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Conserved domains on  [gi|315131461|emb|CBY82087|]
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hypothetical protein HFELIS_00010 [Helicobacter felis ATCC 49179]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
92-492 1.43e-08

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  92 RAYAQIMEQEKTRRKELERAHKEQLESLQANTENQQTELQAlqqektTLEQTNTALTQENTELknlnaTQERTHQQTLTN 171
Cdd:COG1196  213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA------ELEELEAELAELEAEL-----EELRLELEELEL 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 172 KEQAYQQALELKNASIHALYHKNTTLSQENQTLKDNKTELETTLIDLVT--IFVSQDKQDKKLTIKEAKPLLESVRKQMI 249
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEAEAELA 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 250 TINQGLgdlklftQEDYRALRALKDDGLSINGLKKRITQIEQEAKKRYEKLQEQYKDYlspkqvedkitatkalyedyls 329
Cdd:COG1196  362 EAEEAL-------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL---------------------- 412
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 330 psavQELKQEHTKELESREQSHSKALQEKDIEHAQVLKEKDKTLEKVAQELKAKERQVQEHARDLADSNKALEKLTQELK 409
Cdd:COG1196  413 ----LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 410 AKDTEHTKELEALQTQHAKELEKARNEIDKDTKLQGYVGKVKDLLQKFVDQVINPMLEKLQ---TEKGAELKAVIQWKKD 486
Cdd:COG1196  489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivVEDDEVAAAAIEYLKA 568

                 ....*.
gi 315131461 487 NEKEKA 492
Cdd:COG1196  569 AKAGRA 574
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
92-492 1.43e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  92 RAYAQIMEQEKTRRKELERAHKEQLESLQANTENQQTELQAlqqektTLEQTNTALTQENTELknlnaTQERTHQQTLTN 171
Cdd:COG1196  213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA------ELEELEAELAELEAEL-----EELRLELEELEL 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 172 KEQAYQQALELKNASIHALYHKNTTLSQENQTLKDNKTELETTLIDLVT--IFVSQDKQDKKLTIKEAKPLLESVRKQMI 249
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEAEAELA 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 250 TINQGLgdlklftQEDYRALRALKDDGLSINGLKKRITQIEQEAKKRYEKLQEQYKDYlspkqvedkitatkalyedyls 329
Cdd:COG1196  362 EAEEAL-------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL---------------------- 412
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 330 psavQELKQEHTKELESREQSHSKALQEKDIEHAQVLKEKDKTLEKVAQELKAKERQVQEHARDLADSNKALEKLTQELK 409
Cdd:COG1196  413 ----LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 410 AKDTEHTKELEALQTQHAKELEKARNEIDKDTKLQGYVGKVKDLLQKFVDQVINPMLEKLQ---TEKGAELKAVIQWKKD 486
Cdd:COG1196  489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivVEDDEVAAAAIEYLKA 568

                 ....*.
gi 315131461 487 NEKEKA 492
Cdd:COG1196  569 AKAGRA 574
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
95-525 3.51e-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: 46.97  E-value: 3.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461    95 AQIMEQEKTRRKELERAHKE----QLESLQANTENQQTELQALQQEKTTLEQTNTALTQENTELknlnatqeRTHQQTLT 170
Cdd:TIGR02168  209 AEKAERYKELKAELRELELAllvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL--------RLEVSELE 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   171 NKEQAYQQALELKNASIHALYHKNTTLSQENQTLKDNKTELETTLIDLvtifvSQDKQDKKLTIKEAKPLLESVRKQMIT 250
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-----ESKLDELAEELAELEEKLEELKEELES 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   251 INQGLGDLKLFTQEDYRALRALKDDglsINGLKKRITQIEQEAKKRYEKLQEQYKDYLSPKQVEDKITATKALYEDYLSP 330
Cdd:TIGR02168  356 LEAELEELEAELEELESRLEELEEQ---LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   331 SAVQELKQEHTKELESREQshskaLQEKDIEHAQVLKEKDKTLEKVAQELKAKERQVQEHARDLAdsnkalekltqelka 410
Cdd:TIGR02168  433 AELKELQAELEELEEELEE-----LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD--------------- 492
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   411 kdtehtkELEALQTQHAKELEKARNEIDKDTKLQGYVGKVKDLL------QKFVDQVINPMLEKLQTEKGAELKAVIQWK 484
Cdd:TIGR02168  493 -------SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdegyEAAIEAALGGRLQAVVVENLNAAKKAIAFL 565
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 315131461   485 KDNEKEKAqyhahlATLAYDLLAGKFPKINAIALLISRGGV 525
Cdd:TIGR02168  566 KQNELGRV------TFLPLDSIKGTEIQGNDREILKNIEGF 600
PLN02939 PLN02939
transferase, transferring glycosyl groups
73-394 4.02e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 46.82  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  73 PFKSRGVDKRISKVKRIEPRAYAQIMEQEKTRRKELERAHKEQLESLQANTENQQ---------------------TELQ 131
Cdd:PLN02939  87 PQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEknilllnqarlqaledlekilTEKE 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 132 ALQQEKTTLEqtnTALTQENTELKNlnATQERTH----QQTLTNKEQAYQQALELKNASIHALYHKNTTLSQENQTLKDN 207
Cdd:PLN02939 167 ALQGKINILE---MRLSETDARIKL--AAQEKIHveilEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDD 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 208 KTELETTLIDLvtifvsQDKQDKKLTIKEAKPLLESVRKQMitinqglgDLKLF-TQEDYRALRALKDDGL--SINGLKK 284
Cdd:PLN02939 242 IQFLKAELIEV------AETEERVFKLEKERSLLDASLREL--------ESKFIvAQEDVSKLSPLQYDCWweKVENLQD 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 285 RITQIEQEAKKrYEKLQEQYKDYlsPKQVeDKITATKALYEDYLSPSAVQELKQEHTKELESREQSHSKALQEKDIEHAQ 364
Cdd:PLN02939 308 LLDRATNQVEK-AALVLDQNQDL--RDKV-DKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQE 383
                        330       340       350
                 ....*....|....*....|....*....|
gi 315131461 365 VLKEKDKTLEKVAQElkAKERQVQEHARDL 394
Cdd:PLN02939 384 SIKEFQDTLSKLKEE--SKKRSLEHPADDM 411
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
397-482 3.41e-04

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153327  Cd Length: 231  Bit Score: 42.44  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 397 SNKALEKLTQELKAKDTEHTKELEALQTQHAKELEKARNEIDK---DT-KLQGYVGKVKDLLQKFVD---QVINPMLEKL 469
Cdd:cd07643   91 TSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKkssDTiRLQKKARKGKGDLQPQLDsamQDVNDKYLLL 170
                         90
                 ....*....|....
gi 315131461 470 -QTEKGAELKAVIQ 482
Cdd:cd07643  171 eETEKKAVRNALIE 184
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
314-448 3.99e-04

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 43.55  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  314 EDKITATKALYEDYLSP---SAVQELKQEHT-----KELESREQSHSKALQEKDIEHAQVLKEKDKTLEKVAQELKAKER 385
Cdd:NF033875  149 ENEANKSTSIPKEFETPdvdKAVDEAKKDPNitvveKPAEDLGNVSSKDLAAKEKEVDQLQKEQAKKIAQQAAELKAKNE 228
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315131461  386 QVQEHARDLADSNKALEKLTQELKAKDTEHTKELEALQTQHAKELEKARNEIDKDTKLQGYVG 448
Cdd:NF033875  229 KIAKENAEIAAKNKAEKERYEKEVAEYNKHKNENGYVNEAISKNLVFDQSVVTKDTKISSIKG 291
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
107-488 5.62e-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: 39.82  E-value: 5.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   107 ELERAHKEQLESLQANTENQQTELQALQQEKTTLEQTNTALTQENTElkNLNATQERTHQQTLTNKEQAYQQALELKNAS 186
Cdd:pfam12128  340 ETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE--QNNRDIAGIKDKLAKIREARDRQLAVAEDDL 417
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   187 IHALYHKNTTLSQENQTLKDNKTELETTLIDL-VTIFVSQDKQDKKLTIKEAKPLLESVRKQMITINQGLGDLklftQED 265
Cdd:pfam12128  418 QALESELREQLEAGKLEFNEEEYRLKSRLGELkLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERL----QSE 493
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   266 YRALRALKDDGLSINGlkkRITQIEQEAKKRYEKLQEQykdyLSP----------KQVED------KITATKALYEDYLS 329
Cdd:pfam12128  494 LRQARKRRDQASEALR---QASRRLEERQSALDELELQ----LFPqagtllhflrKEAPDweqsigKVISPELLHRTDLD 566
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   330 PSAVQE--------------LKQ-------EHTKELESREQSHSKALQEKDIEHAQVlkekDKTLEKVAQELKAKERQVQ 388
Cdd:pfam12128  567 PEVWDGsvggelnlygvkldLKRidvpewaASEEELRERLDKAEEALQSAREKQAAA----EEQLVQANGELEKASREET 642
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   389 EHARDLADSNKALEKLTQELKAKDTEHTKELEAlqtqHAKELEKARNEIDKDTKLQGYvgKVKDLLQKFVDQvinpmLEK 468
Cdd:pfam12128  643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAE----RKDSANERLNSLEAQLKQLDK--KHQAWLEEQKEQ-----KRE 711
                          410       420
                   ....*....|....*....|
gi 315131461   469 LQTEKGAELKAVIQWKKDNE 488
Cdd:pfam12128  712 ARTEKQAYWQVVEGALDAQL 731
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
92-492 1.43e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  92 RAYAQIMEQEKTRRKELERAHKEQLESLQANTENQQTELQAlqqektTLEQTNTALTQENTELknlnaTQERTHQQTLTN 171
Cdd:COG1196  213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA------ELEELEAELAELEAEL-----EELRLELEELEL 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 172 KEQAYQQALELKNASIHALYHKNTTLSQENQTLKDNKTELETTLIDLVT--IFVSQDKQDKKLTIKEAKPLLESVRKQMI 249
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEAEAELA 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 250 TINQGLgdlklftQEDYRALRALKDDGLSINGLKKRITQIEQEAKKRYEKLQEQYKDYlspkqvedkitatkalyedyls 329
Cdd:COG1196  362 EAEEAL-------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL---------------------- 412
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 330 psavQELKQEHTKELESREQSHSKALQEKDIEHAQVLKEKDKTLEKVAQELKAKERQVQEHARDLADSNKALEKLTQELK 409
Cdd:COG1196  413 ----LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 410 AKDTEHTKELEALQTQHAKELEKARNEIDKDTKLQGYVGKVKDLLQKFVDQVINPMLEKLQ---TEKGAELKAVIQWKKD 486
Cdd:COG1196  489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivVEDDEVAAAAIEYLKA 568

                 ....*.
gi 315131461 487 NEKEKA 492
Cdd:COG1196  569 AKAGRA 574
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
93-329 7.05e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.24  E-value: 7.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  93 AYAQIM--EQEKTRRKELERAHK---EQLESLQANTENQQTELQALQQEK--TTLEQTNTALTQENTELKN-LNATQERt 164
Cdd:COG3206  156 ALAEAYleQNLELRREEARKALEfleEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESqLAEARAE- 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 165 hQQTLTNKEQAYQQALELKNASIHALyhkntTLSQENQTLKDNKTELETTLIDLVTIFvsqdkQDKKLTIKEAKPLLESV 244
Cdd:COG3206  235 -LAEAEARLAALRAQLGSGPDALPEL-----LQSPVIQQLRAQLAELEAELAELSARY-----TPNHPDVIALRAQIAAL 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 245 RKQmitINQGLGDLKLFTQEDYRALRAlkddglSINGLKKRITQIEQEAkKRYEKLQEQYKDYlspkqvEDKITATKALY 324
Cdd:COG3206  304 RAQ---LQQEAQRILASLEAELEALQA------REASLQAQLAQLEARL-AELPELEAELRRL------EREVEVARELY 367

                 ....*
gi 315131461 325 EDYLS 329
Cdd:COG3206  368 ESLLQ 372
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
95-525 3.51e-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: 46.97  E-value: 3.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461    95 AQIMEQEKTRRKELERAHKE----QLESLQANTENQQTELQALQQEKTTLEQTNTALTQENTELknlnatqeRTHQQTLT 170
Cdd:TIGR02168  209 AEKAERYKELKAELRELELAllvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL--------RLEVSELE 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   171 NKEQAYQQALELKNASIHALYHKNTTLSQENQTLKDNKTELETTLIDLvtifvSQDKQDKKLTIKEAKPLLESVRKQMIT 250
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-----ESKLDELAEELAELEEKLEELKEELES 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   251 INQGLGDLKLFTQEDYRALRALKDDglsINGLKKRITQIEQEAKKRYEKLQEQYKDYLSPKQVEDKITATKALYEDYLSP 330
Cdd:TIGR02168  356 LEAELEELEAELEELESRLEELEEQ---LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   331 SAVQELKQEHTKELESREQshskaLQEKDIEHAQVLKEKDKTLEKVAQELKAKERQVQEHARDLAdsnkalekltqelka 410
Cdd:TIGR02168  433 AELKELQAELEELEEELEE-----LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD--------------- 492
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   411 kdtehtkELEALQTQHAKELEKARNEIDKDTKLQGYVGKVKDLL------QKFVDQVINPMLEKLQTEKGAELKAVIQWK 484
Cdd:TIGR02168  493 -------SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdegyEAAIEAALGGRLQAVVVENLNAAKKAIAFL 565
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 315131461   485 KDNEKEKAqyhahlATLAYDLLAGKFPKINAIALLISRGGV 525
Cdd:TIGR02168  566 KQNELGRV------TFLPLDSIKGTEIQGNDREILKNIEGF 600
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
104-437 3.92e-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: 46.97  E-value: 3.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   104 RRKELERaHKEQLESLQANTENQQTELQALQQEKTTLEQTNTALTQENTELknlnaTQERTHQQTLTNKEQAYQQALELK 183
Cdd:TIGR02168  675 RRREIEE-LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-----SRQISALRKDLARLEAEVEQLEER 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   184 NASIHalyHKNTTLSQENQTLKDNKTELETTLIDLvtifvSQDKQDKKLTIKEAKPLLESVRKQMITINQGLGDLKLFTQ 263
Cdd:TIGR02168  749 IAQLS---KELTELEAEIEELEERLEEAEEELAEA-----EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   264 EDYRALRALKDDglsINGLKKRITQIEQEAKKRYEKLQEQYKDYLSPKQVEDKIT-ATKALYEDYLSPSAVQELKQEHTK 342
Cdd:TIGR02168  821 NLRERLESLERR---IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEsELEALLNERASLEEALALLRSELE 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   343 ELESREQSHSKALQEKDIEHAQvLKEKDKTLEKVAQELKAKERQVQEHARDLAdsnkaleKLTQELKAKDTEHTKELEAL 422
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEE-LREKLAQLELRLEGLEVRIDNLQERLSEEY-------SLTLEEAEALENKIEDDEEE 969
                          330
                   ....*....|....*
gi 315131461   423 QTQHAKELEKARNEI 437
Cdd:TIGR02168  970 ARRRLKRLENKIKEL 984
PLN02939 PLN02939
transferase, transferring glycosyl groups
73-394 4.02e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 46.82  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  73 PFKSRGVDKRISKVKRIEPRAYAQIMEQEKTRRKELERAHKEQLESLQANTENQQ---------------------TELQ 131
Cdd:PLN02939  87 PQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEknilllnqarlqaledlekilTEKE 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 132 ALQQEKTTLEqtnTALTQENTELKNlnATQERTH----QQTLTNKEQAYQQALELKNASIHALYHKNTTLSQENQTLKDN 207
Cdd:PLN02939 167 ALQGKINILE---MRLSETDARIKL--AAQEKIHveilEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDD 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 208 KTELETTLIDLvtifvsQDKQDKKLTIKEAKPLLESVRKQMitinqglgDLKLF-TQEDYRALRALKDDGL--SINGLKK 284
Cdd:PLN02939 242 IQFLKAELIEV------AETEERVFKLEKERSLLDASLREL--------ESKFIvAQEDVSKLSPLQYDCWweKVENLQD 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 285 RITQIEQEAKKrYEKLQEQYKDYlsPKQVeDKITATKALYEDYLSPSAVQELKQEHTKELESREQSHSKALQEKDIEHAQ 364
Cdd:PLN02939 308 LLDRATNQVEK-AALVLDQNQDL--RDKV-DKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQE 383
                        330       340       350
                 ....*....|....*....|....*....|
gi 315131461 365 VLKEKDKTLEKVAQElkAKERQVQEHARDL 394
Cdd:PLN02939 384 SIKEFQDTLSKLKEE--SKKRSLEHPADDM 411
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
223-564 7.55e-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: 7.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   223 VSQDKQDKKLTIKEAKPLLESVRKQMITINQGLGDLKLFTQEDYRALRALKDD----GLSINGLKKRITQIEQE----AK 294
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarlEAEVEQLEERIAQLSKEltelEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   295 KRYEKLQEQYKDYLSPKQVEDKITATKALYEDYLSPSAVQELKQEHTKELESREQSHSKALQEKDIEHAQVLKEKDKTLE 374
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   375 KVAQELKAKERQVQEHARDLADSNKALEKLTQELKAKDTEHTKELEALQTQHA---------KELEKARNEIDKDT-KLQ 444
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSeleelseelRELESKRSELRRELeELR 921
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   445 GYVGKVKDLLQKFvDQVINPMLEKLQTEKGAELKAVIQWKKDNEKEKAQYHAHLATLAydllagkfpkiNAIALLisrgG 524
Cdd:TIGR02168  922 EKLAQLELRLEGL-EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE-----------NKIKEL----G 985
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 315131461   525 VKNAMNPEYFESIAKdrRDRFLNKHINEIEKSLNQELKPI 564
Cdd:TIGR02168  986 PVNLAAIEEYEELKE--RYDFLTAQKEDLTEAKETLEEAI 1023
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
225-439 9.44e-05

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: 45.14  E-value: 9.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 225 QDKQDKKLTIKEAKPLLESVRKQMITINQGLGDLKLFTQEDYRALRALKDDGLSINGLKKRITQIEQEAKKRYEKLQEQY 304
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 305 KDYLspkqvedkitatKALYEDYLSPSAVQELKQEHTKELESREQSHsKALQEKDIEHAQVLKEKDKTLEKVAQELKAKE 384
Cdd:COG4942  107 AELL------------RALYRLGRQPPLALLLSPEDFLDAVRRLQYL-KYLAPARREQAEELRADLAELAALRAELEAER 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 315131461 385 RQVQEHARDLADSNKALEKLTQELKAKDTEHTKELEALQTQhAKELEKARNEIDK 439
Cdd:COG4942  174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE-LAELQQEAEELEA 227
PRK12704 PRK12704
phosphodiesterase; Provisional
307-432 1.06e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.15  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 307 YLSPKQVEDKITATKALYEDYL--SPSAVQELKQEhtKELESREQSHskalqEKDIEHAQVLKEKDKTLEKVAQELKAKE 384
Cdd:PRK12704  23 FVRKKIAEAKIKEAEEEAKRILeeAKKEAEAIKKE--ALLEAKEEIH-----KLRNEFEKELRERRNELQKLEKRLLQKE 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 315131461 385 RQVQEHARDLADSNKALEKLTQELKAKDTEHTK---ELEALQTQHAKELEK 432
Cdd:PRK12704  96 ENLDRKLELLEKREEELEKKEKELEQKQQELEKkeeELEELIEEQLQELER 146
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
80-212 1.40e-04

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


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 44.33  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   80 DKRISKVKRIEPRAYAQIMEQEKTRRKELERAhKEQLESLQANTENQQTELQALQQEKTTLEQtntALTQENTELKNLNA 159
Cdd:TIGR04320 235 DSYIADGNKFDKTPIPNPPNSLAALQAKLATA-QADLAAAQTALNTAQAALTSAQTAYAAAQA---ALATAQKELANAQA 310
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 315131461  160 TQERTHQQTLTNKEQAYQQA-LELKNAsihalyhkNTTLSQENQTLKDNKTELE 212
Cdd:TIGR04320 311 QALQTAQNNLATAQAALANAeARLAKA--------KEALANLNADLAKKQAALD 356
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
269-502 2.90e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 269 LRALKDDGLS--INGLKKRITQIEQEAKKRYEKLQEQYKDYlspKQVEDKITATKALYEDYLSPSAVQELKQEHTKELES 346
Cdd:COG1196  229 LLLLKLRELEaeLEELEAELEELEAELEELEAELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 347 REQSHSKALQEKDIEHAQVLKEKDKTLEKVAQELKAKERQVQEHARDLADSNKALEKLTQELKAKDTEHTKELEALQTQH 426
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315131461 427 AKELEKARNEIDKDTKLQGYVGKVKDLLQKfvdqvinpmLEKLQTEKGAELKAVIQWKKDNEKEKAQYHAHLATLA 502
Cdd:COG1196  386 EELLEALRAAAELAAQLEELEEAEEALLER---------LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
397-482 3.41e-04

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153327  Cd Length: 231  Bit Score: 42.44  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 397 SNKALEKLTQELKAKDTEHTKELEALQTQHAKELEKARNEIDK---DT-KLQGYVGKVKDLLQKFVD---QVINPMLEKL 469
Cdd:cd07643   91 TSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKkssDTiRLQKKARKGKGDLQPQLDsamQDVNDKYLLL 170
                         90
                 ....*....|....
gi 315131461 470 -QTEKGAELKAVIQ 482
Cdd:cd07643  171 eETEKKAVRNALIE 184
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
314-448 3.99e-04

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 43.55  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  314 EDKITATKALYEDYLSP---SAVQELKQEHT-----KELESREQSHSKALQEKDIEHAQVLKEKDKTLEKVAQELKAKER 385
Cdd:NF033875  149 ENEANKSTSIPKEFETPdvdKAVDEAKKDPNitvveKPAEDLGNVSSKDLAAKEKEVDQLQKEQAKKIAQQAAELKAKNE 228
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315131461  386 QVQEHARDLADSNKALEKLTQELKAKDTEHTKELEALQTQHAKELEKARNEIDKDTKLQGYVG 448
Cdd:NF033875  229 KIAKENAEIAAKNKAEKERYEKEVAEYNKHKNENGYVNEAISKNLVFDQSVVTKDTKISSIKG 291
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
99-439 1.11e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  99 EQEKTRRKELERAHKEQLESLQANTENQQTELQALQQEKTTLEQTNTALTQENTELKNLNATQERTHQQTLTNKEQAYQQ 178
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 179 ALELKNASIHALYHKntTLSQENQTLKDNKTELETTLIDLVTIFVSQDKQDKKLTIKEAKP-LLESVRKQMITINQGLGD 257
Cdd:COG1196  510 VKAALLLAGLRGLAG--AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAaKAGRATFLPLDKIRARAA 587
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 258 LKLFTQEDYRALRALKDDGLSINGLKKRITQIEQEAKKRYEKLQEQYKDYLSPKQVEDKITATKALYEDYLSPSAVQELK 337
Cdd:COG1196  588 LAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR 667
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 338 QEHTKELESREQSHSKALQEKDIEHAQVLKEKDKTLEKVAQELKAKERQVQEHARDLADSNKALEKLTQELKAKDTEHTK 417
Cdd:COG1196  668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
                        330       340       350
                 ....*....|....*....|....*....|.
gi 315131461 418 ELEALQ---------TQHAKELEKARNEIDK 439
Cdd:COG1196  748 LEEEALeelpeppdlEELERELERLEREIEA 778
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
285-502 1.22e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 285 RITQIEQEAKKRYEKLQEQ------YKDYlspKQVEDKITATKALYEDYLSpSAVQELKQEHTKELESREQSHSKALQEK 358
Cdd:COG1196  190 RLEDILGELERQLEPLERQaekaerYREL---KEELKELEAELLLLKLREL-EAELEELEAELEELEAELEELEAELAEL 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 359 DIEHA---QVLKEKDKTLEKVAQELKAKERQVQEHARDLADSNKALEKLTQELKAKDTEHTKELEALQTQHAKELEKARN 435
Cdd:COG1196  266 EAELEelrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315131461 436 EIDKDTKLQGYVGKVKDLLQKFVDQVINpmLEKLQTEKGAELKAVIQWKKDNEKEKAQYHAHLATLA 502
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAE--LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
93-296 1.25e-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: 41.67  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  93 AYAQIMEQEKTRRKELER---AHKEQLESLQANTENQQTELQALQQE----KTTLEQTNTALTQENTELKNLNATQERTH 165
Cdd:COG4942   17 AQADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRiaalARRIRALEQELAALEAELAELEKEIAELR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 166 QQTLTNKEQ-------AYQQ------ALELKNASIHALYHKNTTLSQENQTLKDNKTELETTLIDLVTIFVSQDKQDKKL 232
Cdd:COG4942   97 AELEAQKEElaellraLYRLgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315131461 233 --TIKEAKPLLESVRKQMITINQGLGDLKLFTQEDYRALRALKDDGLSINGLKKRITQIEQEAKKR 296
Cdd:COG4942  177 eaLLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
PTZ00121 PTZ00121
MAEBL; Provisional
80-493 1.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   80 DKRISKVKRIEP---------RAYAQIMEQEKTRRKELERAHKEQLESLQANTENQQTELQALQQEKTTLEQTNTALTQE 150
Cdd:PTZ00121 1223 AKKAEAVKKAEEakkdaeeakKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  151 NTELKNLNATQERTHQQTLTNKEQAYQQALELKNASIHALYHKNTTLSQENQTLKDNKTELETTLIDlvtifvSQDKQDK 230
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA------EKKKEEA 1376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  231 KLTIKEAKPLLESVRKQmitinqglGDLKLFTQEDYRALRALKDDGLSinglKKRITQIEQEAKKRYEKLQEQYKDYLSP 310
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKA--------DEAKKKAEEDKKKADELKKAAAA----KKKADEAKKKAEEKKKADEAKKKAEEAK 1444
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  311 KQVEDKITATKALYEDYLSPSAVQELKQEHTKEL--ESREQSHSKALQEKDIEHAQVLKEKDKTLEKVAQELKAKERQVQ 388
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  389 EHARDLADSNKALEKLTQELKAKDTEHTKELEALQTQHAKELEKARNEIDKDTKLQGYVGKVKDLLQKFVDQVINpMLEK 468
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK-LYEE 1603
                         410       420
                  ....*....|....*....|....*
gi 315131461  469 LQTEKGAELKaviqwKKDNEKEKAQ 493
Cdd:PTZ00121 1604 EKKMKAEEAK-----KAEEAKIKAE 1623
COG5283 COG5283
Phage-related tail protein [Mobilome: prophages, transposons];
71-186 2.34e-03

Phage-related tail protein [Mobilome: prophages, transposons];


Pssm-ID: 444094 [Multi-domain]  Cd Length: 747  Bit Score: 40.99  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  71 NQPFKS------RGVDKRISKVKRIEPRAYAQI--MEQEKTRRKELERAHKEQLESLQ-------ANTENQQTELQALQQ 135
Cdd:COG5283    9 DKPFKSalesakQRVAALAQALKALEAPTRALAraLERAKQAAARLQTKYNKLRQSLQrlrqaldQAGIDTRQLSAAQRR 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 315131461 136 EKTTLEQTNTALTQENTELKNLNATQERthqqtLTNKEQAYQQALELKNAS 186
Cdd:COG5283   89 LRSSLEQTNRQLERQQQRLARLGARQDR-----LKAARARLQRLAGAGAAA 134
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
92-468 2.55e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  92 RAYAQIMEQEKTRRKELERAHKEQLESLQANTENQQTELQALQQEKTTLEQTNTALTQentELKNLNATQERTHQQTLTN 171
Cdd:COG4717  170 AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE---ELEQLENELEAAALEERLK 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 172 KEQAYQQALelknASIHALyhknTTLSQENQTLKDNKTELETTLIDLVTIFVSQDKQDKKLTIKEAKPLLESVRKQMITI 251
Cdd:COG4717  247 EARLLLLIA----AALLAL----LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEE 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 252 NQGLGDLKLFTQEDYRALRALKDDGLSINGLKKRITQIEQEAKK-RYEKLQEQYKDYLSPKQVEDKitatkalyEDYLSP 330
Cdd:COG4717  319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDE--------EELRAA 390
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 331 SAVQELKQEHTKELESREQshskALQEKDIEHAQVLKEKDKtlEKVAQELKAKERQVQEHARDLADSNKALEKLTQELka 410
Cdd:COG4717  391 LEQAEEYQELKEELEELEE----QLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAEL-- 462
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 315131461 411 KDTEHTKELEALQTQHAKELEKARNEIDKDTKLQGYVGKVKDLLQKFVDQVINPMLEK 468
Cdd:COG4717  463 EQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
46 PHA02562
endonuclease subunit; Provisional
219-455 2.69e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 219 VTIFVSQDKQDKKLtIKEAKPLLESVRKQMITINQglgdlKLFTQEDY-RALRALKDDGLS-----INGLKKRITQIEQE 292
Cdd:PHA02562 162 ISVLSEMDKLNKDK-IRELNQQIQTLDMKIDHIQQ-----QIKTYNKNiEEQRKKNGENIArkqnkYDELVEEAKTIKAE 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 293 AKKRYEKLQEQYKDYLSP----KQVEDKITATKA----------LYEDY-LSPSAVQELKQEHTKELESREQ----SHSK 353
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPsaalNKLNTAAAKIKSkieqfqkvikMYEKGgVCPTCTQQISEGPDRITKIKDKlkelQHSL 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461 354 ALQEKDIEHAQVLKEKDKTLEKVAQELKAKERQVQEHARDLADSNKALEKLTQELKAKDTEHTKELEALQtQHAKELEKA 433
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQ-DELDKIVKT 394
                        250       260
                 ....*....|....*....|..
gi 315131461 434 RNEIDKDtklQGYVGKVKDLLQ 455
Cdd:PHA02562 395 KSELVKE---KYHRGIVTDLLK 413
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
291-438 3.50e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  291 QEAKKRYEKLqEQYKDYLSPKQVEDKITATKALYEDylspsaVQELKQEHTKELESREQSHSKALQEKDIEHAQVLKEKD 370
Cdd:COG4913   265 AAARERLAEL-EYLRAALRLWFAQRRLELLEAELEE------LRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315131461  371 KTLEKVAQELKAKERQVQEHARDLADsnkaLEKLTQELKAKDTEHTKELEALQTQHAKELEKARNEID 438
Cdd:COG4913   338 DRLEQLEREIERLERELEERERRRAR----LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
82-444 3.80e-03

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: 40.34  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461    82 RISKVKRIEPRAYAQIMEQEKTRRKELERAHKEQLESLQANTENQQTELQALQQEKTTLEQTNTALTQENTELKNLNATQ 161
Cdd:TIGR00618  268 RIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   162 ERTHQQTLTNKEQAYQQALELKNAS--------IHALYHKNTTLSQENQTLKDNKTEL--ETTLIDLVTIFVSQDKQDKK 231
Cdd:TIGR00618  348 QTLHSQEIHIRDAHEVATSIREISCqqhtltqhIHTLQQQKTTLTQKLQSLCKELDILqrEQATIDTRTSAFRDLQGQLA 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   232 LTIKEAKPLLESVRKQMITINQGLGDLKL---FTQEDYRALRALKDDGLSINGLKKRITQIEQEAKKRYEKLQEQYKdyL 308
Cdd:TIGR00618  428 HAKKQQELQQRYAELCAAAITCTAQCEKLekiHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPC--P 505
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   309 SPKQVEDKITATKALYEDYLSPSAVQELKQEHTKELESREQSHSKALQEKdiEHAQVLKEKDKTLEKVAQELKAKERQVQ 388
Cdd:TIGR00618  506 LCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER--KQRASLKEQMQEIQQSFSILTQCDNRSK 583
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 315131461   389 EHARDLADSNKALEKLTQELkakdTEHTKELEALQTQHAKELEKARNEIDKDTKLQ 444
Cdd:TIGR00618  584 EDIPNLQNITVRLQDLTEKL----SEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
93-187 3.86e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461  93 AYAQIMEQEKTRRKELERAHKEQLESLQANTENQQTELQALQQEKTTLEQTNTALTQENTELKNLN---ATQERTHQQTL 169
Cdd:COG3206  292 DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLErevEVARELYESLL 371
                         90
                 ....*....|....*....
gi 315131461 170 TNKEQAY-QQALELKNASI 187
Cdd:COG3206  372 QRLEEARlAEALTVGNVRV 390
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
107-488 5.62e-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: 39.82  E-value: 5.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   107 ELERAHKEQLESLQANTENQQTELQALQQEKTTLEQTNTALTQENTElkNLNATQERTHQQTLTNKEQAYQQALELKNAS 186
Cdd:pfam12128  340 ETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE--QNNRDIAGIKDKLAKIREARDRQLAVAEDDL 417
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   187 IHALYHKNTTLSQENQTLKDNKTELETTLIDL-VTIFVSQDKQDKKLTIKEAKPLLESVRKQMITINQGLGDLklftQED 265
Cdd:pfam12128  418 QALESELREQLEAGKLEFNEEEYRLKSRLGELkLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERL----QSE 493
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   266 YRALRALKDDGLSINGlkkRITQIEQEAKKRYEKLQEQykdyLSP----------KQVED------KITATKALYEDYLS 329
Cdd:pfam12128  494 LRQARKRRDQASEALR---QASRRLEERQSALDELELQ----LFPqagtllhflrKEAPDweqsigKVISPELLHRTDLD 566
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   330 PSAVQE--------------LKQ-------EHTKELESREQSHSKALQEKDIEHAQVlkekDKTLEKVAQELKAKERQVQ 388
Cdd:pfam12128  567 PEVWDGsvggelnlygvkldLKRidvpewaASEEELRERLDKAEEALQSAREKQAAA----EEQLVQANGELEKASREET 642
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   389 EHARDLADSNKALEKLTQELKAKDTEHTKELEAlqtqHAKELEKARNEIDKDTKLQGYvgKVKDLLQKFVDQvinpmLEK 468
Cdd:pfam12128  643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAE----RKDSANERLNSLEAQLKQLDK--KHQAWLEEQKEQ-----KRE 711
                          410       420
                   ....*....|....*....|
gi 315131461   469 LQTEKGAELKAVIQWKKDNE 488
Cdd:pfam12128  712 ARTEKQAYWQVVEGALDAQL 731
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
99-442 6.90e-03

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: 39.57  E-value: 6.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461    99 EQEKTRRKELERAHKEQLESLQANTENQQTELQALQQEKTTLEQTNTALTQENTEL-----KNLNATQERTHQQTLTNKE 173
Cdd:TIGR00618  197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQeeqlkKQQLLKQLRARIEELRAQE 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   174 QAYQQALELKNASIHA--LYHKNTTLSQENQTLKDNKTELETTLIDLVTIFV-SQDKQDKKLTIKEAKPLLESVRKQMIT 250
Cdd:TIGR00618  277 AVLEETQERINRARKAapLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMkRAAHVKQQSSIEEQRRLLQTLHSQEIH 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   251 INQGLGDLKLFTQEDYRALrALKDDGLSINGLKKRITQIEQEAKKRYEKLQEQYKDYLSPKQVEDKITATKALYEDYLSP 330
Cdd:TIGR00618  357 IRDAHEVATSIREISCQQH-TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQEL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461   331 SAVQELKQEHTKELESREQSHSKALQEKDIEHAQVLKEKDKTLEKVAQELKAKERQVQEHARDLADSNKALEKLTQELKA 410
Cdd:TIGR00618  436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP 515
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 315131461   411 K---------DTEHTKELEALQTQHAKELEKARNEIDKDTK 442
Cdd:TIGR00618  516 ArqdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
92-213 9.65e-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: 39.27  E-value: 9.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315131461    92 RAYAQIMEQEKTRRKELERAhKEQLESLQANTENQQTELQALQQEKTT--LEQTNTALTQENTELKNLNATQERTHQQtl 169
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERL-EARLERLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEA-- 462
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 315131461   170 tnkEQAYQQALELKNASIHALYHKNTTLSQENQTLKDNKTELET 213
Cdd:TIGR02168  463 ---LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
 
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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