.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 320 TKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLETAIADAEQRgdcaLKDARAKLDELEGA--LH 397
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYEEQLGNVRNNkeYE 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 226246663 398 QAKEELARMLREYQELVSLKLALDMEIATYRKLLESEE 435
Cdd:COG1579   93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 180-433 7.90e-03

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: 38.59  E-value: 7.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 180 ISNLQKQLEmlsgdgvRLDSELRNMQDLVEDYKKRYEVEINRRTAAENEFVVLKKDVDAAYMNKVELQAKVDSLTDEIKf 259
Cdd:COG4942   22 AAEAEAELE-------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 260 fkcLYEGEITQIQSHISDTSIVLSMDNNRDldldsiiaevraqYEEIALKSKAEAET-----LYQTKIQELQvtagQHGD 334
Cdd:COG4942   94 ---ELRAELEAQKEELAELLRALYRLGRQP-------------PLALLLSPEDFLDAvrrlqYLKYLAPARR----EQAE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 335 DLKLTKAEISELNRLIQRIRSEIgnvKKQCADLETAIADAEQrgdcALKDARAKLDELEGALHQAKEELARMLREYQELV 414
Cdd:COG4942  154 ELRADLAELAALRAELEAERAEL---EALLAELEEERAALEA----LKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                        250
                 ....*....|....*....
gi 226246663 415 SLKLALDMEIATYRKLLES 433
Cdd:COG4942  227 ALIARLEAEAAAAAERTPA 245
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 177-351 9.03e-03

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: 38.07  E-value: 9.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   177 EGYISNLQKQLEMLSGDGVRLDSELRNMQDLVEDYKKRYEV---EINRRTAAENEFVVLKKDVDAAymnkveLQAKVDSL 253
Cdd:smart00787 143 EGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDAleeELRQLKQLEDELEDCDPTELDR------AKEKLKKL 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663   254 TDEIKFFKclyeGEITQIQSHISDTSIVLSMDNNRDLDLDSIIAEVRAQYEEIALKSKAEAETLyQTKIQELQVTAGQHg 333
Cdd:smart00787 217 LQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKL-KEQLKLLQSLTGWK- 290

                          170
                   ....*....|....*....
gi 226246663   334 dDLKLTKAEIS-ELNRLIQ 351
Cdd:smart00787 291 -ITKLSGNTLSmTYDREIN 308
PRK09039 PRK09039
peptidoglycan -binding protein;
265-405 9.92e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.02  E-value: 9.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226246663 265 EGEITQIQSHISDTSIVLSMDNNRDLDLDSIIAEVRAQYEEiALKSKAEAETLY---QTKIQELQVTAGQHGDDLKLTKA 341
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLaelAGAGAAAEGRAGELAQELDSEKQ 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226246663 342 EISELNRLIQRIRSEIGNVKKQCADLETAIADAEQRGdcalKDARAKLD----ELEGALHQAKEELAR 405
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
 
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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