|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
258-344 |
2.26e-18 |
|
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.
Pssm-ID: 197361 [Multi-domain] Cd Length: 87 Bit Score: 79.32 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 258 MQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQ 337
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 1008909414 338 REYSKLK 344
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
259-344 |
6.91e-18 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 78.49 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 259 QLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQR 338
Cdd:pfam16516 15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94
|
....*.
gi 1008909414 339 EYSKLK 344
Cdd:pfam16516 95 QNQQLK 100
|
|
| NEMO |
pfam11577 |
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ... |
44-110 |
6.19e-16 |
|
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.
Pssm-ID: 431942 [Multi-domain] Cd Length: 67 Bit Score: 71.74 E-value: 6.19e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909414 44 EQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLE 110
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-371 |
9.27e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 55 LEENQELRDAIRQSNQI--LRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQ 132
Cdd:COG1196 218 LKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAA 212
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 213 LRMERQAASEEKRKLAQLQVAYHQLfQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQhk 292
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL-- 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909414 293 ivmetvpvLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPA 371
Cdd:COG1196 455 --------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
393-418 |
1.48e-11 |
|
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin (optic neuropathy inducing protein) and NF-kappa-B essential modulator (NEMO) furthermore, it can be found in kinase TBK1, a member of the IKK (inhibitor of nuclear factor kappa-B kinase) family. The C-terminal region, which carries the zinc finger domain, constitutes the regulatory domain of NEMO, as it receives the activation signal from upstream molecules, and subsequently transmits this activation to the kinases bound to the N-terminal domain. The isolated NEMO zinc finger is thought to be involved in protein-protein rather than protein-DNA interaction.
Pssm-ID: 436483 Cd Length: 26 Bit Score: 58.37 E-value: 1.48e-11
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
87-321 |
4.56e-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: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 87 REEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKE 166
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 167 CQALEGRARAASEQARQLESEREALQQqhsvQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIK 246
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008909414 247 SSVVGSErkrgmQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREK 321
Cdd:TIGR02168 839 RLEDLEE-----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
133-233 |
2.13e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQ--GQSVE 210
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQ 224
|
90 100
....*....|....*....|....*
gi 1008909414 211 AALRMErqAASEEKRKL--AQLQVA 233
Cdd:PRK11448 225 AAKRLE--LSEEETRILidQQLRKA 247
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
146-287 |
3.81e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 146 VTSLLGELQESQSRLEAATKECQALEGraraaseQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKR 225
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRG-------QIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEA 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909414 226 KLAQLQVAYHQLFQEYDNHiKSSVVGSERKRGMQLEDLKQQL--------QQAE---------EALVAKQEVIDKLKEE 287
Cdd:pfam09787 115 ELERLQEELRYLEEELRRS-KATLQSRIKDREAEIEKLRNQLtsksqsssSQSElenrlhqltETLIQKQTMLEALSTE 192
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
139-323 |
5.27e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.51 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 139 KASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQ 218
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 219 AASEEKRKLAQ-LQV----AYHQ--LFQEYDNH--------IKSSVVGSERKRGMQLEDLKQQ----LQQAEEAlVAKQE 279
Cdd:NF012221 1617 AVTKELTTLAQgLDAldsqATYAgeSGDQWRNPfagglldrVQEQLDDAKKISGKQLADAKQRhvdnQQKVKDA-VAKSE 1695
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1008909414 280 VidkLKEEAEQHKivmetvpvLKAQADIYKADFQAERQAREKLA 323
Cdd:NF012221 1696 A---GVAQGEQNQ--------ANAEQDIDDAKADAEKRKDDALA 1728
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
258-344 |
2.26e-18 |
|
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.
Pssm-ID: 197361 [Multi-domain] Cd Length: 87 Bit Score: 79.32 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 258 MQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQ 337
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 1008909414 338 REYSKLK 344
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
259-344 |
6.91e-18 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 78.49 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 259 QLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQR 338
Cdd:pfam16516 15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94
|
....*.
gi 1008909414 339 EYSKLK 344
Cdd:pfam16516 95 QNQQLK 100
|
|
| NEMO |
pfam11577 |
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ... |
44-110 |
6.19e-16 |
|
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.
Pssm-ID: 431942 [Multi-domain] Cd Length: 67 Bit Score: 71.74 E-value: 6.19e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909414 44 EQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLE 110
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-371 |
9.27e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 55 LEENQELRDAIRQSNQI--LRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQ 132
Cdd:COG1196 218 LKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAA 212
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 213 LRMERQAASEEKRKLAQLQVAYHQLfQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQhk 292
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL-- 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909414 293 ivmetvpvLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPA 371
Cdd:COG1196 455 --------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
393-418 |
1.48e-11 |
|
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin (optic neuropathy inducing protein) and NF-kappa-B essential modulator (NEMO) furthermore, it can be found in kinase TBK1, a member of the IKK (inhibitor of nuclear factor kappa-B kinase) family. The C-terminal region, which carries the zinc finger domain, constitutes the regulatory domain of NEMO, as it receives the activation signal from upstream molecules, and subsequently transmits this activation to the kinases bound to the N-terminal domain. The isolated NEMO zinc finger is thought to be involved in protein-protein rather than protein-DNA interaction.
Pssm-ID: 436483 Cd Length: 26 Bit Score: 58.37 E-value: 1.48e-11
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-290 |
1.73e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 49 ETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHL 128
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 129 KRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHsvqvDQLRMQGQS 208
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL----ERLEEELEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 209 VEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVvgSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEA 288
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA--ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
..
gi 1008909414 289 EQ 290
Cdd:COG1196 504 EG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
87-321 |
4.56e-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: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 87 REEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKE 166
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 167 CQALEGRARAASEQARQLESEREALQQqhsvQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIK 246
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008909414 247 SSVVGSErkrgmQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREK 321
Cdd:TIGR02168 839 RLEDLEE-----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-323 |
1.68e-08 |
|
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: 56.99 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 49 ETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHL 128
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 129 KRCQQQMAEDKASVKAQVTSLLGELQESQSRLE-------AATKECQALEGRARAASEQARQLESEREALQQQhsvqvdq 201
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLEslerriaATERRLEDLEEQIEELSEDIESLAAEIEELEEL------- 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 202 lrmqgqsvEAALRMERQAASEEKrklAQLQVAYHQLFQEYDNhiKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEV- 280
Cdd:TIGR02168 868 --------IEELESELEALLNER---ASLEEALALLRSELEE--LSEELRELESKRSELRRELEELREKLAQLELRLEGl 934
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1008909414 281 ---IDKLKEE-AEQHKIVMETVPVLKAQADIYKADFQAE-RQAREKLA 323
Cdd:TIGR02168 935 evrIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRlKRLENKIK 982
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
49-363 |
3.06e-08 |
|
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: 55.84 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 49 ETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEF----LMCKFQEARKLVERLGLEKLDLKRQKEQALRE 124
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYegyeLLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 125 VEHL-KRC---QQQMAEDKASVKA-------QVTSLLGELQESQSRLEAATKECqalEGRARAASEQARQLESEREALQQ 193
Cdd:TIGR02169 260 ISELeKRLeeiEQLLEELNKKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEK---ERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 194 QHS----------VQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYD--NHIKSSVVGSERKRGMQLE 261
Cdd:TIGR02169 337 EIEelereieeerKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 262 DLKQQLQQAEEALVAKQEVIDKLKEEAEQhkiVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYS 341
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKED---KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
330 340
....*....|....*....|..
gi 1008909414 342 KLKASCQESARIEDMRKRHVEV 363
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEV 515
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
117-382 |
3.14e-08 |
|
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: 55.16 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 117 QKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHS 196
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 197 VQVDQLRmqgqsveaalrmerqaaseekrklAQLQVAYHQLFQEYDNHIKSSVVGSERKRGMQ-LEDLKQQLQQAEEALV 275
Cdd:COG4942 101 AQKEELA------------------------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 276 AKQEVIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREysKLKASCQESARIED 355
Cdd:COG4942 157 ADLAELAALRAELEAERAELEA---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAE--LQQEAEELEALIAR 231
|
250 260
....*....|....*....|....*..
gi 1008909414 356 MRKRHVEVSQAPLPPAPAYLSSPLALP 382
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALKGKLPWP 258
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
39-322 |
4.27e-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: 52.37 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 39 LHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKL------ 112
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerl 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 113 -DLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREAL 191
Cdd:TIGR02168 312 aNLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 192 QQQhsvqvdqlrmqgqsvEAALRMERQAASEEKRKLaqlqvayhqlfqeydnhikssvvgsERKRGMQLEDLKQQLQQAE 271
Cdd:TIGR02168 392 ELQ---------------IASLNNEIERLEARLERL-------------------------EDRRERLQQEIEELLKKLE 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1008909414 272 EAlvAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKL 322
Cdd:TIGR02168 432 EA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-360 |
7.25e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 101 RKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAqvtslLGELQESQSRLEAATKECQALEGRARAASEQ 180
Cdd:COG4913 210 DDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 181 ARQLesEREALQQqhsvQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQlfqeydnhikssvVGSERkrgmqL 260
Cdd:COG4913 285 FAQR--RLELLEA----ELEELRAELARLEAELERLEARLDALREELDELEAQIRG-------------NGGDR-----L 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 261 EDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKI-VMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQRE 339
Cdd:COG4913 341 EQLEREIERLERELEERERRRARLEALLAALGLpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
250 260
....*....|....*....|.
gi 1008909414 340 YSKLKascqesARIEDMRKRH 360
Cdd:COG4913 421 LRELE------AEIASLERRK 435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-279 |
1.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 98 QEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDK---------ASVKAQVTSLL---GELQESQSRLEAATK 165
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELERLDassDDLAALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 166 ECQALEGRARAASEQARQLESEREALQQqhsvQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNhi 245
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE-- 773
|
170 180 190
....*....|....*....|....*....|....
gi 1008909414 246 kssvvgserkrgmQLEDLKQQLQQAEEALVAKQE 279
Cdd:COG4913 774 -------------RIDALRARLNRAEEELERAMR 794
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-323 |
2.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 154 QESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSV--QVDQLRMQGQSVEAA------LRMERQAASEEKR 225
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAereiaeLEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 226 KLAQLQVAYHQLFQEYDNHIKssvvgserkrgmQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQA 305
Cdd:COG4913 686 DLAALEEQLEELEAELEELEE------------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
170
....*....|....*....
gi 1008909414 306 DIYKADFQA-ERQAREKLA 323
Cdd:COG4913 754 RFAAALGDAvERELRENLE 772
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-360 |
3.22e-05 |
|
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: 46.20 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 104 VERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQ 183
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 184 LESEREALQQQH-----------------SVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIK 246
Cdd:TIGR02168 314 LERQLEELEAQLeeleskldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 247 SsvVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKadfqAERQAREKLAEKK 326
Cdd:TIGR02168 394 Q--IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE----ELERLEEALEELR 467
|
250 260 270
....*....|....*....|....*....|....
gi 1008909414 327 ELLQEQLEQLQREYSKLKASCQESARIEDMRKRH 360
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-290 |
5.04e-05 |
|
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: 45.82 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 49 ETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVErlgleklDLKRQKEQALREVEHL 128
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSEDIESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 129 KRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHS---VQVDQLRMQ 205
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAqleLRLEGLEVR 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 206 GQSVEAALRMERQ-----AASEEKRKLAQLQVAYHQLFQ-----------------EYDnhikssvvgSERKRgmqLEDL 263
Cdd:TIGR02168 938 IDNLQERLSEEYSltleeAEALENKIEDDEEEARRRLKRlenkikelgpvnlaaieEYE---------ELKER---YDFL 1005
|
250 260
....*....|....*....|....*..
gi 1008909414 264 KQQLQQAEEALVAKQEVIDKLKEEAEQ 290
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
55-196 |
1.13e-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: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 55 LEENQELRDAIR-----QSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERL-------GLEKLD-LKRQKEQA 121
Cdd:COG4913 271 LAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaqirgnGGDRLEqLEREIERL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 122 LREVEHLKRCQQQMAE-----------DKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREA 190
Cdd:COG4913 351 ERELEERERRRARLEAllaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
....*.
gi 1008909414 191 LQQQHS 196
Cdd:COG4913 431 LERRKS 436
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
52-356 |
1.21e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 52 QRCLEENQELRDAIRQSNQILRERCEELLhfQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRC 131
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 132 QQQMAEDKASVKAqVTSLLGELQESQSRLEAATKECQALEGRaRAASEQARQLESEREALQQQHSVQVDQLRMQGqsvEA 211
Cdd:TIGR00618 385 QQQKTTLTQKLQS-LCKELDILQREQATIDTRTSAFRDLQGQ-LAHAKKQQELQQRYAELCAAAITCTAQCEKLE---KI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 212 ALRMERQAASEEKRKLAQLQVaYHQLFQEYDN---HIKSSVVGSERKRGMQLEDLKQQLQQAEEaLVAKQEVIDKLKEEA 288
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQ-IHLQETRKKAvvlARLLELQEEPCPLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTY 537
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1008909414 289 EQHKIVMETV----PVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDM 356
Cdd:TIGR00618 538 AQLETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
133-233 |
2.13e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQ--GQSVE 210
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQ 224
|
90 100
....*....|....*....|....*
gi 1008909414 211 AALRMErqAASEEKRKL--AQLQVA 233
Cdd:PRK11448 225 AAKRLE--LSEEETRILidQQLRKA 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
59-362 |
2.16e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 59 QELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVErlGLEKLDLKRQKEQALREVEHLKRCQQQMAED 138
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 139 KASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQ 218
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 219 AASEEKRKLAQLQVAYH--------QLFQEYDNHIKSSVVGSERKRGMQLEDLK----QQLQQAEEalVAKQEVIDKLKE 286
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKkkeaEEKKKAEE--LKKAEEENKIKA 1663
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909414 287 EAEQHKIVMEtvpvlKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKAScQESARIEDMRKRHVE 362
Cdd:PTZ00121 1664 AEEAKKAEED-----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-EELKKAEEENKIKAE 1733
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
55-283 |
3.05e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 55 LEENQELR-DAIRQSNQILRERCEELLHfQASQREEKeflMCKFQEARKLV-----ERLGLEKL-DLKRQKEQALREVEH 127
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRK-ELEEAEAA---LEEFRQKNGLVdlseeAKLLLQQLsELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 128 LKRCQQQMAEDKASVKAQVTSLLG--ELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQ 205
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 206 -------GQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNhikssvvgsERKRGMQLEDLKQQLQQAEEALVAKQ 278
Cdd:COG3206 318 leaeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV---------ARELYESLLQRLEEARLAEALTVGNV 388
|
....*
gi 1008909414 279 EVIDK 283
Cdd:COG3206 389 RVIDP 393
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
146-287 |
3.81e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 146 VTSLLGELQESQSRLEAATKECQALEGraraaseQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKR 225
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRG-------QIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEA 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909414 226 KLAQLQVAYHQLFQEYDNHiKSSVVGSERKRGMQLEDLKQQL--------QQAE---------EALVAKQEVIDKLKEE 287
Cdd:pfam09787 115 ELERLQEELRYLEEELRRS-KATLQSRIKDREAEIEKLRNQLtsksqsssSQSElenrlhqltETLIQKQTMLEALSTE 192
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
44-362 |
4.09e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 44 EQGAPETLQRCLEENQELRDAIRQSNQiLRERCEELLHfQASQREEKEFLMCKFQEARKLVErlGLEKLDLKRQKEQALR 123
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAA-AKKKADEAKK-KAEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEEAKK 1464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 124 EVEHLKRCQQ--QMAEDKA---SVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQ 198
Cdd:PTZ00121 1465 KAEEAKKADEakKKAEEAKkadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 199 V---DQLRMQGQSVEAA-LRMERQAASEEKRKLAQLQVAyHQLFQEYDNHIKSSVVGSERKRGMQLEDLK---------Q 265
Cdd:PTZ00121 1545 KkkaDELKKAEELKKAEeKKKAEEAKKAEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKkaeeakikaE 1623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 266 QLQQAEEALVAKQEVIDKLKEE---AEQHKIVMETVPVLKAQAdiyKADFQAERQAREKLAEKKELLQEQLEQLQREysk 342
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEkkkAEELKKAEEENKIKAAEE---AKKAEEDKKKAEEAKKAEEDEKKAAEALKKE--- 1697
|
330 340
....*....|....*....|
gi 1008909414 343 lkasCQESARIEDMRKRHVE 362
Cdd:PTZ00121 1698 ----AEEAKKAEELKKKEAE 1713
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
51-310 |
4.11e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 51 LQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEflmckfQEARKLVERLGLEKldLKRQKEQALREVEHLKR 130
Cdd:COG5185 255 LEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTK------EKIAEYTKSIDIKK--ATESLEEQLAAAEAEQE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 131 CQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEG--RARAASEQARQLESEREALQQQHSVQVDQLRMQGQS 208
Cdd:COG5185 327 LEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGevELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 209 VEAALrmeRQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSV-VGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEE 287
Cdd:COG5185 407 ILATL---EDTLKAADRQIEELQRQIEQATSSNEEVSKLLNeLISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDL 483
|
250 260
....*....|....*....|...
gi 1008909414 288 AEQHKIVMETVPVLKAQADIYKA 310
Cdd:COG5185 484 NEELTQIESRVSTLKATLEKLRA 506
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
83-359 |
4.98e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 83 QASQREEKEflmcKFQEARKLVErlgLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQS-RLE 161
Cdd:PTZ00121 1538 EAKKAEEKK----KADELKKAEE---LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKmKAE 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 162 AATKECQAlegraRAASEQARQLESEREALQQ------QHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAyh 235
Cdd:PTZ00121 1611 EAKKAEEA-----KIKAEELKKAEEEKKKVEQlkkkeaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA-- 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 236 qlfqEYDNHIKSSVVGSERKRGMQLEDLKQQlqQAEEALVAKQevidkLKEEAEQHKIVMETVPvLKAQADIYKAD-FQA 314
Cdd:PTZ00121 1684 ----EEDEKKAAEALKKEAEEAKKAEELKKK--EAEEKKKAEE-----LKKAEEENKIKAEEAK-KEAEEDKKKAEeAKK 1751
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1008909414 315 ERQAREKLAEKKELLQEQLEQLQREYsklKASCQESARIEDMRKR 359
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEK---EAVIEEELDEEDEKRR 1793
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
139-323 |
5.27e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.51 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 139 KASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQ 218
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 219 AASEEKRKLAQ-LQV----AYHQ--LFQEYDNH--------IKSSVVGSERKRGMQLEDLKQQ----LQQAEEAlVAKQE 279
Cdd:NF012221 1617 AVTKELTTLAQgLDAldsqATYAgeSGDQWRNPfagglldrVQEQLDDAKKISGKQLADAKQRhvdnQQKVKDA-VAKSE 1695
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1008909414 280 VidkLKEEAEQHKivmetvpvLKAQADIYKADFQAERQAREKLA 323
Cdd:NF012221 1696 A---GVAQGEQNQ--------ANAEQDIDDAKADAEKRKDDALA 1728
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
120-352 |
5.98e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 120 QALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQV 199
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 200 DQLRMQGQSVEAalrmerqaaseekrkLAQLQVAyhQLFQEYDNHIK--SSVVGSERKRGMQLEDLKQQLQQAEEALVAK 277
Cdd:COG3883 93 RALYRSGGSVSY---------------LDVLLGS--ESFSDFLDRLSalSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008909414 278 QEVIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESAR 352
Cdd:COG3883 156 LAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
83-358 |
6.29e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 83 QASQREEKEFLMCKFQEARKLVErlglekldLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEA 162
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 163 ATKECQALEGRARAASEQARQLESEREALQ--QQHSVQVDQLRMQGQSVEAALRMERQAasEEKRKLAQLQVAyhqlfqe 240
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEKKKADEAKKkaEEDKKKADELKKAAAAKKKADEAKKKA--EEKKKADEAKKK------- 1439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 241 ydnhikssvvGSERKRGMQLEDLKQQLQQAEEALVAKQEV--IDKLKEEAEQHKIVMETVPvlKAQADIYKADFQAERQA 318
Cdd:PTZ00121 1440 ----------AEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKK--KAEEAKKKADEAKKAAE 1507
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1008909414 319 REKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRK 358
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
45-292 |
8.26e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 45 QGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEF--LMCKFQEARKLVERLGL--EKLDLKRQKEQ 120
Cdd:TIGR00618 215 DTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqLRARIEELRAQEAVLEEtqERINRARKAAP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 121 ALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRL--EAATKECQALEGRARAASEQARQLESE----REALQQQ 194
Cdd:TIGR00618 295 LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVkqQSSIEEQRRLLQTLHSQEIHIRDAHEVatsiREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 195 HSVQvDQLRMQGQSVEAALRMErQAASEEKRKLAQLQVAYHQLFQEYDN------HIKSSVVGSERKRGMQLEDLKQQLQ 268
Cdd:TIGR00618 375 HTLT-QHIHTLQQQKTTLTQKL-QSLCKELDILQREQATIDTRTSAFRDlqgqlaHAKKQQELQQRYAELCAAAITCTAQ 452
|
250 260
....*....|....*....|....
gi 1008909414 269 QAEEALVAKQEVIDKLKEEAEQHK 292
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQ 476
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
56-366 |
9.00e-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: 41.59 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 56 EENQELRDAIrQSNQILRERCEELLHFQASQREEKEFLMckfQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQM 135
Cdd:TIGR02169 674 AELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQEL---SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 136 AEDKASVKAQVTSLLGELQESQSRLEAATKECQALEgrARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRM 215
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 216 ERQAASEEKRKLAQLQvayhqlfqEYDNHIKSsvvgserkRGMQLEDLKQQL----QQAEEALVAKQEVIDKLKEEAEQH 291
Cdd:TIGR02169 828 KEYLEKEIQELQEQRI--------DLKEQIKS--------IEKEIENLNGKKeeleEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008909414 292 KIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQA 366
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
48-230 |
9.99e-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: 41.58 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 48 PETLQRCLEENQelrdairQSNQILRERCEELlhfqasqREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEH 127
Cdd:TIGR02168 318 LEELEAQLEELE-------SKLDELAEELAEL-------EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 128 LKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQAL-----EGRARAASEQARQLESEREALQQQHSVQVDQL 202
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEAL 463
|
170 180
....*....|....*....|....*...
gi 1008909414 203 RMQGQSVEAALRMERQAASEEKRKLAQL 230
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARL 491
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
56-354 |
1.57e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 56 EENQELRDAIRQSNQILRERCEELLHFQASQREEKEflmckfqearklvERLGLEKLDLKRQKEQALREVEHLKRCQQQM 135
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-------------ALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 136 AEDKasvkaQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRM 215
Cdd:pfam02463 240 DLLQ-----ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 216 ERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSsvvgSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVM 295
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKE----LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909414 296 ETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIE 354
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
153-316 |
2.04e-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: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 153 LQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHsvqvDQLRMQGQSVEAALrmerqAASEEKRKLAQLQV 232
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDY----DGATAQLRAAQAAV-----KAAQAQLAQAQIDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 233 AYHQLFQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQhKIVMETVPVLKAQADIYKADF 312
Cdd:pfam00529 127 ARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRS-ELSGAQLQIAEAEAELKLAKL 205
|
....
gi 1008909414 313 QAER 316
Cdd:pfam00529 206 DLER 209
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
117-234 |
2.60e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 40.00 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 117 QKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLgelqesqsRLEAATKECQAlEGRARAASEQarqlESEREALQQQHS 196
Cdd:PTZ00491 669 RHQAELLEQEARGRLERQKMHDKAKAEEQRTKLL--------ELQAESAAVES-SGQSRAEALA----EAEARLIEAEAE 735
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1008909414 197 VQVDQLRMQGQSVEAA-----LRMERQAASEEKRKLAQLQVAY 234
Cdd:PTZ00491 736 VEQAELRAKALRIEAEaelekLRKRQELELEYEQAQNELEIAK 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-194 |
3.46e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 51 LQRCLEENQELRDAIRQSNQILRERCEELLHFQ---ASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEH 127
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909414 128 LKRCQQQMaeDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQ 194
Cdd:TIGR02168 433 AELKELQA--ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
139-233 |
3.53e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 139 KASVKAQVTSLLGELQESQ---SRLEAATKEcqaLEGRARAASEQARQLESEREALQQQHS----------VQVDQLRMQ 205
Cdd:PRK09039 76 NQDLQDSVANLRASLSAAEaerSRLQALLAE---LAGAGAAAEGRAGELAQELDSEKQVSAralaqvellnQQIAALRRQ 152
|
90 100
....*....|....*....|....*...
gi 1008909414 206 GQSVEAALRmerqaASEEKRKLAQLQVA 233
Cdd:PRK09039 153 LAALEAALD-----ASEKRDRESQAKIA 175
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-225 |
6.94e-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: 38.90 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 41 LPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEflmckfqearklverlgleklDLKRQKEQ 120
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE---------------------KLKREINE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 121 ALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVD 200
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
170 180
....*....|....*....|....*
gi 1008909414 201 QLRmQGQSVEAALRMERQAASEEKR 225
Cdd:TIGR02169 484 ELS-KLQRELAEAEAQARASEERVR 507
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
27-291 |
8.97e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 38.67 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 27 LGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQS-NQILRERCEELLHFQASQREEKEFLMCKFQEARKLVE 105
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 106 RLGLEKLD-LKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQAL-----EGRARAASE 179
Cdd:pfam12128 326 ALEDQHGAfLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiagikDKLAKIREA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 180 QARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQeydnhIKSSVVGSERKRGMQ 259
Cdd:pfam12128 406 RDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQ-----LENFDERIERAREEQ 480
|
250 260 270
....*....|....*....|....*....|..
gi 1008909414 260 LEDLKQQLQQAEEALVAkqeviDKLKEEAEQH 291
Cdd:pfam12128 481 EAANAEVERLQSELRQA-----RKRRDQASEA 507
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
47-366 |
1.00e-02 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 47 APETLQRCLEENQELRDAIRQSNQILR----ERCEELLHFQASQREE---KEFLMCKFQEARKLVERlglEKLDLKRQKE 119
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDARKaeeaRKAEDARKAEEARKAEdakRVEIARKAEDARKAEEA---RKAEDAKKAE 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 120 QALREVEHLKRCQQQMAEDKASVKAqvtsllGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQV 199
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEA------ARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 200 DQLRMQGQSVEAALRMERQAAsEEKRKLAQLQVAYHQlfQEYDNHIKSSvvgsERKRGMQLEDLKQQLQQAEEALVAKQE 279
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKA-EEARKADELKKAEEK--KKADEAKKAE----EKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909414 280 V---IDKLKEEAEQHKIVMEtvpVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDM 356
Cdd:PTZ00121 1327 AkkkADAAKKKAEEAKKAAE---AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
330
....*....|
gi 1008909414 357 RKRHVEVSQA 366
Cdd:PTZ00121 1404 KKKADELKKA 1413
|
|
|